Dr. Amino Acid
Dr. Aydın Duygu
ISTANBUL MEDICAL BOOKS
© Istanbul Medical Publishing SCIENTIFIC WORKS
Dr. Amino acid
Dr. Aydın Duygu
2nd Edition 2017
ISBN - 978-605-4949-65-6
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Karadeniz Technical University Faculty of Medicine, 1998.
2002 Specialty at Sisli Etfal Educational Research Hospital and became a Family Physician specialist. In 2010, he completed his master's degree at Bogazici University Institute of Biomedical Engineering. He currently conducts 3P Medicine in his own clinic. It applies amino acid analysis and amino acid treatments in preventive medicine and personalized medicine applications. Athlete's health and nutritional support are among the leading working areas. He is also the Medical Director of Biotailor Labs, headquartered in Sweden.
Dear readers,
If you read this book and know what it is about health, you will know that you will have a full life; I would like to state that you will find topics that are free from repeated information.
In this book you will read the amino acids that make up the building blocks of living things and how amino acids affect every moment of life.
Nowadays, with all kinds of speculative information about health spreading right away, you will be amazed why you have never heard of the studies of respected science centers that produce solutions that can prevent and prevent disease risks for years.
We have long discovered the way to preserve developed world health and improve physical and mental performance when we are taking boxes of pills without knowing whether it is necessary or not.
This book describes two important concepts that will revolutionize the protective tactics of AMINO ACID ANALYSIS and AMINO ACID TREATMENTS .
Dr. All information contained in Amino Acid is based on scientific evidence and references are presented extensively at the end of the chapter.
My primary school teacher who taught me the letters is Aysen Tecer.
Over the last 10 years, books have been published frequently in healthy nutrition, wellness and the like.
The vast majority of the society is following the publications on health, and the health is more in the media.
However, neither a book nor a detailed article related to AMINO ACIDS has been written to this day .
75% of the body's dry weight excluding water is from amino acids; It is interesting to observe that about 1.5% of minerals and vitamins are 1.5%, which ignores 75% of health and wellness science and economics which has been continuing for 1.5 years. This area has been passed by the word of protein until now. On the other hand, although it is attributed importance as a building stone of the body because it is a complicated, detailed and troublesome area, these two words are imprisoned.
HALBUKI BÜCÜDUN BUILDING STONE ...
At birth, amino acids form the source of life. All the structure and all the functions in our body are made up of 20 amino acids alone or in combination to form proteins. Almost all of the DNA, RNA, skins, bones, muscles, tendons, blood, antibodies, nerves, all enzymes, hormones are made up of amino acids of all chemicals that carry out brain functions.
20 amino acids are sufficient and we are physically and mentally healthy at the necessary balances. Genes (DNA, RNA) only function through these 20 amino acids.
The most important thing is that the amino acids are derived from the foods. Especially if 9 of the 20 ami- no acids are not taken with food, there is no chance of producing the body.
The amino acids that form the basis of life must be the main topic when the subject is nutrition . Because amino acids are the basis of all kinds of physical and psychological discomfort. For this reason, 20 amino acids can not be understood at all without knowing how to feed properly, how nutrition is related to diseases and health.
Amino acids can not become conscious without being known healthy ...
Health consciousness is unfortunately only carried out through auxiliary substances today. All vitamins and minerals are aids to the functioning of amino acids.The main thing is neglected. Amino acids are found in pharmacy showcases and vitamin shops, full of unconscious and dangerous assumptions of doping of the athletes.
People want to be healthy, to improve performance, to feel good, constant vitamins, minerals and so on. support. However, everybody has different ways of eating, life style, biochemistry and genetic background. It is now possible to determine by biochemical analysis which support and where to buy it.
In order to be healthy in humans, early diagnosis is advanced. However, almost all of the tests done with the name of check-up are positive when the patient is ill.So whether there is disease or not, it analyzes it; does not analyze the processes leading to the disease.
When the blood levels of amino acids were analyzed, it was determined that specific changes occurred at amino acid levels years before diabetes, cancer, and many other diseases occurred. For this reason, amino acid analysis can predict disease risks very early and is the most appropriate test for preventive medicine.For example, Harvard University and the Swedish Malmö Diabetes and Cancer Research Institute reported in 2013 that amino acids signaled about 10 years before type 2 diabetes and heart disease developed.
How society can understand why amino acids are based on life, how nutrition and movement need to be built on amino acid consciousness, how amino acids have informed health risks many years ago and how the right amino acids, vitamins and minerals have reduced risks has been summarized from hundreds of scientific articles published since 1930 a dille " Amino Acid "in my book. At the same time, we have published articles in important medical journals, such as obesity, diabetes, cancer, depression and Alzheimer's, which we have desperately dismissed. For this reason, the book aims to draw attention of health professionals (doctors, nurses, dietitians, physiotherapists, exercise consultants, sports scientists) to the very fast advancing amino acid studies in the world.
I have noticed from the feedback of my precious readers who read my book in a year, the amazement and astonishment of the listeners in the seminars and trainings that I gave: I have never thought about the difference between living and inanimate as the only purpose is the health, What is the simplest living thing?We did not ask for what is dead.
For this reason, I think that it is easiest to understand how important amino acids are in response to this basic question.
WHAT WILL YOU HAVE? Bacteria, fungi, viruses, algae, herbs, trees
insects, reptiles, vertebrate animals and people ....
THE MOST LIBERAL DNA, RNA INCLUDED
WHAT IS COMMON FEATURE? So if there is DNA, there is vitality, if there is no DNA,
it is impossible to talk about.
DNA LIVING HOW TO MANAGE all of the same 20 amino acids of DNA in all living things? how the cell will work.
20 AMINO ACID WHERE DOES ALL BE OBTAINED FROM HERBAL AND ANIMALS? obtained.
Eleven of them can be synthesized by the human body at the same time, while 9 of them must be obtained from absolutely pure grains.
NUTRITION WHAT ARE THE FUNDAMENTALS OF THE BODY, INCLUDING AMINO ACIDS? materials that can not be produced (essentials)
to collect.
DNA PROVIDES ONLY 20 AMINO ASIDI FOR THE BASIC AMENITIES FOR THE TREATMENT OF THE AMINO ACTIVITY ONLY.
AMENOUS ACID IS A MORE IMPORTANT NON-BREATHED NUTRITION WITH MORE OPINION.
AMINO ACIDS ROLE PLAY EVERY HEART ABOUT HEALTH.
Food, Amino Acid, Health Relation
cell
chromosome
human
core
DNA
amino acid chain
FOOD
- WHAT AMINO ACID? one
- AMINO ACIDS NUTRITION BASIC APPROPRIATE 3
Since the body can generate energy from all kinds of food, what is the prospect of which one we choose? 6
Essential (the body can not produce, the food has to take
items) 7
- AMINO ACIDS LIFE WONDER 9
Amino acids are used in all structures and functions of the body. 11th
The surprise in the meteoric: amino acids 16
- GEN-AMINO ACID-PROTEIN RELATIONSHIP 18
Genetic code and protein synthesis 19
Effect of amino acids on genes 21
- RESTRICTING AMINO ACID 23
The body has enough essential amino acid to produce every protein every moment
do you have? 24
If the situation is so sensitive (Essential) does amino acid deficiency occur? How is it? 24
Why are amino acids reduced? 24
How is quality protein provided? 25
What should be done so that sufficient amounts of restrictive amino acids can be taken? 26
Do plants lack sufficient protein and amino acids? 27
Complementary proteins 30
How do the balances be provided that all of the foods contain amino acids at different rates? 30
Dried beans + rice 31
6. FREE AMINO ACID POOL 33
Elements affecting the free amino acid pool 34
What is the restaurant? 36
Free article: Eat it! Eat it! 38
Free article: "Light Warm Milk Inside" vs. "Talat İte Et Et" 40
- AMINO ACIDS STRUCTURE AND FUNCTIONS 41
- DOCTORUM AMINO ACIDS 47
L-Lysine 50
L-Tryptophan 52
Branched chain amino acids: L-leucine, L-isoleucine, L-Valin 54
L-Phenylalanine 56
L-Histidine 57
L-Threonine 59
L-Arginine 60
Free article: Viagra? L-Sitrulin? 62
Glycine 64
L-Prolin 65
L-Serine 66
- request 66
- Irozin 68
Cooking 71
L-Glutamic acid 72
5. Tatami 73
L-Aspartic acid 74
L-Asparagine 75
L-Alanin 76
ALT, AST, GGT? 76
- DIAGNOSTIC VALUE OF AMINO ACIDS 82
Parameters analyzed in amino acid analysis 85
Amino acid analysis clearly reflects nutritional status 87
Amino acid analysis is not a food intolerance test 88
Check-up with amino acid analysis: Amino acid analysis indicates the current health status or future risks 90
Problems with existing check-ups: 90
3P MEDICINE (Predictive, Preventive, Personalized Medicine) /
PERSON SPECIAL MED 93
Family Medicine 94
10. PROTECTIVE AND TREATMENT CHARACTERISTICS OF AMINO ACIDS 97
What is the limit for increasing the amount of protein? one hundred
Free amino acids may be added to healthy persons or kidney patients
create a load? one hundred
11. TYPE II DIABETES AND INSULIN DIRECTOR 103
Amino acid analysis of type II diabetes and insulin resistance
notify before 103
Amino acid analysis reports the development of insulin resistance approximately 6 years ago 107
Free amino acid supplementation prevents diabetes and insulin resistance 108
Free amino acids can cause complications of diabetes and diabetes
is effective in treatment 108
Free amino acid supplement regulates blood sugar 109
Free amino acids prevent complications of diabetes 110
- AMINO ACID ANALYSIS RISK OF HEART DISEASES PRELIMINARY 116
- OBESITY 121
Deficiencies and mistakes in existing diets and treatment methods 122
How does obesity develop? 123
Homeostatic pathway 123
Hedonic path (pleasure and pleasure) 124
Food dependency 125
Why should we go to sweet food when under stress? 127
Does love weaken? 128
Weight control with free amino acid supplementation and obesity treatment 129
How does free amino acid support obesity and related diseases
cures? 131
Damaging effects of inadequate and low calorie diets 132
Is permanent weight control possible? 133
Is it the only goal in obesity treatment to give weight? 133
- SARCOPENIUS: LOSS OF MUSCLES 137
muscle mass and quality 137
Why is everyone's life different? 137
Sarcopenia 138
Specific amino acid supplements prevent fainting in the elderly and
prolong the life expectancy. 142
The field of medicine that prolongs human life and increases the quality of life? 143
Life-prolonging food: yogurt 143
Free article: "Anti-aging" Out "Reverse aging" In 147
Free article: What is the most effective method for treating wrinkles? 149
15. CANCER 151
Amino acid support for cancer patients 152
- THE AMINO ACTIVITY EFFECT ON BEHAVIOR AND MENTALITY 156
Diseases causing alteration in amino acid levels 159
Effects of free amino acid supports 159
Solar antidepression 161
Why are we more sweet in the winter? 162
Nutritional support in psychiatric disorders 162
Why does sadness / stress make you sick? 163
Why is sick person depressed? 163
Major depression 164
Motion antidepression 164
Chronic fatigue / burnout syndrome is not helpless 165
Puerperium depression 167
Free amino acid support in puerile 171
Attention deficit hyperactivity disorder (ADHD) 171
Autism 173
Alzheimer's 174
- NUTRIENT SUPPORT, SPORTS HEALTH AND AMINO ACID 179
Do I need to use Supplement? 185
Sports support 186
How does testosterone and other anabolic hormones work? 188
Essential amino acid supplement is used in young and old muscle protein
increase synthesis 189
To increase muscle protein synthesis, non-essential amino
no acids needed 189
Effect of the amount and quality of imported protein on muscle protein synthesis 190
Does a healthy athlete need protein or amino acid support? .. 192 How long is protein needed and difficult to cover? 194
Possible amino acid deficiencies 194
What is the difference between protein supplements and free amino acid supplements? .. 196 In what situations can amino acid support be useful? 200
Effects of free amino acid reinforcement on the athlete 200
Free article: Oscar and dede 205
Amino acids are building blocks that form proteins. It forms the basis of our life, and although we are not aware of it, every moment of life depends on the amino acids. So we are not limited to eating foods full of protein, such as meat, milk, eggs, that are related to amino acids.
For example, to act, to think, to forget, to remember, to feel hungry, fullness is due to amino acids.
Growth, wound healing, hair, nail growth is due to amino acids. Being energetic or exhausted is influenced by amino acids.
Almost all the tests your doctors want are related to amino acids. Hormones, red blood cells, white blood cells, enzymes, urea, creatinin are all functions of amino acids.
20% OF THE BODY WEIGHT CONSISTS OF AMINO ACIDS.
On average 60-65% of an adult's body weight comes from water. Half of the remaining part is composed of amino acids. For example, an adult weighing 70 kg is 14 kilograms of amino acid.
Minerals produce a maximum of 5% of body weight and 1% of carbohydrates1. The total weight of vitamins is less than 1% of body weight3,4.
It does not mean that it is insignificant if it is small, but we should not know much more about the amino acids occupying the most space in the body after water when we think about vitamins which are less than 1% and minerals which are 5% It is open.
DAY VITAMIN NEEDS 100 MILLIGRAPH 4, DAY-AMINO ACID APPROXIMATIVE 60 GRAMMAR FOR ADULT HUMAN. AMANO AMINE ACID NEEDS VITAMIN 600 FLOOR.
Minerals say that we are talking about many different substances such as iron, calcium, sodium, potassium, zinc. For each mineral we can find a lot of information about the health effect. When we refer to vitamins in the same way, our mind is not a single concept, but A, B, C, D, E, K. Our knowledge of fats is more than proteins. At least we are not far from the concepts of saturated, unsaturated, trans-fat, and more importantly we know the importance of essential oils (omega 3, omega 6).
But when we say protein, there is no more. Whereas we need food containing protein, it is because of the amino acids it contains. The amino acid composition of every protein containing protein is not the same. Just as lemon C vitamin is rich in almond E vitamins, the amino acid composition of the proteins contained in the meat and the amino compounds of the proteins contained in the legumes are different.
Because amino acids are the basic building blocks of the body, each stone is a big one, and one can not hold the other. In other words, how much of the essential amino acids (essential amino acids) is consumed in the body rather than how much protein is consumed per day is vital.
THE ORGANIZATION IS THE LARGEST PARTS PROTEIN TRANSITIONED AND ITS NOT POSSIBLE TO DETERMINE THE DETERMINATION OF LOCAL SITUATION ON HEALTH AND FEEDING.
REFERENCES:
- Janaway RC, Percival SL, Wilson AS (2009). "Decomposition of Human Remains". In Percival,
- Textbook of medical physiology / Arthur C. Guyton, John E. Hall. -11th ed. ISBN 0-7216-0240-1
- Sandra Alters. Biology: understanding life. 3rd Edition, Jones and Bartlett Publishers, 2000, ISBN: 0-7637-0837-2
- Combs, Gerald F. The Vitamins Fundamental Aspects in Nutrition and Health. Third Edition, Elsevier Inc. 2008, ISBN 13: 978-0-12-183493-7
The basis of health is nutrition, the basis of nutrition is the amino acids.
The main element of nutrition is Amino Acid. Nutrition pyramids, algorithms or discourses you see so far are probably different. The basic element of nutrition is amino acids, we use a revolutionary expression. When we understand the scientific basis of this statement, the mistakes and complications that arise when it is nourished abandon.
When the first is called healthy nutrition, the fruit and vegetable school that first comes to mind is destroyed. People can not live by eating fruit and vegetables.Healthy
Did I get enough protein (amino acid) to come to mind first? (Fruit is understood to be negligible).
Secondly , the pyramids of classical nutrition, which stated that carbohydrates derived from bread, cereal, rice and macaroni constitute 50-60% of daily energy, are destroyed.
Thirdly, the importance of amino acids, the building blocks of proteins, is understood instead of the importance of proteins.
Definition of nutrition: Growing the body, development, maintenance, repair and supply of various energy to provide the necessary energy .
Living things have to feed for three reasons:
- Providing the energy required for the body to work: Energy items
- Providing the building blocks of the body: Building materials
- To provide the necessary materials for the functions of the body:
- carbohydrates
- oils
- proteins
- vitamins
- Vitamin-like substances (flavonoids, ubiquinone, choline etc.)
- Minerals
- Water
- Fiber
- Probiotics
It uses protein, oil, carbohydrates and some minerals (calcium, phosphorus) for synthesis and synthesis (muscle, bone, hair, enzyme, hormone, cell wall etc.).
It uses vitamins, minerals and water to act on metabolic processes.
The fiber is necessary for the digestive and excretion system to work well.
Probiotics play a role both in digestion and elimination and in metabolic processes.
INCORRECT BIOLOGICAL ENERGY = CARBONHYDRATE (SUGAR) DOES NOT MEAN. Carbohydrate is only one of the energy sources.
The point that needs to be taken care of for energy is that the third of the protein, fat and carbohydrate is the energy source.
For all functions, the energy used by the body is called ATP (ADE-NOSINE TRIFOSTATE). Carbohydrates are produced by the oxidation (burning) of fat or proteins (amino acids) and energy (ATP). More produced energy than needed (ATP) is stored as oil under all conditions.
Even reaching the distinction of this concept gives us clues as to where we are making mistakes in weight control and obesity.
Just as it is wrong to load carbohydrates for energy
It's also wrong to say that I get all the carbohydrates out of the diet and eat as much protein and oil as I want.
Let's not forget that extra protein is stored as energy.
RENOVATION OF RENEWED FOOD
FIGURE 2. Fate of foods 2,3
The figure above summarizes the fate of food in its simplest form.
- All of the carbohydrates are used for energy.
- All of the oils are used for energy. Very few are building blocks.
- Proteins provide the essential substances (essential amino acids) needed by the body. Amino acids are used for the synthesis of new proteins such as enzymes, hormones, collagen.
BASAL ENERGY:
As the energy is known, it is necessary not only for movement but for all our organs that work like machines even in case of sleep. The respiratory, circulatory and nervous systems that never go through the field will consume energy all the time.
Since the body can produce energy from all three food types, what is the prospect of which one we choose?
The main purpose of nutrition is to consume a lot of building stones that the body has to produce and which it has to take from the food. Because foodstuffs containing building stones will also provide reasonable energy at the same time. However, food containing simple sugars and non-essential oils will only supply a high amount of energy instead of building blocks, vitamins and minerals.
The body can synthesize some of its necessary substances during metabolism itself. However, some substances can not be produced in any way and they must be taken through nutrition. ZO-
RUNNING THESE MATERIALS ESSENTIAL PARTNER.
FOOD HAS A HIGH POTENTIAL EQUIPMENT WHICH HAS A HIGHEST ESSENTIAL INGREDIENT AMONG THE ENERGY QUANTITY.
ESSENTIAL (PROPERTIES THAT CAN NOT BE PRODUCED FROM OBSTACLES, HAVE TO GET FROM NUTRIENTS)
Essential fatty acids: linolenic acid (omega-3), linoleic acid (omega-6).
Amino acids: Valine, leucine, isoleucine, threonine, methionine, lysine, phenylalanine, tryptophan and Histidine for children. Apart from these amino acids are obtained from both the food, as well as the body can produce other amino acids.
Minerals (calcium, iron, etc.) can not be synthesized in the organism, it is necessary to take them with food.
Most of the vitamins are considered essential. Some can be produced by intestinal bacteria or metabolic processes.
The most desirable of all is the essential amino acids. For this reason, the primary criterion for a healthy diet should be that of essential amino acids. Sufficient consumption of animal proteins and plant proteins, which are the highest quality sources of amino acids, will also meet the need for vitamins, minerals, essential fatty acids and digestive-promoting fibers. THERE WILL NOT BE CAUSE OF ENERGY EXCESS.
As a result, even if you are fed with any kind of food, we can not say that you are feeding well when the nutrients are not as high as your ability or not balanced with each other. This long term, which we can refer to as inadequate or unbalanced nutrition, will lay the groundwork for various health problems later on. Iron deficiency, vitamin or amino acid deficiencies observed in thousands of overweight patients, even when they are not starving at all, clearly show the difference between satiety and nutrition.
THE MOST IMPORTANT FEATURE OF HEALTHY NUTRITION AMINO ACID.
Carbohydrates CHO
Proteins CHO N
Oils CHO
FIGURE 3. Protein, fat, carbohydrate relationship 4
Carbohydrates and oils are C: carbon, H: hydrogen and O: oxygen, while for amino acids N: nitrogen (nitrogen) is also required.
Our body transforms the materials we need into a massive metabolism. No new protein production is possible unless N (nitrogen) is supplied to the body. Some amino acids can be produced in the body, but they are the ONLY RESOURCES OF ESSENTIAL OILS. THIS CAN NOT BE DEMOCRATED AS A LONG TIME.
The direction of the arrows is basically this way. Note that the protein turns to glucosone (gluconeogenesis). However, contrary to what is wrongly known, fats do not tend to convert to glucosone. Only a very small portion (glycerol) is converted to glucosamine according to the need for metabolism.
When the above figure is made in the wrong diet, it clearly shows why the loss of muscles is not primarily caused by fat.
But let's not miss it and remember energy = sugar . The oils turn into energies (ATP). It's also a terrific resource. For glucose and energy needs, the best way to prevent muscle breakdown is to feed the muscle richly from the amino acids and encourage the use of fat, not muscle, for energy.
This, too, is only possible if you have the BODY AMINO ACIDS AT ANY QUIET QUALIFIED AMOUNT AND MAKE YOUR ACT.
REFERENCES:
- Fukagawa NK. Protein and amino acid supplementation in older humans . Amino Acids. 2013 Jun; 44 (6): 1493-509.
- Lieberman M. Marks' Basic Medical Biochemistry Fourth, North American Edition Lippincott Williams & Wilkins 2013
- Textbook of medical physiology / Arthur C. Guyton, John E. Hall.-11th ed. ISBN 0-7216-0240-1
- Dioguardi FS. Wasting and the substrate-to-energy controlled pathway: a role for insulin resistance and amino acids. Am J Cardiol. 2004 Apr 22; 93 (8A): 6A-12A.
Amino Acids are the Source of Life
a: vitamins, minerals, fatty acids, glucose, water
FIGURE 4. Life-saving amino acids 1
The basis of the tree of life is 20 amino acids. Genes generate proteins using these 20 amino acids. Water, sugar, fatty acids, vitamins and minerals are helpful in body structure and function.
In all living things, all of the proteins are made up of amino acids. Nearly 500 amino acids have been identified in the environment2. However, only 20 of these amino acids are used in protein production (proteogenic amino acids). That is, millions of different proteins are composed of 20 amino acids.
These 20 amino acids are the letters of life's alphabet. 20 letters come together in different numbers and combinations to form chains of different lengths. When at least two amino acids are combined, it is called the peptide. The peptides come together to form proteins.
The chains on which amino acid is formed by 50 or more are called proteins. For example, from the hormones that we know very well, insulin forms a chain of 51 amino acids. The greatest known protein is a muscle protein that titillates and
It consists of 27,000 amino acid chains3.
20 aminos that form the basis of life 11 of the 20 amino acids required for the synthesis of the aTP protein can be produced by the body. The remaining 9 amino acids are the only source of food. These amino acids are called essential (obligatory) amino acids. The other 11 amino acids are non-essential (non-essential) amino acids. This notion does not mean that they are not necessary, but that they can produce the body when it is needed. All of the non-essential amino acids can still be taken from food.
Essential Amino Acids (EAA) 4
- permission (Lysine)
- etionine (Methionine) L-Tryptophan (Tryptophan) Lleucine (Leucine)
L-Treonin (Threonine)
L-Phenylalanine (L-Histidine)
The name of the amino acids in Turkish was Metabolism Atlas reference 4
Non-Essential Amino Acids (NEAA) 4Glycine (Glycine)
L-Arginine (Arginine)
L-Glutamine (Glutamine)
- erin (Serine)
- irozine (Tyrosine)
L-Cysteine (Cysteine)
L-Alanin (Alanine)
- spartic acid-Aspartate- (Aspartic Acid) L-Glutamic acid-Glutamate- (Glutamic Acid) L-Asparagine (Asparagine)
Non-essential amino acids mainly arginine, glutamine, cysteine, tyrosine, mainly infection, wound healing, surgery etc. depending on the situation, there are processes in which the body is reduced and it must be taken more with food. For this reason they are called conditional amino acids.
Amino acids are used in all structures and functions of the body:
- Muscle tissue is all composed of amino acids. For example, myosin 153 comes from the ami- no acid chain.
FIGURE 5. Muscle fibers composed of amino acids 5
- Collagen forms one-third of all the proteins in the body. Tendon, connective tissue, mainly skin, cornea, bone, cartilage, veins are formed by collagen.Glycine and Prolind are the most common amino acids in the collagen structure.
FIGURE 6. Collagen fibers are composed of amino acids 6
- The dead top layer, which protects hair, nails and skin from external influences, is composed of keratin named protein. The most abundant amino acid in the structure of keratin is the system. Cysteine and Methionine contain sulfur. Because of this, sulfur is of special importance for hair, nails and skin health.
Amino acids forming keratin7
FIG. 7. Keratin consists of amino acids
• Natural moisturizing factor 8: The uppermost layer of the skin is covered with a hard keratin layer. The skin is soft and non-irritated by its natural moisturizing factor.
The natural moisturizing factor is composed of 42% amino acids and 7%. The demineralization product of the urea amino acids comes from the ammonium form and is usually excreted in the urine and in small quantities. That is,
FIGURE 8. Deep structure
class = Section36> is provided by large amino acids. The most abundant of the natural moisturizing factor is the Serine amino acid.
- Carrier proteins consist of hemoglobin, albumin, transferrin and lipoproteins (HDL, LDL, VLDL, known as cholesterol) amino acids 9,10.
- All enzymes are made up of amino acids. Therefore, all the chemical reactions in our body are responsible for the amino acids (Amylase, pepsin, lipase, ALT, AST) 9,10.
- L-Carnitine is a well-known peptide widely used as food supplements. It is necessary for fat metabolism. It consists of two amino acids, Lysine and Methionine.
- Creatine muscles are used for instant energy needs. Glycine and Arginine 9,10.
Insulin, glucagon, growth hormone, etc. All of the hormones are made up of amino acids. Only steroid-containing hormones such as testosterone, estrogen, and cortisone are synthesized through enzymes from cholesterol, not amino acids. Once synthesized, the blood is transported by the proteins and becomes functional. All of the enzymes and carrier proteins involved in the synthesis are composed of amino acids.
FIGURE 9. Amino acid sequence of insulin and glucagon hormones 9,10
FIGURE 10. Thyroid hormones consist of L-Tyrosine amino acid 11
Growth hormone 191, Leptin 146, Ghrelin, for example, consists of 28 amino acid chains.
The thyroid hormone is the most important hormone that determines the rate of metabolism of the body, and originates from a single amino acid called "Tyrosine" instead of the amino acid chain.
The Phenylalanine obtained with foodstuffs turns into Tyrosine with auxiliary substances such as Biopterin and iron. Tyrosine is converted to thyroid hormone with the help of iodine.
- All neurotransmitters that provide neuroendocrine (nerve-hormone) communication in all tissues, especially in the brain, are composed of amino acids 9,10,11,12.
The hormone of happiness, known as serotonin, and the sleep regulator Melatonin are synthesized from a single amino acid, "Tryptophan".
FIGURE 11. Synthesis of neurons (synapse) 13
FIGURE 12. Neurotransmitters are composed of amino acids 12
Enkephalin (Tyr-Gly-Gly-Phe-Met) peptide is effective against pain sensation in the brain.
- The cells that make up the immune system (antibodies, white blood cells, coagulation proteins) come from amino acids.
FIGURE 13. Amino acids forming glutathione 9,15
Glutathione is the most important antioxidant in the immune system. While taking glutathione orally does not increase the amount in the body, amino acids in the structure, especially Cysteine support, provide a significant increase in glutathione. Intravenous glutathione, on the other hand, does not stabilize for a long time and is rapidly cleaved into amino acids that make up the structure15,16,17.
- Proteins are produced by means of genes, but amino acids are also needed in the construction of DNA and RNA. The stair steps (nucleotides) in DNA and RNA structure consist of aspartic acid, glutamine, glycine and sugar.
FIG. 14. Amino acids 9,16 in DNA bases (purine, pyrimidine)
- Amino acids come together to form proteins, but each has many functions alone. There are multiple effects such as sedative, energizing, painkiller, appetite suppressant, sexual stimulant. You can see the properties of each in chapter 8.
pH Balance
Appetite Control
Body Composition
FIG. 15. Amino acids are involved in all body structures and functions 14
Amino acids are probably the source of life, as they are the building blocks of life.
Glycin, Alanin, Proline, Valine, Leucine, Isoleucine, Aspartic acid and Glutamic acid were detected on the Murchinson meteor falling to Australia in 196917,18,19,20.
THE ONLY MESSAGE CAN BE REMOVED HERE: THE AMINO ACIDS LIFE IS BASIC.
REFERENCES:
- Tochikubo O. Amino acids and lifestyle-related diseases. Explore the latest aminograms in life sciences. (Women's nutrition University Press, 2009)
- Wagner I. New Naturally Occurring Amino Acids . Angewandte Chemie International Edition No-
- Opitz CA. Damped elastic recoil of the titin spring in myofibrils of human myocardium. Proc. Natl. Acad. Sci. USA 2003; 100 (22): 12688-93.
- Görmüşü, Ergena, Zeybek U. Metabolizma Atlası 3rd Edition Istanbul Medical Publishing
- http://muscle.ucsd.edu/musintro/fibril.shtml
- Shoulders MD. Collagen structure and stability . Annu Rev Biochem. 2009; 78: 929-58.
- Clarence R. Chemical and Physical Behavior of Human Hair . Springer Berlin Heidelberg 2012
- Spiler H. Analytical and functional physiology of the skin surface . Hautarzt. 1956 Feb; 7 (2): 55-60.
- Lieberman M. Marks' Basic Medical Biochemistry Fourth, North American Edition Lippincott Williams & Wilkins 2013
- Textbook of medical physiology / Arthur C. Guyton, John E. Hall.-11th ed. ISBN 0-7216-0240-1
- Richard S. Ed. Lord Laboratory Evaluations for Integrative and Functional Medicine 2nd Edition Me- tametrix Institute, 2008
- Hinz M. Relative nutritional deficiencies associated with centrally acting monoamines. Int J Gen Med . 2012; 5: 413-30.
- Figure caption: http://fibroenergy.com/brain-chemicals-neurotransmitters/
- Wu G. Functional amino acids in growth, reproduction, and health. Adv Nutr. 2010 Nov; 1 (1): 31-7
- Sekhar RV. Glutathione synthesis is diminished in patients with uncontrolled diabetes and restored by dietary supplementation with cysteine and glycine. Diabetes Care. 2011 Jan; 34 (1): 162-7
- Witschi A. The systemic availability of oral glutathione. Eur J Clin Pharmacol. 1992; 43 (6): 667-9.
- Aebi S. High-dose intravenous glutathione in man. Pharmacokinetics and effects on cysts (e) ine in plasma and urine. Eur J Clin Invest. 1991 Feb; 21 (1): 103-10.
- Jones ME. Pyrimidine nucleotide biosynthesis in animals: Genes, enzymes, and regulation of UMP biosynthesis. Ann. Rev. Biochem. 1980; 49 (1): 253-79.
- Cronin JR. Enantiomeric excesses of meteoritic amino acids . Science. 1997. 275: 951-955.
- Pizzarello S. Non-racemic amino acids in the Murray and Murchison meteorites. Geochim Cos- mochim Acta. 2000 Jan; 64 (2): 329-38.
- Pizzarello S. Molecular and chiral analyzes of some protein amino acid derivatives in the Murc- hison and Murray meteorites . Meteoritic Planet Sci. 2001. 36: 897-909.
- McMurry, JE; Begley, TP (2005). The organic chemistry of biological pathways. Roberts & Comany. ISBN 978-0-9747077-1-6.
Gen-Amino Acid-Protein
In our body, every kind of structure and function is controlled by genes. While all cells have the same genes, the skin cells are collagen, the intestines are many different enzymes, and the pancreas is the insulin secretion.
In a living being, why do all cells have the same genes, and why do they differ in function? We can think of genes as folders of all the files that encode the human.In this case all cells will have the same folder (the same genes). However, each cell is responsible for reading a different file from this folder. For this reason, only the cell in the deep can open the file of the collagen and the pancreas beta cell can open the file of the insulin hormone. When the files are opened, the commands and the passwords are collagenous, and the genes in the nuclei of the cells in order to convert them to insulin synthesize proteins using amino acids through DNA and RNA. That is, since different parts of genes in different cells are active, each cell can synthesize different proteins.
Section45 class =>
FIG. 16. Genes lining amino acids side by side to form proteins 1,2,3
Genetic Code and Protein Synthesis The nucleotides, which are arranged in triplet groups similar to the ladder steps in DNA, constitute the genetic code. All events occurring in the cell are organized according to this genetic code. DNA has genetic codes corresponding to each amino acid. Genetic codes are used to synthesize protein by transferring messenger ribonucleic acid (mRNA).
FIG. 17. Codons determine amino acids 1,2,3
In RNA, the triplets corresponding to the codes in DNA are codonized to the nucleotide sequences. There are 4 nucleotides (ladder-like) on the RNA consisting of the letters A, U, G, These 4 nucleotides form 64 different codons in groups of 3. Each codon points to an amino acid.
64 amino acids can be considered as 64 amino acids. Since some of the different codons point to the same amino acid (such as synonyms), only 20 amino acids are used for protein synthesis. The task of 3 out of 64 is to give STOP (terminate protein production) order4.
FIGURE 18. Universal codons valid for all living organisms 4 . Small changes in some bacteria have been detected.
There are some interesting situations during the protein software. All proteins start with the AUG codon, that is, the methionine named amino acid. Otherwise it is not possible.
Due to genetic error or subsequent genetic damage (mutation), changes in the order of amino acids, such as amino acid deletion or addition, lead to different diseases. For example, sickle cell anemia is a serious genetic disorder caused by valine infusion instead of 6th glutamic acid. 5. Hemoglobin contains only one amino acid change in the 146 amino acid subunit, normally ring-shaped erythrocytes (red blood cells) r. Kanda causes blockages in small vessels of erythrocytes carried in this way.
Normal hemoglobin (HbA)
Sickle cell hemoglobin (Hbs)
FIG. 19. Genetic errors are caused by a change in the amino acid sequence.
The Effect of Amino Acids on Genes Until recently, our genetic makeup did not think we had a chance to intervene at all. However, with the concept of epigenetics , we have learned that even if the DNA sequence does not change at all, the expression of the gene, ie, the type of protein and how much it can be produced can vary.
Environment, Lifestyle and Nutrition are the three most important factors affecting the expression of the gene. It may lower or increase the activity of the genes.That is, external influences can cause genes to work less or more without making any changes in the DNA sequence.
In fact, we often witness this situation. The fact that someone who has no problems with insulin secretion in the pancreas until the age of 40 can not produce insulin in the onset of diabetes, does not mean that the genetics of this person has changed. However, it can be thought that the gene expression related to insulin has changed6,7.
The epigenetic effect of nutrition, and in particular the change in amino acid levels, has been demonstrated through scientific studies of the expression of gene expression by the presence of amino acids. See. References 8, 9, 10.
In summary, DNA can only function as protein synthesis with amino acids. The environment, lifestyle and nutrition ultimately influence the amino acid levels. Our genes can change the expression according to their amino acid levels positively or negatively. For example, if a child is fed poorly for a long period of time, the child's genes will reduce growth hormone production and cause growth retardation.
THIS IS STILL HOW TO PATIENT HIM I CAN PATIENT OR HEALTHY.
REFERENCES:
- https://jdidcott999.wordpress.com/cell-division-genes-prontiens/
- http://biosocialmethods.isr.umich.edu/epigenetics-tutorial/epigenetics-tutorial-gene-expression-from-dna-to-protein /
- Lieberman M. Marks' Basic Medical Biochemistry Fourth, North American Edition Lippincott Williams & Wilkins 2013
- Koonin EV. Origin and evolution of the genetic code: the universal enigma . IUBMB Life. 2009 Feb; 61 (2): 99-111. doi: 10.1002 / iub.146.
- Martin H. Steinber Genetic Modifiers of Sickle Cell Disease . Am J Hematol. August August; 87 (8): 795-803.
- Gilbert ER. Epigenetics: the missing link to understanding b- cell dysfunction in the pathogen-
- In this study, we investigated the effects of human pancreatic islets on type 2 diabetic and non-diabetic donors. PLoS Genet. 2014 Mar 6; 10 (3): e1004160.
- Jousse C. Evidence for multiple signaling pathways in the regulation of gene expression by amino acids in human cell lines. J Nutr. 2000 Jun; 130 (6): 1555-60.
- Bruhat A. Amino acids as regulators of gene expression in mammals: molecular mechanisms.
In mammals, the impact of nutrients on gene expression has become an important area of research. Be- cause amino acids have multiple and important functions, their homeostasis has been finely maintained. Therefore, mammals have to adjust physiological functions involved in the adaptation to amino acid availability. Part of this regulation involves the modulation of numerous gene expression. It has been shown that amino acids by themselves can modify the expression of target genes. This review focuses on the recent advances in the understanding of the mechanisms involved in mammalian gene expression in response to amino acid limitation.
- Kimball SR. Amino acids as regulators of gene expression . Nutr Metab (Lond). 2004 Aug 17; 1 (1): 3.
RESTRICTING (LIMITING) ESSENTIAL AMINO ACTIVE 20 amino acids are needed to produce a protein. The protein to be synthesized uses one or more of the essential amino acids. For example, since methionine is the starting (clippable) amino acid in the production of all proteins, each moiety must be found sufficiently.
The protein synthesis process of the body continues at any time. For example, post-meal pancreas needs to secrete insulin hormone immediately.
The insulin hormone consists of 51 amino acids and most of these 20 amino acids are used in this line. For this reason, all of the essential amino acids must be present in sufficient quantities. There is no problem for those who are not essential
the amount of sensation can be produced immediately in various tissues in the body.
FIG. 20. Insulin hormone amino acid
sequence 4
As in the following example, if leucine and lysine are not stable to form a protein, that protein can not be produced exactly. However, only Leishin and Lysine should be supplied in sufficient quantities so that the structure or function is fully realized.
FIGURE 21. Leucine or Lysine deficiency is restrictive, protein synthesis can not be completed 5
The following barrel example very well describes the essential amino acid requirement for protein production . Lizin determines the amount of protein that can be produced if the water in the barrels is produced as a protein that is produced. Even if the others are very large, production can only take place up to Lysine level. Lysine is the limiting amino acid in these conditions.
FIG. 22. Constraining properties of amino acids 6
Does the body have enough essential amino acids to produce every protein every time? If any of the essential amino acids are not in sufficient order, there is a problem in the synthesis of the protein containing this amino acid in the structure. Depending on the role of the protein in the critical level of the protein to be synthesized, depending on the digestive problems, depression, developmental retardation to obesity, symptoms start to develop, diseases.
This is due to the fact that nutrition (correct nutrition) is the basic condition for being healthy.
If the situation is so sensitive (Essential) does amino acid deficiency occur? How it works?
Unlike what is thought to be a change in the level of an individual amino acid, it is very easy and many deficiencies can occur due to many factors acting.
Why Amino Acids Can Help?
- Aging
- Chronic stress
- Depression
- Drug use (Antacids, antibiotics, chemical treatment drugs)
- Low protein diets
- Uniform nutrition (vegetarian, vegan)
- Excessive consumption of industrial products
- Diseases of the digestive system
- Absorption disorder
- Excessive breakthrough
- Vitamin, mineral imbalance
- Trauma, burns, surgery, chronic diseases
- Obesity surgery, metabolic surgery
If your foods are unbalanced or, for some reason, essential amino acids are not available to you, sooner or later a physical and psychological illness statement will emerge.
THIS IS STILL NOT POSSIBLE TO MEASURE OR SOLVE BY MEANING YOUR BREAD PROTEIN FOOD.
It is to adjust the amount and type of protein according to age, lifestyle, general health status and many other variables.
Excessive protein intake means that the liver and kidney are under more stress because more protein leads to the need to cope with more metabolic waste (ammonia, urea).
During the metabolism of amino acids, ammonia is released as a waste product. Ammonia is toxic to the body. For this reason, the ammonia formed in the cells is transported to the liver and turns into a less toxic urea. Urea is filtered out from the kidneys.
WE WILL OUTLY: If the essential amino acid is not enough, protein production is not possible and we will become ill in a short time.
If you consume too much protein, the liver and kidneys will have to deal with more ammonia and urea. This is not an incident where the body is so difficult asit is dictated and laced in the media . Only liver and liver failure should be treated with caution in high protein consumption 1 .
Balance is achieved by understanding the importance of quantity and quantity concepts in the nutrition model. DO NOT PROTEIN AT HIGH QUALITY, FILL THE HEALTHY TO FEED WITH QUALITY PROTEINS .
How to supply quality protein As mentioned earlier, the foodstuff we need is amino acid, not protein. How do you think about vitamins when you think of a single vitamin type comes to mind, A, B, C, D, E, K, such as a lot of different names, if the protein is called 20 different amino acids must come.
A protein source, rich in some amino acids, can be poor for some amino acids. I mean, a FOOD IS HIGH QUALITY AND PROTEIN INCLUDED, ALL AMINO ACTIVE IS SUFFICIENT
DO NOT TRANSPORT. For example, cereals contain high-protein but this protein is not Lysine-rich.
While animal proteins have the ideal balance and sufficient essential amino acids, plant proteins may not be poor or balanced in one or more of the essential amino acids .
NINE NUMBER NUMBER OF ESSENTIAL AMINO PROTEINED PROTEINS CONTAINING ASYDIA QUALIFIED ORAND. PROTEIN DETERMINATION NOT IN FULL OR MORE ESSENTIAL AMINO ACID COMPOSITION THAT IS NOT A QUIET MIX.
Two Important Concepts for Fruits:
- Enough amount of essential amino acid
- Ideally balanced amino acid content
For this reason, protein-containing food may lead to the lack of some essential amino acids if the ideal balance does not have amino acids. This problem is actually more common in food supplements. Because a supplement containing a few amino acids and vitamins affects the level of other amino acids as a matter of fact. So it must be considered very well whether food reinforcement is actually needed .
What should be done to ensure that enough restrictive amino acids can be taken? The answer to this question will also explain exactly what a balanced and balanced diet is.
Because each protein source contains different amino acids, an accurate and balanced diet is likely to diversify protein sources. To consume too much of a protein source does not mean that enough amino acids will be taken. For this reason, it is necessary to use corn-based protein products (vegetable-derived proteins) that do not lose quality (vegetable, fruit, seeds).
Ideal proteins are animal foods that contain essential amino acids in sufficient and balanced order. Meat, milk and dairy products and eggs are the highest quality amino acid sources.
MEAT, EGG, MILK AND DAIRY PRODUCTS (ANIMAL-PROTEINED PROTEINS) HAVE A RICH AND IDEAL EFFECT FOR ESSENTIAL AMINO ACIDS; FULL PROTEINS 2, 3.
Human growth is dependent on these foods so that they can develop and live a healthy life.
While the speculations surrounding this year's feeding are confusing, the value of animal proteins is now clear
konulmuştur7,8,9,10,11,12,13. It is very clear how a ban on eggs would cause a nutritional error if they completely removed the meat.
Plants do not provide enough protein and amino acids Plants and grains have higher protein content among plants, but the essential amino acids they contain are not balanced. Lysine in cereals, Metisone and Cysteine in pulses are very low. That is, it restricts protein synthesis.
The protein content and essential amino acid ratios of nuts such as walnuts and hazelnut almonds are much higher than other plant sources.
NO VEGETABLE PROTEINS (VEGETABLE, GRAIN, BAKLAGIL, TO-HUMULAR) IS NOT FULL PROTEIN2,3.
LENTILS, BEANS etc. THE PROTEIN VALUE OF THE BANGLASES IS NOT THE SAME OF THE INCOMPLETE MEAT.
TWO IMPORTANT CAUSE: 100 grams of lamb or veal meat contains about 25-30 grams of protein, based on fat. Likewise, it contains about 24-25 grams of protein per 100 grams of lentils or beans. But these values are valid for dry legumes.
100 grams of cooked beans or lentils (for water drains) contain no more than 9 grams of protein. When meat is boiled (because it is losing water), the protein value increases.
A person's childhood, adulthood, pregnancy and so on. The amount of protein and the amount of each essential amino acid that should be taken for the periods were determined. A person weighing 70 kg per day needs to take 0.8 mg / kg (56 grams) of daily protein, while the amount of essential amino acid needed per day is about 12 grams. For example, daytime leucine requirement is 39 mg / kg, Lysine requirement is 30 mg / kg.
Imagine that an adult person has to supply daily protein needs from only one type of protein source .
If this person tries to maintain the daily protein requirement only from red meat: the total protein that will provide 100 grams of lean meat is 30 grams. That is, when 200 grams of meat are eaten, daily essential protein requirements are met and all essential amino acids are taken in sufficient quantities14.
If this person only tries to obtain protein from cereals (wheat, rice, oats): Cereals are not good for Lysine. Adults need to consume 6,600 grams of grains to cover the daily needs of Lysine. When the 6.5 kilogram scale is defeated, but enough Lysine is taken, other amino acids are brought to metabolism in excess amount14.
If this person only tries to obtain protein from legumes (lentils, beans, kidney beans): Legumes are especially rich in sulfur-containing amino acids (Methionine, Cysteine). Lysine is not as much as it is in ette. Adults must consume about 2500 grams of legumes in order to meet the full daily Lysine and Sulfur amino acid needs. In this case, the other amino acids will be taken more than necessary.
If this person only tries to obtain protein from dry nuts (walnuts, hazelnut almonds): Approximately 700 grams of walnuts are enough to get the daily amino acids needed. However, when the whole protein is taken from hazelnut or ceviz-type dried nuts, about 4500 calories are taken. This calorie is more than the daily energy requirement of an adult person.
Nuts are protein deposits, but most are energy deposits (due to high fat content). So it should be used very carefully when dieting.
If this person only tries to obtain protein from fruits and vegetables: he must consume a full 12 kg of vegetables and fruits a day to meet sulfur-containing amino acids14.
VEGETABLES AND FERTILIZERS HAVE AN EQUIVALENT PROTEIN WITH ANIMAL FOODS.
Table 1. As seen in the table, 100 grams of raw uncooked beans or lentils have protein content as much as 100 grams of cooked meat, but not in Lysine. There is also no possibility of consuming raw meat. From this point of view, the quality is not equivalent
The total protein value as well as the ete equivalent 15 .
100 grams
Protein gram
Lysine gram
Lamb meat
24.75
2.19
Veal
25.83
2.13
Haricot bean
23.36
1.6
Dry beans cooked
8.67
0.60
Lentil
23.91
1.74
Lentil cooked
9.02
0.63
Rice raw
6.81
0.24
Rice cooked
2.36
0.08
Bulgur cooked
3.08
0.08
Spinach boiled filtered
2.97
0.18
COMPLEMENTARY PROTEINS
Amino acids form the basis of healthy nutrition. Every day you need to get enough protein and enough amino acids to get enough amino acid.
For a healthy diet, it is the ideal way to get uniform nutritional and vegetable protein in balanced proportions. For this reason, ESSENTIAL AMINO ACIDS BASED ON NUTRIENTAL HEALTHY OLDER AND WEIGHT CONTROLLING GUARANTEED.
On the other hand, vegans have to blend grains, legumes, nuts, fruits and vegetables in order to fully meet the daily essential amino acid requirement. Herbal foods are not sufficient and balanced in terms of protein, but they are very rich in terms of carbohydrates.
SALT VEGAN - VEGETARIAN DIET IS NOT IDEAL FOR LIVING LIVER AND PROTECTION OF WEIGHT. ACCIDENT CAN HAVE LIQUID WHEN THE CONTENT OF HIGH CARBONHYDRATE IS INCREASED.
REDUCE THE DAY OF THE FOOD THROUGH DAILY FOOD INCLUDED IN THE TOTAL INCLUDING REAL ESTATE ANIMAL PROTEIN.
How do we balance each other according to the fact that each food contains amino acids in different proportions? Et is an ideal source of protein, but compulsory means wrong. Other animal proteins (eggs, milk, cheese, kefir, etc.) should be strongly recommended for people who do not eat meat. It is enough to know which kinds of essential amino acids will be completed if they are taken together. All the secrets of proper nutrition are already available in traditional cuisines. For example, a kitchen that serves dry bean rice with rice and crowns it with tournaments has many clues about proper nutrition.
Grains (bulgur, rice pilaf) are not as good as lysine, while pulses are poor in terms of sulfur-containing amino acids. When both are served together, both Lysine and Sulfur amino acids and flavor are completed.
Table 2. Restriction amino acid content of different foods 16
Lysine
mg / g protein
Sulfur Containing Amino Acids mg / g protein
Legumes (lentils, beans, etc.)
64 ± 10
25 ± 3
Grains (rice, wheat, bulgur, oats)
31 ± 10
37 ± 5
Dried beans + Pilaf: Unity comes from strength
FIG. 23. Example of complementary nutritional supplementation of restrictive amino acids
There are hundreds of examples of dishes in the Turkish kitchen that bring together complementary protein sources in the right way:
Rice or bulgur in vegetable dishes
Almonds, peanuts or vegetables joined in pilaf
A piece of meat, bone
Wheat, chickpeas yoghurt balls
Garlic yogurt pouring over vegetable dishes ...
All this does not just increase the flavor, it also allows us to get the amino acids completely.
FIGURE 24. Complementary nutrition model
NUTRITIONAL ESSENTIAL AMINO ACIDS MUST BE FULLY OR CONFIDENTIAL OF THE FULL AND INCOMPLETE PROTEIN RESOURCES FOR THE DEFICIENCY OF INCOMPLETE AMINO ACIDS.
REFERENCES:
- Donald KL. Defining meal requirements for protein to optimize metabolic roles of amino acids . Am J Clin Nutr. 2015 Apr 29.
- Dietary Reference Intakes for Energy, Carbohydrate, Fiber, Fatty Acids, Cholesterol, Protein, and Amino Acids (2005) Institute of Medicine (US). Panel on Macronutrients. II. Insti- tute of Medicine (US). Standing Committee on the Scientific Evaluation of Dietary Reference Intakes. ISBN 978-0-309-08525-0
- Jennifer J. Otten, The Essential Guide to Nutrient Requirements. The Natinal Academies Press Washington, D. http://www.nap.edu/ catalog / 11537.html
- Textbook of medical physiology / Arthur C. Guyton, John E. Hall.-11th ed. ISBN 0-7216-0240-1
- Figure quote: http://www.admani.com/beef/Beef%20Technical%20Bulletins/Beef%20 Amino% 20 Gain% 20Co% 20Product% 20Grower.htm
- Figure quote: http://www.nutrientsreview.com/proteins/amino-acids
- Alessandra V. Branched-chain amino acids, mitochondrial biogenesis, and healthspan: an evolutionary perspective . Aging. May 2011; 3 (5): 464-478.
- Li-Qiang Qin, INTERMAP Cooperative Research Group. Higher Branched-Chain Amino Acid Inta- ke Is Associated with a Lower Prevalence of Being Overweight or Obese in Middle-Aged East Asian and Western Adults. J Nutr. 2011 February; 141 (2): 249-254.
- Erin E Quann. Consuming the daily recommended amounts of dairy products would reduce the prevalence of inadequate micronutrient intakes in the United States . Nutr J. 2015; 14: 90
- Astrup A. Yogurt and dairy product consumption to prevent cardiometabolic diseases: epide- miologic and experimental studies . Am J Clin Nutr. 2014 May; 99 (5 Suppl): 1235S-42S.
- Mackowiak PA. Recycling metchnikoff: probiotics, the intestinal microbiome and the quest for long life . Front Public Health. 2013 Nov 13; 1:52.
- Fuller NR. Egg Consumption and Human Cardio-Metabolic Health in People with and without Diabetes. Nutrients. 2015 Sep 3; 7 (9): 7399-420.
- Micha R. Red and processed meat consumption and risk of incident coronary heart disease, stroke, and diabetes mellitus: a systematic review and meta-analysis. Circulation. 2010 Jun 1; 121 (21): 2271-83.
- Estelle Levetin. Plants & Society, 6 / e. Online learning center The University of Tulsa ISBN: 0073524220
- National Nutrient Database for Standard Reference Release 28 Software v.2.3.2. The National Agricul- tural Library http://ndb.nal.usda.gov/ndb/foods.
- Young VR. Plant proteins in relation to human protein and amino acid nutrition. Am J Clin Nutr. 1994 May; 59 (5 Suppl): 1203S-1212S.
- Larsson SC. Red meat and processed meat consumption and all-cause mortality: a meta-analy- sis. Am J Epidemiol. 2014 Feb 1; 179 (3): 282-9.
The availability of free amino acids in the tissues is very important in terms of body protein (nitrogen) balance. Preservation and functioning of organs depend on protein balance. 75-80% of the amino acids released during protein conversion are reused for new protein synthesis.
In addition to protein synthesis, amino acids also have other important functions1.
It is a glucogenic (convertible to sugar), Kanda nitrogen,
They are the precursors of hormones, muscle activity regulators,
Neurotransmitters (brain biochemicals) are involved in the synthesis of enzymes,
ligament
They participate in tendon and bone matrix formation, They manage the protein cycle,
They transmit chemical signals, are involved in the DNA RNA structure1.
Amino acids with such vital pres- ence do not have any deposits in the body, such as glucose (sugar) and fats (lipids). On the other hand, the nutritional status of the person with the amino acid levels and any kind of stresten (trauma, infection, extreme physical activity, fever, sadness, depression, etc.) are easily affected.
For all these reasons, it is necessary for the amino acid homeostasis (balance) to be very well coordinated by all the organs. In other words, amino acids, which are sources of all proteins, enzymes and hormones, must always exist in the body.
20% of the weight of an adult human (about 14 kg) consists of amino acids. However, the amount of amino acid that circulates freely in all tissues and in all tissues is only 50-70 grams. This amount forms the free amino acid pool and must be constantly filled for critical functions.
FIGURE 25. Free amino acid pool 1,2,3
What influences the free amino acid pool?
- Protein construction and degradation
- Oxidation of amino acids (energy expenditure)
- Amino acid intake by food
- New amino acid synthesis
- Amino acids support the synthesis of other molecules
- A healthy adult consumes an average of 50-100 grams of protein a day with nutrients.
- A healthy person who is adequately fed contributes 300-600 grams of body protein per day to the free amino acid pool.
- In contrast, protein is reproduced as much as it is destroyed every day (300-600 grams).
- 30-40 g of non-essential amino acids are produced per day from this pool.
- Approximately 120 g of amino acid degrades. The carbon content is used for energy, while the nitrogen content of the degraded amino acids constitute the other nitrogen requiring compounds.
For example, when amino acids are reduced due to protein-poor feeding, the genes reduce IGF-1 (insulin-like growth factor) and GHBP (growth hormone-
protein that binds the nu- cle), thereby reducing the effect of this hormone and slowing down. When growth slows down, amino acid requirement is also reduced6.
When the protein content is low or when the amino acid content is fed with an insufficient amount of food, that is, it increases the level of food insulin that is rich in carbohydrates and fats, but poor in protein. Increased insulin improves fat synthesis (lipogenesis). Contrary to what is known, even if insulin is elevated, protein synthesis can not take place when there is not enough amino acid 7,8,9.
Ultimately, mammals must adjust their physiological functions to the presence of amino acids. Many genes play role in this regulation. The amino acids themselves have been shown to be regulatory in the expression of target genes 10,11,12 .
Approximately 80% of the amino acids found in the body are located in the muscles. With this, the rate of muscle building and destruction is the most influential factor in the rate of free amino acids circulating.
Especially in cases of fasting, significant amounts of amino acid are released by the breakdown of muscle proteins.
The edible proteins break down various enzymes from the midgut into the intestines and release amino acids. Amino acids obtained by digestion from the intestines and amino acids obtained by destroying the muscles contribute to the formation of the required proteins by joining into the free amino acid pool. If the body needs energy, it is used as fuel.
Constantly repackaging body proteins ensures that there is no shortage of amino acids that are needed when there is a specific protein need (eg, antibodies need to be made due to infection). This is how healthy it is if it can achieve this compensation process.
class = Section65> BODY AMINO ACIDS CREATE COMBINATION PROTEINS AND A STANDING STABILIZATION OF AMINO ACIDS NEEDED TO PROTEINS 13 .
The most important point to note is that the amino acid pool begins to become ineffective when amino acids are missing for a long time or when protein synthesis needs to increase (injury, trauma, infection, excessive exercise, rapid growth, etc.). The only way to prevent this is to regularly consume amino acids-rich vegetables.
Despite the repressed work in the disease process, the body needs more nutrients. In particular, high-quality proteins are needed to compensate for increased nitrogen loss. In these processes, which have a low appetite but in need of amino acids and vitamins, your mother is best served with plenty of lemon juice. In short, in the case of disease, the appetite decreases, so it is necessary to choose foods that are low in amount but high in nutritional value. Even if proteins are consumed in high quantities at high quality, they will be able to recover more quickly and uncomplicated diseases because more nutrients can be obtained from other foods.
Section66 class =>
REFERENCES:
- Pierre F. Amino acid regulation of gene expression . Biochem. J. (2000) 351, 1-12
- https://www.studyblue.com/notes/note/n/unit-1-book-terms-/deck/5044821
- Marks' Basic Medical Biochemistry (Lieberman, Marks's Basic Medical Biochemistry) Fourth, North American Edition Edition by Alisa Peet MD
- Poortmans JR. Protein turnover, amino acid requirements and recommendations for athletes and active populations. Braz J Med Biol Res. 2012 Sep; 45 (10): 875-890.
- Guillet C. An integrative approach to in vivo protein synthesis measurement: from whole tissue to specific proteins. Curr Opin Clin Nutr Metab Care. 2004 Sep; 7 (5): 531-8.
- Jousse C. Physiological concentration of amino acids regulates insulin-like-growth-factor- binding protein 1 expression . Biochem. J. 1998 Aug 15; 334, 147-153
- Yoshizawa F. Translational regulation of protein synthesis in the liver and skeletal muscle of mice in response to refeeding . Nutr. Biochem. 1995 6, 130 ± 136
- Svanberg E. Postprandial stimulation of muscle protein synthesis is independent of changes in insulin. Am. J. Physiol. 1997; 272, E841-E847
- Volpi E. Contribution of amino acids and insulin to protein anabolism during meal absorption . Diabetes 1996; 45, 1245-1252
- Bruhata. Amino acids as regulators of gene expression in mammals: molecular mechanisms.
- Kimball SR. Amino acids as regulators of gene expression. Nutr Metab (Lond). 2004 Aug 17; 1 (1): 3.
- Jousse C. Evidence for multiple signaling pathways in the regulation of gene expression by amino acids in human cell lines . J Nutr. 2000 Jun; 130 (6): 1555-60
- Deutz NE. Is there a maximal anabolic response to protein intake with a meal? Clin Nutr. 2013 Apr; 32 (2): 309-13.
- Sevan Nisanyan. "Etymological Dictionary of Contemporary Turkestan - restaurant" . Date of access: October 10, 2010.
- Metzner Paul. Spectacle, Skill, and Self-Promotion in Paris during the Age of Revolution. Berkeley: University of California Press, 1998
Free article
"You will eat them and you will not be able to eat them ..." You open the paper "these foods are miracles ... Do not you think about these foods ... The bomb is effective ..." Your friend, who went to work,
Pharmacy glass is the venue of all products to remedy all the troubles ...
You are very lucky to understand. Everything is thought, everything is under your hands. In fact, we are so healthy that doctors are cooking pots instead of seeing patients; how do we live longer?
But wisdom, everyone is even more sick. At least 2-3 plazas of hospitals in each district.
Let's leave it all in one place so many grown-ups like adults, apples, carrots, dill, artichoke etc. If you see this very healthy saying is not black humor? If the subject is not missed by any of the distinguished presenters, it is worth the effort ... "Black radish? Red radish? Broccoli? White cabbage? Rocket is over, crawl? "Questions are echoing in a row. I even heard you ask if it would be wrong if I cut the side of the salad.
Ladies please come to yourself ... Do not let these people who you have cooked for years to mock you.
You, as judges of the Turkish kitchen, already know the right dishes.
If you have the practical knowledge you need, say:
Everything in the trap / at the sea Few things in the pastry Everything natural at the lark Everything in the puller
Is not Turkish cuisine the best synthesis of all these foods anyway?
Healthy nutrition has a single basis. THE ABOVE FOOD GRUPS- CONSUMPTION AS ALL OF NIN.
Because there is no point in what you eat for your body. The expectation from the body is that the substances that are absorbed by the intestines after they have been absorbed are the essential materials for the survival of the living.
The seven essential nutrients that a nutritional meal should contain after it is digested are:
Carbohydrates, proteins, fats, vitamins, minerals, water and fiber.
The body can synthesize some of its necessary substances during metabolism itself. However, some items can not be produced in any way and they must be taken through nutrition.
The items that the body can not produce must necessarily be taken from the outside:
Essential fatty acids: linoleic acid (omega-6), linolenic acid (omega-3).
Essential Amino Acids: In general, some of the essential amino acids in plant proteins are insufficient. For this reason, animal proteins should be involved in feeding.
Minerals (calcium, iron, etc.) can not be synthesized in the organism, they must be taken from the outside.
The more energy these foods contain, the higher the nutrient value.
On the other hand, the essential balance of correct nutrition is the fact that the fat and amino acid species contained in the foods we eat together are mutually balanced. This is to increase the diversity of the foods we balance as well as the way we basically eat healthy.
For this reason, a piece of meat placed in a dry bean, along with rice, is a complete meal.
For this reason, eating a fleshy vegetable and a slice of grain bread is a good meal. For this meat, meatballs, fish, salad, piyaz or mash plenty of good food.
So much so that pastries (pasta, ravioli, pasta, etc.) are made instantly productive with plenty of yoghurt sauce in Turkish cuisine. Sufficient to eat at a reasonable level.
In short, when all food is diversified and there is food, better vegetables among vegetables, better fish among fish, and so on. suggestions just envy.
I have an offer!..
It is imperative that members of the health care provider are provided with nutritional advice in the right settings. Because proper nutrition and movement is essential to be healthy. But this is not to choose vegetables in vegetables and cook them in a magazine figurine in the form of education and awareness raising. On the other hand, the chefs who should have a basic job taste, please do not suggest treatment. Do not even tell me what's good for you. If necessary we learn from our nobles.
So the doctors look sick, the chefs cook! .. At present, we can eat delicious food at least because it can not be healthier.
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At my age, primary school teachers tried to teach reading and writing with LIGHT MILK INTERNAL. The school is the institution where literacy is taught as well as where life is taught. And he knew that the word was lying, and that he would also live in the same way as life. That teacher is lukewarm
he knew that drinking milk was good for children. His mind was not mixed by the nutritionists and the post-miscellaneous philosophers.
But my mind is badly mixed when my son starts to read. I experienced a serious trauma when I saw the "Talat İte Et Et" citation on my assignment. Have I forgotten- I am compatible with this plug, or what is the object of what? "It" has been a word for the arrow ever since. Come on I'm giving up this place ... The luster of the wreckage has ruined me. Please bring the action in front of you. Revive the rudeness of the meat, the ugliness. See a picture of the disrespect of both animals and animals from a graceful person.
I try to summarize: It is not possible to accurately grasp the nutrition of children who are so precious and thankful that their children eat magazines every day in the media, and children who are more literate and learning-minded in their minds do not drink warm milk but are tired of throwing meat.
The only thing that needs to be done is remembering again that there is a DAMAGE, an ENERGY AND A SUSPICION .
Structure and Functions of Amino Acids
FIG. 26. Molecular structure of amino acids 1
In our body, all of the organic compounds are composed of carbon, oxygen and hydrogen. All of the amino acids consist of a carboxyl group as well as an amino group containing Nitrogen (Nitrogen). For this reason, amino acids are the body's nitrogen suppliers and are responsible for the protection of this balance. The side chain is variable for each amino acid.
What do the letters "L" in the names of amino acids mean? When amino acids are considered as three-dimensional molecules, the molecules that are attached to the central carbon atom may be on the right or left side. Except for glycine, the other 19 amino acids are in nature both the right (D) and the left (L) form. VERYINTERESTED IN THE HUMANS PROTEINS ONLY AND ONLY AMINO ACIDS IN L (LEFT) FORM . D
amino acids in the form of some bacteria and simple living organisms are located. D form is present in foods and its role in human metabolism is being investigated. Exemplary D-Phenylalanine is an analgesic for human painkillers
.
FIG. 27. Symmetrical forms of amino acids 2
Standard 20 amino acids are used in protein synthesis. There are also amino acids that are not used in protein synthesis but have very different biological functions in the cell.
The primary task of amino acids involved in digestion is to produce new proteins that are needed. Amino acids break down during metabolism and the molecules involved in the structure are used for different purposes.
FIG. 28. Duties of amino acid subgroups in metabolism 1
Amino group: The amino subunit provides the necessary nitrogen (nitrogen) for the formation of DNA, RNA and neurotransmitters. Much ammonia (nitrogen compound) is released during the metabolism of amino acids. Ammonia is toxic to all tissues and must be removed immediately. Ammonia thus released is converted into "URE" in the liver and is excreted in the urine from the kidneys. Ammonia is also removed from the kidneys by combining with the hydrogen (H) ion. PRACTICES THAT MUST BE PROVIDED TO THE IMPORTANT ACID BASE RATE. That is,
the base balance is regulated by amino acids. Kanda Histidine, in the kidneys Glutamine is the main amino acid that acts as the acid base buffer. NO EFFECTIVE EFFECT ON GIDALA-RIN BLOOD ACID BASE EXCEPTION (PH) .
It should be known that alkaline diets or alkaline products claiming to protect the bones from cancer by preventing the cancer from making more alkaline blood are non-scientific commercial activities 3.
Carbon group: The carbon group is determined according to the physiological condition (fasting / satiety) of the individual amino acid residues in the solution.Glucose, ketone bodies are formed in the liver from carbon skeletons of amino acids to provide energy according to the severity of fasting. Together, the carbo-skeletons of extra amino acids carry glycogen (triglyceride) and triglyceride in the liver. So the protein turns into an excess oil .
FIG. 29. Protein can be converted to carbohydrates and oils 5
All non-essential amino acids are glucogenic (can be converted to glucosamine). Only thyrozine is both glucogenic and ketogenic. Essential amino acids Histidine, Methionine, Threonine and Valine are glucogenic; Isoleucine, Phenylalanine, Tryptophan glucokoetigenic; Leucine and Lysine are only ketogenic in nature, Table 31.
Table 3. Glucogenic and ketogenic amino acids 1
glucogenic
Glucogenic and Ketogenic
ketogenic
Non-Essential
alanine
tyrosine
arginine
asparagine
Aspartic acid
cysteine
Glutamic acid
glutamine
glycine
proline
Cool
Essential
histidine
isoleucine
leucine
methionine
phenylalanine
Lysine
Treo
tryptophan
the Governor
FIG. 30. Use of other amino acids for energy in restrictive amino acid insufficiency 7
WHY IS MY LOW CARD AND WHY KILLS NORTHERN? This shape is actually " VERY LOW GRANTS WHY WHY KILO VEREMİYO-
RUM "in the name of the people who ask. This figure also discloses the condition of those who can not lose weight when they are fed mainly with fruit. Only vegetable and other amino acids are consumed excessively while the fruit is consumed (restraining) essential amino acids. As the amount of amino acid that restricts the new protein production capacity is determined, the excess amino acids will be degraded. Because amino acids can not be stored in the body like sugar and fat. As a result, the carbon rings of the amino acids that are destroyed contribute to the energy production, while the nitrogen rings turn into urea and are thrown into the urine.
ESSENTIAL AMINO ACID LEVELS INCREASING THE DEFICIENCY - YOU CAN KNOW IF YOU REDUCE THE AMOUNT OF FOOD. If you have seven-
If your diet is insufficient in terms of essential amino acids, you will have more energy-separated portions of your cats, so you will have difficulty in weight loss if you eat less. Nutrition models that meet your essential amino acid needs (nutrition from animal proteins and vegetables in an amount that will not overfill) protect your health and enable you to lose weight.
R group (side chain): The free ring of 18 amino acids other than methionine and cysteine contains carbonyl, oxygen and hydrogen in different numbers, Methionine and Cysteine additionally Sulfur (S). All of the body's sulfur (sulfur) source is met almost from these two amino acids. It is a mandatory essence to take methionine with food. The amino acids Taurine and Cystine, which are not involved in protein structure, also contain sulfur in its structure.
Sulfur: It is found in high amounts in the proteins that make up joints, hair, nails and skin structures. The most abundant amino acid in the keratin that forms the hair is the Systeine. The insulin hormone contains too much Cysteine.
Sulfur is especially useful for glutathione, which is the most potent antioxidant in the immune system and in the body. For this reason, the consumption of amino acids containing sulfur strengthens the immune system. The most important amino acid for glutathione synthase is Cysteine due to its sulfur content, and other essential amino acids are Glutamic acid and Glutamine.
class = Section76> REFERENCES:
- Lieberman M. Marks' Basic Medical Biochemistry Fourth, North American Edition Lippincott Williams & Wilkins 2013
- GH Wagnière, & quot; On Chirality and the Universal Asymmetry: Reflections on Image and Mirror Image & quot ;, Wiley-CH, (2007).
- Fenton TR. Systematic review of the association between dietary acid load, alkaline water and cancer. BMJ Open. 2016; 6 (6)
- Fenton TR. Milk and acid-base balance: proposed hypothesis versus scientific evidence. J Am
Milk and dairy products to produce acid upon metabolism nor cause metabolic acidosis, and SYSTE- MIC PH IS NOT INFLUENCED BY DIET. Measurement of an acidic pH value does not reflect meta- bolic acidosis or an adverse health condition. The modern diet, and dairy product consumption, does not make the body acidic. ALKALINE DIETS ALTER URINE PH BUT DO NOT CHANGE SYSTEMIC
pH.
- Choi HK. Purine-rich foods, dairy and protein intake, and the risk of gout in men. N Engl J Med. 2004 Mar 11; 350 (11): 1093-103.
- Jamnik J. Fructose intake and risk of gout and hyperuricemia: a systematic review and meta-analysis of prospective cohort studies. BMJ Open. Oct 6; 6 (10): e013191.
- Sautin YY. Uric acid: the oxidant-antioxidant paradox. Nucleosides Nucleotides Nucleic Acids. 2008 Jun; 27 (6): 608-19.
- Dioguardi FS. Wasting and the substrate-to-energy controlled pathway: a role for insulin resistance and amino acids. Am J Cardiol. 2004 Apr 22; 93 (8A): 6A-12A.
- Textbook of medical physiology / Arthur C. Guyton, John E. Hall.-11th ed. ISBN 0-7216-0240-1
- Professor Osamu Tochikubo, Medical School, Yokohama City University ITU Workshop on "E-health services in low-resource settings: Requirements and ITU role" Tokyo, Japan, 4-5 February 2013.
Getting Familiar with Our Doctors
Amino acids combine to incorporate both into protein structure and function separately in different functions. The variable R in the structure of the functions of amino acids determines the group. Each amino acid group R is different from the other. The structure of this side chain specifies that the amino acid is acidic, basic, contains electrical charge, contains sulfur, contains aromatic rings, or is branched chain.
AMINO ACIDS RELATED TO THE BODY LEVELS OF TOTAL PROTEINS AND NOT ANY SEPARATE ANALYSIS
IMPORTANT INFORMATION GIVES. Again, the administration of amino acids as a support differs from each other due to the specific function of each.
20 amino acid When we consider the effect on our health, it is possible to perceive all amino acids as a member of the health team and each as a doctor with different expertise.
Amino acids do not have a single task in the body as an individual. Surveys reveal that certain amino acids are specialized for some health conditions and treatment. The amino acids can be attributed to expertise based on their prominent properties.
1. Essential Amino Acids (Only taken from foods, can not be synthesized in the body):
L-Methionine1-14: Methyl and Sulfur Source, Antioxidant
Methionine was discovered in 1922.
Methionine is the essential amino acid for humans. Some bacteria may synthesize Methionine from Aspartic acid. Large intestine bacteria in the case of shortage Methionine can be supplied because without methionine RNA can not produce any protein. The initial codon for the synthesis of all proteins is Methionine. So we can call it the chief physician for the role of Métonion in the representation of Dr.Amino Acid.
Resources that are rich:
- Meat, fish, dairy products, liver
- Egg
- Whole grains, seeds
- Garlic, onion, leek
- Cabbage, broccoli, cauliflower
Functions: Metabolism has two vital functions.
- Methyl supplier: Methyl group is necessary for the work of genes.
SAM is involved in the construction of neurotransmitters. Noradrenaline, adrenaline, is supplied by the methyl S-adenosylmethionine (SAM) required for phosphatidyl coin synthase. Another source of methyl is the Cylinder, which is also obtained from the grapes.
The ability of each cell to perform different tasks, even if the genes are the same in all cells, can be explained by the methylation of DNA. DNA methylation differences in humans and changes in gene expression are directly related to feeding, revealing that it is often in the hands of a person to be healthy.
- Sulfur provider: Sulfur is necessary for Antioxidants.
Sulfur-containing amino acids neutralize free radicals. Sulfide is required for the synthesis of glutathione, the strongest antioxidant.
Instant energy source for muscles Creatine is synthesized from Glycine and Arginine through the methyl group from SAM.
Sulfur is in the keratin structure. Hair, skin, nails are necessary for health.
Methionine, together with lysine, is a building block of carnitine: it lowers cholesterol levels.
It cleans toxic substances in the liver. It allows lead to be thrown away by binding heavy metals such as mercury.
Possible deficiencies:
Liver dysfunction Skin, hair nail quality deterioration
Low methionine during pregnancy causes neurological damage to the baby.
Methionine level is low in chemical exposure and poisoning.
In vegan and vegetarian diets, the level of methionine is reduced.
Medical applications:
Paracetamol (frequently used painkiller) poisoning Depression, inflammation, liver diseases Chronic pain and high cholesterol
All sulfur-containing amino acids are protective against radiation.
In heroin dependence, usually Histamine is high and pain threshold is low. It reduces the Histidine of the Met- rite, hence the Histamine.
Methionine supplementation in barbiturate or amphetamine withdrawal syndrome is beneficial. Copper poisoning
Interaction 13,14 :
Homocysteine occurs in the process of methionine metabolism, and a high rate of onset leads to an increased risk of cardiovascular disease. B12 and Folic acid, which play a crucial role in methionine metabolism, decrease Homocysteine levels.
There are studies showing that methionine is an essential amino acid taken with food, but it extends the life span of methionine restriction in animal experiments15. Therefore, it is very important to use appropriate doses and appropriate cofactors (vitamins, minerals) in the treatment of amino acids.
L-Lysine 3, 16-21: Anti-viral, Herpes simplex,
Lysine was discovered in casein in 1889.
The amount of Lysine in plant proteins is very low. Lizine deficiency is a serious risk for vegetarians and vegans who can not diversify plant proteins.
Resources that are rich:
- Red meat, poultry, fish
- Milk
- Permese cheese
- Egg
- Soy
- Beans, lentils, beer yeast
Functions:
Growth development
It is necessary for calcium absorption.
Antiviral effect
Carnitine synthesis: The amino acids of lysine and methionine are synthesized with the help of vitamin C. The conversion of carnitine fatty acids into energy is necessary for metabolism.
Bone, cartilage, tendon and skin are involved in the formation of collagen.
Possible deficiencies:
- Growth retardation
- Chronic fatigue
- Dizziness
- Loss of appetite
- Anemia
- Agitation
- Weight loss
- Hair loss
- Reproductive problems (infertility)
- Triglyceride height
- In sports (due to increased need) Lysine is reduced
- Lizin is reduced in burns
- Lizzine deficiency can be seen in vegetarians and vegans. Vegans must consume beans, berries, kinoa and nuts with a lot of other foods.
Medical applications:
Herpes simplex virus (HSV): Double-blind randomized controlled trials have shown that lysine is effective in herpes treatment and prophylaxis with its antiviral ability17,18.
Osteoporosis: Lysine helps calcium absorption and reduces urinary calcium excretion. Lysine and Arginine supplementation reduces bone loss, increases collagen production and protects against osteoporosis.
Type II Diabetes: Blood sticks to body proteins when blood sugar is too high. This is called glycation . Proteins loaded with sugar start blocking the small vessels, causing diabetes to disrupt all of the body's systems. Lysine support reduces insulin sensitivity by reducing glycemia and blood sugar
27% of the population 20,21.
Interaction:
Because Arginine and Lysine use the same pathways in metabolism, they lower the levels of Arginine and Lysine.
L-Tryptophan 1-2,22-31 : Sleep and Happiness
Triptofan was discovered in 1901.
Resources that are rich:
- Turkey, chicken, red meat, fish
- Milk, cheese, yoghurt
- Egg
- Pumpkin seeds, sunflower seeds, sesame seeds, almonds, peanuts, cocoa
- Oat, brown rice
- Banana, date
Functions:
It is the precursor of Serotonin, also known as the hormone of happiness. Tryptophan Serotonine turns into Serotonin Melatonin.
Melatonin adjusts the body's biological clock (rythmia). Melatonin is an antioxidant.
Melatonin is dark for synthesis and sleep is essential. Vitamin B3 (Niacin) is the precursor.
Deficiency:
Depression Premenstrual syndrome
Circadian rhythm disorders (eg hormones secreted in a particular cycle) Insomnia (insomnia)
Numbness
Anxiety due to lack of serotonin, temperament disorder, increased appetite may cause aggressive behavior and addictions.
Tryptophan and magnesium deficiency can lead to coronary artery spasm.
Tryptophan-deficient nutrition causes Pellegra disease (dermatitis, diarrhea, dementia).
Vulnerable crimes have been reported to occur more frequently in regions where corn is poorly triptophan-deficient23.
B6 vitamin deficiency Tryptophan reduces serotonin levels even if it is normal.
Hartnup disease (neutral amino acids in the intestine and renal abscess) may develop.
Medical applications:
Sleep Disorders: Triptofan has been found effective in the treatment of insomnia. THE NEGATIVE EFFECTIVE EFFECT ON SOME OTHER MEDICINES GIVEN SLEEPING, SLEEPING DOES NOT SLEEP 24.25.
Depresyon26,27
Seasonal mood disorder 28 Premenstrual syndrome
Reduce symptoms of menopause. It prevents carbohydrate intake. Reduce appetite. Do not smoke. Nicotine reduces its effects29.
It is effective in the treatment of hyperactivity in children.
US Tryptophan Proportion: In 1989, the US disease control center announced and denied evidence of the association of triptophan supplements with eosinophilic myalgia syndrome (EMS). It was later determined that the main cause was toxic bacterial contamination (contamination) in a series of products imported from Japan at that time. On top of that, the use of Tryptophan was allowed only for infant formulas and supplements which were prepared under the doctor's prescription with enteral nutritional products. Tryptophan supplements have been released in the USA since 1994, but stringent rules for importation have been introduced30.
Interaction:
When tryptophan crosses the brain tissue, the LNAA group competes with amino acids (Tyrosine, Phenylalanine, Leucine, Isolensin, Valine) 31.
Pyridoxal-5-phosphate (P5P), the vitamin B6 form, is required to translate tryptophan to serotonin.
Stress, insulin resistance, magnesium, vitamin B6 deficiency and aging block the enzyme (Tryptophan hydroxylase) that converts Tryptophan 5-HTP.
Insulin kana causes the amino acids of leucine, isoleucine, valine that pass through the brain tissue of tryptophan to pass into the muscle tissue and cause the relative concentration of tryptophan to increase blood concentration. For this reason, carbohydrates that increase insulin rapidly and milky sweets with high ratio of Tryptophan and chili are happiness.
High protein meals (such as excessive meat consumption) increase the level of Tryptophan in the blood, reducing the level in the brain.
Branched Chain Amino Acids (BCAA) 32-39: Physical and Mental Performance
you LLO
L-Isoleucine L-Valine
Lösin 1819, Valin 1901, Izolösin was discovered in 1904.
These three amino acids constitute two-thirds of all the proteins in the body. Three are also known as branched-chain amino acids (BCAAs) because they are metabolized by the same enzyme (branched-chain alpha-keto acid dehydrogenase complex-BCKDH-).
Resources that are rich:
- Meat, poultry, fish
- Dairy products
- Egg
- Cereal, soy, peanut
- Sesame, lentil
- Vegans are lacking, plants are not enough for BCAA.
Functions:
Protein synthesis plays a role in energy and stress metabolism. For energy requirement:
- Valine only converts to glucoside (Glucogenic)
- Leucine only turns into oil (Ketogenic)
- Isoleucine can be converted to both glucoose and fat (glucokoetic)
BCAAs increase muscle mass, muscle strength and durability. BCAAs accelerate recovery after exercise.
BCAAs, but especially leucine, inhibit protein degradation, stimulate muscle protein synthesis.
Visceral oil increases. This fatigue is normally resistant to dieting and exhaustion.
BCAAs compete with amino acids that cross the blood brain barrier and control the passage of Tryptophan, Phenylalanine and Triosin into brain tissue. It affects the psychological state.
Decreases in BCAAs:
Liver diseases (hepatitis, hepatic coma, cirrhosis, bilir atrezi) Increase of aromatic amino acids (AAA: Tyrosine, Tryptophan, Phenylalanine) Anorexia
Upgrades of BCAAs:
Insulin resistance and type II diabetes
All catabolic processes (cancer, high fever, trauma, diabetes)
Maple syrup urine disease:
It is caused by the inability to metabolize leucine, isoleucine and valine amino acids. When the " branched-chain alpha-keto-acid dehydrogenase complex ", which provides for the metabolism of these three amino acids, is inadequate, intermediate products are accumulated in the body. Patient's urine smells like maple syrup.The diets of these patients should be kept under control and the amount of BCAA they ingest should be reduced.
Medical applications:
BCAA is useful for lowering Phenylalanine levels in patients with Phenylketonuria. BCAA prevents muscle proteins from breaking down due to trauma and stress.
Clinical studies The amount of leucine has shown that high protein diets lose more fat and increase muscle mass.
BCAA is used as anabolizan by bodybuilding athletes. Using BCAA instead of steroids is safe and effective.
It benefits in the treatment of anorexia.
BCAA accelerates recovery after intense exercise. Used to enhance mental and physical performance.
L-Phenylalanine2,40-42: Pain reliever, Antidepressant
Phenylalanine was discovered in 1879.
Phenylalanine has D, L and DL forms. The amino acids in form D are normally not used by the body. D-Phenylalanine and D-Methionine can be converted to L form in the liver.
Resources that are rich:
- Meat, cheese
- Fish, milk, yogurt, soy products
- Oily seeds
Functions:
Tyrosine is the precursor of amino acid.
Phenylalanine is an antidepressant and pain reliever.
Aspartame used as a sweetener consists of Phenylalanine and Aspartic acid.
There is phenylalanine in the structure of narcotic drugs such as morphine, codeine, mescaline, papaverine.
D and DL Phenylalanine is effective in pain treatment.
Indications in the absence:
Reduced energy, headache, loss of appetite, weakness, growth retardation, muscle loss.
Medical applications:
As a sweetener in diabetics (Aspartame). Chronic pain
DL-Phenylalanine is effective in arthritis pain. Premenstrual syndrome pain
Depression (dopamine increases the level of norepinephrine)
Low energy, memory problems, reduced attention, appetite loss treatment. Increases UVA effect in vitiligo patients40.
Attention deficit hyperactivity disorder treatment.
Phenylketonuria 42 :
Phenylalanine hydroxylase (PAH) enzyme, which converts tyrosine amino acid to phenylalanine in liver, does not work in this disease. For this reason, excessive accumulation of Fenilanin in the brain fluid of the brain leads to intellectual retardation, neurological problems and developmental retardation.
Since the disease is genetic, all newly born babies are screened for blood from the heel.
Interaction:
In the metabolism of phenylalanine, biopterin acts as a cofactor for iron, B3, B6, copper and vitamin C.
The phenylketone byproducts that result from the inability of the phenylalanine to convert to Tyrosine, inhibit the conversion of glutamate to the GABA neurotransmitter, the sedative effect.
When it can not turn into tyrosine, the synthesis of melanin pigment, which is formed from tyrosine and gives the skin color, is prevented.
L-Histidine42-46: Allergy, Arthritis
Histidine was discovered in 1896.
Histidine can not be synthesized in children, and in adults it can be synthesized by the body very little. For this reason, it is an essential amino acid that must be taken with food. Carnosine, found in hemoglobin and muscle proteins, acts as a reserve for Histidine.
Resources that are rich:
- Red meat, poultry
- The fish
- Dairy products
- Egg
- Rice, wheat, barley, beans, corn
- Cauliflower, mushroom, banana
Functions:
Kanda is located in the structure of the hemoglobin molecule that carries oxygen.
It consists of Histamine Histidine. Histamine is an important component of the immune system that you often hear in allergic conditions.
The immune system plays a role in allergic and inflammatory processes. It acts in the formation of antioxidants (superoxide dismutase)
The work (very few) takes place in the use and regulation of elements such as iron, zinc, copper, manganese.
It plays a role in the removal of radiation and heavy metals.
Histidine is required for the formation and maintenance of myelin sheaths that protect nerves.
It protects nerves from degener- ation and prevents degenerative diseases such as Alzheimer's and Parkinson's.
By adjusting the blood pH level, it acts as an acid base buffer.
Conditions that can be seen in the absence / excess:
Blood in rheumatoid arthritis Histidine and histamine levels fall. There is an increase in allergic symptoms.
At low levels of Histidine, sexual arousal and orgasm are strong. Premature ejaculation may occur at high Histidine levels.
Excessive height of the hystidine causes psychiatric problems such as stress and anxiety. Schizophrenia Histidine levels are high.
Histidine is low in patients with chronic renal failure.
In the case of folic acid deficiency, Histidine degradation product, FIGLU (N-formiminoglutamate) accumulates and is excreted in urine (used to detect folate deficiency).
Medical applications:
In arthritis treatment: 4 grams of histidine per day has been reported to be effective in patients with severe rheumatoid arthritis43.
It is effective in allergic diseases.
Treatment of anemia: Treatment of anemia due to deficiency of folic acid44. To strengthen the immune system.
Histidine is the vasodilatation (vasodilatation) by loosening the vessel walls, thereby reducing blood pressure and protecting the heart45.
Histamine acts as a neurotransmitter in the brain, and histidine supple- mentation increases the efficacy of antiepileptic drugs and reduces side effects of drugs.
A decrease in the level of histidine increases inflammatory activity. This is caused by oxidative stress.
Histidine supplementation may reduce the mortality rate in chronic renal failure patients because it reduces inflammation46.
Interaction:
Histidine level is the indicator for the zinc level. Low cholesterol levels are low in the low Histidine levels and low in the high Histidine levels.
Methionine has the ability to lower the level of Histidine.
Antiinflammatory drugs such as aspirin and steroid treatment reduce the level of Histidine. Histidine is converted to Histamine via the vitamins B3 and B6.
L-Threonine 1,2, 47,48 : Anti-Spasticity
Threonine is the last discovered amino acid. It was discovered in 1935.
Resources that are rich:
- Meat and dairy products, cottage cheese
- Egg
- Wheat, nuts, beans, lentils
Functions:
It synthesizes Glycine and Serine amino acids, which are essential for collagen, elastin and muscle building.
It plays a role in the construction of the tooth mines. Prevents fatty liver.
It is necessary for mental health. It stimulates the team to build the antibody.
Possible deficiencies:
Depression
Neurological dysfunctions: Spasticity
ALS (Amyotrophic lateral sclerosis)
Epilepsy
Medical applications:
It is used in the symptomatic treatment of ALS. Multiple sclerosis
spasticity
Threonine supplementation gives positive results in depressive patients. To improve the quality of elastin, collagen and tooth mines.
To strengthen the immune system.
2. Non-essential amino acids (taken from foods and synthesized in the body):
L-Arginin 1-3, 49-57: Cardiovascular Protector, Antioxidant, Immunomodulator
Arginin was discovered in 1886.
While Arginine is the essential amino acid for pets, mice, and other mammals, it is essential in humans only when the need arises.
Essential cases: Rapid growth, pregnancy, trauma, burns, protein insufficiency, ammonia accumulation in the body, excess Lysine.
Resources that are rich:
- Meat, dairy products, eggs
- Pumpkin seeds, pine nuts, walnuts, nuts, sesame seeds, lunar kernel
- Poultry
- Salmon, lobster
- Pumpkin seeds 5 g / 100 g
- Pine nuts 2.4 g / 100 g
- Walnut 2.2 g / 100 g
- Chicken breast 1.4 g / 100 g
Functions:
Nitric Oxide (NO) is the precursor material that arises from the endothelium that forms the artery for the vessel. The main function of NO is to adjust the vessel tone (loosity-hardness). It plays a regulatory role in endocrine and immune system. NO blood pressure lowering protects the heart muscle and protects against oxidative damage.
The 1998 Nobel Prize for Medicine was awarded to scientists named Luis Ignarro, Robert Furchgott and Ferid Murad for their work on Nitric Oxide.
Arginine induces NO synthesis in the lining of the endothelium, causing vasodilatation in the vascular smooth muscles.
Growth hormone (Growth hormone) plays a role in the production and release. It is necessary for sperm construction.
Increases collagen synthesis.
It activates the immune system. Antibody producing stimulates the thymus gland. Thymus produces T lymphocytes.
It helps to remove the ammonia.
Creatine (which is found intensely in the muscles and provides instant energy production) consists of Arginine and Glycine amino acids. SAM (S-adenosylmethionine) is required during the metabolism.
During the metabolism of arginine, Ornithine and Sitrullin are released. The body can synthesize Sitrulin- den Arginine.
Ornithine and Sitrulin are not between 20 amino acids involved in protein software (not proteogenic).
Incomplete cases:
Since arginine is intense in the breed, the shortage causes sexual development.
It is low in AIDS patients, chronic fatigue syndrome, fungal infection (Candida).
It is associated with constipation, liver fatigue, cirrhosis, and liver coma.
In the absence of arginine, insulin synthesis, glucose tolerance, and liver fat metabolism are impaired.
Deficiency of arginine causes skin rancidity, hair loss, hair breakage, difficulty in wound healing.
Medical applications: Cardiovascular diseases 50-53:
Increases NO synthesis to expand vessels. It lowers blood pressure.
Agmatine arises from arginine in the brain. Agmatin is antihypertensive.
It increases exercise capacity and quality of life in anger and congestive heart failure.
It is effective in intermittent claudication (walking pain) disease. It prevents the clustering of thrombocytes. So it prevents the formation of clots. It protects cardiovascular health.
Erectile dysfunction54,55:
By providing enlargement of the penis veins, it facilitates the initiation of the erection and extends the duration of the erection (see Free article, page 52).
Infertility 49,56 :
Arginine increases the number of sperm and sperm motility. In studies conducted in females, Arginin increased overreport and pregnancy rate.
Athletic performance : Anabolic effect by stimulating growth hormone of arginine. Arginine has an increasing effect on muscle mass.
Ammonia detoxification:
In urea cycle disorders, Arginine-supplemented Ornithine transcarbamoylase uptake is useful in the treatment of argininosuccinate synthetase and argininosuccinate lyase deficiencies.
Wound healing : Collagen synthesis stimulates, accelerates wound healing.
Attention!
It strengthens the immune system of arginine but may cause the multiplication of viruses such as Herpes, Cytomegalovirus, and Ebstine bar.
The reverse is the effect of Lysine on virus multiplication.
Free article
In the modern world of everything, there is almost nothing left untouched by nature. When you say that you eat naturally from your food, naturally, we all envy the people of the cave.
The search for naturalness has been reflected to relate. A male patient told me. His wife wanted to take advantage of the most thriving field of medicine esthetically and mentioned a number of procedures. He told me how beautiful it would be if he had them done. Our patient was immediately opposed and I did not like artificial beauty, I said that I love the nature of everything. But the wife gave the answer badly ... If so, why do you get pre-intercourse medication because of this naturalness?
I can summarize the risk of encountering a similar quarrel between the couples in the following way. According to the Massachusetts Male Aging study,
40% have a hardening problem, and 70% are up to 70%.
In other words, women have a very big trump card.
But the male dominant society, the consciousness, immediately mobilized and fortunately, aspirin, pe-
He created the fourth miracle after nisiline and steroids. Sildenafil, Vardenafil, Tadalafil, which are the most effective solutions to the problem of hardening, are the first solutions to this widespread problem.
However, some patients with cardiovascular diseases (infarcts, angina pectoris, uncontrolled hypertension, etc.) and other drugs or substances they used to fear using these medicines, as well as those who favor or are forced to do so, have sought other searches. Since the problem was important and widespread, it continued to provide medical services based on the evidence. Recent studies have shown that for those who can not use or do not use such medicines, there may be a solution for the two amino acid hardening problems called L-Arginine and L-Sitrulin.
We can understand why they can be a good solution through the mechanism of action of sildenafil and L-arginine. In order for the penis to harden, a high amount of blood must be injected into the penis. The endothelium covering the vein wall produces nitric oxide, a very potent vasodilator, in which the penis is filled and hardened. Sildenafil and similar drugs temporarily block the Nitric Oxide-reducing enzyme (phosphodiesterase type 5), during which time the penis vessels may be filled with sufficient blood.
Nitric oxide is produced from the amino acid named L-Arginine in the body. That means more Arginine means more Nitric Oxide. However, due to the short duration of action of L-Arginine and side-effects such as nausea, dizziness, hot flashes at high doses, another amino acid, L-Sitrulin, became important in therapy.L-Sitrulin is transforming into Arginine in the body, creating reserves for Arginin, which is rapidly disappearing.
A study published in Urology 77: 119-122, 2011 reported that 50% of patients taking L-Sitrulin could be suitable for patients who had problems with erectile dysfunction and were afraid to use medications such as Viagra, Levitra, and Cialis.
Thus, blood-based medicine has proposed two important natural amino acids that are aimed at solving the problem fundamentally, not just as drugs.
Watermelon is the best solution for ultra organic wrinkles that do not use drug-like substances, even with amino acids. Because watermelon is a complete L-Sitrulin and L-Arginine store. 3 kg of watermelon contains approximately 10 grams of L-Arginine (approximately two days' dose). Moreover, all pumpkin varieties are rich in L-Sitrulin.
To make sure our idols do not come out of paradise ...
I would like to remind that L-Arginine and L-Sitrulin are produced by the body and interact with other amino acids when taken from the outside. If it is necessary to take it for this reason, it should be adjusted by your doctor according to the amino acid analysis to be taken with the doses and the supports.
Glycin57-61: Antipsychotic, Calming, Collagen
Glycine was discovered in 1820. Glycine from the 20 amino acids is not in L or D form.
The simplest is the amino acid in the structure. The taste is called Glycine because it resembles glucose.
Resources that are rich:
- Fish meat
- Dairy products
- Beans, soy, spinach, zucchini, cabbage
- Kiwi, banana
Functions:
It is used for DNA, phospholipid, collagen production and energy supply.
One third of the collagen structure comes from the Gliss. For this reason, wound healing is not possible without Glycine.
Makes it deeply healthy and flexible.
It is an inhibitor neurotransmitter such as GABA in the nervous system. Sedadif is a feature.
It is involved in hemoglobin structure.
Serine and Alanine together with the third important glulogenic (glucosome-translucent) aminoc acid.
Creates Creatine with Arginine to meet your muscle's instant energy needs. It regulates the synthesis of bile acids which are responsible for the digestion of fats.
One of the 3 amino acids (Cysteine, Glu-tamic acid, Glycine) that constitutes the most potent anti-oxidant Glutathione is Glisindir.
Glycine and Taurine conjugated with bile acids bring about the bile salts necessary for the digestion of fats.
Glycine deficiency is seen:
Glycein level is low in depressive and epileptic patients. Chronic fatigue syndrome
hypoglycemia
Anemia
Viral infections Candida infections
Glycine level increases in starved starvation.
Medical applications:
Glycine supplementation in schizophrenia patients with a low glycemic level has a significant benefit60,61.
Myasthenia gravis, muscular diseases, prostate growth, high cholesterol disease Benefits from glycine treatment.
Manic episodes and manic depressions calms epilepsy and spasticity. It prevents excessive sugar.
L-Prolin57: Connective tissue, Collagen
Prolin was discovered in 1900.
Resources that are rich:
- Gelatine
- Meat
- Egg whites
- Wheat flour
Functions:
It produces collagen and prevents collagen reduction due to aging.
Proline and Hydroxyproline, together with Glycine, are the most important amino acids involved in collagen formation.
It is the basic structure of cartilage, joints, tendons and ligaments. The heart makes your muscles strong.
Provides elasticity of the vein.
Medical applications:
Working with vitamin C, it strengthens tendon, joint, connective tissue and heart muscle.
L-Serine57: Natural skin moisturizer
The cool was isolated from silk in 1865.
Resources that are rich:
- Meat, dairy products
- Egg
- Gluten contains soya and peanuts high in coolness.
Functions:
It is used in the construction of phospholipids required for the construction of all cells.
The parasympathetic nervous system is required for the production of the neurotransmitter acetylcholine.
It is a natural moisturizer. Myelin is located in the sheath structure.
Used in the construction of a cool immunoglobulin.
Serine is required for the metabolism of fat and fatty acids. Plasma Serine / Glycemic rate is associated with depression.
Possible deficiencies:
Cool low causes chronic fatigue and fibromyalgia.
Medical applications:
It is frequently used in cosmetic products because of its moisturizing effect.
Interactions:
Metabolism requires vitamin B6 and folic acid.
L-Cysteine 57, 62-66 : Antioxidant
It was discovered in 1810.
Cysteine is a non-essential amino acid containing sulfur. It is synthesized from methionine in the body.
Resources that are rich:
- Red meat, chicken
- Egg
- Dairy products
- Whole grains
Functions:
It is the basic amino acid for glutathione synthesis.
The amount of glutathione present in all tissues depends on the ratio of Cysteine.
Glutathione removes lead, mercury, radiation, pesticide, herbicide fungicide, plastic, nitrate, cigarette smoke toxins, birth control pills and all other medicines from the liver.
Radiation is a protection against all kinds of pollution, UV and free radicals.
Protect the liver from the toxic effects of alcohol, cigarettes and medicines. Nail, skin and hair structure main structure of stone keratin Systeinde. Chondritin is the main precursor of sulphate in cartilage (front matter).
Cysteine is a free radical scavenger with selenium and vitamin E.
It has anti-aging properties by increasing glutation in the lung, kidney liver and bone marrow.
Medical applications:
It is involved in the structure of many medicines (eg Sputa Solvent N-Acetylcysteine).
Paracetamol poisoning threatens life by reducing glutathione in the liver. Cysteine is an antidote to paracetamol and prevents liver damage.
COPD, bronchitis, emphysema and tuberculosis are involved in the treatment of mucus.
It is used to remove the toxic effects of lead and other heavy metal poisonings, chemotherapy and radiotherapy62.
Cysteine is normally needed in chronic diseases such as rheumatoid arthritis, arteriosclerosis, cancer.
Hair loss (trichotillomania): Cysteine treatment was found to be very effective.
Skin Picking Disorder activity shown 64 .
Obsessive compulsive disorders 65. Bipolar disorders66.
To lower high homocysteine levels.
Synthetic derivatives of N-acetylcysteine can be used to maintain liver glutathione levels and to protect the liver from the use of high-dose paracetamol.
L-Tyrosine 57,67-72: Anti-Stress and Energy
Tyrosine was discovered in 1846. Under normal conditions, it is synthesized from Phenylalanine amino acid in the body.
Resources that are rich:
- Fish, meat, dairy products, eggs
- Almonds, pumpkin seeds, sesame seeds
- Avocado, banana, beans
Functions:
Dopamine is synthesized from tyrosine of noradrenalin, adrenaline, thyroid hormone, and melanin, which is the color of the skin.
Dopamine, adrenaline and noradrenalin are biochemicals of the sympathetic nervous system, and Phenylalanine and Tyrosine, taken from foods, determine the amount of synthesis of these biochemicals in the body.
It has a role in the formation of thyramine from amino acids that increase brain blood pressure by increasing the contractility of blood vessels.
FIG. 31. The role of tyrosine in metabolism
Conditions with tyrosine deficiency:
Intensive stress Depression
Chronic fatigue syndrome Hypothyroidism
Parkinson's disease Restless legs syndrome Substance abuse
Lack of tyrosine increases the susceptibility to skin cancer due to melanin depletion.
phenylketonuria
Medical applications:
Treatment of depression with norepinephrine deficiency68.
In the case of stress, the need for tyrosine increases. Thus, supplementation prevents stress-induced norepinephrine depletion.
In the treatment of chronic fatigue.
To prevent tyrosine deficiency in phenylketonuria patients.
L-Dopa Tyrosine and used in Parkinson's disease. Tyrosine can be used as a food supplement in Parkinson's.
Tyrosine is useful in the treatment of addictions such as codeine, amphetamine, alcohol. Lack of attention.
It prevents excessive sleepiness (narcolepsy) 70.
Tyrosine increases energy, opens mind, increases concentration 71. It shows pain relief by increasing enkephalin levels. The appetite suppresses.
Interaction:
A deficiency of vitamin B6 (pyridoxal-5-phosphate) reduces norepinephrine levels even if the tyrosine level is normal.
Folic acid, copper, vitamin C It acts as a cofactor in the metabolism of tyrosine. BCAA height Reduces tyrosine absorption and brain penetration.
L-Glutamin57, 72-80: Intestine, Nervous and Immune System
Glutamine was first isolated in 1883 from beet root.
Krebs discovered in 1935 that glutamine was synthesized from amanook and glutamic acid.
Despite the presence of catabolic states (cancer, surgery, heavy exercise, infection), there is a growing need. In such cases, food consumption containing glutamine should be increased. It can be supplemented if necessary.
Resources that are rich:
- Cabbage, spinach, parsley, beet
- Meat, chicken, fish
- pulse
- Dairy products
- Egg
Glutamine is damaged when the plant and animal proteins are overcooked.
Functions:
It is involved in DNA synthesis
Glutamine is the highest amino acid in the body and the most active in metabolic processes.
The main energy source of small intestine cells is Glutamind. It is life for bowel and normal brain functions. Glutamine is needed for the reproduction and repair of rapidly renewing intestinal cells.
Increases muscular strength and stamina. It provides anabolism and catabolism balance74.
Glutamine is used for 50% of the energy, 20% is converted to glucoside, used in the synthesis of the rest protein.
Provides acid base balance in the kidneys. Adjust the blood pH.
The most important amino acid in the removal of toxic ammonia is Glutamind. It is a source of gluconeogenesis, one of the pathways of glucose formation.
When the amino acids are destroyed, the nitrogen becomes clear. The released nitrogen turns to amoebae during metabolism and when it increases, it shows toxic effect especially for the brain. Glutamine occurs when the liver is converted to ammonia urea or combined with nitrogen Glutamic acid.
Glutathione is necessary for synthesis and immune system. Lymphocytes and macrophages use a high amount of Glutamine in cases requiring immunological response.
Glutamine acts as a nitrogen carrier for the synthesis of many different neurotransmitters in the brain.
When the level of glutamine is lowered:
Glutamine can be synthesized by the body under normal conditions. However, Glutamine deficiency can be observed in severe exercise, stress, serious infections, liver diseases because the need is more than production.
Medical applications:
Arthritis is helpful in the treatment of autoimmune diseases, fibrosis, intestinal diseases, peptic ulcer, connective tissue diseases (polymyositis, scleroderma), and radiotherapy damage72,73.
Glutamine contributes to the recovery of ischemic heart. Keep the heart. It is beneficial for epilepsy, chronic fatigue, impotence and old age treatments. Reduce sugar intake.
Glutamine supplementation reduces alcohol use and desire. Increase mental capacity.
Glutamine support in intestinal inflammation protects intestinal integrity, preventing uncontrolled intestinal permeability. Thus, the passage of bacteria, toxins and large proteins into the blood is prevented. Prevents flare-up of colitis76-78.
Aftenes are useful in the treatment of mucosal wounds due to chemotherapy and radiotherapy.
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L-Glutamic acid57: Neuro stimulant, Mind opener, Flavor
Glutamic acid was isolated from gluten in 1866.
Resources that are rich:
- Meat, poultry, fish
- Egg
- Dairy products, lettuce cheese
- Tomatoes, mushrooms
Functions:
The two exciters that trigger neurons in the central nervous system are the neurotransmitters. Other Aspartic acid.
It is also the precursor of GABA, a sedative neurotransmitter.
GABA inhibitor is a neurotransmitter and epileptic diseases occur in deficiency.
GABA analogues (like molecules) are used in the treatment of epilepsy and hypertension.
It opens the mind, increasing attention and wakefulness. Raise the mood.
It increases energy.
It prevents alcohol and sugar flakes. It accelerates wound and ulcer healing.
FIG. 32. Amino acid content of mother's milk (according to the scale) 81
Glutamic acid can not cross the blood brain barrier, but the brain may leak a small amount when the rate is high. Glutamine is the only way to combat ammonia, which is toxic to the brain. Glutamine can easily pass through your brain.
5. Tatumi
It was known that the presence of receptors that perceive bitter, sweet, salty and sour tastes in our tongue, and that all tastes are associated with these four main tastes.
In 1908, the Japanese scientist Dr. Kikunae Ikeda noticed that there was more of a different taste, except four flavors in a kind of seaweed soup.
As a result of his research, he discovered that this taste- enhancing substance was Glutamic acid, and gave it the name UMAMI , meaning "delicious" in Japanese . It was later understood that the nucleotides tasted like umami.
Most importantly, the umami taste proved to be the same as the other four flavor receptors .
What kind of taste is Umami? Mature tomatoes, mushrooms, meat, meat juices, lettuce cheese, green tea are the most distinctive umami flavors.
However, human familiarity comes from the mother's milk. The most abundant amino acid in the mother's milk is Glutamic Acid .
The umami's characteristic is that it increases the taste of other tastes from its own taste.
I think that this means that the food with tomato sauce, meat juice and cheese is much more delicious .
Currently, many ready-made food and restaurants use glutamic acid derivatives (Monosodium glutamate-E621, Monopotassium glutamate-E622, Calcium diglutamate-E623, Monoammonium glutamate-E624, Magnesium diglutamate) that are commercially available to enhance flavor.
L-Aspartic acid 57: Neuron stimulant
It was isolated from lentils in 1868.
Resources that are rich:
- meats
- Sprouted seeds
Functions:
Aspartic acid is in continuous conversion with Asparagine, so its functions are common.
Increase durability.
Aspartic acid is a neurotransmitter. It is involved in DNA and RNA structure.
It strengthens the immune system by participating in antibody production. It is compulsory for clarity of mind and increases brain energy level. Protect your brain, nervous system and liver from excessive ammonia.
It is the important amino acids of the urea cycle.
In the transamin- ation reactions, the liver enzyme AST (aspartate aminotransferase) plays a role.
Situations where incompleteness is observed:
The levels of depression and brain atrophy decrease.
Lack of calcium and magnesium in low levels of aspartic acid should be investigated.
High zinc and magnesium reduce Aspartic acid functions.
High viewing situations:
ALS (Amyotrophic lateral sclerosis) After epileptic seizure
Stroke
L-Asparagin57: Against chronic fatigue
Asparagine is the first discovered amino acid. In 1806 it was isolated from asparagus.
Resources that are rich:
- Meat, chicken, seafood
- Dairy products
- Asparagus, soy, whole grain
Functions:
Asparagine is an essential amino acid necessary for protein synthesis and can be synthesized in the liver. Asparagine consists of Aspartic Acid + ATP (adenosine triphosphate).
It is the most important amino acids that resist fatigue. It is important for athletic endurance.
Removes harmful chemicals (ammonia). It plays a balancing role in the nervous system.
It prevents being overly angry and over-calm.
In the absence of:
Asparagine deficiency leads to slower metabolism, decreased urea production. This means ammonia accumulation and toxicity.
Depression, blurring of consciousness, headache develops.
L-alanin57,83-86: Anti-Hypoglycemic (Blood sugar regulating)
The area was discovered in 1850.
Area resources:
- Meat
- Poultry
- Dairy products, cottage cheese
- The fish
- Avocado
Functions:
Amino acid is the most important role in the mechanism of glucose.
The area plays a regulatory role in glucose metabolism. Prevents hypoglycemia, ketosis is reduced.
Alanine-Glucose is present between the tissues and the liver.
FIGURE 33. Domain-Glucose Cycle
Alanin, especially given to the bloodstream from the running muscles, is taken up by the liver and is transcribed into the liver by transaminization.
Protect the tissues from destruction by providing energy in heavy physical activities. The prostate is located high in the prostate and prevents prostate growth.The field plays an important role in the transport of America from the muscles to the liver. Vitamin B6 (Pyridoxal phosphate) is essential for its metabolism.
Possible deficiencies:
hypoglycemia
Increased muscle fatigue Fatigue
Susceptibility to viral infections
In the case of BCAA deficiency, the plasma area is low.
REFERENCES:
- Hoffer Abram, Prousky Jonathan (2006) Naturopathic Nutrition, A Guide to Nutrient-Rich Food & Nutritional Supplements for Optimum Health, CCNM Press
- Stargrove Mitchell Bebell, Treasure Jonathan, McKee Dwight L (2008) Herb, Nutrient, and Drug Inte- rations, Clinical Implications and Therapeutic Strategies. Mosby
- Hendler Sheldon S. Rorvik David (Editors) (2008) PDR for Nutritional Supplements, Medical Economics Company Inc.
- Pizzorno Joseph E. Murray (2005) Textbook of Natural Medicine, Third Edition, Elsevier
- Clark BF. How proteins start . Sci. Am. 1968; 218 (1): 36-42.
- Adams JM. N-formylmethionyl-sRNA as the initiator of protein synthesis . Proc. Sci USA 1966; 55 (1): 147-155.
- Vale JA. Treatment of acetaminophen poisoning. The use of oral methionine . Arch Intern Med 1981; 141: 394-6.
- Larsson SC . Methionine and vitamin B6 intake and risk of pancreatic cancer: a prospective study of Swedish women and men .Gastroenterology. 2007; 132 (1): 113-118.
- Coelho CND. Methionine and neural tube closure in cultured rat embryos: morphological and biochemical analyzes. Teratology. 1990; 42: 437-451.
- Haneke E. Micronutrients for hair and nails. Nutrition for healthy skin, 2011; Volume 2, pp. 149-163.
- Delle Chiaie R. Efficacy and tolerability of oral and intramuscular S-adenosyl-L-methionine 1,4-butanedisulfonate (SAMe) in the treatment of major depression: comparison with imipramine in 2 multicenter studies . Am J Clin Nutr. 2002; 76 (5): 1172S-1176S.
- Brosnan JT. The sulfur-containing amino acids: an overview. J Nutr. 2006 Jun; 136 (6 Suppl): 1636S- 1640S.
- Niculescu MD. Diet, methyl donors and DNA methylation: interactions between dietary folate , methionine and choline . J Nutr. 2002 Aug; 132 (8 Suppl): 2333S-2335S.
- Clarke R. Assessment of homocysteine as a cardiovascular risk factor in clinical practice . Anna
- Ables GP. The First International Mini-Symposium on Methionine Restriction and Lifespan.
- Flodin NW . The metabolic roles, pharmacology, and toxicology of lysine . J Am Coll Nutr. 1997 Feb; 16 (1): 7-21.
- Griffith RS. Success of L-lysine therapy in recurrent herpes simplex infection. Treatments and prophylaxis. Dermatologica. 1987; 175: 183-190.
- Milman N. Lysine prophylaxis in recurrent Herpes simplex labialis: a double-blind, controlled crossover study. Acta Derm Venereol. 1980; 60: 85-87.
- Civitelli R. Dietary L-lysine and calcium metabolism in humans . Nutrition 1992; 8: 400-405.
- Ramakrishnan S. Decrease in glycation of lens proteins by lysine and glycine by scavenging of glucose and possible mitigation of cataractogenesis . Exp. 1993; 57 (5): 623-628.
- Ramakrishnan S. Free lysine, glycine, alanine, glutamic acid and aspartic acid reduce the glycation of human lens proteins by galactose . Indian J. Biochem. Biophys. 1997; 34 (6): 518-523.
- L-Tryptophan. Monograph . Altern Med Rev. 2006 Mar; 11 (1): 52-6.
- Mawson AR. Corn Consumption, Tryptophan, and Cross-National Homicide Rates. Orthomolecular Psychiatry. Volume 7, Number 4, 1978, pp. 227 - 230
- Schneider-Helmert D. Evaluation of L-tryptophan for treatment of insomnia: a review. Psychop- harmacology (Berl). 1986; 89: 1-7.
- Korner E. Sleep-inducing effect of L-tryptophane . Eur Neurol. 1986; 25: 75-81.
- Lindseth G. The effects of dietary tryptophan on affective disorders. Arch Psychiatr Nurs. 2015 Apr; 29 (2): 102-7
- Markus CR. Dietary amino acids and brain serotonin function; implications for stress-related affective changes . Neuromolecular Med. 2008; 10 (4): 247-58.
- Ghadirian AM. Efficacy of light versus tryptophan therapy in seasonal affective disorder . J Afect Disord. 1998; 50: 23-27
- Bowen DJ. Tryptophan and high carbohydrate diets as adjuncts to smoking cessation therapy. J
- Kilbourne EM. Tryptophan produced by Showa Denko and epidemic eosinophilia-myalgia syndrome . J Rheumatol Supp.l 1996; 46: 81-88
- Caballero B. Plasma amino acids and insulin levels in obesity: response to carbohydrate intact andtryptophan supplements . Metabolism. 1988 Jul; 37 (7): 672-6.
- Yoshizawa F. New therapeutic strategy for amino acid medicine: notable functions of branched chain aminoacids as biological regulators . J Pharmacol Sci. 2012; 118 (2): 149-55.
- Fernstrom JD. Branched-chain amino acids and brain function . J Nutr. 2005; 135 (6 Suppl): 1539S- 46S
- Garlick PJ. The role of leucine in the regulation of protein metabolism . J Nutr. 2005; 135 (6 Suppl): 1553S-6S
- Layman DK. Potential importance of leucine in the treatment of obesity and the metabolic syndrome . J Nutr. 2006; 136 (1 Suppl): 319S-23
- De Bandt JP. Therapeutic uses of branched-chain amino acids include burn, trauma, and sepsis . J Nutr. 2006; 136 (1 Suppl): 308S-13S
- Calder PC. Branched-chain amino acids and immunity. J Nutr. 2006; 136 (1 Suppl): 288S-93S
- Newsholme EA. Branched-chain amino acids and central fatigue. J Nutr. 2006; 136 (1 Suppl): 274S- 6S
- Berry HK. Valine, isoleucine, and leucine. A new treatment for phenylketonuria . Am J Dis Child. 1990; 144 (5): 539-43
- Camacho F. Treatment of vitiligo with oral and topical phenylalanine: 6 years of experience . Arch Dermatol. 1999; 135 (2): 216-217.
- Fernstrom JD. Tyrosine, phenylalanine, and catecholamine synthesis and function in the brain.
- Moats RA. Brain phenylalanine concentrations in phenylketonuria: research and treatment of adults. Pediatrics 2003; 112 (6 Pt 2): 1575-1579.
- Gerber. Low free serum histidine concentration in rheumatoid arthritis. A measure of disease activity . J Clin Invest. 1975 Jun; 55 (6): 1164-73.
- Blumenkrantz MJ. Histidine supplementation for treatment of anemia of uraemia. Br Med J. 1975; 2: 530-3.
- Tuttle KR. Dietary amino acids and blood pressure: A cohort study of patients with cardiovascular disease. AM J Kidney Dis. 2012 Feb 28
- Makoto W. Consequences of low plasma histidine in chronic kidney disease patients: associa- tions with inflammation, oxidative stress, and mortality . American Journal of Clinical Nutrition; Vol. No. 87. 6, 1860-1866, June 2008
- Lee A. A double blind study of L-threonine in patients with spinal spasticity . Acta Neurol Scand. 1993; 88: 334-8.
- Hauser SL. An antispasticity effect of threonine in multiple sclerosis. Arch.neurol. 1992; 49 (9): 923-926.
- L-arginine. Monograph. Altern Med Rev. 2005 Jun; 10 (2): 139-48.
- Lekakis J. Oral l-arginine improves endothelial dysfunction in patients with essential hyperten- sion . J Am Coll Cardiol. 2001: 260.
- Ceremuzynski L. Effect of supplemental oral L-arginine on exercise capacity in patients with stable angina pectoris. Am J Cardiol. 1997; 80: 331-333.
- Rector TS. Randomized, double-blind, placebo-controlled study of supplemental oral L-arginine in patients with heart failure . Circulation. 1996; 93: 2135-2141.
- Siani A. Blood pressure and metabolic changes during dietary L-arginine supplementation in humans. Am J Hypertens. 2000 May; 13 (5 Pt 1): 547-51.
- Schacter A. Treatment of oligospermia with the amino acid arginine. J Urol. 1973; 110: 311-313
- Chen J. Effect of oral administration of high-dose nitric oxide donor L-arginine in men with orbital erectile dysfunction: results of a double-blind, randomized, placebo-controlled study . BJU Int. 1999 Feb; 83 (3): 269-73.
- Battaglia C. Adjuvant L-arginine treatment for in vitro fertilization in poor responder patients . Hum Reprod. 1999; 14: 1690-1697.
- Lieberman M. Marks' Basic Medical Biochemistry Fourth, North American Edition Lippincott Williams & Wilkins 2013
- Gusev EI. Neuroprotective effects of glycine for treatment of acute ischaemic stroke. Cerebrovasc Dis. 2000; 10: 49-60.
- Yin M. Glycine accelerates recovery from alcohol-induced liver injury . J Pharmacol Exp Ther. 1998; 286: 1014-9 ..
- Heresco-Levy U. Double-blind, placebo-controlled, crossover trial of glycine adjuvant the- rapy for treatment-resistant schizophrenia. Br J Psychiatry. 1996 Nov; 169 (5): 610-7.
- Heresco-Levy U. Efficacy of high-dose glycine in the treatment of enduring negative symptoms of schizophrenia. Arch Gen Psychiatry. 1999 Jan; 56 (1): 29-36.
- Block KI. Impact of antioxidant supplementation on chemotherapeutic toxicity: a systematic review of the evidence from randomized controlled trials . Int.J Cancer. 9-15-2008; 123 (6): 1227-1239.
- Grant JE. N-acetylcysteine, a glutamate modulator, in the treatment of trichotillomania: a double-blind, placebo-controlled study . Arch Gen Psychiatry. 2009 Jul; 66 (7): 756-63.
- Miller JL. An open-label pilot study of N-acetylcysteine for skin-picking in Prader-Willi syndrome . Am J Med Genet A. 2014 Feb; 164A (2): 421-4.
- Deepmala . Clinical trials of N-acetylcysteine in psychiatry and neurology: A systematic revi- ew . Neurosci Biobehav Rev. 2015 Aug; 55: 294-321.
- Berk M. N-acetyl cysteine for depressive symptoms in a double-blind randomized placebo-controlled trial . Biol Psychiatry 9-15-2008; 64 (6): 468-475.
- L-tyrosine. Monograph . Altern Med Rev. 2007 Dec; 12 (4): 364-8.
- Gelenberg A. Tyrosine for depression . J Psychiatr Res. 1982-1983; 17: 175-180.
- Banderet LE. Treatment with tyrosine, a neurotransmitter precursor, reduces environmental stress in humans. Brain Res Bull. 1989; 22: 759-762.
- Mouret J. Treatment of narcolepsy with L-tyrosine. Lancet. 1988 Dec 24-31; 2 (8626-8627): 1458-9. Patients with narcolepsy were treated with oral tyrosine. Within six months all were free from daytime sleep attacks and cataplexy .
- Neri DF. The effects of tyrosine on cognitive performance during extended wakefulness . Aviat Space Environ Med. 1995; 66: 313-9
- Wilmore DW. Role of glutamine in immunologic responses . Nutrition. 1998; 14 (7-8): 618-26.
- Bozzetti F. Glutamine supplementation in cancer patients receiving chemotherapy: a double-blind randomized study. Nutrition. 1997; 13: 748-51.
- Ziegler TR. Glutamine: from basic science to clinical applications . Nutrition. 1996; 12 (11-12 Suppl): S68-70.
- Song QH. Glutamine supplementation and immune function during heavy load training . Int J Clin Pharmacol Ther. May 2015; 53 (5): 372-6.
- Zhou YP. The effect of supplemental enteral glutamine on plasma levels, gut function, and out- comes in severe burns: a randomized, double-blind, controlled clinical trial. JPEN J. Parenter. Enteral Nutr. 2003; 27 (4): 241-245.
- Akobeng AK. Double-blind, randomized, controlled trial of glutamine-enriched polymeric diet in the treatment of active Crohn's disease . J Pediatr Gastroenterol Nutr. 2000; 30: 78-84
- Alverdy JC. Effects of glutamine-supplemented diets on immunology of the gut . JPEN J Parenter Enteral Nutr. 1990; 14: 109S-13S.
- Huang E. Oral glutamine to alleviate radiation-induced oral mucositis: a pilot randomized trial. Int.j.radiat.oncol.biol.phys. 2-1-2000; 46 (3): 535-539.
- Skubitz KM. Oral glutamine to prevent chemotherapy induced stomatitis: a pilot study . J Lab Clin Med. 1996; 127: 223-8.
- Zhiying Zhang. Amino Acid Profiles in Term and Preterm Human Milk through Lactation : A
- Chandrashekar J. The receptors and cells for mammalian taste . Nature. 2006 Nov 16; 444 (7117): 288-94 .
- Battezzi A. Splanchnic utilization of the enteral field in humans. Metabolism. 1999; 48: 915-21.
- Bodamer OA. The effects of L-alanine supplementation in late-onset glycogen storage disease type II. Neurology. 2000; 55: 710-2.
- Mundy HR. The effect of L-alanine therapy on a patient with adult onset glycogen storage disease type II. J Inherit Metab Dis. 2006; 29: 226-9.View abstract.
- Koeslag JH. Post-exercise ketosis in post-prandial exercise: effect of glucose and alanine ingestion in humans . J Physiol. 1985; 358: 395-403.View abstract.
Diagnostic Value of Amino Acids
Why go to the doctor?
- To diagnose:
- For treatment:
- To be protected:
These three facts actually explain why I say "Doctor" to amino acids. Because Dr. Amino Acid carries out all diagnostic, treatment and preventive medicine applications.
Dr. The services that can be taken when applied to Amino Acid are:
- It gives information about current health status.
- It shows how the nutritional status underlying health is.
- What is the course of your health? It informs about possible health problems that may be seen when current conditions continue.
- It makes a diagnosis of health problems.
- It provides preventive (prophylaxis) and treatment of health problems.
Dr. How does amino acid achieve this? The advances in technology and the rapidly evolving "metabolomics" have made significant advances in the analytical analysis of amino acids. These developments have shown that amino acids can be used as biomarkers (biomarkers) in determining the risk of disease, monitoring progression, and selecting the correct treatment.
Amino acids constitute 20% of body weight and are present in all cells, in intercellular circulation, and in all body fluids.
If we look at the processes of amino acids in their body:
It passes into the blood by digestion of food and is incorporated into the free amino acid pool. It is used in protein synthesis.
They are again incorporated into the amino acid pool by destroying the proteins.
Some are excreted through urine and feces.
In other words , until the time of digestion , the amino acids function in all the points and functions of the body . In this cycle, all of the body-tissue proteins are renewed every 2-3 months. On the other side, amino acids that are constantly active in muscle, liver, brain, kidneys, and small intestines play a role in all the metabolic processes in these organs, so amino acids show differences in the blood-normal (physiologic) and in the pathways (pathological)processes .
The free plasma amino acids that make up the amino acid pool are kept in a certain range by several different control mechanisms in healthy individuals. Like trying to keep blood sugar in a constant range on fasting and fasting (70-110 mg / dL on fasting, 140 mg / dL on satiety).
Hundreds of studies have shown that many diseases of the liver, kidney, nervous system and endocrine system affect the plasma amino acid balance1-13.
Amino acid analysis:
Since all the functions and structures are responsible for amino acids, measuring and evaluating the amount of amino acids in tissue, blood, and other body fluids gives you comprehensive information about our health. PHYSICAL AND SPIRITUAL MATTERS DETERMINED SPECIFIC CHANGES IN THE MOST OF AMINO ACIDS LEVELS .
FIG. 34. Function of amino acids 14
Amino acid analysis generally evaluates bloodstream by advanced laboratory methods (HPLC and LC-MS / MS). Everyone has its own unique profile like the amino acid profile fingerprint and does not show any major changes in a short time without intervention.
For this reason, the test reflects the current amino acid profile and needs very well. Analysis of amino acids gives clear information on our current health and nutritional status.
Amino acid analysis is an EARLY ALARM SYSTEM for possible future health problems or undiagnosed diseases. It has already signaled about future cardiovascular disease, diabetes, insulin resistance, neurological and mental illnesses.
Amino Acid Analysis:
- Kanda shows increasing or decreasing amino acids and metabolites.
- It shows the ratio of amino acids to each other.
- It is the perfect blend of nutrition.
- Protein and amino acid deficiency
- Vitamin and mineral deficiency, increased need (B6, B3, B12, B9, Zinc, Magnesium etc.)
- Liver and kidney disorders
- Digestion and absorption deficiencies
- Intestinal microflora impairment
- Detoxification inadequacy
- Oxidative stress
- Sexual arousal, early or late ejaculation problems
- Catabolic (muscle destruction) or anabolic process (muscle building).
- Developing diseases:
- Type II diabetes and insulin resistance 2,16
- Cardiovascular diseases17
- Kanser9
- Psychological / neurological diseases18-20
Parameters studied in amino acid analysis:
- Essential and non essential (20) amino acid blood value
Result
Unit
Least
Most
Lysine
160
mmol / L
120
318
methionine
19.3
mmol / L
14
48
tryptophan
47
mmol / L
31
83
Result
Unit
Least
Most
isoleucine
48
mmol / L
36
107
leucine
104
mmol / L
74
196
the Governor
151
mmol / L
146
370
Result
Unit
Least
Most
phenylalanine
58
mmol / L
42
95
histidine
73
mmol / L
57
114
Treo
93
mmol / L
73
216
Result
Unit
Least
Most
arginine
102
mmol / L
29
137
Taurine
128
mmol / L
29
136
glycine
212
mmol / L
155
518
Cool
113
mmol / L
60
172
glutamine
390
mmol / L
372
876
tyrosine
27
mmol / L
38
110
proline
122
mmol / L
90
363
ornithine
46
mmol / L
28
117
Result
Unit
Least
Most
alanine
295
mmol / L
230
681
asparagine
55
mmol / L
31
90
Aspartic acid
27
mmol / L
2.9
33
Glutamic acid
53
mmol / L
24
214
2. The blood value of the metabolites (amino acid degradation products)
metabolites
Result Unit Minimum
Most
cystine
15.8 μmol / L 0.8
27.5
Taurine
128 μmol / L 29
136
citrulline
12.5 μmol / L 18
57
a-aminoadipic
acid
1 μmol / L 0.5
1.5
a-aminobutyric
acid (a-ANB)
11 μmol / L 0.5
39
b-Alanine
1.7 μmol / L 0.2
5
ethanolamine
1 μmol / L 0.2
28
OH-proline
3.1 μmol / L 0.2
26
OH-Lysine
0.1 μmol / L 0.2
0.6
1-Methyl-histidine
1 μmol / L 0.2
28
3-Methyl-histidine
3 μmol / L 2
9
3. Ratio of amino acids to each other (Amino indices): Marker for diseases
Amino Acid Rates
Result at least
Most
eaas / neaas
0.48 0.44
0.53
BCAAs
303 387
535
Phenylalanine / Tyrosine
2,15 0
1.1
Glutamic acid / Glutamine
0,14 0,06
0.23
OH-Prolin / Prolin
0,03 0
.152
Alpha-ANB / Leucine
0,11 0
0.22
Tryptophan / LNAA
0.12 0.09
0,102
Tyrosine / LNAA
0.07 0.1
0.14
TSM ratio
5,87 1,3
6
Fischer ratio
3,56 3
10
Arginine / UAE
0.37 0.16
0.23
The analysis table presented above is not a routine laboratory output, but an analytical software that combines several amino acid indices published in the medical literature as disease markers *. This method allows different health problems or risks to be diagnosed by a single analysis.
- It has been developed by Dr.Ayday Duygu for the effective use of amino acids in medical applications (3P Medicin) that offer a preventive and personalized treatment approach.
Amino acid analysis clearly reflects the nutritional status: "It is not possible to assess nutritional status without amino acid analysis"
What would be the answer to the idea that someone who is predominantly vegetable-fed would think that I am fed very well, and that almost anyone who eats a meat should think I am healthier? The answer to this question, unfortunately, has to rely on general discourses. Discussions are misleading that the outcomes of work done in small groups will be generalized and correct for the whole society. For this reason every day a new fashion diet comes out. These adventures sometimes make the meat stand out, sometimes the egg stains, sometimes the fruit. Cereals have begun to increase in thousand years of poison ... Fortunately, there is no bad vegetable leaves yet ...
However, scientific reasoning requires that if human beings live by feeding, AN ANALYSIS TO INDICATE THE EFFECTS AND POTENTIAL LEVELS OF THESE NUTRIENTS SHOULD BE DELIVERED, AND WHO KNOW WHAT THEY HAVE A UNIVERSAL RELATIONSHIP.
I have mentioned about the nutrients that are absolutely necessary to be taken with food for our bodies. These are essential amino acids, vitamins, minerals and fatty acids. The level of body-wasting will depend on the nutrition of these substances and the periods of their growth and decline in the body by the influence of their lifestyle. The analysis of the ESSENTIAL items that are required to be taken with food reveals how healthy the person is.
However, nowadays, without these analyzes or with other alternative tests, comments are made about the nutritional or health status of people and even treatment is being organized. Many people are using nutritional supplements that miracles wait for when they do not know the level in their blood.
Let's look at how these foods (micronutrients) that are essential to the body are now being analyzed and reinforced on the basis of:
Vitamin analysis: Very few of the vitamins are routinely measured. B12, folic acid, vitamin D are vitamins that can usually be measured. According to the result, we often witness that there are deficiencies. Serum, B3, B1, B5 vitamins and similarly CoQ10, Alpha lipoic acid and so on. on what basis when materials are not measured
It is? And almost one in three. Unfortunately, postmodern medicine, alternative medicine, is proposed in the mind of planters. "Use is good" mentality is given to the supplements. The eye-catching ads of the industry reinforce confidence.
Is it harmful? If the food supplements are eger pure (not contaminated by other active substances), we can not say that you will suffer immediate damage as the medicines, because the benefit is harmful dose range. However, if the substance is not missing in the body or the need for that substance is not increased, it is not useful either. It is consumed in vain. On the other hand, all vitamins affect the metabolism and function of amino acids. Because amino acids are the cofactor.For this reason, the use of the blood level or the amino acid level associated with it is completely unreasonable and long-term harmful. Vitamins and minerals can not show activity unless amino acids are present in proper proportion.
Analysis of minerals: Most minerals can be studied in routine analyzes. Some trace elements can be specially studied when requested. It is illogical to use minerals without this assay or knowing the level of amino acids that are relevant.
Fat analysis: Essential fatty acid supplements are common. Omega 3, omega 6 levels have been analyzed more often. There is no harm in giving essential oils to a doctor who is thought to be deficient in the nutrition story.
Analysis of amino acids: Because amino acids are the main element of feeding, each amino acid level gives important information about the nutritional status.Today, all amino acids are measurable. The proportions of amino acids also reveal which vitamins, minerals and other cofactors are needed, apart from extensive information on health.
AMINO ACID ANALYZES A SINGLE ANALYZE WHICH SETS THE FUTURE OF THE NUTRITION. AMINO ACID ANALYSIS FOOD IS NOT INTOLERANCE TEST.
Amino acid analysis can provide sensitive data that is too good to be good, bad and normal to eat. The following example reflects the amino acid analysis of 88 obese patients in Japan who were involved in the 2011 earthquake and 300,000 people exposed to the catastrophic aftermath of the tusunami. 88 patients did not need special diets, and were examined in three groups as the normal diet, the doctor's recommendation, the well-fed diet, the doctor's diet, and the bad diet.Figure 35 shows how the amino acids vary in sensitivity to good, bad and normal nutritional status21.
Difference in amino acid level between two bad and well-fed groups
Difference in amino acid level between two groups that are bad and normally fed
class = Section124>
- Difference in amino acid level between two groups that are good and normally fed
FIGURE 35 ABC: Effect of nutrition on amino acids 21
There is a significant difference between good and bad nutrition, and there are significant differences even between normal and good nutrition.Significant differences in the stars (p <0.05) indicate the observed amino acids.
Check-Up with Amino Acid Analysis: Amino acid analysis shows the current state of health or future risks. Why go to the doctor?
- To diagnose
- For treatment
- To be protected
Problems with existing Check-ups:
- Most of the analyzes performed during check-up are tests done when we have any discomfort or illness. Since we are not sick at the moment and we have no complaints, that is to say that all our systems are intact, these tests will most likely be normal.
- None of the chronic diseases occur in one day. The transition from healthy state to illness occurs within a certain period of time. You can scan this transition process-
parameters that give information about the len and possible future problems are insufficient.
- Analyzes are only aimed at evaluating physical functions. Methods that can assess the psychological state or even perform risk analysis for the future are lacking.
- Check-ups that are offered in menus and selected in accordance with your budget are tailored to your needs. For example, a men's menu over the age of 40 can overlook many situations specific to you.
FIGURE 36. What should be the ideal check-up?
In this regard, most of the existing check-ups can be defined as the most advanced check-ups. It is the most practical method to incorporate the analysis of our mood-altering amino acids into the check-up program, which manages all our physical structures and functions for an ideal check-up .
Genetic analyzes, family history, and environmental factors are test amino acid analyzes that can best pinpoint the stage at which this risk is present, that is, what the body is doing, even if it raises a specific risk.
For example, genetic analysis of a person susceptible to heart attacks have detected polymorphism. This is an increased risk, but for the person now or in the near future
we can say whether there is such a possibility with amino acid and other biochemical assays other than interventional applications and imaging .
The amino acid profile of blood and other tissues varies according to different physiological conditions and diseases. Amino acid analysis with this property:
- It is a method that can be used for the diagnosis of diseases, on the scales and for the analysis of the risk.
- Amino acid analysis to determine the specific nutritional status of different diseases and specific conditions (growth, lactation, old age, intense exercise, etc.) is a very useful display.
The following clinical approach demonstrates how amino acid analysis informs all systems in addition to general physical examination, biochemical and physiological assessments. All functions are definitely related to amino acids21.
FIG. 37. Amino acid analysis study areas and feedback system 21
3P MEDICINE (Predictive, Preventive, Personalized) MEDICINE / PERSONAL SPECIFIC TYPE:
Personal medicine continues to develop as the most robust and promising field of modern medicine. Genera and treatment conception based on a certain community can not be sufficient because it does not adequately consider individual differences (genetic and biochemical). The three possibilities encountered in the use of any medication or treatment clearly show how important it is for person-specific medicine. The first possibility is the expected benefit from the treatment; the second possibility is not affected by the treatment, and the third possibility is the side effect. This means that even though treatment and illness are the same, the effects vary due to individual differences. Otherwise, it would have to work for a herbal medicine which is very good for a person's pain.
The result here is that the treatment should be person-specific. A system that predicts the response to treatment will protect both the unnecessary and side effects of treatments and also save them from unnecessary costs. But the ultimate goal of 3P medicine is not limited to this. MORE THAN ONE MORE THAN ANYTHING TO DEVELOP THERAPEUTICAL TREATMENTS IN THE DISEASES AND PREVENT THE DISEASE RISK AND PREVENT THE DEVELOPMENT.
METABOLO- MICS, which is a rapidly developing scientific field to realize this aim, aims to create markers for diseases by examining biochemical values which are totally influenced by genes and environmental factors (nutrition, lifestyle, living environment, climate etc.). In genomics, transcriptomics, proteomics, metabolomics that metabolize metabolites constitute the last of the science of "OMICS". AMINO-MICS , which metabolizes amino acids among the metabolites, reveals clinical trials that will revolutionize the cure in recent years, together with developing analytical methods.
Amino acid analysis and amino acid treatments are fairly straightforward for 3P medical ratios. Amino acid analysis is an early warning system for possible health problems or undiagnosed diseases that will be explained in the following sections . It has been shown that blood levels and improved indices of amino acids that make up all the constituents and play a role in all functions are " PREDICTIVE" for many diseases. Among these diseases are insulin resistance, Type II diabetes, cardiovascular diseases, obesity and cancer.
Amino acid analysis gives clear information about our current health and nutritional status. In addition to the need to develop a nutritional / therapeutic model to prevent and eliminate the risk or current health problems, amino acid, vitamin and mineral supplements can be supplemented at the right proportions and balances. Amino acids are " PREVENTIVE" to prevent risks.
Amino acid supplements can be given exclusively to that individual based entirely on the analysis of the individual; ie person-specific "PERSONALIZED" .
The concept of 3P Medicine is spreading all over the world and scientific committees bringing together different branches carry out important studies. One of the most important goals of these committees is to increase their awareness of 3P in all countries. It is a fact that many professionals are not aware of this medical concept yet. 2020 is the targeted year, especially for the development and implementation of strategies26,27. For this reason, the work of 3P organizations is very valuable. In this context, while we try to set targets for the year 2020, the following sentences in China's first Medical Book, written in the year 2600,
Bad doctor treats the disease
Mediocre doctor destroys the disease without any symptoms Good doctor avoids the disease
Huang Dee nai-Ching (2600 BC 1st Chinese Medical text)
Family Medicine
Preventive medicine is the responsibility of all physicians, but it is the basic duty of the Family Physicians.
The only way to prevent rapidly spreading chronic diseases, primarily obesity and type II diabetes, is the lifestyle change, and the most important physician group to implement it is the Family Physicians.
Lifestyle modification may be of importance to the patient and the physician as a therapeutic approach, but only through scientific methods based on analysis and monitoring. The developments in the field of metabolomics, and especially the amino acid analysis, provide new evidence almost every month that disease risks can be determined in advance.
Family Physicians who undertake responsibility for the entire population from infancy to old age must be one of the strongest prescriptions for community health to have the right nutrition and mobility advice. The formation of a healthy society, all the information about proper nutrition and movement will be possible only if the people learn from their own Family Physicians, not those who are not competent.
Nutrition can be monitored with concrete evidence and these analyzes can provide suggestions that can prevent risks . A field that needs to be learned and developed for Family Physicians .
REFERENCES:
- Kimura T. Plasma amino acid analysis for diagnosis and amino acid-based metabolic net- works . Curr Opin Clin Nutr Metab Care. 2009 Jan; 12 (1): 49-53.
- Wang TJ. Metabolite profiles and the risk of developing diabetes. Nat Med. 2011; 8 (4): 448-453.
- Cheng S. Metabolite profiling identifies pathways associated with metabolic risk in humans.
- Rosen HM. Plasma amino acid patterns in hepatic encephalopathy of differing etiology . Gastroenterology. 1977 Mar; 72 (3): 483-7.
- Suliman ME. Inflammation contributes to low plasma amino acid concentrations in patients with chronic kidney disease . Am J Clin Nutr. 2005 Aug; 82 (2): 342-9.
- Ravaglia G. Plasma amino acid concentrations in patients with amnestic mild cognitive impairment or Alzheimer disease. Am J Clin Nutr. 2004 Aug; 80 (2): 483-8.
- Hisamatsu T. Novel, objective, multivariate biomarkers composed of plasma amino acid profiling for the diagnosis and assessment of inflammatory bowel disease. PLoS One. 2012; 7 (1): e31131.
- Kimberly WT. Metabolite profiling identifies a branched chain amino acid signature in acute cardioembolic stroke. Stroke. 2013; 44: 1389-1395.
- Miyagi Y. Plasma free amino acid profiling of five types of cancer patients and their application for early detection. PLoS One. , 2011; 6: e24143.
- Ihata Y. Amino acid profile index for early detection of endometrial cancer: verification as a novel diagnostic marker . Int J Clin Oncol. 2014; 19: 364-372.
- Degrell I. Amino acid concentrations in cerebrospinal fluid in presenile and senile dementia of Alzheimer type and multi-infarct dementia . Arch Gerontol Geriatr. 1989; 9: 123-35.
- Tudor I. A study of aminoacidemia and aminoaciduria in epileptic children . Neurol Psychiatr (Bucur) 1976; 14: 277-82.
- Ferenci P. Plasma amino acids in hepatic encephalopathy . J Neural Transm Suppl. 1978; 14: 87 94.
- Wu G. Functional amino acids in growth, reproduction, and health. Adv Nutr. 2010 Nov; 1 (1): 31-7
- Aydin A. Otizme Solution exists. Hayykitap. 4. Edition. Istanbul, 2015
- Wurtz P. Branched-chain and aromatic amino acids are predictors of insulin resistance in yo- ung adults. Diabetes Care. 2013; 36: 648-655.
- Yang R. Association of branched-chain amino acids with carotid intima-media thickness and coronary artery disease risk factors . PLoS One.Jun 9; 9 (6): e99598.
- Hüfner K. Levels of neurotransmitter precursor amino acids correlate with mental health in patients with breast cancer.Psychoneuroendocrinology. 2015 Oct; 60: 28-38
- Buist R. The therapeutic predictability of tryptophan and tyrosine in the treatment of depressi- on. Int J Clin Nutr Rev. 1983, 3: 1-3
- Young SN. The role of serotonin in human mood and social interaction. Insight from altered tryptophan levels. Pharmacol Biochem Behav. 2002 Apr; 71 (4): 857-65.
- Kuroda M. Tailor-made preventive medicine integrating amino acid checkup and its applicati- on toward disaster-stricken areas. Conf Proc IEEE Eng Med Biol Soc. 2012; 2012: 2116-9.
- Stapel SO, EAACI Task Force. Testing for IgG4 against foods as a diagnostic tool: EAACI Task Force Report. Allergy. 2008 Jul; 63 (7): 793-6.
- Gahl A. Referral of the food hypersensitive patient to the specialist. Allergy societies confirm: immunoglobulin G tests are inaccurate. Is Kinderkrankenschwest. 2010 Feb; 29 (2): 72.
- Carr S. CSACI Position statement on the testing of food-specific IgG. Allergy Asthma Clin Immunol . 2012 Jul 26; 8 (1): 12.
testing for the purposes of identifying or predicting adverse reactions to food. We also wish to remind the
medical community that blood testing is not a substitute for consultation with a trained and accredited medical professional such as an Allergist / Immunologist for the diagnosis and management of adverse reactions to food.
- http://www.epmanet.eu/
- Golubnitschaja O. Predictive, Preventive and Personalized Medicine as the Hardcore of 'Horizon 2020': EPMA position paper . EPMA J. 2014 Apr 7; 5 (1): 6.
- Lemke HU. Towards personal health care with model-guided medicine: long-term PPP-related strategies and realization opportunities within 'Horizon 2020' . EPMA J. 2014 May 30; 5 (1): 8. At the international EPMA Summit carried out in the EU Parliament (September 2013), the main chal- lenges in Predictive, Preventive andPersonalized Medicine have been discussed and strategies in order to implement scientific and technological innovation in medicine and healthcare. as 'Horizon 2020' .
- Duygu A. Predictive and Preventive Value of Type 2 Diabetes for Amino Acids . Journal of Clinical Tıp Bilimleri Volume: 3 Issue: 2 - April 2015
Amino Acids Protective and
Therapeutic Features
In today's conditions it is possible to analyze amino acids from whole body fluids and tissues. Hundreds of studies continue to show that blood amino acid analyzes can be used to detect many diseases early. In addition, amino acid analysis allows you to identify and follow what nutritional therapy is needed in physiological processes (pregnancy, growth, menopause, aging, exercise) and pathological conditions.
We clearly know that amino acids are the building blocks of proteins, and proteins function in all the functions and structures of our bodies.
Amino acids are obtained by digestion of food. However, it is also possible to give free amino acids as a supplement. Free amino acids are rapidly absorbed into the blood when taken orally. Amino acids inside the cell support protein structure and resist catabolic processes. For this reason, free amino acid supplementation counteracts the metabolic consequences of many hypercatabolic diseases such as liver diseases, diabetes, heart failure. Some of the diseases in which amino acid supplements are effective are shown in Fig.
FIGURE 38. Some of the diseases reported to be effective in amino acid supplements in clinical trials
Foods and protein powders contain a constant amount of essential amino acid content . For this reason, it is not a suitable stoichiometric condition to meet any essential amino acid requirement4,5.
Low or unbalanced amino acid levels balanced free
It is possible to correct with EAA formulation. AMINO ACID PERSON CAN BE FORMED SPECIFICALLY FOR MEETING DEFICIENCY OR MEETING METABOLIC NEEDLE 4-6 .
It takes at least three hours to digest protein powders and foods while the amino acids are fully absorbed in as little as 15-30 minutes. When amino acids are supplemented, both food and pharmacologically active proteins (proteins) only affect health as a food. This explains why free amino acid supplements may be insufficient for protein-containing foods or protein powders instead of amino acids 6,7 .
Table 4. Comparison of free amino acid and protein 6.7 .
FREE AMINO ACID
PROTEIN
Method of Application
Medicine, Cosmetics, Food
food
Allergenicity
No
Yeah
Essential amino acid ratio
0-100% Adjustable
It is fixed between 30-40%
Need for digestion
No
Compulsory
Absorption time
Max 30 minutes
3-4 hours
Pharmacological effect
Yeah
No
Nutritive value
Yeah
Yeah
ONE OF THE LARGEST HEALTH CARE MUST HAVE A PROTEIN RESTRICTION AND THE SPECIFIC STANDARDS WILL NOT BE ABLE TO ALL THE PUBLIC IN ALL TALKS. Amino
rich sources of acids are very limited by the fact that animal proteins are first converted to cholesterol and saturated fats and then to problems with processed products as well as to unprocessed products. In the arguments against this understanding (Atkins, Dukan), animal proteins have begun to be proposed more than necessary.
At this point, the position of the amino acid supplements is the period where the greatest increase in protein requirement is the periods where growth and development are fastest and catabolism is increased. The period from infancy to adulthood is the period of growth-development; processes in which the person develops chronic catabolic diseases (diabetes, heart failure, liver diseases, cancer) and natural aging (post-60-65) are catabolic periods.
AMOUNT ASI-TE NEEDS MORE MORE PROTEINS TO TAKE AN OPTIMIZED NEEDS IN GROWTH DEVELOPMENT PERIOD, TO INCREASE TISSUE AND BRIDGE DECREASE IN CATABOLIC PROCESSES.
However, the situation we see is exactly the opposite. Protein is especially reduced in chronic diseases and elderly people. The biggest reason for this is the fear that consuming too much protein and wrong will damage the kidneys and liver.
In the consensus report of the International Society for Renal Nutrition and Metabolism (2013), if kidney patients do not need dialysis, the daily protein intake should be 0.6 - 0.8 g / kg but not in the presence of any catabolic disease it should be increased to 1 g / kg when restricting movement. It is recommended that daily protein intake be greater than 1.2 g / kg in renal patients receiving dialysis8. The recommended daily protein intake for a healthy adult in all classical medical books is 0.8 g / kg.
In a randomized controlled trial conducted in type II diabetics, protein consumption over the standard (90-120 grams per day) for 2 years did not have a negative effect on renal function9.
So you will understand that for years, if you take too much protein in people, your kidneys will be harmed, but INTERNATIONAL RENOVATED WORKSHOP SUGGES TO INCREASE PROTEIN PACKAGE IN THE DISEASE.
High protein diets have gained importance in recent years and have yielded successful results. In another randomized controlled trial that lasted for two years, the effects of high-protein / low-carbohydrate diet and Mediterranean diet on type 2 diabetes and healthy subjects were compared and investigated to determine how they affect renal function. As a result, the Mediterranean diet has been shown to be healthy on high-protein / low-carbohydrate diet kidney functions10.
What is the limit to increase the amount of protein? Despite all these publications, there are studies that report that excessive protein consumption is wrong11.The existence of these studies is important in the name of knowing what the limit will be. Concerns about high protein consumption are concentrated on the possibility that the kidneys will over-filter, increase blood pressure, increase risk of kidney stones, and increase sodium intake with protein. In order to see these possible side effects, the daily amount of protein anxiety consumed is over 2 g / kg. Since the daily amount required for a sedentary adult is 0.8 g / kg, the amount of concern is a very high limit. For example, a 70 kg adult needs 140 grams of protein to consume 2 g / kg protein. 100 grams of steak contain about 25-30 grams of protein. In this case 500 grams of meat per day is required to consume the specified amount of protein which may be objectionable. Or 20 eggs. Under no circumstances does anyone need such an excessive amount of animal protein.
Do free amino acids create an additional burden on healthy people or kidney patients? Even if you are not warm enough to consume too much protein yet, amino acids make the job much easier5.
100 grams of fat-free (containing 10% fat) protein contains about 26 grams of protein, only 8 to 9 grams of essential amino acids. In addition to 100 grams of meat and 9 grams of essential amino acid, 11 grams of fat, 88 mg of cholesterol and 217 kcal are taken 12.
Only the person or patient who avoids fat, cholesterol or caloric load is only to be given 8-9 GRAM ESSENTIAL AMINO ACID SUPPLEMENT
With 32-36 kcal, zero fat and zero cholesterol, it offers the ability to meet the full daily essential amino acid requirement.
FREE AMINO ACID RESPONSE PERSON DAILY ONLY ONE YU-
PROTEIN LOADS TO MURDO. In contrast, cholesterol does not build up fat and calories .
The state of protein dusts is just like protein-containing foods. This is explained in more detail in the section on support for the topic (Chapter 17).
REFERENCES:
- Kimura T. Plasma amino acid analysis for diagnosis and amino acid-based metabolic net- works. Curr Opin Clin Nutr Metab Care. 2009 Jan; 12 (1): 49-53.
- Pasini E. Amino acids: chemistry and metabolism in normal and hypercatabolic states. Am J
Amino acids are the "alphabet" of protein structure, determining many of the properties of proteins. Amino acids are readily absorbed and readily available in the blood. In the cell, amino acids maintain protein stores and counteract hormone-mediated catabolic stimuli. Thus, amino acid supplementation may be effective in counteracting the metabolic and morphologic consequences of the hypercatabolic state of chro- nic, such as heart failure, diabetes mellitus, or liver cirrhosis.
- Dioguardi FS. Wasting and the substrate-to-energy controlled pathway: a role for insulin resistance and amino acids. Am J Cardiol. 2004 Apr 22; 93 (8A): 6A-12A.
An amino acid formulation suitable for match energy needs, control carbohydrate and lipid flow into the TCA cycle, and promote protein synthesis in contracting cells is detailed in this article.
- To Valerio . Branched-chain amino acids, mitochondrial biogenesis, and healthspan: an evoluti- onary perspective. Aging (Albany NY). May May; 3 (5): 464-78.
- Dioguardi FS. Clinical use of amino acids as dietary supplement: pros and cons . J Cachexia Sarcopenia Muscle. 2011 Jun; 2 (2): 75-80.
SUPPLEMENTING DIET WITH EAA IS AN EFFICIENT METHOD TO INCREASE EFFICIENCY OF NITROGEN SUPPLY AND MAINTAINING INTEGRITY OF THE LARGEST RESERVOIR OF AMINO ACIDS, SKELETAL MUSCLES, WHILE OPTIMIZING UREA SYNTHESIS.
- http://www.ajiaminoscience.com/research/articles.aspx
- Pasini E. malnutrition, muscle wasting and cachexia in chronic heart failure: the nutritional approach. Ital Heart J. 2003 Apr; 4 (4): 232-5
- Twins TA. Prevention and treatment of protein energy wasting in chronic kidney disease Patients : a consensus statement by the International Society of Renal Nutrition and Metabolism. Kidney Int. 2013; 84 (6): 1096-107.
- Jesudason DR. Weight-loss diets in people with type 2 diabetes and renal disease: a randomized controlled trial of the effect of different dietary protein levels . Am J Clin Nutr. 2013; 98: 494-501.
- Tirosha . Renal function following three distinct weight loss dietary strategies during 2 years of a randomized controlled trial. Diabetes Care.2013 Aug; 36 (8): 2225-32.
<176 mmol / L. Potential improvement is likely to be mediated by weight loss-induced improvements in
insulin sensitivity and blood pressure.
- MARCKMANN P. HIGH-PROTEIN DIETS AND RENAL HEALTH. J REN NUTR. 2015 JAN; 25 (1): 1-5.
- http://ndb.nal.usda.gov/ndb/foods/
Amino Acid Analysis Report Type II Diabetes and Insulin Resistance Before They Happen
Type II diabetes is spreading rapidly in our country as it is in the whole world. The data of the comprehensive studies investigating the frequency of diabetes in our country are quite frightening. Made in 1998 and 2010, according to TURDEP-I-II study completed TURDEP 12 years, diabetes prevalence in Turkey
90%, and the obesity frequency increased by 44%.
According to TURDEP-II, the frequency of diabetes in the Turkish adult population has reached 13.7%. It is useful to review the TURDEP-II conclusion report which shows how large the risk is.
"Istanbul University Faculty of Medicine by the Ministry of Health's sa- hada performed with logistic cooperation" Turkey Diabetes, Hypertension, Obesity and Endocrinology Diseases Prevalence Study-II (TURDEP-II Trial) 's field research in January 2010-June 2010 between 15 floors were completed in 540 centers.26499 people aged 20 and over participated in the study, randomly selected and invited in accordance with the population structure . "
- According to TURDEP-II, the frequency of diabetes in Turkish adult population has reached 13.7%.
- According to the TURDEP-II study, the population from the age group of 40-44
- In TURDEP-I, the prevalence of diabetes above 10% was beginning in the 45-49 age group. Based on diabetes in 1998, according to Turkey considered as stylish as yakla- begin no earlier than 5 years of age.
- In general, 2/3 of the Turkish population in adult ages is overweight or obese.
- The prevalence of obesity in our study was found in Turkey by 32%.
- The rate of hypertension was around 30% as it was in the previous study, and the difference between women and men and urban-rural disappeared.
- As a result, in 1998, it made by the newly completed TURDEP TURDEP-I and II studies in Turkey for 12 years, diabetes prevalence by 90%, while obesity has increased 44%.
In other words, it is pointed out that obesity and diabetes are the most important public health problems in our country. In the coming generations, an urgent action plan to encourage the lifestyle of obesity and prevention of diabetes must be established and put into practice immediately so that these problems can be reduced1 ( http://www.diabetcemiyeti.org/c/turdep-2-sonuclarin-ozeti ) .
Another important research that clearly koymaktadır2 TEKHARF how rapidly increased in type II diabetes Turkey s year-end.
FIG. 39A. Distribution of type II diabetes prevalence (in percent) determined by TEKHARF participants in the last 12 years by age group and three time periods. It is understood that the frequency of sighting increases at a very high rate of 5% per annum.
FIG. 39B. The incidence of type II diabetes worldwide "Lancet Diabetes Endocrinol. 2014 Sep; 2 (9): 740-753 & quot;
On the world map published by the Lancet magazine, fields marked with burgundy indicate the countries where the type II diabetes is most common. When we look at these countries, it is not possible to see that there are too many similarities in lifestyle except for the similarity of type II diabetes. The most obvious common feature is the relatively easy access to industrial food and, most importantly, very little physical activity.
Unfortunately, I would like to convey to you a piece of information that has not been touched to this day . This information reveals why we have to be so serious about diabetes, and how MULTI-OF-THERAPY works to prevent diabetes.
Cardiovascular (cardiovascular) complications of diabetes are the most important causes of morbidity and mortality. Even with very intensive anti-diabetic treatment to prevent diabetes mellitus and its complications, the results of cardiovascular complications are disappointing. Patel and colleagues report thatintensive blood glucose control reduces macro- and microvascular (large and small vessel) complications by only 10% 3 , Duckworth noted thatintensive blood glucose control does not significantly alter major cardiovascular events and death 4 .
Both of these studies have been published in The New England Journal of Medicine ( NEJM ), one of the most respected medical journals . You can find the articles at the end of the chapter 3,4 .
Owing to all these reasons, it should be the main goal without DIABETIC PATIENT . The only way to do this is to change the lifestyle. It is obvious that changing your lifestyle will not be easy in a short time. Therefore, determining the risk of diabetes too early will provide important advantages.
Risk factors such as family history, age, sex, and obesity are the most important predictors of type II diabetes risk. It can be assumed that genetic factors and variability (polymorphism) can predict diabetes in advance. At least 40 genetic variants searched to date have more predictive value than the current predictors (family history, obesity, biochemical data, age) in determining type II diabetes risk
. GENETIC ANALYSIS IN THE CURRENT SITUATION IS NOT POSSIBLE TO DETERMINE TYPE II DIABETES RISK 5,6 .
On the contrary, each year a new clinical trial has reported that AMINO ACID-RIN TYPE II IS PREDICTIVE FOR DIABETES.
AMINO ACID ANALYSIS TYPE II RISK OF DIABETES DEVELOPMENT 12 YEARS NOTICE!
Summary of clinical trials:
From the Framingham Heart Study group, Wang and colleagues found that the increase in the concentration of branched chain (isoleucine, leucine, valine) and aromatic amino acids (Tyrosine, Phenylalanine) was predictive of diabetes development7. At the beginning of the study, 2422 people who were not diabetic (normoglisemic) were seen for 12 years. Several metabolites, including amino acids, of all individuals (more than sixty metabolites) were measured at baseline.Changes in the baseline levels of isoleucine, leucine, valine, tyrosine and phenylalanine were highly significant for diabetes developed after 12 years. Individuals with high blood levels of isoleucine, tyrosine, and phenylalanine were 5-7 times more likely to have diabetes risk after 12 years than those with low blood levels (p = 0.007 - 0,0009).
The same scoring was later applied by the independent Malmö Diet and Cancer Study Group. It was shown that individuals with high amino acid concentrations had a 4-fold increased risk of diabetes compared to those with low levels (p = 0.006) 7.
In addition, several recent studies have shown that amino acid analysis can be used for early diagnosis and risk screening of diabetes, insulin resistance and cardiovascular diseases. In addition, the Department of Endocrinology and Metabolism at the University of Duke and the Department of Nutrition Physiology at Munich Technical University (2014-2015) states that branched-chain amino acids should be examined as a routine clinical marker for diabetes, metabolic syndrome and obesity12,13 .
The clinical study I outlined above was conducted under the leadership of Harvard University, and the amino acid analysis reports that the development of diabetes was reported 12 years in advance. In addition, studies conducted in different countries and societies have reported similar results.
AMINO ACID ANALYSIS PROVIDES INNSULIN DIRECTOR'S DEVELOPMENT APPEARANCE BEFORE 6 YEARS This is not a wish. Many scientific studies have reported that amino acids point to developing insulin resistance many years ago. Almost every month, a clinical study from a different country in a different medical journal reports that amino acids are predictive of insulin resistance in their community.
INSULIN DIRECTIN'S RELEVANCE WITH OBESITY, DIABETES, HEART DISEASES, CANCER, AND MORE SUSCEPTIBILITY
It is KNOWN. It is a medical error not to be aware of the existence of an analysis that presents a risk without the occurrence of insulin resistance and to not use it.
Because it is so important, it will be useful to share some of the clinical studies that demonstrate this scientific fact in detail.
Summary of clinical trials:
In the "Cardiovascular Risk in Young Finns Study" study by Würtz et al., The amino acid values and various metabolites of 1680 young adults between 27-37 years of age with normal blood sugar levels were measured. The aim was to determine whether amino acids are predictive of future insulin resistance in healthy young people. During the initial and 6-year follow-up, insulin resistance was assessed by the HOMA-IR test we used frequently today.
Blood glucose levels in the study were found to be predictive of insulin resistance developing after 6 years (p <0,05) 14) Concentrations of branched chain and aromatic amino acids measured in normal young adults 14.
A similar study was conducted in children and adolescents aged 8-18 years, under the leadership of Massachusetts General Hospital and Harvard Medical School. Amino acid analysis has shown early warning for future insulin resistance even in this age group15.
Amino acids have been shown to detect insulin resistance in Asians with a relatively low risk of obesity, yet not obese or diabetic [16]. The study in Japan in 2015 gave the same result as previous studies and showed that amino acids are predictive for future insulin resistance in non-diabetic Japanese [17].
In Asian populations where Western society and obesity are less common, it has been reported that amino acids are pre-stimulating metabolites for insulin resistance 14,15,16,17,18,19,20. I also observe in the analyzes of my patients or clinicians that I am not a minority in the Turkish population.
If there are no health problems in the fit or present, patients and athletes who check-up at the time of amino acid analysis are at risk for insulin resistance, or even if they say that resistance has developed. But is not the purpose of the check-ups already in advance of exposing the risks?
FREE AMINO ACID REINFORCEMENTS DIABETES AND INSULINARY PRECAUTIONS FREE AMINO ACIDS ARE EFFECTIVE IN THE TREATMENT OF DIABETES AND DIABETES COMPLICATIONS
The main function of the insulin hormone is to transport the blood sugar into the cell, store it and use it as energy. The most important target that can perform this function is muscle mass. Muscle mass makes up 50% of all the proteins in the body. ANNABOLIZED EFFECT BETWEEN INSULIN PROTEIN METABOLISM, BUT QUALITY ORANDA AMINO ACID POSSIBLE
MAY MAKE. 75% of the glucose obtained after meals is used by the muscles. For this reason, muscle tissue is the main player in the regulation of blood sugar.The target tissue to prevent health problems such as obesity, diabetes and insulin resistance is muscle mass21.
Decreased muscle mass and function cause deterioration of blood glucose usage and storage. Decreased muscle mass with age prepares the insulin resistance, glucose intolerance and diabetic footing. This increases the need for amino acids in order to prevent muscle breakdown and improve protein synthesis, particularly in the elderly with diabetes22.
Amino acids lower blood sugar. This effect is shown by increasing protein production in tissues and by restoring insulin resistance by improving the cellular function of the pancreas23.
FREE AMINO ACID REACTION Blood Sugar Reforms Clinical trials have shown that fasting amino acid supplements lower blood sugar and reverse insulin resistance in patients with type II diabetes. In a 60-week study, specific diabetes medications were used to treat type II diabetes and special amino acid supplementation was given in addition to 34 diabetic patients (65-83 years) with insufficient blood sugar control (HbA1c <7) despite insulin. From the second week onwards, toughness began to decrease in blood sugar, but from the 8th week onwards, there was a significant decrease in fasting blood sugar, insulin resistance and HbA1c levels compared to the placebo group, and the decrease was more prominent in the fourth month. HBA1c levels continued to decline during 60 weeks of application and no adverse effects on the use of amino acids were observed during this period23.
A.
FIG. Blood sugar change under amino acid therapy 23
class = Section144>
B.
FIG. Insulin resistance (HOMA-IR) change under amino acid treatment 23
PREVENTION OF FREE AMINO ACIDIC DIABETES COMPLICATIONS Diabetes is the leading cause of kidney failure, nerve damage, blindness and cardiovascular disease. Damage to small and large vessels in diabetics is caused by the adherence of sugars to proteins (glycation) and disrupting cell structure and function.
Lowering blood sugar prevents microvascular (small vessel) complications of diabetes, but has little protective effect on macrovascular (large vessel) complications. It has been shown that free amino acid supplementation can prevent macrovascular complications in addition to contributing to regulation of blood glucose and reducing microvascular complications.
For example, Lizinin has been reported to delay cataract formation in the eye. The most important reason for this is the antiglycolytic properties of lysine amino acid, that is, the effect of sugar on the adhesion of other molecules. The same effect is reported for other amino acids26.
Many complications of type II diabetes have been shown to be due to reduced antioxidant capacity against increased oxidative stress. In particular, the concentration of glutathione in the cells is reduced. Glutamine , Glutamic acid, and Cysteine, most amino acids, have antioxidant activity and reduce the oxidative stress caused by hyperglycemia27.
FREE AMINO ACID SUPPORT
- Reduces insulin resistance 21,23 .
- Hunger and satiety reduce blood sugar 21,23,26 .
- Prevents glycation 26,30 .
- Decreases oxidative stress by antioxidant effect 26,27,30 .
- Prevents muscle destruction and increases muscle protein synthesis 28,29 .
- Weighs 25 .
- Has a preventive effect on heart diseases 31 .
- Prevents fatty liver 32 .
REFERENCES:
- Satman I. TURDEP-II Study Group. Twelve-year trends in prevalence and risk factors of diabetes and prediabetes in Turkish adults. Eur J Epidemiol. 2013 Feb; 28 (2): 169-80.
- Onat A. Turkish Adult Risk Factor survey 2013: rapid rise in the prevalence of diabetes . Turk Cardiol Dern Ars. 2014 Sep; 42 (6): 511-6.
- ADVANCE Collaborative Group, Patel A. Intensive blood glucose control and vascular outcomes in patients with type 2 diabetes. N Engl J Med.2008 Jun 12; 358 (24): 2560-72 .
- Duckworth W, VADT Investigators. Glucose control and vascular complications in veterans with type 2 diabetes. N Engl J Med. 2009 Jan 8; 360 (2): 129-39.
- Vassy JL. Is genetic testing useful to predict type 2 diabetes? Best Pract Res Clin Endocrinol Me- tab. 2012 Apr; 26 (2): 189-201.
- Lyssenko V. Clinical risk factors, DNA variants, and the development of type 2 diabetes. N Engl J Med. 2008 Nov 20; 359 (21): 2220-32.
- Wang TJ. Metabolite profiles and the risk of developing diabetes. Nat Med. 2011 Apr; 17 (4): 448-53. Cardiovascular Research Center, Massachusetts General Hospital, Harvard Medical School, Boston, Massachusetts, USA.
- Magnusson M. A diabetes-predictive amino acid score and future cardiovascular disease . Eur Heart J. 2013 Jul; 34 (26): 1982-9.
- Drábková P. An Assay of Selected Serum Amino Acids in Patients with Type 2 Diabetes Mellitus . Adv Clin Exp Med. 2015 May-Jun; 24 (3): 447-51
- Tillin T. Diabetes risk and amino acid profiles: cross-sectional and prospective analyzes of ethnicity, amino acids and diabetes in a South Asian and European cohort from the SABER study. Diabetologia. May 5, 58 (5): 968-79.
Branched-chain and aromatic AAs, especially tyrosine, may be a focus for identifying novel aetiological mechanisms and potential treatment targets for diabetes in South Asian populations and may contribute to their excess risk of diabetes
- Wang-Sattler R. Novel biomarkers for pre-diabetes identified by metabolomics. Mol Syst Biol. 2012; 8: 615.
- Batch BC. Branch chain amino acids: biomarkers of health and disease. Curr Opin Clin Nutr Metab Care. 2014 Jan; 17 (1): 86-9.
- Giesbertz P. Branched-chain amino acids as biomarkers in diabetes. Curr Opin Clin Nutr Metab Care. 2015 Oct 20.
- Würtz P. Branched-chain and aromatic amino acids are predictors of insulin resistance in yo- ung adults. Diabetes Care. 2013 Mar; 36 (3): 648-55.
- Mc Cormack SE. Circulating branched-chain amino acid concentrations are associated with obesity and future insulin resistancein children andadolescents . Pediatric Obes. 2013 Feb; 8 (1): 52-61. Elevated levels of circulating BCAAs are significantly associated with obesity in children and adolescents, and may predict future insulin resistance.
- Tai ES. Insulin resistance is associated with a metabolic profile of altered protein metabolism in Chinese and Asian-Indian men. Diabetologia.2010 Apr; 53 (4): 757-67.
These findings demonstrate that perturbations in amino acid homeostasis, but not inflammatory markers or NEFAs, are associated with IR in individuals with relatively low body mass.
- Yamada C. Association between insulin resistance and plasma amino acid profile in non- diabetic Japanese subjects. J Diabetes Investig. 2015 Jul; 6 (4): 408-15 .
- Wurtz P. Metabolic signatures of insulin resistance in 7,098 young adults . Diabetes. 2012 Jun; 61 (6): 1372-80.
Nonetheless, metabolic signatures extend beyond obesity and lipid abnormalities, and the degree of insulin resistance is evidenced in young, normoglycemic adults with sex-specific fingerprints.
- Huffman KM. Relationships between circulating metabolic intermediates and insulin action in overweight to obese, inactivemen and women.Diabetes Care. 2009 Sep; 32 (9): 1678-83.
- Newgard CB. A branched-chain amino acid-related metabolic signature that differentiates obesa and lean humans and contributes to insulin resistance . Cell Metab 2009; 9: 311-326.
- Solerte SB. Metabolic effects of orally administered amino acid mixture in elderly subjects with poorly controlled type 2 diabetes mellitus. Am J Cardiol. 2004 Apr 22; 93 (8A): 23A-29A.
- Dioguardi FS. Clinical use of amino acids as dietary supplement: pros and cons . J Cachexia Sarcopenia Muscle. 2011 Jun; 2 (2): 75-80.
- Solerte SB. Improvement of blood glucose control and insulin sensitivity during a long-term (60 weeks) randomized study with amino acid dietary supplements in elderly subjects with type
The reduction of muscle mass may be responsible for reduced insulin sensitivity and decreased glucose uptake, thus increasing the risk for hyperglycemia and insulin-resistance syndrome in elderly subjects with type 2 diabetes mellitus. We therefore wanted to determine the effect of a special mixture of oral amino acids (AAs) on elderly subjects with type 2 diabetes.
Fasting and postprandial (1 hour and 2 hours) blood glucose, serum insulin, and homeostatic model assessment of insulin resistance . There was a significant reduction in HbA (1c) levels found in thro- ughout the study. No significant adverse effects were observed during the active treatment. We suggest that nutritional supplementation with a special mixture of oral AAs is safe and significantly improves metabolic control and insulin sensitivity in elderly subjects with type 2 diabetes. This effect was consistent during the long-term observation period of 60 weeks and was also present after the crossover from AAs to placebo.
- Solerte SB . Nutritional supplements with oral amino acid increase the whole-body lean mass and insulin sensitivity with infertile subjects with sarcopenia. Am J Cardiol. Jun Jun 2; 101 (11A): 69E-77E. These preliminary data indicate that the nutritional supplements with the oral AA were significantly increased in the whole-body lean mass in elderly subjects with sarcopenia. The IGF-1 availability was assessed in terms of the IGF-1 availability.
- Klaus J. Petzke. Beyond the Role of Dietary Protein and Amino Acids in the Prevention of Diet- Induced Obesity. Int. J. Mol. Sci. 2014, 15, 1374-1391
- Natarajan Sulochana K. Effect of oral supplementation of free amino acids in type 2 diabetic patients- a pilot clinical trial. Med Sci Monit. 2002 Mar; 8 (3): CR131-7.
- Sekhar RV. Glutathione synthesis is diminished in patients with uncontrolled diabetes and restored by dietary supplementation with cysteine and glycine. Diabetes Care. 2011 Jan; 34 (1): 162-7. Patients with uncontrolled type 2 diabetes have severely deficient synthesis of glutathione attributed to limited precursor availability. Dietary supplementation with GSH precursor amino acids can restore GSH synthesis and lower oxidative stress and oxidant damage in the face of persistent hyperglycemia.
- Volpi E. Essential amino acids are primarily responsible for the amino acid stimulation of muscle protein anabolism in healthy elderly adults .Am J Clin Nutr. 2003 Aug; 78 (2): 250-8.
- Paddon-Jones D. Amino acid ingestion improves muscle protein synthesis in the young and elderly . Am J Physiol Endocrinol Metab. 2004 Mar; 286 (3): E321-8.
Essential amino acid supplementation acutely stimulated muscle protein synthesis in both young and elderly individuals
- Anuradha CV. Aminoacid support in the prevention of diabetes and diabetic complications . Curr Protein Pept Sci. 2009 Feb; 10 (1): 8-17.
- Drake KJ. Amino acids as metabolic substrates during cardiac ischemia. Exp Biol Med (Maywood ). 2012 Dec; 237 (12): 1369-78. DESPITE CLEAR EVIDENCE THAT AMINO ACIDS EXIT CARDIOPROTECTIVE EFFECTS IN ISCHEMIA AND OTHER CARDIAC DISORDERS, RELATED TO THEIR ISCHEMIC HEART .
- Theytaz F. Effects of supplementation with essential amino acids on intrahepatic lipid con- centrations during fructose overfeeding in humans .Am J Clin Nutr. 2012 Nov; 96 (5): 1008-16.
Amino Acid Analysis Predicts Risk of Heart Disease
Heart attack (myocardial infarction) accounts for 30% of all deaths in the world1 . Coronary disease and heart failure in diabetic patients are three times more common than in the normal population. Diabetes causes damage to both the heartbeat cell and disrupts the function of the heart. In diabetic patients, imbalance occurs in the amino acid levels of the heart muscle. This makes it difficult to use amino acids as a source of energy, and it also reduces the muscle contraction of the heart muscle, which is composed of amino acids2.
As is the case with diabetes, the basis of protection from coronary heart disease is also the style of life change. A life without smoke and a healthy life is a precondition for the prevention of a healthy nutrition from a heart attack. However, metabolic markers that can predetermine the risk of such a widespread and deadly disease are the most important need to be protected from the disease.
Diabetes, high blood pressure, high cholesterol, and obesity are known risk factors for coronary artery disease. Several recent studies have shown that branched-chain amino acids are risk takers for coronary disease, independent of all these known risk factors. According to clinical studies, each percentile increase in BCAA levels doubles the risk of coronary heart disease3,4.
It has been reported that amino acids, especially branched-chain (BCAA) amino acids, are also risk factors for cardiovascular diseases such as insulin resistance and diabetes. The high risk for type II diabetes has proven that the presumptive amino acid scoring is a risk indicator for cardiovascular disease and that diabetic patients can show early on their susceptibility to heart disease5,6.
AMINO ACIDS HEALTH CARE7-13 Amino acids are effective in metabolic, mechanical and electrical activities of the heart. Amino acids protect against cardiac ischemia (cut-off of blood flow) and anoxia (cardioprotective).
The heart needs high energy as a continuously functioning organ. Each day, an average of 35 kg of ATP is produced, which uses 10% of all oxygen in the body.The body pumping blood to the whole body needs a continuous supply of energy to produce energy and oxygen. Heart functions are energy dependent (ATP) and sufficient ATP urea-
If not, all functions are degraded within minutes. Even if there is not enough oxygen and ischemic conditions, the heart muscle must be able to continue acting as a pump. For this reason, the heart can use different substances such as fatty acids, glucose, lactate, ketone bodies and amino acids as an energy source7.
NORMAL CONDITIONS (WITH OXYGEN COMPETENCE) HEALTH PRIORITY- ENERGY RESOURCE OIL ACTIVITY AND LACTATURE.
However, ischemia, lack of oxygen and many heart disease, fat burning is blocked and the heart is directed to other sources for energy. As the energy resources are producing ATP, they need oxygen and form a dense acidic waste product. Amino acids have the potential to produce energy without oxygen (non-oxidative metabolism) and are less insensitive to acidic waste leaving the heart for critical moments. That is, oil and keton objects can not be used for energy when the heart is left without oxygen in a shape and can not be absorbed. Glucose can not be used because of the intense acidic environment. In this case, the only option is amino acids. Amino acids are like generators that are switched on shortly after power failure for the heart .
to
B
FIG. 41A-B. Effect of amino acids on ischemic heart 9
Experiments in mice have shown that long-term administration of amino acids reduces damage caused by heart attack. The heart of the long-term amino acid-administered mice (1 g / kg amino acid for 20 days) produced more ATP in the 30-minute ischemic period than did the non-amino acid mice and was better restored in mice given amino acid after left ventricular ischemia.
In diabetic patients, amino acid supplementation promotes the physiological metabolism of the heart muscle and enables more efficient production of cardiac proteins. In other words, amino acid supplementation inhibits the structure and function of the heart muscle in diabetic patients10.
In a study with amino acid support for 6 months, 103 patients with type II diabetes and 104 patients with type II diabetes treated with placebo were evaluated for echocardiography at baseline and 6 months after left ventricular function. In the study, administration of free amino acids with ACE inhibitor medication reduced left ventricular dilatation and impaired cardiac function11.
FREE AMINO ACID SUPPORT
- Provides support for heart muscle energy (ATP) production 7,8 .
- It destroys enzymes that block energy production 7,8 .
- Provides NADH (nicotinamide adenine dinucleotide) which will provide rapid energy after ischemia 7,8 .
- Increases glutathione level, which protects the heart from free oxygen radicals 7,8 .
- Reduces blood triglycerides, total cholesterol, VLDL (very low density cholesterol) levels and reduces liver fatigue 12 .
- IGF-1 (Insulin-Like Growth Factor-1) increases the release of the hormone. IGF-1 protects the heart cells infarct, reduces cardiac load, and prevents heart growth and ventricular enlargement 13,14 .
REFERENCES:
- World Health Organization . World Health Statistics 2008 . Geneva : WHO ; 2008 .
- Avogaro A. Diabetic cardiomyopathy : a metabolic perspective . Am J Cardiol. 2004 Apr 22; 93 (8A): 13A-16A. Review.
- Bhattacharya S. Validation of the association between a branched chain amino acid metabolite profile and extremes of coronary artery disease in patients referred for cardiac catheterization. Atherosclerosis. 2014 Jan; 232 (1): 191-6.
- Yang RY. Association of branched-chain amino acids with coronary artery disease: A matched -pair case-control study. Nutr Metab Cardiovasc Dis. 2015 Oct; 25 (10): 937-42.
- Batch BC. Branch chain amino acids: biomarkers of health and disease . Curr Opin Clin Nutr Metab Care. 2014 Jan; 17 (1): 86-9.
- Magnusson M. A diabetes-predictive amino acid score and future cardiovascular disease . Eur Heart J. 2013 Jul; 34 (26): 1982-9.
- Drake KJ. Amino acids as metabolic substrates during cardiac ischemia . Exp Biol Med (Maywod ). Dec 237 (12): 1369-78.
- Marazzi G. The role of amino acids in the modulation of cardiac metabolism during ischemia and heart failure. Curr Pharm Des. 2008; 14 (25): 2592-604.
- Pasini E. Effect of amino acid mixture on the ischemic heart. Am J Cardiol. 2004 Apr
Data show that uptake of amino acids correlates with myocardial oxygen consumption after aortic cross-clamp in humans; This suggests a direct link between amino acids and myocardial energy metabolism. WA
conclude that long-term supplementation of an amino acid mixture reduced myocardialische- mic damage.
- Scognamiglio R. Early myocardial dysfunction in the diabetic heart: current research and clinical applications. Am J Cardiol. 2004 Apr 22; 93 (8A): 17A-20A.
- Scognamiglio R. Effects of oral amino acid supplements on cardiac function and remodeling in patients with type 2 diabetes mellitus-to-moderate left ventricular dysfunction . Am J Cardiol. Jun Jun; 101 (11A): 111E-115E.
- Børsheim E. Amino acid supplementation reduced plasma and liver triacylglycerols in elderly.
Hypertriglyceridemia is a risk factor for coronary heart disease. DIET SUPPLEMENTATION WITH AAS LOWERS PLASMA TG, TOTAL CHOLESTEROL, AND VERY LOW-DENSITY LIPOP- ROTEIN CHOLESTEROL CONCENTRATIONS AND LIVER LIPID CONTENT IN IMPAI- RED GLUCOSE TOLERANT ELDERLY.
- Pasini E. Amino acids: chemistry and metabolism in normal and hypercatabolic states. Am J
Amino acid supplementation may be effective in counteracting the metabolic and morphologic condi- tions of the hypercatabolic state of chronic diseases such as diabetes mellitus, or liver cirrhosis.
- Jennings A. Amino Acid Intakes Are Inversely Associated with Arterial Stiffness and Central Blood Pressure in Women. J Nutr. 2015 Sep; 145 (9): 2130-8.
Obesity
Obesity is the most important public health problem of our time.
While we acknowledge that obesity is a cosmetic problem, the problem is that we do not know that the real problem is diabetes, heart attack, liver fatigue, high blood pressure, paralysis, sleep apnea, infertility and many cancer types1.
All metabolic processes leading to obesity (eg insulin resistance) are also among the causes of chronic illnesses. Obesity can be perceived as an important symptom in the developmental process of all these diseases. Unfortunately, it is very likely that the process of development of these diseases has begun on the body before reaching the size which will disturb the people.
For this reason, the more important the weight loss effort is, the more difficult it is to observe and address the health problems associated with obesity.
We can say that people are sensitive about health problems caused by obesity. However, weight loss efforts and most of the treatment proposals are generally REALLY GOOD TO VIEW GOOD VISIBILITY IN HEALTHY.
To understand what this is, it is enough to have a brief look at health programs, health pages, product advertisements. With three drops of water, trash, and ultra, mega etc. Let's say we have lost ten pounds with three-day shock dies with attractive devices. Do you think these methods can prevent the disease processes that start to develop before the kilo is formed?
On the other hand, it is obvious that weight loss is not the correct way to lose weight by exposing hundreds of diagnoses and treatments to a person who wants to look good.
For this reason, there is a need for practical and comprehensive treatment and treatment methods for obesity treatment and weight control. PERSONS SHOULD BE PROTECTED AS PENALTY, HEART CRISIS, DIABETES, AND PATIENTS THROUGH THEM.
Hundreds of dietary recommendations and hundreds of products for obesity treatment and weight control have been introduced. However, although the rate of dieting increases and every day a remarkable diet or success of the product is mentioned, obesity is becoming more common and the kilograms are getting back up quickly.
EXISTING METHODS INCREASED OR COMPLETELY INCORRECTED This claim does not require much evidence. Because obesity rate increases rapidly.The whole world is under the threat of obesity and the diseases it causes . In our country, one out of every three (32%) reached the limit of obesity 2 .
THE MOST OCCURRENT RESULTS IN THE PRESENT DIET AND TREATMENT METHODS:
- Not fat, muscle loss
- During the diet, fatigue, unhappiness, angry mood
- Leaving the diary / treatment for a long time
- I can not lose enough weight
- Quick and more retrieval of given kilos
- Degradation of health due to diet or applied treatment
CURRENT DIESES AND TREATMENT METHODS DEFICIENCY AND MALFUNCTIONS:
- Obesity is perceived only as a cosmetic problem; obscures the causes of obesity.
- It does not elaborate the metabolic processes that cause obesity. Only obesity is perceived as a problem of carbohydrate (sugar) metabolism.Carbohydrate, fat and protein metabolism should be evaluated as a whole in the treatment of obesity.
- It ignores neurotransmitters that determine appetite and appetite-mood relationship. Trying to lose weight without controlling appetite or ensuring a favorable mood is reversed at the torture and the smallest break.
- When I say calorie restriction, essential essences (amino acids, vitamins and minerals, fatty acids) must be restricted. As a result, the balance of all enzymes, neurotransmitters and hormones changes and deteriorates.
HOW IS OBESITY DEVELOPED? Transformation of the yemen, a normal and necessary action, to the disease-making process People's eating and drinking move through two different pathways 3 .
1. Homeostatic pathway
Homeostasis is a physiological response that balances vital elements so that living things can survive. For example, when we are cold, trembling and sweating in the heat provide the heat balance of the body. When blood sugar rises, insulin increases, and when it falls, glucagon elevation balances blood glucose levels that are vital for erythrocytes and the brain.
Living things have to be fed for two reasons:
- To provide materials that are necessary for life but can not be produced by the body (amino acids, some fatty acids, vitamins, minerals, water).
- In order to be able to move and to energize the necessary energy for the organs to work
Unhealthy feeding of the person is attempted to be avoided by energy imbalance or homeostatic mechanism which is deficient in basic foods. However, when the homeostatic mechanism is subjected to prolonged unhealthy nutrition, normal functioning begins to harm. Because homeostatic pathway deficiencies (essentials and energy) are attempted to cope with an increase in the process of destruction called catabolism or by continuous eating . The excess energy is stored in the body in the form of a mass of fat that can be stored in the body at least with weight and with the most energy.
The homeostatic pathway is based on the body energy balance and is associated with the regular operation of two hormones called Lepthin, Ghrelin which gives a "eat" signal to stabilize the energy and "birth" signal. Ghrelin is released from the midline, leptin fat tissue. The role of insulin and glucagon hormones is to adjust the blood level. When sugar rises, it falls through insulin. It increases due to Glucagon when the sugar level falls 3.
In the simplest terms, weight gain and obesity are caused by the fact that the energy received is long-lived and energy-intensive. The most important reason for the widespread use of obesity is the consumption of more energy-intensive foods than those containing the necessary ingredients for the body.
2. Hedonic path (pleasure and pleasure)
The most important difference in the way people feed on animals is that they can be eaten for pleasure or pleasure, even if it is imperative. The most basic determinant of the hedonic path is taste. Enjoyed foods are flavor-focused, but the socio-cultural environment (economic status, beliefs) and lifestyle are also influential and different for everyone. However, it is a fact that the vast majority of obese or weight-related people are addicted to carbohydrates. Especially because the simple sugars that simple carbohydrates provide to the body stimulate the areas where addictive substances such as cannabis and heroin are targeted. For this reason, many people enjoy more sugar-containing foods. Nowadays, foods are the easiest foods that can be reached easily and contain high sugar and fat; the consumption of natural proteins and vegetables containing elements such as vitamins, minerals, and amino acids for the body has decreased.The proteins contained in most ready-made foods and fast foods are far from being quality protein sources due to industrial processes and cooking processes.
When the micronutrients (amino acids, vitamins, minerals, essential fatty acids) needed by the cells are not retrieved due to the poor eating style (high carbohydrate, trans fat) from the nutritive elements, the body sends "eat" signals to meet this compulsory need and the person goes on searching for food. The person with the freedom to choose food will prefer the food they will enjoy most in this case, especially the carbohydrate-containing foods. Thus, because of the need for addictive and arbitrary reasons, as well as the micro nutrients of metabolism, the person is constantly involved. In other words, the signals given to meet the micro nutrient requirement lead the person to high nutrient-poor foods again due to the hedonic mechanism. This situation is similar to a thirsty person drinking different drinks such as tea, cola, fruit juice every time instead of drinking water. So hundreds of calories are taken for the need to be solved with a glass of water.
FEED OF THE UNEMPLOYED ENERGY AND MICROBESIN (homeostatic route), FEEDING AND ADDICTION (hedonistic route) Causes Excessive Diet.
HEDONISTRY ROUTE AND ESTABLISHMENT MECHANISMS HUMAN EVERY DAEM
The crucial thing is that this extraordinary system is able to turn us into a form of stronger physical and psychological struggle in hunger, disease, and illness.
The only culprit in weight gain is not the increased nutritional value of low carbohydrate and trans fat consumption. WHICH IF HEALTHY EVERYTHING IS EVERYWEIGHT, THEY COULD MAKE COVERAGE THROUGH AMOUNT.
WHAT IS YOUR HEALTHY GENERAL, WHAT HAPPENED
It affects the KILOMUZU . One of the reasons for unsuccessful diets is that this condition is ignored.
Although addiction in food dependence is classified as a psychiatric disorder, food dependence and nutritional dependence should be considered separately from each other5-6. Flavor enhancing substances such as sugar, fat and salt can create food dependence. It is known that sugar cane uses the same way as cannabis. However, eating and drinking habits are common without a special food orientation.
For a person who is nervous and angry at the time of opening, but after a satisfying and calm sense, your eating, especially the sugary food, is beyond being food. This undoubtedly surpasses satiation and is an indication of an addiction you are not aware of. Well, you can not open it, it is not you anymore. The food industry has already solved this trick for its own benefit. We will also shed light on why we should not be fed from now on, unless we know why we are not, when our hunger changes our mood.
There are many different pathways to reach happiness and pleasure in our minds and they all adapt according to our lifestyle (sleeping, getting up, loving, loving, belief, eating and drinking etc.) and environmental factors (climate, sun, stress). All human functions (movement, feeling, learning, remembering, judging, seeing, pain, etc.) are controlled by specialized regions in the brain. Happiness or pleasure center also has a specialized zone. Nucleus accumbens is the center of the reward system of the brain and wants to be rewarded consistently.
Brain functions are governed by chemicals called neurotransmitters. Serotonin, dopamine, glutamate, GABA, and morphine, which are produced by the body themselves, are neurotransmitters that are effective at the prize-winning center of happiness. Dopamine controls feelings about feeling good. This is a feeling of well being
FIGURE 42. Localization of the nucleus accumbens in the brain 7
dopaminin is the result of interaction with other brain biochemicals such as serotonin, endorphin. For example, low serotonin causes depression, while increased endorphin causes a good feeling. The increase of neurotransmitters, the decline of the neurotransmitters, the nudges, the mizacin, the behaviors of the people that are in certain equilibria.
DOPAMIN AS THE OBESEARS HAVE BEEN ADDED TO THE ADDENDA
REDUCTION IN THE RESPONSIBILITIES. For this reason, obese people tend to stimulate dopamine receptors with food. Delicious foods and addictive substances cause sudden dopamine increases in the award center. Volkow and colleagues have shown that sudden increases in dopamine in individuals predisposed to addiction completely suppress homomostatic mechanisms. Brain imaging methods have shown that food and substance dependence show similar neurological functional disorders [8].
Animal and human experiments have proven that delicious food triggers reward centers such as cocaine and heroin. Delicious foods are defined as SUGAR, SALT AND OIL RATE high foods. The reward signal generated by these foods continues to eat, delighting beyond the signal that the tokens give 9,10,11. It should not be forgotten that the salt also affects dopamine receptors, such as sugar, even though sugar has been at the forefront of food dependence12 . Many people who are suffering from weight problems are wondering why they do not gain weight or not gain weight if they do not have sugar on their mouths.
When we think that ghrelin and leptin hormones are effective on dopamine, it can be understood that the elements that balance the energy level are at the same time intertwined with the pleasure states3.
The stimulating effect of food, especially sugar, on the reward center was similarly observed in other addicts. In short, excessive eating passion, substance abuse, alcohol dependence,
gambling addiction, exercise addiction, internet addiction and sex addiction are all caused by an effort to satisfy this reward mechanism.
When we evaluate all this, the easiest way for everyone to satisfy the award center is to offer plenty of sugar to this region.
The natural end result of plenty of sugar or excessive fat is weight gain and obesity. The most important outcome here is that eating or food dependency is walking through the same mechanism as alcohol and substance dependence.
For this reason, it is necessary to treat obesity treatment as substance addiction treatment. THE MOST EASY JOURNEY TO LOWER YOU. THEY ARE A SIMPLE SOLUTION TO MOVE AND MUCH MORE MINUTES. ANYWHERE THEY WEAK GROWS.
How difficult it is for someone to eat less. Because obese people are mostly food addicts. A dependent person may take a break from the item he or she wants to get rid of, but the brain chemicals that are changing and disorienting cause the person to go back to eating such a meal that the result is the same and usually more weight recovery within a year9,13.
KEEPING THE CHEMICALS TO THE BALANCE TO THE BALANCE FUNCTIONS TO CREATE A PERMANENT CLEAN CONTROL BASIS.
Neurotransmitters (dopamine, serotonin, GABA, epinephrine, norepinephrine etc.) that control brain functions are all physiological, mental activity, nutrition, hormone, etc. it remains at a certain level, affected by many factors. Neurotransmitters must be present in the body sufficiently to protect the equilibrium in all conditions (anger, sadness, joy, physical factors). SINGLE SOURCE REQUIRED FOR PRODUCING NEURROT-RANSMITTER OF THE BODY AMINO
ACTIVE . Drugs do not increase the amount of neurotransmitter; (synapses) to the extent that they exist.
For this reason, we need to supply enough amino acid in our body so that the brain can synthesize the neurotransmitter it needs.
STRESS IF YOU ARE GOING UNDERWEAR FOODSTUFFS First of all, psychological stress does not affect the search for flavor as it increases the incidence of eating in many people. When the stress hormonal effect is examined, it increases the amount of Ghrelin, and "Leptin reduces the hormone".
Stress-induced over-eating is often used by the body to please itself. Tryptophan is known for the synthesis of serotonin, known as the hormone of happiness, and tyrosine is essential for the synthesis of dopamine, which gives a feeling of well-being, pleasure and pleasure. Thyrozine and tryptophan are crossed to the dopamine / norepinephrine
and to be serotonin more stable than other amino acids. Rapidly rising sugar and subsequent insulin elevation when carbohydrates are taken allows the tyrosine and tryptophan to enter the muscle, which blocks the passage of the amino acid (BCAA) into the brain. Tryptophan and tyrosine, which are increasing in proportion, rapidly migrate to the brain and more Serotonin and Dopamine can be synthesized.
This is the attack of the first biscuit or chocolate that someone sees when angry or stressed. Or the person who does not sleep at night gets up and attacks a jar of rice, jam or nutella jar for a saucepan, and Triptofan is quickly transferred to the serotonine and melatonin. Melatonin, the next step in the serotonin, is the sleep hormone.
In fact, exercise similarly increases the incidence of Tryptophan and Tyrosine in brain tissue. Exercise BCAA competes with tryptophan to increase the intracellular penetration of amino acids, and the blood level of tryptophan is relatively high. Many of these people feel happy during the sport.When the concentration of tryptophan in brain tissue increases too much, this is the cause of fatigue.
AMINO ACIDS ROLE IN OBESITY TREATMENT
Amino acids are effective at every step of the treatment of obesity.
AMINE ACID ANALYSIS BENEFITS IN OBESITY TREATMENT
- Detects metabolic processes causing obesity in detail.
- It gives information about the neurotransmitters that determine our appetite and mood. It examines the blood levels of amino acids, neurotransmitters (dopamine, adrenaline, noradrenaline, serotonin), and blood lead levels.
- Determines the need for amino acids, vitamins and minerals that must be taken as a compulsory.
- Amino acid analysis provides information about intestinal flora by measuring metabolites produced by bacteria.
FREE AMINO ACID SUPPORT WITH KIRO CONTROL AND OBESITY TREATMENT The only way to reduce the daily amount of energy is to reduce the amount of energy. I have not forgotten that the only way to reduce energy is to burn more energy. However, it is necessary to make a clear fact. EXERCISE TO EXCHANGE WITHOUT THE EARTHQUAKE, IT IS NOT POSSIBLE TO GIVE LIGHTS WITHOUT EXERCISING REDUCING THE FOOD.
Two slices (100 g) are required to walk at medium speed for one hour to consume 450 calories to make the cake. Do not go out of the way here and it does not matter if it is trivial or not done. Moving beyond calorie burning has many regulatory effects on the bowel, muscle, brain, mitochondria, and many other metabolic processes at the cellular level. Indexing exercises just to spend calories is the most important mistake made in the weight-loss process. Calories will be inflicted with the understanding made exercise the same diet as he- yec it to start, a time after boring not to and to the left is doomed.
Exercise when many features, such as time, type, severity, are personalized:
Determining which energy source the metabolism will use Adjust bowel permeability
Increase muscle mass Increase fat breakdown
Prevent and relieve depression Increase metabolic rate
and regulate many metabolic functions15. It is very surprising
that exercise, which regulates dozens of different mechanisms in the process of weight loss and weight control, is reduced to the calorie expenditure function which is inadequate to lose weight . The essence is that you just can not afford to lose weight if you are doing sports! The main purpose of weight loss is to reduce the fat mass, but at least 25% of the skeletal muscle is lost during weight loss. In particular, it is the most important cause of extreme lacerations and inability to lose weight after a period of loss of mothers' pauperism. Because of the loss of muscle, there are negative changes in the metabolic rate and the cycle of protein production-destruction 16-19. In such a case , with approaches such as METABOLISMIZE ASSUMPTION (?) , Weighting the diet or increasing the exercise will cause further destruction of the muscle mass. Such a weight loss program does not have a chance to drive for a couple of months. THE ONLY WAY OF PROTECTION PROVIDES SUPERIOR AMINO ACID PURIFICATION DURING DIET. MUCH LESS FURTHER MAKE SIGNIFICANCE FOR WEAKNESSING THE MORE THAN THE PERSON WHO MUCH MORE LIKE, BUT WHAT CAN I CONTINUE TO GIVE MORE LESS THAN A HUMAN MORE THAN MORE? Amino acid analysis determines the levels of amino acids, vitamins and minerals that are required to be taken, ie what is missing, what is missing in terms of micronutrients in the body of the person who wants to weaken. It also examines the balance of biochemicals that control appetite. Amino acids, vitamins, minerals and probiotic requirements are determined according to analytical needs. Supports prepared in this way are shown in Figure 43. Equilibrium of free amino acid support or protein-rich metabolic effects 20 (UCP, uncoupling protein, mTOR, mammalian target of rapamycin) neurotransmitters and intestinal secretions controls appetite. The person just starts to eat as much as he needs, the interest of the food that is dependent is reduced, he loses by itself. When we lose weight, the muscle mass loss that we do not desire is reduced to a minimum. It is even possible to increase muscle mass with appropriate support. When this treatment protocol is applied, the given doses do not cause metabolic problems, there is no will to fight due to decreased appetite, fatigue and depressive mood do not occur. HOW FREE AMINO ACID SUPPORT TREATS OBESITY AND RELATED DISEASES?
- Proteins are the most long-lasting food. Free amino acids send both satiety-suppressing signals and suppress the appetite over neurotransmitters. Thus reducing food intake20.
- Free amino acids increase UCP (uncoupling proteins) in mitochondria, brown fat tissue and subcutaneous white fat tissue (grayish adipocytes). UCPs energize energy by increasing heat rather than producing energy (ATP). Leptin, adrenaline, thyroid hormone UCPs increase 20.
- When amino acids are metabolized in the body, high energy is consumed. This ratio is 0-3% for fats, 5-10% for carbohydrates and 20-30% for proteins. In other words, at least 20% of the energy from the proteins we eat is already used for protein metabolism. This is the thermal effect of the protein . The most important part of the work is the thermal effect of each protein is different from the other. The amino acids in the protein's composition determine the ratio of this thermal effect. The amino acid composition of protein-containing foods is different 21 .
The amount of energy that each Amino Acid diffuses into 1 mole of ATP is constant. For example, 153 kJ (36 kcal) / ATP is spent for cysteine whereas 99 kJ (23 kcal) / ATP is consumed for glutamic acid. Essential amino acids have more thermal effects than non-essential amino acids. Therefore, animal proteins rich in essential amino acids consume more energy than non-essential amino acids rich in plant proteins 22 .
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- Protein weighted diet and free amino acids stimulate fat burning for the body's energy needs. Reduces fat mass and helps balance blood oil20.
- It increases muscle protein synthesis through free amino acids and even the leucine mTOR molecule alone, and reduces muscle destruction. As a result, it increases muscle mass23,24. Increasing effect of amino acids on muscle mass is explained in the chapter "FOOD SUPPORTS".
- Amino acid supplement stimulates both insulin secretion and facilitates the use of glucose by the musculoskeletal and liver. Thus, free amino acids regulate the blood sugar level20 .
EFFECTIVE EFFECTS OF INSUFFICIENT QUANTITY OR LOW LOW CALCARIAN DIET A meal is definitely a weight loss, but such a diet has two consequences.
- When the amount of food decreases, the need for increased vitamins, minerals and amino acids adversely affects all systems, especially weakness of the immune system and malaise.
- Rapid and negative changes in neurotransmitters make the person stressful, angry and unhappy. These diets, which are made without appetite control, make the person to consume more food and drink soon after the effects of the brain biomaterials.
The first priority for breaking the vicious circle in diets should be to provide the micro nutrients that are constantly needed and diminished in the body. When the needs of the person are precisely identified and met appropriately, they do not feel constantly hungry. Obese people are carbohydrates and food addicts. The dependent person may give a break for some time to get rid of the substance, but in this process the brain chemicals, which are at the bottom of the balance, push the person to such a diet that the result is that they return mostly more often within one year at the latest.
PERMANENTLY WEIGHT CONTROL MULTIMEDIATE MANAGER Keeping the chemicals that carry out brain functions as the basis for weight loss is the basis for sustained weight loss. When the levels of amino acids are determined and replaced, the reward center will not give a "reward me" signal to warn you accordingly. This means that neurotransmitters need to be synthesized easily and excessive appetite suppression.
Reducing the amount of food to lose weight, restriction of carbohydrates, but only when the neurotransmitter balance is achieved at the same time does not lead to willfulness and does not turn into a disturbance.
Should OBESITY TEND ONLY ONE PURCHASE LABEL? If the obese person is able to lose enough weight, a very important step is taken for the current health.However, the reasons that make a person obese are also the reasons why he or she will have diabetes, high blood pressure or heart disease. Insulin resistance, little work of the adrenal glands, little work of the thyroid gland are just a few of these reasons.
It is imperative to investigate the underlying causes in the person who is focused on weight loss. Current surveys are positive if the disease has occurred in the person. For example, if the thyroid hormone is reduced, the blood supply is very clear. However, the tests will be normal if the problems do not affect the hormone levels. Amino acid analysis reveals obesity-related conditions, such as insulin resistance, diabetes, and hypothyroidism, as a very early risk even if there is no problem in current surveys. For example, insulin resistance can provide information about 6 years for resistance development and 12 years for development of diabetes25,26. Determining the risks in advance ensures that the nutrition needs to be done and that the treatments and supports needed to remove the risks are properly organized. For example, the building block of thyroid hormone is named amino acid of tyrosine. Tyrosine can only be found in the body in sufficient quantities by food intake of its own or Phenylalanine named amino acid. The risk of hypothyroidism in a person with low blood levels of tyrosine and phenylalanine is unavoidable. The usual dose of Tyrosine or Phenylalanine supplementation makes it easy to lose weight.
When properly supplemented, amino acids offer versatile treatment for obesity, not only through appetite and addiction, but also against physical and psychological causes such as insulin resistance, hypothyroidism, catecholamine depletion (adrenaline, noradrenaline) and depressive moods that lead to obesity.
FREE AMINO ACID SUPPORT
- Controls appetite by balancing neurotransmitter and intestinal secretions 10,11,13. The interest in the dependent food disappears.
- Normally, muscle loss due to diabetes does not occur because of the amino acid tag. Conversely, appropriate amino acids increase muscle mass 16, 24 .
- All the essential amino acids needed by the body are healthier and more energetic than the one needed by the individual 21, 22, 24.
- Insulin resistance, hypothyroidism, depression, and stress, both making the obesity groundbreaking and making it difficult to lose weight, are both treated and controlled 20,21.
REFERENCES:
- Overweight and Obesity Statistics 04-4158 Updated October 2012
- Satman I. TURDEP-II Study Group. Twelve-year trends in prevalence and risk factors of diabetes and prediabetes in Turkish adults. Eur J Epidemiol. 2013 Feb; 28 (2): 169-80.
- Lutter M. Homeostatic and hedonic signals interact in the regulation of food intake . J Nutr. 2009 Mar; 139 (3): 629-32.
- Lieberman M. Marks' Basic Medical Biochemistry Fourth, North American Edition Lippincott Williams & Wilkins 2013
- Hebebrand J. "Eating addiction", rather than "food addiction", better captures addictive-like eating behavior. Neurosci Biobehav Rev. 2014 Nov; 47: 295-306
- Albayrak Ö. Food addiction - substance use disorder or behavioral addiction? Z Kinder Jugendps- ychiatr Psychother. 2015 May; 43 (3): 173-81
- Nora D. Volkow. Presentation on theme: "NATIONAL INSTITUTE ON DRUG ABUSE NIDA NIA- AA National Institute Alcohol Abuse and Alcoholism.National Institute on Drug Abuse
- Volkow ND. Obesity and addiction: neurobiological overlaps . Obes Rev. 2013 Jan; 14 (1): 2-18.
- Blum K. Dopamine Genetics and Function in Food and Substance Abuse . J Genet Syndr Gene Ther. 2013 Feb 10; 4 (121).
- Volkow ND. Reward, dopamine and the control of food intake: implications for obesity . Trends Cogn Sci. 2011 Jan; 15 (1): 37-46.
- Lenoir M. Intense sweetness surpasses cocaine rew d. PLoS One. 2007 Aug 1; 2 (8): e698.
- Cocores JA. The Salted Food Addiction Hypothesis may explain overeating and the obesity epidemic. Med Hypotheses. Dec 2009 73 (6): 892-9.
- Lindblom J. Increased mRNA levels of tyrosine hydroxylase and dopamine transporter in the VTA of male rats after chronicfood restriction. Eur J Neurosci. 2006 Jan; 23 (1): 180-6. Dieting as a strategy to reduce body weight often fails as it causes food cravings leading to bingeing and weight regain.
- Takahashi K. Imaging the passionate stage of romantic love by dopamine dynamics . Front Hum Neurosci. 2015 Apr 9; 9: 191.
- Physical Activity Guidelines Advisory Committee report, 2008. To the Secretary of Health and Human Services. Part A: executive summary. Nutr Rev.2009 Feb; 67 (2): 114-20.
- Pasiakos SM. Effects of high-protein diets on fat mass and muscle protein synthesis on follo- wing weight loss: a randomized control trial .FASEB J. 2013 Sep; 27 (9): 3837-47.
- Ebbeling CB. Effects of dietary composition on energy expenditure during weight-loss maintenance . JAMA. June 27, 307 (24): 2627-34.
- Ravussin E. Reduced rate of energy expenditure as a risk factor for body-weight gain . N Engl J Med. 1988 Feb 25; 318 (8): 467-72.
- Stein TP. Effect of reduced dietary intake on energy expenditure, protein turnover and glucose cycling in man . Metabolism. 1991 May; 40 (5): 478-83.
- Klaus J. Petzke. Beyond the Role of Dietary Protein and Amino Acids in the Prevention of Diet- Induced Obesity. Int. J. Mol. Sci. 2014, 15, 1374-1391
- MS Westerterp-Plantenga. Dietary protein, metabolism, and body-weight regulation: dose- response effects. International Journal of Obesity. (2006)30, S16-S23.
- van Milgen J. Modeling biochemical aspects of energy metabolism in mammals . J Nutr. 2002 Oct; 132 (10): 3195-202.
- Hay N. Upstream and downstream of mTOR. Genes Dev. 2004 Aug 15; 18 (16): 1926-45.
- Layman DK. Defining meal requirements for protein to optimize metabolic roles of ami- no acids . Am J Clin Nutr. 2015 Apr 29
- Mc Cormack SE. Circulating branched-chain amino acids are associated with obesity and future insulin resistancein children and adolescents .Pediatric Obes. 2013 Feb; 8 (1): 52-
Elevated levels of circulating BCAAs are significantly associated with obesity in children and adolescents, and may predict future insulin resistance.
- Wang TJ. Metabolite profiles and the risk of developing diabetes. Nat Med. 2011 Apr; 17 (4): 448-
A combination of three amino acids predicted future diabetes (with a more than fivefold hig- each risk for individuals in top quartile). The results were replicated in an independent, prospective cohort. These findings underscore the potential role of amino acid metabolism in the early stages of diabetes and suggest that amino acid profiles could aid in diabetes risk as- sessment .
Sarcopenia: Muscle Loss
THE MOST IMPORTANT FEATURE WHICH ARE ELDERLY OR NEEDED TO BE A KAS KITTLES AND QUALITY. We have to know that we will age even if we live with zero errors. It is the different processes of old age that we have to distinguish at this point. The most important element that a person can intervene is an elderly, frowned and diseased life or a healthy life with high quality of life.
The person who is moving, exercising and eating well is only old; the person suffering from muscle loss due to inactivity and malnutrition is quickly condemned to old age.
When we look at the human life, we see that it reaches 120 years. So, as a species, one has a genetic structure that will live 120 years or more.
So why is it that many people can not reach this age when they are allowed to live for 120 years or why is everyone's lifetime different?
Genes and environmental factors are determinants of life span. Genes determine the age limits of a specific species. For example, the mouse has 3 years and the chimpanzee has a maximum of 60 years. Gene polymorphism (changes) has a life-time contribution of 20-30% 1. In this case, the most important factor affecting the life span is environmental effects and lifestyle. Along with nutrition, habits (smoking, alcohol) and movement that come to mind first when lifestyle is mentioned, living environment and medical interventions are the main determinants of life span.
- As long as people live in an environment protected from danger (protection from infections, vaccinations, hygienic environments, appropriate climatic conditions, etc.)
- As appropriate medical interventions are made against health problems
- As you reach adequate food sources
- As long as it moves, life span increases.
Aging individuals have special structural and functional changes in aging. The aging process is at a different rate depending on the factors that are exposed to each person.
Systems become corrupted as you age2:
- Body composition changes: muscle mass decreases, fat mass increases.
- Skin: Collagen production is reduced.
- Musculoskeletal system: Muscle destruction, bone loss.
- Gastrointesitnal system: The bowel system ages, its functions deteriorate.
- Vision, hearing functions decrease, may deteriorate.
- Nervous system perception and skill level decreases.
- Endocrine and reproductive system: Hormone levels change, menopause develops in women. Reproductive ability continues in males, but functional deficiency develops.
- Cardiovascular system: Cardiovascular diseases are the primary cause of death.
FIGURE 44. Body composition changing with age 3
Muscle fat rate changes during aging process. With age, both visceral (internal organ) and subcutaneous and intramuscular fat accumulation increase; insulin resistance develops. Research in recent years reports that changes in muscle mitochondria are effective in all these processes. Changes in mitochondrial activity in the elderly lead to increased fat, increased oxidative stress and decreased glucose tolerance, even if the person is not obese4,5.
SARCOPENI: It is SARCOPENI to decrease muscle mass and function in aging process. From the age of 30, muscle mass and strength begin to decrease. Next
the loss lasts 3-8% every 10 years, further deterioration in later ages. Aging itself causes sarcoma, but chronic diseases, malnutrition and inactivity increase the severity of sarcoma. Increased muscle loss and muscle strength increase the risk of fainting and mortality in the elderly4,5,6.
FIGURE 45. Age-related sarcopenia and accelerating factors 6
Muscle protein loss, muscle balance between destruction and muscle destruction, is caused by increased destruction. However, although aging increases the destruction process and makes it easier to reduce the construction process, this depends entirely on how the person lives. A physically inactive life and malnutrition accelerate muscle loss6.
FIGURE 46. Muscle kinetics, nutrition, movement and disease relation 7
CHARACTERISTICS = CHRONIC EXERCISE DEFICIENCY + CHRONIC NUTRITION DEFICIENCY In addition to muscle loss, the number and function of mitochondria in muscle cells decrease. For this reason, muscle cells produce less energy and muscle weakness develops. Antioxidant activity decreases in muscle against free radicals, oxidative stress increases 4,5.
With aging
- Muscle weight and muscle function are reduced.
- The number of mitochondria decreases, their functions deteriorate.
- Oxidative stress increases, antioxidant capacity decreases.
FIGURE 47. Changes to the aging intestine are possible to improve or reduce the effects of these changes as they age 5
.
- Resistance exercises and amino acid supplementation increase muscle mass and strength.
There are hundreds of clinical trials that show that essential amino acids increase muscle mass, muscle strength, walking and workability in the elderly, and reduce the risk of illness. The most important reason for the high level of work carried out on this subject is the rapid increase in the elderly population in developed societies and the
are the costs caused by health problems. It is among the priorities that the elderly should be able to act independently and to maintain high quality of life. For thisreason , it is the most effective way to combat sickness in preventing or eliminating many problems related to old age . The most successful method of this challenge is the appropriate exercise and nutritional model or support that will not leave essential amino acids 9,10 .
Inactivity (immobility) is the most important factor that accelerates muscle loss in the elderly. Unfortunately, the elderly can be restricted due to the illness, or the age when they are dependent on the bed. In such cases, essential amino acid supplementation is the only effective and safe option for the prevention of muscle loss in the elderly11,12,13,14 .
Especially in patients with paralysis, essential amino acid therapy should be given to prevent muscle loss. The exercise of patients with chronic heart failure and chronic obstructive pulmonary disease (COPD) is challenging and daily activities are very limited. They get tired quickly, they have trouble breathing. For this reason, it is difficult for them to overcome the exercise. Even though exercise therapy is very important in both diseases, the number of patients who can receive and receive this rehabilitation is very low.
Chronic heart failure given 8 grams of free essential amino acid support for 3 months and the exercise capacity of COPD patients increased significantly. On the other hand, in patients unable to exercise, amino acid supplementation gave equivalent results to exercise therapy. So far the results have been summarized as "Rehabilitation without Rehabilitation" in one article15. See. Table 5.
Table 5. "Rehabilitation without rehabilitation" Exercise and Essential Effect of Amino Acid Support 15
Exercise therapy
EAA support
Exercise capacity
Max O2 uptake (oxygen use)
Increases
Increases
6 min. Walking distance
Increases
Increases
Anaerobic threshold
Increases
Increases
Max Exercise duration
Increases
Increases
Resting ejection fraction
Slight increase
Significantly slight increase
Resting Lactate production
Unspecified
decreased
Muscle structure and function (animal experiment)
Muscle cross-sectional area
Increases
Increases
Muscle fiber thickness
Increases
Increases
Type I fiber count
Increases
Increases
Number of mitochondria
Increases
Increases
Muscle dynamic force
Increases
Increases
Muscle fatigue
decreases
decreases
2. Amino acid supplement increases the number and function of mitochondria in the skeleton and heart. The most important cause of the disease is the decrease in the number of mitochondria in the muscles. Amino acid support directly affects the number of mitochondria. Animal studies have shown an increase in the number of mitochondria by 31% in the skeleton and 40% in the heart by amino acid supplementation. Mitochondrial volume increased by 28% 16,17,18.
3. Amino acid supplement reduces oxidative stress and inflammation. Free amino acid support reduces blood levels of inflammation markers such as IL-6, IL-10 and TNF-alpha. The body's most potent antioxidant, the glutathione, is produced by the body itself from amino acids. However, with many factors, prolonged blood glucose levels cause a decrease in glutathione levels and increased tissue damage due to oxidative stress. Supplementing amino acids, the building blocks of glutathione, increases glutathione synthesis and reduces oxidative stress and damage caused by hyperglycemia17,18,19,20.
SPECIFIC AMINO ACID SUPPORTS EXCEPTIONAL ASPECTS AND EXPENSIVE HEALTHY LIFE EXPECTATIONS.
- Essential amino acid supplement increases muscle mass in the elderly 8-14, 21,22,23 .
- Essential amino acid support shortens the time elderly are dependent on the bed 10-14 .
- Amino acid supplementation increases quality of life in the elderly and heart patients 10,24,25 .
- Amino acid supplementation reduced the rate of infection in the elderly 26 .
- Amino acid support protects the heart 27 .
- Amino acid supplementation lowers cholesterol, triglyceride levels. Prevents fatty liver 28 .
- Amino acid supplementation does not impair kidney function in the elderly 29 .
- Essential amino acid supplement reduces insulin resistance, regulates blood flow 30,31 .
- The effects of branched-chain amino acids (BCAAs) on different breeds and cultures (Asian and European populations) have been investigated and it has been reported that middle-aged people who consume high amounts of BCAA have a lower risk of obesity [ 32] .
The field of medicine that prolongs human life and enhances quality of life: Dentistry
In my opinion, no progress in medicine has affected the average age of society as much as the improvements in Dentistry.
To survive and be healthy is to reach and benefit from the sources of essential nutrients. This is the most basic instinct of all living things.
If people lost their teeth and could not be replaced, the multitude of foods would not make any sense.
The ability to easily consume protein in advanced age is the secret of long life.
In order to live a long life with a high quality of life, everyone in the middle and advanced age should go to a nutrition model that will not lose essentialamino acids.
Life Extending Food: Yoghurt
One of the most talked about topics about staying healthy today is how intestinal microflora plays a decisive role.
This theory is not new, but developed 100 years ago by Russian scientist Élie Metchnikoff . Nobel Prize-winning Metchnikoff, the father of natural immunology, told 100 years ago that chronic diseases are caused by intestinal microflora and that microflora-regulating nutrition will prevent diseases and delay aging.
Yogurt and the Lactobacillus bulgaricus bacteria in it claimed that the drug to delay the aging by regulating the microflora is the bacteria . The concreteevidence of Metchnikoff was the Bulgarian and other Balkan peasants who lived for a hundred years at that time (early 1900s) and were eating yogurt .
Another scientist who uses the drug for intent is the Thessaloniki doctor Isak Carasso. Karasu, who immigrated to Barcelona during the Balkan War, prescribes probiotics and sells them as medicines to patients suffering from gastrointestinal problems known to the Balkans but not known to Western Europe. In 1919 he established the world famous yogurt brand, Danone, whose son gave his name .
Apart from the probiotic properties of kneading , the most important feature that prolongs life and makes people healthy is full food . There is no other foodcontaining amino acids, vitamins, minerals and fats that are perfectly balanced and contain plenty of water and probiotic . Modern medicine has proven theeffectiveness of yogurt and dairy products in reducing cardiovascular disease with clinical trials 35 .
When Metchnikoff lived (1845-1916) If we thought that the dentist did not develop and that everybody lost their old age and lost their lives due to malnutrition, the Balkan villagers could live for many years thanks to yoghurt, which probably does not need healthy teeth .
143
REFERENCES:
- VB Hjelmborg J. Genetic influence on human lifespan and longevity . Hum Genet. 2006 Apr; 119 (3): 312-21.
- Richard W. Besdine. Pharmacokinetics and Drug Interactions in the Elderly Workshop . Washington DC, National Academy Press, 1997, pp. 8-9. I www.merckmanuals.co
- http://learning.hccs.edu/faculty/deborah.mcginty/psyc2314/chapter-18
- Johannsen DL. Ectopic lipid accumulation and reduced glucose tolerance in elderly adults are accompanied by altered skeletal muscle mitochondrial activity . J Clin Endocrinol Metab. 2012 Jan; 97 (1): 242-50.
- Peterson CM. Skeletal muscle mitochondria and aging: a review. J Aging Res. 2012; 2012: 194 821. Muscle mitochondria are thought to play a primary role in this process. Mitochondria are the major producers of reactive oxygen species, which damage DNA, proteins, and lipids if not rapidly quenched.
- English KL. Protecting muscle mass and function in older adults during bed rest. Curr Opin Clin Nutr Metab Care. 2010 Jan; 13 (1): 34-9.
- Evelyn B. 'Sarcobesity': A metabolic conundrum. Maturitas. 74 (2013) 109-113
- Cruz-Jentoft AJ. Prevalence of and intervention for sarcopenia in aging adults: a systematic review. Report of the International Sarcopenia Initiative (EWGSOP and IWGS). Age Age- ing. 2014 Nov; 43 (6): 748-59.
b- methylbutyric acid (HMB) supplements, show some effects in improving muscle mass and function parameters. Protein supplements have not shown consistent muscle mass and function.
Physicians should screen for sarcopenia in both community and geriatric settings, with diagnosis based on muscle mass and function. Supervised resistance exercise is recommended for individuals with sarco-penia. EAA (with leucine) and HMB may improve muscle outcomes.
- Kim HK. Effects of exercise and amino acid supplementation on body composition and physician function in community-dwelling elderly Japanese sarcopenic women: a randomized controlled trial . J Am Geriatr Soc. 2012 Jan; 60 (1): 16-23.
- Rondanelli M. Effect of essential amino acid supplementation on quality of life, amino acid profile and strength in institutionalized elderly patients. Clin Nutr. 2011 Oct; 30 (5): 571-7 .
Oral supplementation with essential amino acids improves the quality of life in insulin-dependent elderly patients, including depressive symptoms, nutrition, muscle function and daily life activity.
- Ferrando AA. EAA supplementation to increase nitrogen intake improves muscle function du- ring bed rest in the elderly . Clin Nutr. 2010 Feb; 29 (1): 18-23.
- Brooks N. Resistance training and timed essential amino acids protect against the loss of muscle mass and strength during 28 days of bed rest and energy deficit . J Appl Physiol. 2008 Jul; 105 (1): 241-8.
- Paddon-Jones D. Amino acid supplementation for reversing bed rest and steroid myopathies . J
- Drummond MJ. Bed rest impairs skeletal muscle amino acid transporter expression, mTORC1 signaling, and protein synthesis in response to essential amino acids . Am J Physiol Endocrinol Metab. May 15, 302 (9): E1113-22.
- Aquilani R. Essential amino acids and exercise tolerance in elderly muscle-depleted subjects with chronic diseases: a rehabilitation without rehabilitation? Biomed Res Int. 2014; 2014: 341603. Exercise intolerance remains problematic in subjects with chronic heart failure (CHF) and / or chronic obstructive pulmonary disease (COPD). Recent studies show that supplementary essential amino acids (EAAs) may exert beneficial effects on CHF / COPD physical capacitances. Supplemented EAAs can improve the physical autonomy of subjects with CHF / COPD.
- Valerio A. Branched-chain amino acids, mitochondrial biogenesis, and healthspan: an evoluti- onary perspective . Aging (Albany NY). May May; 3 (5): 464-78.
- D' Antona G. Branched-chain amino acid supplementation promotes survival and supports car- diac and skeletal muscle mitochondrial biogenesis in middle-aged mice . Cell Metab. 2010 Oct 6; 12 (4): 362-72.
- Nisoli E. Amino acids and mitochondrial biogenesis. Am J Cardiol. Jun Jun; 101 (11A): 22E-25E. Mitochondria are sources of energy production through their role in the production of adenosine triphosphate for cell metabolism. Defective mitochondrial biogenesis and function play in the pathophysiology of related diseases, including obesity, diabetes mellitus, myopathies, and neurodegenerative diseases. Here, we suggest that some types of nutrients, including specific amino acids, may improve mitochondrial biogenesis and energy production in energy-defective conditions by increasing endothelial NO synthase expression .
- Sekhar RV. Glutathione synthesis is diminished in patients with uncontrolled diabetes and restored by dietary supplementation with cysteine and glycine. Diabetes Care. 2011 Jan; 34 (1): 162-7. Patients with uncontrolled type 2 diabetes have severely deficient synthesis of glutathione attributed to limited precursor availability. Dietary supplementation with GSH precursor amino acids can restore GSH synthesis and lower oxidative stress and oxidant damage in the face of persistent hyperglycemia.
- Manders RJ. Insulinotropic and muscle protein synthetic effects of branched-chain amino acids: potential therapy for type 2 diabetes and sarcopenia . Nutrients. Nov 8; 4 (11): 1664-78 .
- Henderson GC. Potential application of essential amino Acid supplementation to treat sar- copenia in elderly people. J Clin Endocrinol Metab.May 2009; 94 (5): 1524-6.
- Cuthbertson D. Anabolic signaling deficits underlie amino acid resistance of wasting, aging muscle. FASEB J. 2005 Mar; 19 (3): 422-4.
- Dillon EL. Amino acid supplementation increases lean body mass, basal muscle protein synthesis, and insulin-like growth factor-I expression in older women. J Clin Endocrinol Me- tab. May 2009; 94 (5): 1630-7.
- Aquilani R. Oral amino acid supplements improve exercise capacities in elderly patients with chronic heart failure. Am J Cardiol. 2008; 101: 104a-110a
- Scognamiglio R. Impairment in walking capacity and myocardial function in the elderly: is the role of nonpharmacologic therapy with nutritional amino acid supplements? Am J Cardiol. 2008; 101: 78E-81E
- Aquilani R. Effects of oral amino acid supplementation on long-term-care-acquired infections in elderly patients. Arch Gerontol Geriatr. 2011; 52: e123-128
- Drake KJ. Amino acids as metabolic substrates during cardiac ischemia . Exp Biol Med (Maywod ). Dec 237 (12): 1369-78.
- Børsheim E. Amino acid supplementation reduced plasma and liver triacylglycerols in elderly.
Diet supplementation with AAs lowers plasma TG, total cholesterol, and very low-density lipoprotein cholesterol concentrations and liver lipid content in impaired glucose tolerant elderly. AAsupplementation may have a potential role in the treatment of hypertriglyceridemia or hepatic steatosis.
- Bauer J. Evidence-based recommendations for optimal dietary protein intake in older people: a position paper from the PROT-AGE Study Group. J Am Med Dir Assoc. 2013 Aug; 14 (8): 542
- Solerte SB. Improvement of blood glucose control and insulin sensitivity during a long-term (60 weeks) randomized study with amino acid dietary supplements in elderly subjects with type 2 diabetes mellitus. Am J Cardiol. 2008; 101: 82a-88a
- Solerte SB. Nutritional supplements with oral amino acid increase the whole-body lean mass and insulin sensitivity in elderly subjects with sarcopenia . Am J Cardiol. 2008; 101: 69E-77E
- Qin LQ. the INTERMAP Cooperative Research Group. Higher branched-chain amino acid residues are associated with a lower prevalence of obesity in middle-aged East Asian and Western adults. J Nutr. 2011; 141: 249-254
- Mackowiak PA. Recycling metchnikoff: probiotics, the intestinal microbiome and the quest for long life. Front Public Health. 2013 Nov 13; 1:52.
- http://www.danone.com/en/for-all/history/#timeline-1919
- Astrup A. Yogurt and dairy product consumption to prevent cardiometabolic diseases: epide- miologic and experimentalstudies. Am J Clin Nutr.2014 May; 99 (5 Suppl): 1235S-42S.
Apart from sending valuable dairy nutrients, yogurt may also exert beneficial probiotic effects. In this paper, we propose a new method to reduce the risk of fatigue and improve the quality of yogurt .
Free article
We are aware of the signs that our age is progressing, usually aesthetically beginning to disturb us. Wrinkles deepening at the edges of the eye, brown stains on the face and hands, starting to lose tension in the skin and sagging are the most obvious signs. Unfortunately, as our age progresses, health problems begin to increase.
However, what we need to know is that the signs of old age relate to how we live physically and spiritually from years on . For this reason, it is possible to assume that one of the two 50-year-olds is 35 years old and the other is 65 years old, and I am sure that you are often amazed at age and image in your daily life.
In fact, today's conditions present two distinct effects together. Surrounded rapidly by pollution from one side, there are living spaces away from nature and the most harmful forms of feeding; and what you do is impossible to be totally abstract. On the other hand, medicine is rapidly developing, surgical and medical treatments, and even some cosmetics are freezing people. This is why anti-aging is the most popular concept in the last thirty years.
While the concept of anti-aging tries to prevent the present appearance from moving to older ages, the aesthetic and cosmetic procedures we practice today, the correct reinforcements take your present age back almost 20 years. So anti-aging is missing. That's why you will begin to hear the concept of Reverse Aging .
As I mentioned at the beginning, it would be wrong to perceive aging only on aesthetic image. The most important are health problems that increase with age. It is also important how good our mental and physical functions are, how good and energetic we feel, how good and young we look. Eyes tired, depressive attitude and burnout can never coincide with youth when there is no wrinkle on the skin. Apply as many anti-aging as you want, you can not go beyond being other inside.Ideally, whatever your age is, you can be healthy and energetic, and you can remove signs of aging depending on your preferences.
More importantly, measures need to be taken before these symptoms occur. Thus, you will be able to protect both your health and your youthful appearance. For this purpose, external interventions should be supported by internal therapies.
They constitute treatments to replace the bases of internal supports and often contain essential ingredients. In other words, it is necessary to substitute the substances that are necessary to take with food (minerals, vitamins, essential fatty acids and essential amino acids) to the extent that they are missing.
For example, for a skin that starts to wrinkle rapidly and begins to sag, no aesthetic intervention from the outside can produce sufficient collagen production. Our collagenous body mainly produces Glycine, Proline, Hydroxyproline and Hydroxysine from the so-called amino acids and produces some vitamin C and some minerals. Without sufficient raw material in the body, external interventions do not give good results or the results are short-lived.
To summarize, in addition to external interventions in the Reverse Aging protocol, internal support is provided to reverse both psychological and physical signs of aging. For this reason, except for the popular discourse IN and OUT, the treatment approach is Reverse Ageing IN , Anti-Aging OUT (external support).
Free article
Skin wrinkles are at the head of cosmetic problems, which are the most striking and eye-catching, and most aggravated by aging. When our skin is younger or older than our current age, even if genetic factors are effective, our life style, that is, the environmental factors, is the determining factor in the world.
For example, a skin that is prone to premature aging can look younger than its chronological age when looked at well. On the contrary, skin with good geneticity can be aged prematurely, even with sun and scrotum exposure alone. A good look at all health issues is a more effective way to treat.
To look good is to protect from the sun, to moisturize, to sleep well, to less exposure to polluted air and to good nutrition.
A number of methods are proposed for the treatment of skin wrinkles and the three main objectives are considered at the basis of treatment:
- Filling wrinkles with filling materials
- Reduce wrinkles that cause wrinkles
- To force the skin to increase its collagen production, which decreases over time. For this purpose, it is tried to stimulate the production of collagen by applying laser, radio frequency, ultrasonic waves to the skin, or by direct mechanical damage.
Collagen is the most abundant protein produced by the body and consists mainly of amino acids named Glycine, Proline, Hydrociproline and Hydroxylysine. In addition, growth hormone for this complex mechanism, amino acids such as arginine, leucine and glutamine for genetic coding are needed. Vitamin C is essential for these materials to be available even if they are available. From here we can get our nutrition message: To get the necessary amino acids, meat, milk, eggs are okay, but they must be consumed together with the vegetables that provide the vitamins needed for their work.
A study published in Aesthetic Plastic Surgery 2013 Apr; 37 (2): 424-33 gave very important messages and changed our point of view in the right direction. In this study, 33 women aged 43-62 with the same wrinkles on their faces were separated into four different treatment groups.
- Gruba Fractional Laser
- Gruba IPL (Intense Pulse Light)
- Gruba cream containing retinoic acid
- Gruba is supported by amino acids and vitamins.
IPL, retinoic acid cream, and amino acid showed a statistically significant decrease in wrinkle score, but no significant improvement in laser treatment.
Patients' treatment satisfaction was similar in the 4 treatments but the highest satisfaction was seen in the group using amino acids.
As a result, the end result of four different treatments is close to mutual benefit. Amino acid supplementation is very practical and achievable when treatment with laser, IPL, and retinoic acid cream is considered pain, redness, burn, sun exposure.
At least, whatever treatment is done on the skin, it is the point that adding amino acids together will increase the success even further.
AMINO ACID ANALYSIS IN CANCER SCREENING AND DIAGNOSIS The cause of high mortality (morbidity) and mortality (complex disease) due to the complex structure and lack of adequate markers for early detection1.
Early diagnosis for several different types of cancer is a prerequisite for successful treatment. Because of this, studies conducted for early detection are constantly being investigated from genetic analysis to metabolic analyzes and advanced imaging methods. In recent years, the most promising data on the early detection of cancer comes from the science of Aminoscience.
Due to the metabolic changes observed in cancer patients there are differences except for the expected levels of blood amino acid levels. As I mentioned earlier, the blood levels of amino acids are in the range of certain values, just like in glucose, vitamins and minerals. The blood levels of these substances, which are directly related to feeding, are affected both by the way they are fed and by the metabolic processes independently of the feeding. Increased cellular activity in cancer patients directly affects the use and metabolism of amino acids. Clinical trials have shown that formulas obtained from amino acid analysis may be early markers for cancer, as well as diabetes, insulin resistance, liver fibrosis2,3,4,5,6,7,8,9,10,11,12,13,14, 15,16,17,18,19.
In clinical trials conducted in Japan, amino acid analyzes of blood samples from cancer patients and healthy persons were compared. In the study, four times more healthy individuals were examined for each of the 200 cancer cases, 199 stomach cancer, 199 colon cancer, 198 breast cancer and 134 prostate cancer patients. Although the knowledge obtained from the examination of hundreds of metabolites up to now and from the genetic analysis has not yielded very satisfactory results for cancer screening and early detection, it has been shown that AMINO ACID ANALYSIS IN A SINGLE BLOOD EXAMINES LOOKING FOR DIAGNOSTIC AND EARLY DIAGNOSIS OF LUNG, STOMACH, COLUMN, BREAST AND PROSTATE CANCER COULD BE USABLE 2.
Existing studies have shown that amino acids can easily be studied for uterine, ovarian and pancreatic cancers, as well as these five cancer types,
. It is emphasized that amo acid indices in endometrium cancer are superior to CA1253,4,5.
Today, cancer of the pancreas can unfortunately be diagnosed at a very late stage, and so it is advanced when diagnosed. It has been shown that amino acid indices differ significantly between patients with pancreatic cancer and healthy controls, which may be a marker for screening and diagnosis of pancreatic cancer4.
AMINO ACID SUPPORT FOR CANCER PATIENTS
Amino acid supplementation improves treatment success by reducing complications of disease and chemotherapy in cancer patients.
malnutrition observed in patients with anemia affects the course of the illness negatively. Weight loss is caused both by the disease itself and by the treatments given. Improving nutritional status in cancer patients can alter disease course and improve quality of life20.
Excessive weakness in cancer patients is called CASHEX. Approximately 80% of advanced cancer patients develop cachexia. CANCER DISEASES
30% of the deaths are mushy 20,21.
Cachexia is different from the normal weight loss process and the cancerous fat mass
85%, 75% of the muscle mass. This massive loss of muscle mass affects the metabolic processes and immune system in the negative, especially the movement system. Patients quiesce, impair their quality of life and shorten their life span. Due to weakening and loss of respiratory muscles, respiratory failure is the cause of death in 48% of cancer patients22,23.
Standard cancer treatments aim to reduce the tumor volume and prevent its progression. However, it is necessary to take additional precautions and treatments against cachectic, which is seen in 80% of cancer patients and is deadly. Supplementation of nutritional supplements suitable for malnourished cancer patients with malnutrition can reduce complications, increase chemotherapy tolerance or provide better response, shorten hospitalization, and contribute to the prolongation of the life span.
Therefore, the nutritional model that confronts the cachexia should be included in the treatment of cancer alone, not as palliative or secondary treatment. The muscle mass is entirely of amino acids. The only way to counteract severe catabolism in the cachexia process is to apply a nutritional model that provides more essential amino acid support and to act if possible.
It is obvious that proper support and exercise can be initiated before exposure to cachexia in cancer patients24.
The fact that classical nutritional supplements are not sufficient for protein formation in advanced-stage cancer patients suggests that the anabolic response decreases. It is very important, however, to be able to generate anabolic responses to prevent the metabolic disturbances that develop in the muscles and the end result. ESSENTIAL AMINO ACIDS THAT CAN PROVIDE ANALYTICAL RESPONSES IN ELDERLY AND DYNAMIC PATIENTS ARE ANSWERED IN THE TREATMENT OF ADVANCED CANCER 25,26.
According to clinical trial data 20, 26, 27:
- The anabolic response, that is, all essential amino acids must be given in doses sufficient to raise the level of leucine to stop muscle destruction and increase production.
- Glutamine supplementation reduces the toxic effect of chemotherapy on tissues.
- BCAAs reduce morbidity and improve quality of life.
- Arginine supplementation can reduce the frequency of complications and prolong life span.
REFERENCES:
- Tan HT. Cancer proteomics. Mass Spectrom Rev. Sep-Oct; 31 (5): 583-605.
- Miyagi Y. Plasma free amino acid profiling of five types of cancer patients and their applicati- on for early detection. PLoS One. 2011; 6 (9): e24143.
- Miyagi E. Diagnostic Performance and Clinical Utility of Novel Gynecologic Cancer Screening Method Based on "AminoIndex Technology".Official Journal of Japan Society of Ningen Dock Vol. 26 (2011) No. 5 Ningen Dock P 749-755
- Fukutake N. A Novel Multivariate Index for Pancreatic Cancer Detection Based on the Plasma Free Amino Acid Profile. PLoS One. 2015 Jul 2; 10 (7): e0132223.
- Ihata Y. Amino acid profile index for early detection of endometrial cancer: verification as a novel diagnostic marker. Int J Clin Oncol. 2014 Apr; 19 (2): 364-72.
- Shingyoji M. The significance and robustness of a plasma-free amino acid (PFAA) profile-based multiplex function for detecting lung cancer.BMC Cancer. 2013 Feb 15; 13: 77.
a low physical burden on subjects, has great potential for improving early detection of lung cancer.
- Yatabe J. Early detection of colon cancer by amino acid profiling using AminoIndex Technology: a case report. Diagn Pathol. 2013 Dec 10; 8: 203.
- Deng K. High levels of aromatic amino acids in gastric juice during the early stages of gastric cancer progression. PLoS One. 2012; 7 (11): e49434.
- Zhao Q. Plasma and tissue free amino acid profiles and their concentrations correlated with lung cancer. Asia Pac J Clin Nutr. 2014; 23 (3): 429-36.
- Ma H. Plasma free amino acid profiling of esophageal cancer using high-performance liqu id chromatographyspectroscopy. World J Gastroenterol. 2014 Jul 14; 20 (26): 8653-9.
- Xu J. Global and targeted metabolomics of esophageal squamous cell carcinoma discovers diagnostic and therapeutic biomarkers. Mol Cell Proteomics. May 2013; 12 (5): 1306-18.
- Cascino A. Plasma amino acid imbalance in patients with lung and breast cancer . Anticancer Res. 1995; 15: 507-510.
- Heber D. Metabolic abnormalities in the cancer patient . Cancer. 1985; 55: 225 229.
- Kubota A. Amino acid profiles correlate diagnostically with organ sites in three kinds of malig- nant tumors. Cancer. 1992; 69: 2343-2348.
- Lai HS. Plasma free amino acid profile in cancer patients. Seminar Cancer Biol. 2005; 15: 267-276.
- Norton JA. Fasting plasma amino acid levels in cancer patients. Cancer. 1985; 56: 1181-1186.
- Proenza AM. Breast and lung cancer are associated with a decrease in blood cell amino acid content . J Nutr Biochem. 2003; 14: 133-138.
- Maeda J. Possibility of multivariate function of plasma amino acid profiles as a novel screening index for non-small cell lung cancer: a case control study. BMC Cancer. 10: 690.
- Vissers YL. Plasma arginine concentrations are reduced in cancer patients: evidence for arginine deficiency? Am J Clin Nutr. 2005; 81: 1142-1146.
- Paccagnella A. Nutritional intervention for improving treatment tolerance in cancer patients . Curr Opin Oncol. 2011 Jul; 23 (4): 322-30.
Oral supplementation with branched amino acid appears to reduce the length of hospital stay, decrease morbidity and improve quality of life, without any changes in mortality. Perioperative supplementation with arginine has shown a reduced incidence of complications and a significant increase in long-term survival.
- Campos-Ferraz PL. An overview of amines as nutritional supplements to counteract can- cer cachexia. J Cachexia Sarcopenia Muscle. 2014 Jun; 5 (2): 105-10.
- Tisdale MJ. Mechanisms of cancer cachexia. Physiol Rev. 2009 Apr; 89 (2): 381-410.
- Biolo G. Muscle contractile and metabolic dysfunction is a common feature of sarcopenia of aging and chronic diseases: from sarcopenic obesity to cachexia . Clin Nutr. 2014 Oct; 33 (5): 737-48 .
- Demoor-Goldschmidt C. How can we integrate nutritional support in medical oncology? Bull Cancer. 2009 Jun; 96 (6): 665-75.
- Engelen MP. High anabolic potential of essential amino acid mixtures in advanced nonsmall cell lung cancer. Ann Oncol. 2015 Sep; 26 (9): 1960-6.
- Deutz NE. Muscle protein synthesis in cancer patients can be stimulated with a specially formulated medical food. Clin Nutr. Dec 30 (6): 759-68.
- Chevalier S. Do patients with advanced cancer have any potential for protein anabolism in response to amino acid therapy? Curr Opin Clin Nutr Metab Care. 2014 May; 17 (3): 213-8.
The Effect of Amino Acids on Behavior and Mood
Neurotransmitters are biochemicals that provide communication between the brain and the body. The brain uses neurotransmitters when it manages heartbeat, breathing, digestion, thinking, memory, emotion, sleep, in short, all body functions.
Neurotransmitters are present in the vesicles in the extensions of the neurons (nerve cells), and the nerves communicate through this chemistry [1].
NEUROTRANSMITTERS MESSAGE CARRIERS BETWEEN THE IMMUNE SYSTEM, ENDOCRINE SYSTEM, DIGESTION SYSTEM AND NERVOUS SYSTEM. FIGURE 48. Neurotransmitters and neural communication 2
Neurotransmitters are nervous system stimulant (excitator) or sedative (inhibitor) is characteristic. For this reason, the level in blood or tissues affects all emotions and behaviors1.
Neurotransmitters play a role in all functions or diseases such as stress, anxiety, affect, depression, irritability, anger, panic attacks, concentration problems, memory, sleep, headache, weight control, appetite, addictions, libido and digestive problems.
FIGURE 49. Effect of neurotransmitters on mood and behavior 1,3
All Neurotransmitters Occur by Amino Acids or Amino Acids 1,4
FIGURE 50. Neurotransmitter precursor amino acids 1,4
- Neurotransmitters-serotonin Tryptophan, which has a decisive role in mood and behavior; Dopamine, Norepinephrine (noradrenaline) and Epinephrine (adrenaline) are the named amino acids of tyrosine.
- Morphine-like Endorphin, Enkafaline etc. all other neurotransmitters are peptides consisting of a combination of several amino acids.
- Some amino acids directly act as neurotransmitters in the brain itself.
- glycine
- Glutamic acid
- Aspartic acid
- Taurine
Factors affecting neurotransmitter levels: nutrition, chronic stress, neurotoxins, drugs and genetics.
- Malnutrition, especially with stress, is inevitable in the nervous system. Because the only source of neurotransmitters is AMI-NO-ASYLTER, it is essential.
- Physical or psychological stresses such as infections, trauma, intense exercise, work pressure, sadness reduce the level of neurotransmitters due to overuse.
- Neurotoxins: Alcohol, cigarettes, caffeine, chemical treatment, drugs, heavy metals, some foods, food additives, some substances in cosmetics, etc.
- Enzymes that play a role in genetically neurotransmitter metabolism may be inadequate or overactive.
However, it is possible to measure the level of amino acids, the sole source of neurotransmitters, in blood, urine, brain secretions, or tissues. That's why amo acid analysis reveals to us the cause of our mood and behavior biochemically. If the level of Tryptophan or Tyrosine is low or the excretion is high, the amount of serotonin, dopamine will decrease. Reduction, proliferation or alteration of amino acids reveals the current psychological state and informs about the risks that may arise in the future.
Clinical trials have shown that amino acid changes in blood levels in the following cases5-12.
- Depression
- Anxiety
- Chronic fatigue
- Attention deficit / Hyperactivity
- anorexia
- Overeating
- Parkinson's
- Restless leg syndrome
- Alzheimer's
- Autism
- Substance dependency / Sugar dependency
- Sleep problems
- Libido reduction
- Menopause troubles
AMINO ACID ANALYSIS CAN BE USED FOR PRE-DIAGNOSIS OF EARLY DIAGNOSIS AND RISKS OF PSYCHOLOGICAL AND NEUROLOGICAL DISEASES.
FREE AMINO ACID SUPPORT CAN BE USED FOR TREATMENT .
EFFECTS OF FREE AMINO ACID SUPPORT
Table 6. Clinical effects of precursor amino acids 5
Supported Amino Acid
Converted Neurotransmitter
Neurotransmitter function
Problems with amino acid deficiency
Dependencies visible in the absence
Expected effect on amino acid support
L-Tryptophan
serotonin
Low self confidence
Candy
Antidepressant effect
Obsessive compulsive
Alcohol
Solves the answer
failure
Unrest
Starch
insomnia
Sleep problems
counteract
Night snacks
ecstasy
Appetite control
Carbohydrate starvation
Marijuana
In case of emotion
Hot intolerance
Chocolate
improvement
Premenstrual syndrome
Tobacco
Fibromyalgia, Depression
Table 6. Clinical effects of precursor amino acids 5 (Continued)
Supported Conversion Neurotransmitter Amino Acid Neurotrans-function
mitter Problems with amino acid deficiency
Dependencies visible in the absence
Expected effect on amino acid support
L-Phenylalanine Dopamine Motivation, request
Caffeine
Prize center
L-Tyrosine Norepinephrine focus, attention,
Cocaine
excitation
memory, positive stress
Marijuana
Do not clear
(love, exercise, sex)
aspartame
Antidepressant effect
At low levels:
Chocolate
Do not be energetic
Addiction disorders
Alcohol
Mental focus
Concentration
Tobacco
increase
disorder
Candy
Low energy
Starch
Loss of motivation,
Overeating
Depression
Gambling
Focus difficulty
Chronic fatigue
Difficulty in weight loss
Lack of award
syndrome
Higher levels:
Digestive system
issues
Autism
Distraction
Psychosis
Temperament change
Anxiety
Sleeping disorders
L-Glutamine Glutamic acid Stress
GABA Emotional state change Hypoglycemia
Sweet Starch Alcohol
Stress Reducing Stress Relief Energy source for the brain
Emotion regulator
Arranges blood sugar
GABA GABA Calmness, relaxation,
I diazepam
Sedative
Gamma- Gamma- focusing
Alcohol
Relaxing
amino amino Low levels:
Marijuana
bitumaric acid) bituminous acid) Anxiety
Tobacco
Fear
Dessert
Lack of trust
Unrest
Insomnia
Panic
Tension
Table 6. Clinical effects of precursor amino acids 5 (Continued)
Supported Amino Acid
Converted Neurotransmitter
Neurotransmitter function
Problems with amino acid deficiency
Dependencies visible in the absence
Expected effect on amino acid support
DL
endorphin
Physical and psychological
Heroin
Prize center
phenylalanine
enkephalin
pain, wellness, pleasure
Alcohol
excitation
related to
Marijuana
Do not clear
At low levels:
Candy
Mild antidepressant
Sentimentality,
Starch
Satisfaction increase
Lack of sense
Chocolate
Pain reliever
I can not enjoy,
Tobacco
lovelessness
For certain foods or medicines
excessive desire
It should be noted in Table 6 that this lack of neurotransmitter precursor amino acids is inadequate, which unfortunately increases the addictive potency to higher levels. Because the only way a substance can affect the central nervous system is to be able to change the neurotransmitters. If a substance can raise GABA, it has a sedative effect; If norepinephrine can increase dopamine, attention may increase concentration; if it stimulates endorphin, it creates a state of greatness.
THE EFFECTIVENESS WAYS OF THE MOST NUROTRANSMITTERIN CAN BE BEEN CALLED BY SUGAR, TUTUNE AND ALCOHOL. ONLY THIS TABLE PUT YOUR OBESITY, ALCOHOL AND TOBACCO DEPENDENCE 6,7.
When efforts are made to get rid of all of these substance dependencies, appropriate amino acid supplements may relieve or completely abolish the withdrawal syndrome caused by substance dependence. For this reason, addictive treatment centers in developed countries benefit more from these supports. Amino acid supplements should be used to treat the addiction, as well as to remove the substances from the body and repair the damage they give 8 .
class = Section196>
Why are we more sweet in the winter?
Increased melatonin in winter reduces the amount of serotonin. The body needs more Tryptophan to increase the level of serotonin. Tryptophan and branched-chain amino acids use the same carrier system as they pass through the canine brain tissue. That is, when they pass through the brain tissue, they compete and the more the concentration goes, the more passes.
Insulin-stimulated and branched chain amino acids are sent into the muscle and this change in blood level causes Tryptophan and Tyrosine to rapidly migrate to the brain tissue.
Stress and sorrowful moments, this is the reason for the sweets and chocolates. Sweets that increase insulin quickly give instant happiness and relaxation. In the winter, more dessert is consumed, more weight is taken 13 .
High protein foods (eg meats) reduce the ratio of Tryptophan / LNAA. Because the percentage of Tryptophan in high protein foods is 1-2%, the ratio of LNAA (leucine, isoleucine, valine, phenylalanine, tyrosine) is 25% 14 .
The ratio of Tryptophan in the milk is relatively high. The fact that when taken together with sugar, honey, or a small crack that will increase insulin, this is the cause of relaxation, happiness and sleepiness.
POTENTIAL SUPPORT IN PSYCHIATRIC DISEASES
Table 7. Nutritional support in psychiatric disorders
Disease
Probable Disease Reason
Treatment
Major Depression
Serotonin deficiency
Tryptophan 15, 16
Dopamine / norepinephrine deficiency
Tyrosine 17,18,19
GABA deficiency
GABA20
Omega-3 deficiency
Omega-321
Folic acid / vitamin deficiency
Folic acid / B vitamins22,23
Magnesium deficiency
Magnezyum25
SAM lack
SAM26
Bipolar disorder
Acetylcholine receptor abundance
Lithium and Taurin27
Vanadium excess
Vitamin C28
Folic acid / vitamin deficiency
Folic acid / B vitamins29,30
Lack of tryptophan
Triptofan31
Choline deficiency
Lesitin32
Omega 3 deficiency
Omega 333,34
Schizophrenia
Problem of serotonin synthesis Glycine deficiency
Omega 3 deficiency
Tryptophan 35 Glycine 36, 37, 38
Omega 339-42
Obsessive compulsive disorder
hypericin
Hypericin (St John's Wort) 43, 44
Scientific data have shown that appropriate nutritional supplements are useful in the treatment of major depression, bipolar disorder, schizophrenia, anxiety disorders, eating disorders, attention deficit hyperactivity, and autism11,16-44.
Sickness / Stress Causes Illness Tyrosine and Phenylalanine are known as stress amino acids. Phenylalanine can be converted to tyrosine in the body. Tyrosine use increases when stress increases. Dopamine and norepinephrine synthase are reduced from the emotional determinants when sufficient tyrosine can not be obtained by feeding.
Long-term sadness will lead to rapid depletion of neurotransmitters and ultimately to diseases. For example, reduction of tyrosine and tryptophan does not only cause psychological problems. Because these amino acids, which are reduced by chronic stress, are protein building blocks if not properly fed, the synthesis of enzymes, hormones, and repair of tissues will eventually come into the field.
FIG. 51. Tyrosine metabolism
In such a situation, it is inevitable that all kinds of physical diseases are predisposed to stress when neurotransmitters are consumed and nutrition can not provide adequate support.
Patient Man Causes Depressive Bacteria and viruses that cause infections use amino acids that break down the cells they have set up to survive. Thus, in all infections, the catabolic process becomes active and tissue destruction increases. Fever accelerates metabolism. As a result,
the amount of no acid is reduced especially Tryptophan and Tyrosine. Fatigue and depression develop depending on how much of these two norepinephrine -induced amino acids are reduced . The increase in degradation products as well as the decrease in tryptophan (quininerenine) leads to depressive effect. This is also a natural defensive mechanism. If we were depressed when we were sick and were at home rather than resting, we could do more damage to ourselves with the effect of weakening us.
MAJOR DEPRESSION Although the prevalence of major depression varies from country to country, the incidence is reported to be between 8% and 12% in the literature. A number of studies have shown that changes in blood levels of amino acids are predictors of neurotransmitter failure. For this reason, a biologic marker for the diagnosis of AMINO ACID ANALYSIS DEPRESSION is used as an early diagnostic tool for the next-generation depression9.
The reduction of amino acids used in the construction of neurotransmitters is just one of the causes of depression. The amount of neurotransmitter between the nerve cells may also be restricted due to the reduction of receptors. Currently, medical treatments to relieve neurotransmitter deficiency are the most commonly used depression treatment protocol15.
Neurotransmitter reuptake inhibitors do not increase the amount of monoamine neurotransmitters (serotonin, norepinephrine) in the nervous system; it allows to concentrate as much as possible in certain regions. INCREASING THE AMOUNT OF AMINO ACIDS THAT CREATE YOUR SELF-ONLY WAY TO INCREASE OR INCREASE THE NEUTROTRANS-MITTER QUANTITY4.
Side effects such as sedation, high blood pressure, weight loss and sexual health negatively affect the proper use of drugs and are the most important obstacles in the treatment of antidepressants. Another point to keep in mind is that reuptake inhibitors may develop deficiency in another neurotransmitter over time.Therefore, supplementation of neurotransmitter precursors as nutrients or supplements during the use of antidepressant drugs will minimize side effects and increase treatment success4,15.
MOVING ANTIDEPRESENTING We know that moving to depression is good and often our experience is in this direction. But we did not fully know the biochemical mechanism of why the movement was good for depression. In 2014, Swedish scientists have shown through their genetic and metabolic studies that they can actually treat depression in their work published in Cell magazine45.
FIG. 52. Mechanism of antidepressant action of movement 45
As summarized in the picture, Triptofan used in the synthesis of stress serotonin is rapidly destroyed. Tryptophan degradation product Kininurenin has a depressive effect on the brain through the blood-brain barrier. However, Kininurenini Kininucleic acid translating enzyme increases in the muscles when it is moved. Kininurenic acid can not pass through the brain and is easily removed from the urine. Just as the amino acid metabolism is endogenous and the toxic ammonia is converted into urea (not uric acid).
We can better understand why amino acid metabolism is so good for walking in open air (melatonin decreases, orexin and serotonin increase) and movement in sunny weather.
CHRONIC FATIGUE / BLEEDING SYNDROME IS NOT CHARACTERISTICS The most common problems among chronic fatigue syndrome patients. Very interestingly, most patients say they have my chronic fatigue or burnout syndrome at the outset. They are sure that they do not have any physical problems under their condition. Because almost all of the patients have gone through all kinds of check-ups, have done all their cancer screenings, heavy metal analyzes, and have not neglected to clear their intestines. Most of them are using different supplements (from Europe, from America) and at least one antidepressant. In this way, all the processes that I have had in my life when I have done the amino acid analysis of the diseases I have been questioning about how I missed it.
Chronic fatigue syndrome is described as an unrestrained clinical condition that is exacerbated by physical and mental activity that is indeed a medical cause.Fatigue, loss of concentration, forgetfulness, joints
pain, muscle aches, headache, persistent insomnia, even sore throat, and sometimes swelling in the lymph nodes (without infection). But the most obvious complaint is to feel exhausted even when it is resting. No assay performed will give an abnormal result or qualitatively explain the indication48,49.
However, in the majority of patients suffering from chronic fatigue syndrome, there are differences in the level of amino acids that are required. Generally, an increase in the ratio of tryptophan to brain amino acids (LNAA) is detected. That is, when the amount of tryptophan needed for the synthesis of serotonin in the brain is greatly increased, the breakdown product, quininurenine, causes "DEPRESSIVE AND TIRED HIS" SETTINGS 48,49.
As a result, CHRONIC FERTILITY SYNDROME IS A BIOLOGICAL ASSEMBLY AND THROUGH THIS BASIC AMINO ACID ANALYSIS ET-
MEK IS POSSIBLE . In some cases, further analysis of energy metabolism is needed.
to
B
FIG. 53 AB. The amino acid indices of chronic fatigue syndrome vary significantly 48
According to the amino acid analysis, when the specially prepared amino acid supplements are given together with vitamins and minerals, which are cofactors, the majority of patients are getting results in a short period of time. As noted in a clinical trial, 75% of 25 chronic fatigue patients who have been using their special supplements according to the amino acid analysis for three months have not fully recovered, only 10% have not recovered well [50].
AMINO ACID ANALYSIS AND PERSONAL AMINO ACID SUPPORTS AFFECT EFFICIENT TREATMENT OF CHRONIC FATIGUE TREATMENT.
Considering the general health effects of the individual-specific amino acid supplements, it is seen that in addition to chronic fatigue itself, it also targets the symptoms of the disease individually. Because free amino acid support has antioxidant, antidepressant, concentration enhancer, energy enhancer, sleep regulator, pain reliever, muscle mass and sports performance enhancing effects.
INTERESTING DEVELOPMENT: The US Institute of Medicine (IOM) institution changed the name of the disease to " Systemic Exertion Intolerance Disease" in 201549.
Perhaps intolerance may be a practical name. The implied intolerance word does not lead to the production of GAYRET INNOLOGICAL TESTS, inspired by the food intolerance tests without any validity ...
Mothers who live in depressed mothers, according to me, constitute the most deprived and unlucky part of all similar illnesses. Because there is hardly any awareness or knowledge of the community and young families about this post-natal development. In an environment of great love, such as birth, the mother is confronted with many problems that almost no one is aware of, while everyone is interested. The growing sadness, while experiencing the happiness of the baby, feeds the feeling of guilt towards the mother of the mother and improves the feeling of anxiety and worthlessness. In all these processes the mother often tries to get over it.
Lohusa blues (postpartum blues) give symptoms such as unstable mood, insomnia, restlessness, decreased appetite. It develops in the first week after birth and is quite common and is found in 70% of all new mothers. It is important to recognize and recognize the Lohusa soul because these mothers are then 4 times more likely to experience the Lohu depression (postpartum depression) and the intensity52.
The puerperium depression is a major depression after 4 weeks of birth and the risk of being seen within the first 3 months is reported as 13-19%. Dep-
he may have a severe condition such as sadness, fatigue, indifference, anger outbursts, feelings of guilt, anxiety, feeling of worthlessness, and even thought of suicide52,53.
In the days immediately after birth, the estrogen level decreases rapidly from 100 to 1000 times. During the first 5 days of the pancreas, Monoamine oxidase-A (MAO-A) enzyme, which performs serotonin, dopamine and norepinephrine destruction in the brain, begins to increase. Almost 70% of the anals live in puerile sadness, with a maximum on the fifth day52.
Rapid elevation of MAO-A enzyme results in serotonin, dopamine and norepinephrine spurs. In this case, the most needed food for your mother is serotonin and amino acids Tryptophan and Tyrosine which will increase dopamine synthesis.
FIGURE 54. A. Blood estrogen level, B. Kan MAO-A level in the first 5 days postpartum,
- Emotional exchange 52
FIND YOUR INNOVATIVE SOLUTION TO THIS PROBLEM: LOHUSALIK ŞERBETİ
It is known that this sherbet prepared in the first days of the puerperium calms the mother and is a relaxing effect. As I mentioned above in the section "why are we more sweet in the winter," the sugary foods that rapidly increase insulin enable the rapid transmission of Tryptophan and Tyrosine to the brain.
The traditional nutrition teaching, which I have often argued for correctness, is misleading as to how it should be fed together with being extremely correct that poultry should be fed more.
The pituitary gland given in the first week can be considered a genius solution for pooh sadness because of the increasing effect of Triptofan's brain conduction.However, it is obvious that the main purpose of the traditional approach is not the looseness of the loins but the proliferation of the loins that the baby needs.
ANNOUNCER MULTIMEDIA MULTIPLE BURNS WILL NOT INSTALL THE SHARBET OR OTHER CARBON HYDRASTS.
The nutritional needs of the mother who gave her milk increased by at least one and a half times compared to those who did not . The mother needs more proteins than ever to be able to secrete a single source of vital amino acids for the baby. While a daily protein requirement of an adult woman is 0.8 g / kg, this requirement is 1.1 g / kg in pregnancy and 1.3 g / kg in lactation. For example, a woman weighing 60 grams would need 46 grams of protein, while a woman weighing 78 grams would breastfeed. In other words, the milk mother should increase protein consumption by at least 60%. The need for vitamins and minerals (B6, B1, B3, Vit, zinc, manganese), which are cofactors of the amino acids in the breastfeeding mother, is also significantly increased53,54.
Table 8. Daily amino acid requirements of suckling mothers and an adult human 53
An adult human needs daily amino acid
Daily amino acid needs of your suckling mother
histidine
14 mg / kg
19 mg / kg
isoleucine
19 mg / kg
30 mg / kg
leucine
42 mg / kg
62 mg / kg
Lysine
38 mg / kg
52 mg / kg
Methionine + Cysteine
19 mg / kg
26 mg / kg
Phenylalanine + Tyrosine
33 mg / kg
51 mg / kg
Treo
20 mg / kg
30 mg / kg
tryptophan
5 mg / kg
9 mg / kg
the Governor
24 mg / kg
35 mg / kg
TWO DANGEROUS WAITING EXPOSURE:
- Puerperium depression
- Excess weight gain
As a result, either the mother is treated, or the baby remains in the mother's house.
The most effective way to prevent or treat depression that may develop during and after pregnancy is to regulate feeding. In cases where the neurotransmitters are rapidly declining, the blood levels of amino acids fall, and more importantly, when the need for amino acids increases by 60%, it is no doubt that the appropriate amino acid supplement will reduce the risk and severity of puerperal depression. Preventing and treating puerperal depression is not only necessary for maternal health, but will also allow the baby to be breastfed and healthy in relation to the mother55.
LOHUSANIN KILO PROBLEM
The breastfeeding mother tries to give the remaining weight from the pregnancy, but at the same time the need for nutrition is increased. It is not surprising that in the vast majority of women suffering from weight problems, the problem started after the birth.
Breastfeeding mothers will be able to obtain more nutrients with less food by increasing quality proteins rather than carbohydrates imposed by traditional knowledge. Short-term free amino acid supplementation, when necessary, will increase both milk secretion and weight loss as it will fully meet the increased need of the mother .
FREE AMINO ACID SUPPORT 52-55
- It relieves the puer sickness.
- It helps prevent and treat puerperium depression.
- It meets the amino acid requirement, which is increased by 60 % in suckling mothers .
- Food needs are met without any calories.
- Amino acids provide quick weight loss.
- It increases the physical and mental performance of the mother.
CAUTION Lack of hyperactivity disorder (ADHD) The incidence of attention deficit hyperactivity disorder in childhood
Reported as 5-7%. However, when we look at the sales figures of the drugs currently used for the treatment of this disease, it is not possible to be perceived as an avalanche of the disease. At least when I analyzed the patients who applied to me, I could see that 4-5 children on average in a 20-person class receive Ritalin, Concerta type drugs.
The production figures of medicines used in the treatment of ADHD clearly show how rapidly the disease has increased (?) Or how many more children are exposed to these medicines.
Studies investigating brain functions have identified structural and functional abnormalities in brain areas that carry out attention and motor activities in ADHD patients. These functions and pathways are mainly controlled by neurotransmitters called dopamine and norepinephrine. It is seen as the main cause of dopaminergic disease. On the other hand, it has been reported that the action routes of serotonin are also effective on dopamine57.
Drugs used to treat attention deficit hyperactivity (methylphenidate and amphetamine derivatives) act through neurotransmitters. As I mentioned earlier, these drugs increase the amount of neurotransmitters in the central nervous system
US Annual Production (kilogram)
FIGURE 55. Attention Deficit Hyperactivity Disorder The increase in the production of drugs 56
it does not change, it just changes the areas it focuses on. The ability to synthesize dopamine, norepinephrine and serotonin depends entirely on the presence of the amino acids they are on. The ability of both precursor amino acids (Tryptophan and Tyrosine) to cross into the bloodstream of the bloodstream is influenced by the balance of other amino acids (large neutral amino acids, LNAA) using the same transition doors. It is therefore clear that the nutritional model or supportive treatments that may balance blood ammonia levels will affect the nervous system and behavior.
It has been reported that re-uptake inhibitors prescribed for the treatment of depression are more effective at 7- 13% of the placebo than those of attention deficit hyperactivity drugs at the rate of 12-26% of the placebo. In other words, people who are treated for depression
87-93% of patients with ADHD and 74-88% of those with ADHD should not expect more results from the placebo. However, all patients may experience any side effects58.
Neurotransmitters are proteins that we take from foods, such as Tyrosine, Tryptophan, Glycine, Glutamine, Taurine and so on. amino acids. Feeding the brain with healthy proteins increases neurotransmitter production and reduces ADHD symptoms.
Dr. In a study by Mary Hinz, 85 attention-deficit hyperactivity patients between the ages of 4 and 18 were treated for 10 weeks with amino acids serotonin and dopamine precursor (Tryptophan, Tyrosine). 67% of patients reported significant improvement with only amino acid treatment. A statistically significant improvement was achieved in 77% of the patients in total with dose adjustments in children who had not recovered57.
AUTISM
Autism is a developmental disorder of the brain, usually diagnosed before three years of age. Significant features of the disease can be summarized as impairment of social interaction, deterioration of communication, repetitive stereotyped movements and speech.
In the development of the disease, polymorphisms were detected in a genetically disordered population, which is clearly defined as an interaction with other environmental factors. In children with genetic predisposition, environmental pollution, exposure to heavy metals, vitamins, mineral deficiencies, vaccinations, infections are among the causes of autism59.
Approximately 80% of autistic children have been identified for changes in amino acid levels in their blood analysis. Because the behavior is entirely influenced by neurotransmitters, the levels of amino acids that make up excitatory (stimulant) and inhibitory (sedative) neurotransmitters vary significantly from that of normal children in autistic children. In particular, stimulating amino acids are high, soothing amino acids are low 60,61,62.
Amino acid levels of autistic children differ from those of healthy children due to illness or nutritional problems. At any given time, these children's periodic amino acid analyzes and appropriate amino acid supplementation contribute to the physical and neurological development of children.
IMPORTANT DEVELOPMENT: A very promising study was published in 2012 in the Science magazine on the amino acid association of otizmin. All three branched-chain amino acids (leucine, isoleucine and valine) are metabolized by a common enzyme, Branched Chain Ketoacid Dehydrogenase Kinase (BCKDK).Studies in mice and blood analysis of autistic children have shown that the defect in this enzyme leads to a decrease in the level of branched-chain amino acids and to the development of autism.The great news is that the support of leucine, isoleucine and valine is proving to cause neurological problems related to enzyme deficiency in mice. The study group showed that amino acid supplement normalizes blood levels in autistic children with enzyme deficiency. For this reason, autism patients with BCKDK enzyme deficiency can be treated with the support of leucine, isoleucine and valine.
A similar follow-up amino acid study showed that treatment with amino acid levels of leucine, isoleucine and valine in autistic children with BCKDK enzyme deficiency improves amino acid levels, improves physical development and improves behavior 64.
ALZHEIMER
Along with aging, there is a decrease in cognitive functions that are controlled by neurotransmitters. The indices obtained from amino acid analyzes show differences in Alzheimer's disease, which is a significant risk for advancing ages, to healthy individuals. Studies report that specific changes in blood amino acid levels occur in the early stages of the disease. Follow-up of these amino acid indices is crucial to follow-up Alzheimer's disease65,66,67.
The index (TSM) obtained from the amino acids taurine, methionine and serine is very consistent and practically results following learning acuity, mental clarity and forgetfulness. Almost all of the amino acid studies showed a significant difference in the TSM ratio when compared to patients with impaired cognitive function in healthy subjects. The only biochemical supporter of forgetfulness in my advanced age patients is almost this index. The TSM rate is also a very good indicator of learning ability and mental clarity, and is directly proportional to the success of the school children 66.
Amino acid levels play a regulatory role in the synthesis of neurotransmitters. Nutritional changes and appropriate supports that may affect neurotransmitters may prevent disease progression, stop progression, and help improve symptoms68.
REFERENCES:
- Lieberman M. Marks' Basic Medical Biochemistry. Fourth, North American Edition Lippincott Williams & Wilkins 2013
- http://fibroenergy.com/brain-chemicals-neurotransmitters/
- It is http://www.macalester.edu/academics/psychology/whathap/ubnrp/meth08/biochemistry/neurotransmitt.
- Mr Hinze . Relative nutritional deficiencies associated with centrally acting monoamines. Int J Gen Med. 2012; 5: 413-30
- Blum K, J Ross . "Nutritional Gene Therapy: Natural Healing in Recovery. Counselor Magazine, January / February, 2001
- Nogueiras R. The opioid system and food intake: homeostatic and hedonic mechanisms. Obes Facts. 2012; 5 (2): 196-207.
- Volkow ND. Obesity and addiction: neurobiological overlaps. Obes Rev. 2013 Jan; 14 (1): 2-18.
- Ross, Julia. The Mood Cure: The 4-Step Program to Take Charge of Your Emotions-. Penguin Publishing Group. 2012
- Altamura C. Plasma concentrations of excitatory amino acids, serine, glycine, taurine and histidine in major depression . Eur Neuropsychopharmacol. 1995; 5 Suppl: 71-5.
- Mitani H. Correlation between plasma levels of glutamate, alanine and serine with severity of depression. Prog Neuropsychopharmacol Biol Psychiatry. 2006 Aug 30; 30 (6): 1155-8.
- Lakhan SE. Nutritional therapies for mental disorders. Nutr J. 2008 Jan 21; 7: 2.
- Ghanizadeh A. Increased glutamate and homocysteine and decreased glutamine levels in autism: a review and strategies for future studies of amino acids in autism . Dis Markers. 2013; 35 (5): 281-6
- Fadda F. Tryptophan-Free Diets: A Physiological Tool to Study Brain Serotonin Function. News
- Young SN. The role of serotonin in human mood and social interaction. Insight from altered tryptophan levels. Pharmacol Biochem Behav. 2002 Apr; 71 (4): 857-65.
- Ille R. "Add-On" -therapy with an individualized preparation of free amino acids for por- tients with a major depression. Eur Arch Psychiatry Clin Neurosci. 2007 Jun; 257 (4): 222-9.
- Buist R. The therapeutic predictability of tryptophan and tyrosine in the treatment of depression.
- Rot M. Social behavior and mood in everyday life: the effects of tryptophan in quarrelsome in- dividuals. J Psychiatry Neurosci. 2006, 31 (4): 253-262.
- Mc Lean A. The effects of tyrosine depletion in normal healthy volunteers: implications for unipolar depression. Psychopharmacology. 2004, 171 (3): 286-297
- Ruhé HG. Mood is indirectly related to serotonin, norepinephrine and dopamine levels in humans: a meta-analysis of monoamine depletion studies. Mol Psychiatry 2007, 12 (4): 331-359.
- Petty F. GABA and mood disorders: a brief review and hypothesis. J Affect Disord 1995. 34 (4): 275-281
- Adams PB. Arachidonic acid to eicosapentaenoic acid ratio in blood correlates positively with clinical symptoms of depression. Lipids. 1996, 31 (Suppl): S157-S161.
- Young SN. Folate and depression-a neglected problem. J Psychiatry Neurosci. 2007, 32 (2): 80-8
- Bell IR. B complex vitamin patterns in geriatric and young adult inpatients with major depressi- on. J Am Geriatr Soc. 1991, 39 (3): 252-257.
- Eby GA. Rapid recovery from major depression using magnesium treatment. Med Hypotheses. 2006, 67 (2): 362-370.
- DeLeo D. S-adenosylmethionine as an antidepressant: A double blind trial versus placebo. Curr Ther Res. 1987, 41 (6): 865-870.
- Sartori HE. Lithium orotate in the treatment of alcoholism and related conditions. Alcohol 1986,
- Naylor GJ. Vanadium: a possible aetiological factor in manic depressive illness. Psychol Med 1981,
- Hasanah CI. Reduced red-cell folate in mania. J Affect Disord 1997, 46: 95-99.
- Bell IR. Vitamin B12 and folate status in acute geropsychiatric inpatients: affective and cognitive characteristics of a vitamin nondeficient population. Biol Psychiatr 1990, 27 (2): 125-137.
- Green AR. The pharmacokinetics of oral L-tryptophan: effects of dose and concomitant pyridoxime , allopurinol or nicotinamide administration.Adv Biol Psychiatr 1983, 10: 67-81.
- Cohen BM. Lecithin in the treatment of mania: double-blind, placebo-controlled trials. Am J
- Stoll AL. Omega 3 fatty acids in bipolar disorder: a preliminary double-blind, placebo-controlled trial. Arch Gen Psychiatry 1999, 56 (5): 407-412.
- Frangou S. Efficacy of ethyl-eicosapentaenoic acid in bipolar depression: a randomized double- blind placebo-controlled study. Br J Psychiatry 2006, 188: 46-50.
- van der Heijden FM. Amino acids in schizophrenia: evidence for lower tryptophan availability during treatment with atypical antipsychotics?Journal of Neural Transmission 2005, 112 (4): 577-585.
- Javitt DC. Amelioration of negative symptoms in schizophrenia by glycine. Am J Psychiatry 1994,
- Leiderman E. Preliminary investigation of high-dose oral glycine on serum levels and negative symptoms in schizophrenia: an open-label trial.Biol Psychiatry 1996, 39 (3): 213-215.
- Javitt DC. Adjunctive high-dose glycine in the treatment of schizophrenia. Int J Neuropsychophar- macol 2001, 4 (4): 385-391.
- Peet M. International variations in the outcome of schizophrenia and the prevalence of depression in relation to national dietary practices: an ecological analysis. British Journal of Psychiatry 2004, 184: 404-408.
- Christensen O. Fat consumption and schizophrenia. Acta Psychiatr Scand 1988, 78 (5): 587-591.
- Peet M. Eicosapentaenoic acid in the treatment of schizophrenia and depression: rationale and preliminary doubleblind clinical trial results.Prostaglandins Leukot Essent Fatty Acids 2003, 69 (6): 477-485.
- Emsley R. Randomized, placebo-controlled study of ethyl-eicosapentaenoic acid as supplemental treatment in schizophrenia. Am J Psychiatry 2002, 159 (9): 1596-1598.
- Szegedi A. Acute treatment of moderate to severe depression with hypericum extract WS 5570 (St John's wort): randomized controlled double blind non-inferiority trial versus paroxetine. British Medical Journal. 2005, 330 (7494): 759.
- Fava M. A double-blind, randomized trial of St. John's wort, fluoxetine, and placebo in major depressive disorder. J Clin Psychopharmacol. 2005,25 (5): 441-447.
- Agudelo LZ. Skeletal muscle PGC-1-1 modulates kynurenine metabolism and mediates resilience to stress-induced depression Cell. 2014 Sep 25; 159 (1): 33-45
- Fukuda K. The Chronic Fatigue Syndrome Study: A comprehensive approach to its definition and study. International Chronic Fatigue Syndrome Study Group. Ann Intern Med. 1994, 121: 953-959.
- Werbach MR. Nutritional strategies for treating chronic fatigue syndrome. Altern Med Rev. 2000 Apr; 5 (2): 93-108.
- Georgiades E. Chronic fatigue syndrome: new evidence for a central fatigue disorder. Clin Sci (Lond). 2003 Aug; 105 (2): 213-8.
- Malhotra R. Tryptophan and Kynurenine Levels and Their Association with Sleep, Nonphysical Fatigue, and Depression in Chronic Hemodialysis Patients. J Ren Nutr. 2017 Mar 30 pii: S1051-22276 (17) 30053-5.
- Bralley JA. Treatment of chronic fatigue syndrome with specific amino acid supplementation. jo
- Beyond Myalgic Encephalomyelitis / Chronic Fatigue Syndrome: Redefining an Illness. Committee on the Diag- nostic Criteria for Myalgic Encephalomyelitis / Chronic Fatigue Syndrome, Board of the Health of Select Populations, Institute of Medicine. Washington (DC): National Academies Press (US); 2015 Feb 10.
- Sacher J. Elevated brain monoamine oxidase A binding to the early postpartum period. Arch Gen Psychiatry. 2010 May; 67 (5): 468-74.
- Ellsworth-Bowers ER. Nutrition and the psychoneuroimmunology of postpartum depression . Nutr Res Rev. 2012 Jun; 25 (1): 180-92.
- Meyers, Linda D; Dietary Reference Intakes Research Synthesis Workshop (2006 Institute of Medicine (US)); Institute of Medicine (US) Food and Nutrition Board. Washington, DC: Natonal Academies Press, c2007.
- Rechenberg K. Nutritional interventions in depression and perinatal depression. Yale J Biol Med. 2013 Jun 13; 86 (2): 127-37.
- US Department of Justice website: www.usdoj.gov.
- Hinz M. Treatment of attention deficit hyperactivity disorder with monoamine amino acid precursors and organic cationtransporter assay interpretation. Neuropsychiatr Dis Treat. , 2011; 7: 31-38.
- Hinz M. Monoamine depletion by reuptake inhibitors . Drug Healthc Patient Pure. 2011; 3: 69-77. Reuptake inhibitors do not increase the total number of monoamine molecules in the central nervous system. Their mechanism of action facilitates redistribution of monoamines from one place to another ..
- Stokstad E. Development. New hints into the biological basis of autism . Science. 2001 Oct 5; 294 (5540): 34-7.
- Arnold GL . Plasma amino acids profiles in children with autism: potential risk of nutritional deficiencies. J Autism Dev Disord. 2003 Aug; 33 (4): 449-54.
- Tu WJ. Application of LC-MS / MS analysis of plasma amino acid profiles in children with au- tism . J Clin Biochem Nutr. 2012 Nov; 51 (3): 248-9.
- Shimura C. Alteration of plasma glutamate and glutamine levels in children with high-functioning autism . PLoS One. 2011; 6 (10): e25340.
- Novarino G. Mutations in BCKD-kinase lead to a potentially treatable form of autism with epilepsy . Science. Oct 19; 338 (6105): 394-7.
- García-Cazorla A. Two novel mutations in the BCKDK (branched-chain keto-acid dehydrogenase kinase) gene are responsible for a neurobehavioral deficit in two pediatric unrelated patients. Hum Mutat. 2014 Apr; 35 (4): 470-7.
- Fekkes D. Abnormal amino acid metabolism in patients with early stage Alzheimer dementia. J
The reported findings suggest that abnormal amino acid metabolism is present in the early stages of AD. We hypothesize that this abnormality could play a role in the pathogenesis of behavioral changes in later stages of AD .
- Ravaglia G. Plasma amino acid concentrations in patients with amnestic mild cognitive impairment or Alzheimer disease . Am J Clin Nutr. 2004 Aug; 80 (2): 483-8.
- Gueli MC. Alzheimer's disease: amino acid levels and brain metabolic status. Neurol Sci. 2013 Sep; 34 (9): 1575-9.
- Fonteh AN. Free amino acid and dipeptide changes in the body fluids from Alzheimer's disease subjects. Amino Acids. 2007 Feb; 32 (2): 213-24.
Nutrient Supports, Sportsman Health
and Amino Acids
Many people use nutritional supplement products frequently to improve performance, even if they are professional athletes today.
It is reported that almost 60% of elite athletes use one or more nutritional supplements, it is reported that almost all athletes receive support in some sport fields1.
According to the National Health and Nutrition Examination Survey (NHANES ) conducted in the United States, the use of supplement is seen to spread rapidly from 1972 to 20062 .
Table 9. US public health survey 2
NHANES SURVEY% Adults% Adults
50
NHANES I, 1971-74 22% 27%
(Block, et al.)
NHANES II, 1976-80 33% 39
(Koplan, et al.)
NHANES III, 1988-94 40% 46 (NCHS)
NHANES, 1999-2000 45% 60%
(Radimer, et al.)
NHANES, 2003-06% 45% 67
(Bailey, et al.)
It is not wrong to say that the same increase in the last five, ten years also exists in our country. Pharmacy showcases and eye-catching stands in the interior, the increase in vitamin shops, this blood is true. We have already received hundreds of supplements that give the illusion of miraculous signs of vitamins and minerals, which we have witnessed in the early days of fatigue, fatigue, or strengthening the immune system.
Health practitioners say that "the rest of the healthy diet is not important " in practice does not reduce it in any way to the food supplements. The current environment shows that users and even healthcare providers do not have much information about nutritional support. The views are not beyond "USE GOOD INCOMES OR HARMFUL SAFEGUARDS" .
Why is it good or why the harmful issue has been left to the details that no one can touch. In such an environment it is inevitable that there will be a growing market that is open to abuse.
According to the American NHANES 2007-2010 research conducted on 11,956 people, the question "why are you using supplement"
45% answered that their health is better. However, only 23% of the subjects stated that they used the support recommended by the health professional3.
The World Anti-Doping Organization (WADA) follows and frequently publishes nutritional supplements because nutritional supplements pose serious risks to athletes, particularly for doping . WADA's January 24, 2014, Professor at the Paris Symposium. I would like to share Ron Maughan's slide 1 .
"Loss of use of supplement:
- Some products contain foreign materials (insects, lead, glass fragments, animal feces, etc.)
- Some products do not contain the substance listed on the label, but substitute cheap substances *.
- Some products contain toxic substances.
- Special problems with the athlete: Some products contain doping materials if not written on the label " .
- Similar situation regarding the second item Dr. Ahmet Rasim Kucukusu taught in all his explanations that one of the five nutritional supplements belonging to a brand on the market in the market was understood to be "no substances" written on the label, "if it was already ...".
Professor Dr. Maughan's doping claim was based on the work of the International Olympic Committee (IOC) covering 13 countries5.
The committee's work:
Between October 2000 and November 2001, supplement was collected from 13 countries and 215 producers, including 634 hormones. Supplementals were obtained from 578 outlets, 52 via internet, 2 by telephone order and 2 commodities (IOC). All products were analyzed in the IOC accredited doping laboratory in Cologne, Germany.
14.8% OF PRODUCTS DOPİNG HAS NOT WRITTEN IN THE LABEL
THE CONTENT PROVIDED IS DETERMINED. In 66 patients (10.4%), no reliable results were obtained. See. Table 10.
Items indicated as content on the label of products which are detected as doping:
Amino acids, protein, vitamins, minerals, creatine, ribose, BCAA, HMB, Pyrite, CLA, Melatonin, plant extracts, enzymes.
Table 10. Product distribution according to countries and positive rate of doping test 5
Country
Number of products
Number of doped products
Percent
Netherlands
31
8
25.8%
Austria
22
5
22.7%
Britain
37
7
18.9%
America
240
45
18.8%
Italy
35
5
14.3%
Spain
29
4
13.8%
Germany
129
15
11.6%
Belgium
30
2nd
6.7%
France
30
2nd
6.7%
Norway
30
one
3.3%
Swiss
13
-
-
Swedish
6
-
-
Hungary
2nd
-
-
Total
634
94
14.8%
Side Effects of Anabolic Steroids6,7,8: DOPING-AFFECT ANABO-LIQUID STEROIDS WHICH ARE NOT SPECIFIED IN NUTRITIONAL SUPPORT SHOULD MAKE SENSITIVITY FOR EVERYONE'S HEALTH, NOT FOR SPORTS CARE.
17 cases of death have been reported in the literature on caffeine and efedrine, where anabolic steroids can lead to irreversible side-effects [6].
Table 11. Side Effects of Anabolic Steroids
Cardiovascular: Endocrinology / genital
- Increase blood pressure in men
- Makes negative changes in blood oils • Gynecomastia
- • Heart shrinkage • Testicular shrinkage
- Hematocrit (increase in blood cell count) • Decrease in sperm count
- Thromboembolism (increased risk of coagulation) • Libido change
- Heart rhythm disturbance • Prostate growth
- Sudden death • Prostate cancer
- Liver tumor in women
- Liver damage • Menstrual irregularity
- Early • Maskülinization of pre-pubertal growth plaques (thickening of voice, thickening, muscular structure of shortness due to closure)
- Intramuscular appendage • Libido increase
- Risk of ruptured tendon rupture Psychology
- Acne • Increased self-confidence
- Baldness • Emotional state fluctuation
- Damage to collagen fibers
Reasons for using nutrients:
- Increase muscle mass
- To give more pounds, to dissolve fat
- Expected increase in physical and mental performance
- Strengthening the immune system
- Chronic fatigue
- To increase sexual performance
The following items may be found, if they are not on the label of the majority of the products put on the market to meet these expectations:
- Anabolic steroids for muscle development
- Caffeine, ephedrine in tonics
- Sibutramine banned for weight loss
- Sildenafil (Viagra and similar agents)
In this case, the question might come to mind: Does the product SUPPLY EVER work? Maughan's thought on this subject is quite understandable, especially for athletes' products:
- If the supplement works, there is a prohibited substance not specified in it
- If it does not contain a prohibited substance, it probably will not work
- There may be some exceptions
The most decisive factor when we do not benefit or suffer is how and why we buy the product.
But we know that the most important determining factor when we buy support products is unfortunately the product advertisement. In addition to an effective advertisement in the magazines, on TV, on the internet or in showcases, product brand awareness has improved and the confidence given by being in the pharmacy is the most important factor. However, since these products are not in the drug class, the entry and advertising provisions of the country are far from being controlled and restricted. For this reason, it can be sold easily except for the pharmacy.
FIGURE 56. Sample labels for
supplements LIFE COACH, SPORTS TRAINER, COACHER, MASSAGE, TRANSMITTER, DIETER-NEW, NURSE, PHARMACOLOGY, COMPANY AUTHORIZED, PHARMACEUTICAL, DOCTOR ...
Certainly everyone who uses the product has somehow received or heard from one of these people. Therefore, it uses any standard product.
FIGURE 57. Supplement examples
Everyone
- genetic
- Biochemistry
- Nutrition and lifestyle
THE SUPPORT PRODUCT AND THE DOSE IS DIFFERENT WHEN EVERY NEED. THIS IS A SPECIFIC STANDARD SUPPLEMENT PARTY IS NOT EXPECTED TO MEET THE PROBLEMS OR THE NEEDS.
Is there a need to use a supplement? The answer to this problem is important and is included in the problem "Must I NEED TO USE ?" The presence of each substance / compound in the Supplement must already be increased in our bodies or the need for that substance must be increased so that support is needed. THIS USES A SUPPORT TO DETERMINE THAT THE USE OF A SUPPORT IS NOT REQUIRED. For example, when no one stops or fatigue, fatigue, etc. he does not want an iron pill from his pharmacy because of his complaints. If you are sure of the iron deficiency, consult a doctor and have blood analysis done. At the level of blood iron, a treatment is proposed, which is offered by intravenous, oral or only iron-rich foods considering the depth of the minus and the characteristics of the person. Here, all supports should be the same way as the ideal way of use, followed by iron reinforcements. Ultimately, all other minerals such as iron, vitamins, hormones and amino acids can be measured by biochemical analyzes. Measurement and examination are the only methods that reveal whether there is a need. There may be periods when essentials are reduced or increased in duration depending on personal and environmental influences. These periods are:
- When buying from Gıdaldan decreases
- If there is a problem with the absorption though the intake from the flowers is sufficient
- If the purchase and the absorption are sufficient but the loss is the subject (bleeding, excessive sweating)
- In a time when need is increased (rapid growth, extreme sports, stress)
SPORTS SUPPORTS: In
addition to intense training and competition programs, sportsmen experience physical and psychological stress due to high performance expectations and their performances decrease accordingly. In addition, many athletes are injured or injured in training and games. In situations where this process is not well managed, it is difficult for the athlete to catch the old performance.
The use of nutritional sup- port is also quite common throughout the world (almost 100%) for those who do fitness such as Professional Sports. Supplement use is mainly focused on muscle development and rapid recovery.
Commonly used products for this purpose are:
- Various proteins (whey, soy, casein)
- Amino acids
- Peptides (Carnitine, creatine)
- Amino acid metabolites (beta alanine, HMB-Hydroxy methyl butyrate-Ornithine, Sitrulin)
- Hormones: Anabolic steroids
In this case, people who are dealing with the science of what information should be respected can come up with ways of doing clinical trials.
However, since the user is not able to know them, the correct logic must be the same again.
"MY I HAVE NEEDS THIS PRODUCT? WHY? "
The analysis gives the most accurate answer to this question. Where analysis is not possible, it is necessary to find out what support and under what circumstances it can work.
All of the frequently used athlete supplements have an effect on amino acid functions.
- Proteins (whey, soy, casein)
- Amino acids
- Peptides (carnitine, creatine)
- Amino acid metabolites (beta alanine, HMB (Hydroxy methyl butyrate), Ornithine, Sitrulin)
- Hormones: Anabolic steroids
ALL THESE SUPPORTS HAVE A SINGLE IMPACT ON THE BODY:
INCREASING THE AMINO ACID RATE AND / OR AFFECTING AMINO ACID FUNCTIONALITIES
Whatever protein is taken, it will be broken down by digestion into amino acids. Carnitine (Lysine + Methionine), Creatine (Glycine + Arginine) can be par- ticulated with amino acids which are the building blocks or absorbed into the peptide as it is small. HMB (Hydroxy methyl butyrate), Ornithine, Beta domain and the like are synthesized during amino acid metabolism.
THE ONE CONDITION FOR INCREASING CUTTING AND DURABILITY: SUPERIOR AMINO ACID SUPPLY + RESISTANT EXERCISE
FIGURE 58. Factors Affecting Muscle Mass 9
mTOR, shown in Figures 58 and 59, shows the effect of amino acids, mechanical stimulation and anabolic hormones on muscle protein synthesis It is an important molecule. growth of the mTOR cell, protein synthesis, etc. plays a role in the management of cellular processes of life9,10.
FIGURE 59. Mechanism of testosterone action 10
How Testosterone and Other Anabolic Hormones Affect? The effect of testosterone and anabolic hormones on amino acids. Anabolic hormones act on the body's ongoing protein-protein degradation process, enabling amino acids that are degraded during the degradation process to be used for muscle reconstruction. In other words, the amino acids that are the result of muscle destruction rather than the external amino acids
are used for muscle building again at high levels. About 300 grams of protein is destroyed in the body during the day. No supplement or nutrition model can effectively gain 300 grams of amino acid into the body .
Because of this, anabolic steroids and other doping agents have a fast and distinct effect.
BUT BUSINESS BUSINESS ONLY DO NOT STAY THE GROWTH OF THE MUSCLE; CREATE AROUND EFFECTIVENESS ON ALL SYSTEMS (Table 11) 6,7,8.
Normally, growth of the cell can cause vascular stiffness, cancer, tendon rupture and many other diseases when over-stimulated with mTOR, testosterone, which plays a role in vital functions such as protein synthesis.
THE MOST SAFE AND EFFICIENT FILLING OF THE AMERICAN ACID SUPPORT AND RESISTANT EXERCISE WHICH HAS A HEALTH THREATENING AND DOPING CHARACTERISTICS FOR THE INCREASING OF CURRENT TESTIRONON AND OTHER ANABOLS.
ESSENTIAL AMINO ACID SUPPORT INCREASES CATHRITIS SYNTHESIS IN YOUTH AND AGE
Protein synthesis is regulated by the molecular mechanisms by which essential amino acids, hormones and mechanical stimuli are involved in the mTOR molecule11,12.
Protein-containing foods contain both essential and non-essential amino acids. However, only the essential amino acids are responsible for induction of muscle protein synthesis. This warning is made especially by Lösin. Even if leukin alone can stimulate muscle protein synthesis, it is essential that other essential amino acids are also sufficient to sustain its induction13,14,15,16.
ANY AMINO ACID INCLUDED IN LOSS BUT BUT OTHER ESSENTIAL AMINO ACIDS ARE FULLY EFFICIENT AND ORAL AVAILABLE TO PROTEIN SYNTHESIS 16,17.
ESSENTIAL AMINO ACID AS REQUIRED TO SUPPORT COSMETIC PROSTHESIS SYNTHESIS 18,19,20,21,22 .
Most of the products sold on the market alone or in different combinations contain non-essential amino acids such as Arginine, Glutamine, Ornithine, although all of the clinical trials precisely state that it is not necessary to give non-essential amino acids as support for muscle protein synthesis. Each of these amino acids can be supplemented in specific health conditions. It is necessary to analyze whether it is needed to be beneficial and to determine the ratios that will not disrupt the balance of other amino acids. If not
, it is necessary and unreasonable to supplement a substance that the body can produce adequately under normal conditions.
Effect of the Amount of Protein Amount and Quality of Muscle on Muscle Protein Synthesis The muscle mass contains the most amino acids. The cycle of construction and destruction of muscle proteins continues continuously. This retrograde control is provided by essential amino acids. Because essential amino acids can stimulate muscle protein synthesis, the amount of essential amino acids that the edible foods contain affects muscle synthesis.
When the protein content is low or when the amino acid
content is fed to an insufficient amount of food, that is, it is rich in carbohydrates and fat, but poor in protein, it increases the level of insulin in the food. Increased insulin enhances lipid synthesis (lipogenesis). Contrary to known, protein synthesis can not be achieved when insulin is not sufficient, even if it is elevated 23,24,25 .
STOP INSINLINE RISE REMOVAL, DO NOT INCREASE MUSCLE 26.
IMPORTANT NOTE: It
is the main purpose of the athlete and the fitness worker to increase muscle mass. The different diets and proposals for obesity are perceived as a magical formula to increase muscle mass on the agenda. And everybody is perceived as the most correct method when a few medical terms are added to the formula! The most critical issue in such a setting is the mechanism of muscle protein synthesis and nutrition. The most misunderstood issue is the effect of INSULIN on muscle mass.
The impact of insulin and amino acids on the muscle mass The last "METANALYSIS (2016)", collecting and analyzing all the studies (from 1946 to 2013) up to now, with much research, clearly demonstrated the truth on this subject. 27.
INSULINA, COSMETIC PROTEIN SYNTHESIS BUT BUT AMONG THE BLOOD AMINO ACID LEVEL AND DO NOT NEED TO HIGH INCENSE LEVEL . BUT INCREASE REDUCES CAST PROTEIN DESTINATION INDEPENDENTLY FROM INCINES LEVEL AMINO ACID LEVEL.
What does this sentence actually tell you?
- It is a scientific statement that you can not increase muscle mass by giving macaroni, lentils, beans, spinach. These foods are not worthless. However, they can not provide enough of the essential amino acids alone. It is imperative to consume full protein.
- Pre-and post-sport Loading simple carbohydrates can provide different benefits but does not provide additional benefit for muscle protein synthesis. It stimulates fat synthesis, not protein synthesis.
- Muscle protein building-demolition cycle is the basis of being healthy. Amino acids that are cleaved as a result of muscle breakdown are reused for the synthesis of the required proteins. Our bodies are not able to synthesize the vital new proteins because they know that every single person can not have enough amino acids.
ABRIUM HEARTS raises insulin to an extreme level if it does not give the body food (amino acid). This long-term feeding prevents the amino acids required for protein synthesis from being destroyed by muscle destruction and prepares the underlying structure of the diseases.
I think it can be understood on the basis of why it is unhealthy for meals with lots of snacks (bread, diet biscuits, etc.).
Using an average of 6 grams of essential amino acids per day is sufficient for muscle protein synthesis . In studies, EAA between 2.5 and 10 g induced muscle protein synthesis due to dose increase, while EAA over 10 grams did not induce more stimuli 26,28 .
In two studies with high quality proteins and whey proteins, the protein dosage increased from 20 grams to 40 grams and from 22 grams to 33 grams increased muscle production as it increased the amount of essential amino acids. However, more protein intake after the threshold level did not produce more stimulation29.
I AM NOW SHOWING THAT I CAN MUCH MORE MURDER-MADE MORE THAN ANY WORKING PROCEDURE.
FIGURE 60. Relationship between protein desensitization and muscle protein synthesis 30 The
green line in Figure 60 shows that 5 grams of protein in young people (mean age 24 years) can stimulate muscle protein synthesis at rest, while at 20 grams the stimulus reaches its maximum value. The dashed line shows the protein intake immediately after the resistance exercise. Exercise + protein intake is faster and more muscular. The blue line indicates that in the elderly group (mean age 70 years) more protein intake is needed to stimulate muscle protein synthesis. The dashed blue line also indicates that exercise + protein and muscle protein synthesis are more stimulated in the elderly. The red line shows that increasing the protein dose in the restricted muscle group does not stimulate muscle building much. Essential amino acid supplementation for this group is the most effective way to prevent muscle loss (see Chapter 14, Sarcopenia).
Is Healthy Athlete Needing Protein or Amino Acid Support?
Athletes or those who exercise intensively lose muscle mass when energy deficits due to malnutrition occur. Decreased muscle mass adversely affects physical performance and increases the risk of injury and trauma 31. This is why it is imperative that athletes or seri- ous exercise people consume enough energy and essential substances . Especially if there is no purpose of weight loss, it is necessary to pay careful attention not to cause energy shortage . The amount of energy and protein that athletes need is more than any other individual.
The work done on 39 healthy individuals belonging to the American Army is
one of the most important studies examining the effect of energy deficit and protein intake on muscle mass . Because the study design (randomized, controlled) and the entire participant are of a similar athletic nature, the level of reliability of the data is very high32.
The amount of energy consumed by the soldiers who are fed with 2500 kcal per day on average is reduced by 30% for one month.
Physical activity was increased by 10% and daily energy intake was adjusted to 1800 kcal.
In this process, the protein consumption of the three different groups was routinely programmed as 0.8 g / kg, twice the routine (1.6 g / kg) and 3 times (2.4 g / kg).
The chart below clearly shows how to nourish and gain weight in order to have a healthy body mass. Those who are trying to give their excess kilograms also carry this chart as a guide to lose fat, not muscle, well.
FIGURE 61. Protective effect of daily amount of protein consumed on muscle mass 32
When the same type of diet is applied to all three groups and physical activity is increased in the same way:
- The group averaged 64 grams of protein a day. He delivered 58% of his weight, and 42% of his fat mass.
- The group averaged 122 grams of protein per day. 30% of the kilograms he gave were gone from muscle mass, 70% fat
- The group averaged 185 grams of protein a day. 36% of the weight he gave was 64% of his muscle mass.
How Long Is Protein Needing and Hard to Meet?
Generally the recommended protein amount is 0.8 g / kg per day. That is 70 kg of an adult consuming an average of 56 grams of protein is enough. The daily amount is recommended as 1.2-1.7 g / kg for those who are doing resistance or resistance sports29,33. When we assume that a 75 kg athlete needs 1.7 g / kg, the amount of protein needed is 75 x 1.7 = 127.5 g.
128 g protein, average protein of the following foods to achieve içerikleri- what let's see:
200 grams of red meat, 60 grams protein,
2 cups milk 14 grams
to 100 grams of cheese 18 grams of
2 slices of bread 4 grams
1 egg 7 grams
per 100 grams of chicken meat 30 grams of
such an a total of 133 grams of protein is obtained by feeding. As you can see, it does not seem very easy to get the daily needed protein and even more.
If your daily protein needs can easily be met, why do you need Amino Acid Support? A HEALTHY SPORTS NORMAL CONDITION SUPPORT PROTECTION IS NEEDED.
Regardless of the protein requirement of the athlete or any person, however, the essential amino acid may be required. Protein is determined relative to the nitrogen source that makes up its content. Nitrogen is also obtained from other amino acids, which in addition are 20 amino acids. For this reason, sufficient protein consumption does not mean that any amino acid will not be deficient even if it meets the needed nitrogen.
If the amino acid composition of the edible food is mostly non-essential amino acids, that is, it is not a complete protein, one or more of the restrictive amino acids will be missing. For example, 300 grams of lentils provide enough protein, but the lentil is very poor in terms of Lysine. Therefore, adequate protein intake does not guarantee that individual amino acids are taken in sufficient quantities.
It is
possible to determine the blood and urine levels of amino acids and to provide support accordingly.
Amino acids are the most comprehensive praxis method that allows accurate analysis of feeding in physiological and pathological conditions34.
Example of amino acid analysis :
An amino acid analysis specifies the following conditions for feeding:
- Reduced amino acids
- Increased amino acids
- The altered amino acid ratios (eg, Glutamic acid / Glutamine; Phenylalanine / Tyrozine; Triptofan / LNAA; Tyrosine / LNAA)
- What vitamins and minerals need is increased.
What is the difference between protein supplements and free amino acid supplements ? the protein needed for the athlete can be taken from the diet. Nonetheless, we see that most athletes, and especially those who work to increase their muscle mass, receive additional protein supplements.
Whey, soy protein and casein type protein supplements are preferred because they provide high amounts of protein. The amino acid components of each are different. Whey protein is often preferred because it contains more essential amino acids and is digested faster. The stimulatory effects of muscle mass differ depending on the essential amino acids the protein supports impart to the body35.
Whey protein has the most essential amino acid composition among protein sources. Table 12 shows the content of a whey protein supplement used in our country. The total essential amino acid content of this product is 45%. The
amount of Essential Amino Acid does not usually reach over 45% unless additional amino acid support is added to the protein products .
Note that in addition to a total of 25.4 grams of protein in a serving dose (30 grams), there is also carbohydrate and fat content. The carbon-hydrate and fat ratios of different whey products may be different. When a service is consumed from this product, the person gets 25 grams of protein, about 11 grams of essential amino acid and 129 kcal.
Table 12. Whey protein content
% Daily value *
Energy
258 kcal
**
Protein
25.4 g
**
Carbohydrate
24.1 g
**
Candy
22.2 g
**
Oil
6.2 g
**
Saturated oil
4.4 g
**
Fiber
1.1 g
**
Sodium
0.2 g
**
B6 vitamini (Pyridoxine)
1 mg
**
Calcium
465 mg
**
Amino Acid Profile for 100 Gram protein
**
Isolesin (BCAA)
6.3 g
**
Leucine (BCAA)
10.3 g
**
Lysine
9.1 g
**
2.3 g of methionine
**
Phenylalanine
3.3 g
**
6.5 g of threonine
**
Tryptophan
1.4 g
**
Valine (BCAA)
6.1 g
**
Arginine
2.8 g
**
Cystine
2.2 g
**
Histidine
1.7 g
**
Tyrosine
2.9 g
**
Area
4.9 g
**
Aspartic acid
11 g
**
Glutamic acid
17.7 g
**
Glycine
1.8 g
**
Proline
5.4 g
**
Cool
4.8 g
**
PROTEIN SUPPORTS AMINO ACID CONTENT DOES
NOT CREATE FREE AMINO ACIDS . For this reason, it needs to digest just like food. The degree to which the product can be digested and the amino acid content of the blood can vary according to the physiological state of the person (gastric acid, pancreatic enzymes, etc.). For this, easily digestible HYDRAULICproducts are presented to the market.
The situation is similar when meat is high in protein rather than protein supplements. The protein content of each meat and the amount of calories it can give can vary according to the nutritional characteristics of the animal and the ratio of fat to meat. However, the most important factor determining bioavailability is the digestive and absorption capacity of the consuming person.
Clinical trials have shown that an average of 6-10 grams of essential amino acid is sufficient to stimulate muscle protein synthesis22. The comparison of free essential amino acid, protein sup- port, and food from this route is given in table 13.
Table 13. Amino acid sources comparison
Source
Quantity of an item's
Included Protein Content
Included EAE Amount
Given Energy
skim biftek36 Whey protein
essential amino acids (EAA),
100 g
30 g
10 g
27.5 g
25 g
10 g
- g
- g
147 kcal
120-256 kcal
40 kcal The
amino acids in the juice have a constant content of essential amino acids. For this reason, it is not in a stoichiometric manner to meet any special essential amino acid requirement37.
Free- form amino acids are fully absorbed without the need for digestive functions such as stomach and pancreas enzymes. While amino acids are fully absorbed in as little as 15 minutes, it takes at least three hours to digest protein powders and foods.
Blood-level low or unbalanced amino acids can be replaced by free Essential Amino Acid formulas. Amino acids can be formulated specifically to meet the needs of the missing or meticulous sufferers. However, long-term singular amino acid supplements may further impair the imbalance because amo- noic acids are competing with each other during absorption and blood crossing the brain barrier37,38.
Protein dust and free amino acid difference 29,39
Table 14. Amino acid protein comparison
FREE AMINO ASIT PROTEIN
Essential amino acid ratio 0-100% Adjustable 30-40% Between fixed Amount of digestion Required Compulsory
Absorption time Max 30 minutes 3-4 hours
Pharmacological effect Yes No
Nutrition value Yes Yes
- Free amino acid support with protein support is completely different in terms of absorption and effect.
- When amino acids are given by analyzing the relative proportions, they show full target-oriented, effective and safe nutritional support.
- Amino acid ratios on protein supplements are standard. There is no chance of giving more or less of any amino acid.
- Protein supplements also need digestion just like food. Once digestion is separated by individual amino acids, absorption may take place.
- Protein supplements pass into the blood after at least three hours and we do not know how long amino acid can pass due to factors affecting digestion and absorption. In this case, the deficit may take a long time to recover, and the deteriorated balance may worsen.
- Amino acids go into the blood in 15 minutes when taken on an empty stomach. They do not have to be digested, they absorb directly. The bioavailability is 100%.
- Protein supplements include all amino acids that are not only needed. Mostly it contains mostly carbohydrates and fat. For this reason, while trying to take amino acids, extra calories are taken. That is to say, at least 100-200 kcal energy is loaded from the individual extract to meet the amino acid requirement in particular with protein dust or food.
- Protein supplements can not be successful in a short period of time, with a good support for increased protein requirement, correcting an existing amino acid imbalance, or bringing a certain amino acid level to a normal level, either with very high or very low blood levels.
UTILITY OF FREE AMINO ACIDS Amino acids are in the food supplement class and do not show toxic effects even at very high doses. On the other hand, long-term aminocarboxylic acid is not used well in the analysis. Because amino acids act on each other's metabolism, and especially when they are emanating from the intestine or competing while passing through the brain tissue, it is inconvenient to increase the concentration of any one without considering the others.
For example, for a long time Arginin's reinforcement reduces the Lysine level. Methionine and Histhine mutually reduce each other. Prolonged BCAA supplementation inhibits the migration of Phenylalanine, Tryptophan and Tyrosine to brain tissue. Decreased transfection leads to reduced synthesis of serotonin and melatonin. Decrease in tyrosine transit
leads to decreased synthesis of dopamine, adrenaline, noradrenaline in the brain . Therefore, long-term use of BCAA requires particular attention. Insulin resistance may develop due to misuse of BCAAs .
HALBUKI AMINO ACIDS TREATED ALL THESE PROBLEMS WHICH WERE USED WITH THE APPROPRIATE DOSE AND BALANCE.
In Which Situations Can Amino Acid Support Be Beneficial?
- In heavy and long-term exercises, physical stress is increased
- Depressed mood, insomnia, restlessness, loss of appetite when your body signals
- In order to recover rapidly after injury, injury, surgery and disease
- When infections are frequent
- In order to protect your existing health and prevent possible risks
- In order to maximize physical and mental performance
THE SPORTS ACTIVITIES OF BALANCED FREE AMINO ACID SUPPLEMENTS 40-51
- Increase muscle mass.
- Reduce muscle pain.
- Reduces fatigue after exercise and provides rapid recovery after exercise.
- Increases fat burning.
- It increases attention and focus.
- Reduce muscle and connective tissue damage.
- Increases oxygen transport capacity (hemoglobin and erythrocyte increase).
- Heavy exercise always increases oxidative stress. Amino acids reduce the inflammation-inducing cytokines (IL-6 IL-10).
- Increase antioxidant capacity.
- It strengthens the heart muscle and provides effective energy use.
- Increases adaptation to intense exercise.
REFERENCES:
- Presentation by Prof. Ron Maughan during the WADA TUE (Therapeutic Use Exemption) Symposium, Paris, 23-24 October 2014. https://www.wada-ama.org/en/resources/therapeutic-use-exemption-tue/th e-hazards of -supplement-use-in-sport
- Annette Dickinson. The Benefits of Nutritional Supplements FOURTH EDITION. Published by Council for Responsible Nutrition (CRN), Washington, DC 2012
- Bailey RL. Why US adults use dietary supplements . JAMA Intern Med. 2013 Mar 11; 173 (5): 355-61. Supplement people reported motivations related to overall health more commonly than supplementing nutrients from food intakes. Use of supplements was related to more favorable health and lifestyle choices. It was recommended by a physician or health care provider.
- http://www.haberx.com/unlu_gida_takviyeleri_fos_cikti(19,w,19901,208).aspx)
- Professor Dr. Wilhelm Schänzer , Institute of Biochemistry German Sport University Cologne http: // www. olympic.org/documents/reports/en/en_report_324.pdf
- Ahrendt DM. Ergogenic aids: counseling the athlete . Am Fam Physician. 2001 Mar 1; 63 (5): 913-22.
- Nieschlag E. Doping with anabolic androgenic steroids (AAS): Adverse effects on non- reproductive organs and functions. Rev Endocr Metab Disord. 2015 Sep 15.
- Kanayama G. Ruptured Tendons in Anabolic-Androgenic Steroid Users: A Cross-Sectional Cohort Study. Am J Sports Med. 2015 Nov; 43 (11): 2638-44.
- Pasiakos SM. Exercise and amino acid anabolic cell signaling and regulation of skeletal muscle mass. Nutrients. 2012 Jul; 4 (7): 740-58.
- Wu BW. Randomized control trial to evaluate the effects of acute testosterone administration on muscle mass, strength, and physical function following ACL reconstructive surgery: rationale, design, methods. BMC Surg. 2014 Dec 6; 14: 102.
- Paddon-Jones D. Amino acid ingestion improves muscle protein synthesis in the young and elderly . Am J Physiol Endocrinol Metab. 2004 Mar; 286 (3): E321-8.
- Walker DK. Exercise, amino acids, and aging in the control of human muscle protein synthesis.
We propose that exercise combined with EAA should be effective only in the improvement of muscle repair and growth in athletes, BFR exercise may be very useful as a countermeasure for sarcopenia and other clinical conditions associated with muscle wasting.
- Glynn EL. Excess leucine intake enhances muscle anabolic signaling but not net protein anabolism
Essential amino acids (EAA) stimulate skeletal muscle protein synthesis (MPS) in humans. Leucine may have a greater stimulatory effect on MPS than other EAA and / or decrease muscle protein breakdown (MPB). We conclude that 10 g of EAA, the leucine content of typical high-quality proteins (~ 1.8 g) is sufficient to induce a maximal skeletal muscle protein anabolic response in young adults, but may play a role in autophagy regulation.
- Escobar J. Amino acid availability and age affect leucine stimulation of protein synthesis and eIF4F formation in muscle . Am J Physiol Endocrinol Metab. 2007 Dec; 293 (6): E1615-21.
- Churchward-Venne TA. Leucine supplementation of a low-protein mixed macronutrient beverage enhances myofibrillar protein synthesis in young men: a double-blind, randomized trial . Am J Clin Nutr. 2014 Feb; 99 (2): 276-86.
- Wilson FA. Stimulation of muscle protein synthesis by prolonged parenteral infusion of leucine is dependent on amino acid availability in neonatal pigs. J Nutr. 2010 Feb; 140 (2): 264-70. Muscle protein synthesis was increased by leucine but only when other amino acids were supplied to ma- intain euaminoacidemia. Thus, prolonged parenteral infusion of leucine activates mTOR and its down- stream targets in neonatal skeletal muscle, but the stimulation of protein synthesis is also dependent upon amino acid availability.
- Pasiakos SM. Supplemental dietary leucine and the skeletal muscle anabolic response to essential amino acids. Nutr Rev. 2011 Sep; 69 (9): 550-7.
- Tipton KD. NONESSENTIAL AMINO ACIDS ARE NOT NECESSARY TO STIMULATE NET MUSCLE PROTEIN SYNTHESIS IN HEALTHY VOLUNTEERS. J Nutr Biochem. 1999 Feb; 10 (2): 89-95.
- Wolfe RR. Regulation of muscle protein by amino acids. J Nutr. 2002 Oct; 132 (10): 3219S-24S. Amino acid availability is a potent regulator of muscle protein synthesis (MPS). A reduction in amino acid availability below basal levels inhibits MPS. INGESTION OF NONESSENTIAL AMINO ACIDS IS NOT NEEDED TO STIMULATE MPS.
- Tipton KD. Postexercise net protein synthesis in human muscle from orally administered ami- no acids . Am J Physiol. 1999 Apr; 276 (4 Pt 1): E628-34.
- Wolfe RR. Effects of amino acid intake on anabolic processes. Can J Appl Physiol. 2001; 26 Suppl: 220-7.
- Børsheim E. Essential amino acids and muscle protein recovery from resistance exercise . Am J
We conclude that NEAA is not necessary for stimulation of NB and that there is a dose-depen- dent effect of EAA ingestion on muscle protein synthesis.
- Yoshizawa F. Translational regulation of protein synthesis in the liver and skeletal muscle of mice in response to refeeding. Nutr. Biochem. 1995 6, 130-136
- Svanberg E. Postprandial stimulation of muscle protein synthesis is independent of changes in insulin. Am. J. Physiol. 1997; 272, E841-E847
- Volpi E. Contribution of amino acids and insulin to protein anabolism during meal absorption . Diabetes 1996; 45, 1245-1252
- Cuthbertson D. Anabolic signaling deficits underlie amino acid resistance of wasting, aging muscle. FASEB J. 2005 Mar; 19 (3): 422-4.
- Abdulla H . Role of insulin in the regulation of human skeletal muscle protein synthesis and breakdown: a systematic review and meta-analysis. Diabetologia. 2016 Jan; 59 (1): 44-55.
- Moore DR. Ingested protein dose response of muscle and albumin protein synthesis after resis- tance exercise in young men. Am. J. Clin. Nutr. 2009 , 89, 161-168.
- Wilson J. Contemporary issues in protein requirements and consumption for resistance trained athletes. J Int Soc Sports Nutr. 2006 Jun 5; 3: 7-27.
- K. Influence of amino acids, dietary protein, and physical activity on muscle mass development in humans . Nutrients. 2013 Mar 13; 5 (3): 852-76.
- Johnson MJ. Loss of muscle mass is poorly reflected in grip strength performance in healthy young men. Med Sci Sports Exerc. 1994 Feb; 26 (2): 235-40.
- Pasiakos SM. Effects of high-protein diets on fat-free mass and muscle protein synthesis Follo- wing weight loss: a randomized controlled trial. FASEB J. 2013 Sep; 27 (9): 3837-47.
- Phillips SM. Dietary protein for athletes: from requirements to optimum adaptation . J Sports Sci. 2011; 29 Suppl 1: S29-38.
- Kimura T. Plasma amino acid analysis for diagnosis and amino acid-based metabolic net- works. Curr Opin Clin Nutr Metab Care. 2009 Jan; 12 (1): 49-53.
- Paul GL. The rationale for consuming protein blends in sports nutrition . J Am Coll Nutr. 2009 Aug; 28 Suppl: 464S-472S.
- National Nutrient Database for Standard Reference Release 28 Software v.2.3.2
- Dioguardi FS . Wasting and the substrate-to-energy controlled pathway: a role for insulin resistance and amino acids. Am J Cardiol. 2004 Apr 22; 93 (8A): 6A-12A.
AMINO ACIDS REQUIRED BY HUMANS . An amino acid formulation suitable for match energy needs, control carbohydrate and lipid flow into the TCA cycle, and promote protein synthesis in contra-
- Pasini E. Amino acids: chemistry and metabolism in normal and hypercatabolic states. cunt
Amino acids are the "alphabet" of protein structure, determining many of the properties of proteins. Amino acids are readily absorbed and readily available in the blood. In the cell, amino acids maintain protein stores and counteract hormone-mediated catabolic stimuli. Thus, amino acid supplementation may be effective in counteracting the metabolic and morphologic consequences of the hypercatabolic state of chro- nic, such as heart failure, diabetes mellitus, or liver cirrhosis.
- http://www.ajiaminoscience.com/research/articles.aspx
- Valerio A. Branched-chain amino acids, mitochondrial biogenesis, and healthspan: an evoluti- onary perspective. Aging (Albany NY). May May; 3 (5): 464-78.
- Dioguardi FS. Clinical use of amino acids as dietary supplement: pros and cons. J Cachexia Sarcopenia Muscle. 2011 Jun; 2 (2): 75-80. Epub 2011 Jun 11.
- Ohtani M. Amino acid mixture improves training efficiency in athletes. J Nutr. 2006 Feb; 136 (2): 538S-543S
- Dorofeyeva EE. Biochemical and heart adaptations to physical training and supplementation with amino acids. J Strength Cond Res. 2004 Nov; 18 (4): 738-40.
- Kingsbury KJ. Contrasting plasma free amino acid patterns in elite athletes: association with fatigue and infection. Br J Sports Med. 1998 Mar; 32 (1): 25-32;
- Portier H. Effects of branched-chain amino acids supplementation on physiological and psychological performance during an offshore sailing race . Eur J Appl Physiol. 2008 Nov; 104 (5): 787-94.
- Greer BK. Branched-chain amino acid supplementation and indicators of muscle damage after endurance exercise. Int J Sport Nutr Exerc Metab. 2007 Dec; 17 (6): 595-607.
- Spradley BD. Ingesting a pre-workout supplement containing caffeine, B-vitamins, ami- no acids, creatine, and beta-alanine before exercise delays fatigue while improving reaction time and muscular endurance . Nutr Metab (Lond). Mar 30, 9: 28.
- Allyson L Walsh. Improved time to exhaustion of the ingestion of the energy drink Amino Impact . J Int Soc Sports Nutr. 2010; 7: 14.
- Wiśnik P. The effect of branched chain amino acids on psychomotor performance during tre- Appl Physiol Nutr Metab. 2011 Dec; 36 (6): 856-62.
- Negro M. Branched-chain amino acid supplementation does not enhance athletic performance but affects muscular recovery and the immune system . J Sports Med Phys Fitness. 2008 Sep; 48 (3): 347-51 .
- Buonocore D. Anti-inflammatory Dietary Interventions and Supplements to Improve Performance during Athletic Training. J Am Coll Nutr. 2015; 34 Suppl 1: 62-7.
Free article
In the awesome documentary film "Chimpanzee" I have found some remarkable points about feeding on the life of the little monkey Oscar and his tribe. Known primates are the closest creatures to man. I thought that it would make sense to take lessons from the lives of these intelligent animals, who are naturally pursued everywhere and whose naturalness is intact.
While he was happily happy with the small Oscar family, the tribe almost had only one job; to trace the quality of food. They found the most delicious fruits, picking honey from their hives, picking plant roots and wood inside.
However, it was a special importance given to the area where careful walnut trees are located. They had no intention of losing hundreds of walnuts they had cut off like humans, and they were struggling to kill other tribes for this region. He even lost his Oscar mother in one of these battles.
The walnut cookies they had for the sake of these creatures with features close to us had to be from the basic sources for life, on the contrary .Carbohydrates, fats and vitamins were supplied from fruits, plant roots and walnuts, but I saw how they were able to consume their ants, caterpillars, and small crawlers profusely when they thought protein consumption was low.
Even if they were infrequent, they would go to basic protein needs by hunting other kinds of monkeys. One of the most important points was that they were eating plenty of leaves immediately after eating the meat. Vitamin, minerals and fiber consumption required for the perfect digestive system were also excellent for the perfect operation of amino acids.
Do not look so focused on what my chimpanzees eat and drink. The film was so sad that if you had such a cry you could not cry. After her mother's death, Oscar's loneliness, and then her grandfather's ownership of her, was heartbreaking. Oscar's grandfather's hair was whitish and his hair was pouring out. And it was clear that I had to treat him with direct medical responsibility. This "ageing" certainly should not have been "anti-aging" you.
I had a break from the film and imagined that the little Oscar's grandfather brought him to a doctor in Istanbul .
continuation
Doctor Oscar's Dear, Look now "... As your first job, you need to live a stratic life away; Move up a bit too. Take at least 45 minutes a day, but do not you be on the treadmill ... be with plenty of oxygen. Also, please reduce the red meat. You get a good brand of water flowing from the mountains ... "he said he saw the little Oscar making strange weird voices and grinning and he got very angry ...
"What are you laughing at?"
Why is it that your doctor grinned so much about why your baby grinned?
5-htp, 53
Adrenaline, 14, 48, 68, 128, 131, 133, 158, 200
Aerobic, 117, 141
Aft, 71
Family medicine, 94
Actin, 11
Albumin, 12
Allergy, 57
Alkali, 42, 43
Alcohol, 4, 43, 67, 69, 72, 127, 159-161
ALS, 59, 74
Alzheimer, 58, 131, 159, 174
Amino acid, 1-16, 18-21, 23-31, 33-40, 47-76,
82-94, 97-100, 116-120, 129, 131, 142, 156,
159, 171, 179-205
aromatic, 55, 71, 107
branched chain, 47, 106, 107, 116, 142, 162, 173
group, 19, 38, 42, 87, 89, 90, 150, 170, 187
192, 193
pool, 33-36, 82, 83
limiting limiting, 23
free, 33-35, 45, 49, 82, 97, 98, 100, 108
109, 110, 111, 118, 129, 130, 131, 132, 134,
142, 159, 167, 196, 197, 198
Ammonia, 12, 16, 25, 42, 60, 62, 73, 83
Anabolic, 84, 153, 182, 183, 188
Anaerobic, 141
Anemia, 20, 51, 64
Anxiety, 52, 58, 156, 163
Anorexia, 55, 159
Antidepressant, 56, 159-161, 164
Antibody, 14, 35, 59, 74
Antioxidant, 14, 43, 48, 60, 66, 100, 111, 167, 200
Arthritis, 57, 67, 70
Acid, 1-16, 23, 25, 30, 159-161, 162, 164, 171, 174,
179, 189
Aspartame, 56, 160
ATP (ADENOSINE TRIFLOSTAT), 4, 6, 8, 75, 116,
118, 131
Nitrogen, 7, 33, 36, 41, 42, 45, 70
Ashram, 53, 70, 72, 159, 161
B6 vit, 52, 53, 59, 66, 69, 196, 197
Connective tissue, 11, 65, 70, 200
Dependency, 52, 68, 124, 125, 133, 156, 159
Immunity, 14, 16, 45, 57, 60, 69, 83, 143, 180
Fish, 39, 48, 54, 56, 64, 68, 76
Base, 42, 43, 70
Basal energy, 6
BCAA, 54, 55, 69, 76, 86, 116, 128, 142, 153, 181,
197, 200
Nutritional support, 13, 186, 199
Biomarker, 82, 106
Bioavailability, 197
Bipolar disorder, 67, 162
Kidney, 67, 70, 83, 84, 97, 99, 100, 110, 142
Growth hormone (growth hormone), 13, 21, 54,
60, 131, 149
Check-up, 90, 91, 108, 165
Chocolate, 128, 159, 160, 161, 162
Core, 11, 15, 20, 49, 51, 58, 65, 67, 84, 105, 138,
143, 186, 189
Depression, 24, 33, 49, 52, 59, 65, 74, 126, 134,
156, 159, 161, 165, 167, 172
Attention deficit / Hyperactivity, 56, 69, 159, 171,
Attention deficit hyperactivity disorder (ADHD), 56, 171
Diabetes, 55, 76, 84, 97, 103, 108, 110, 116, 133
Dentistry, 143
DNA, RNA, 15, 16, 18, 34, 42, 74, 83
Dopamine, 14, 56, 68, 125, 158, 162, 163
Doping, 180, 189
Exercise, 36, 55, 61, 92, 137, 153, 160
Extraction, 159
Elastin, 59
Energy, 3, 4, 6, 7, 44, 54, 68, 83, 116, 117, 123, 131
Enkafalin, 158
Enzyme, 1, 9, 12, 35, 53, 163
Eosinophilic myalgia syndrome, 153 Epilepsy, 59, 65, 70, 72
Epinephrine, 14, 34, 127, 158
Heroin, 49, 124, 126, 161
Cannabis, 124, 159, 161
Et, 1, 40, 162, 194, 197, 205
Phenylketonuria, 55, 57, 68
Folic acid, 49, 58, 87, 162
GABA, 34, 57, 64, 72, 125, 160
Gastronomy, 36
Gen, 15, 18, 19, 21, 34, 48
Ghrelin, 13, 124, 126
Glycation, 51, 110
Glycine, 10-16, 41, 64, 85, 110, 148, 158, 172, 188,
197
Glucagon, 13, 123, 124
Glucogenic, 33, 44, 54
Glucose, 8, 9, 33, 43, 54, 61, 70, 76, 108, 117, 151
demolition, 8
Glutamate, 10, 73, 125
Glutathione, 14, 34, 45, 64, 70
A meteorite, 16
Movement, 1, 6, 8, 39, 62, 94, 99, 116, 123, 137, 164
HbA1c, 84, 109
Hedonic, 124, 125
Hemoglobin, 12, 20, 34, 57, 64, 200
Hydrogen, 7, 42
Hydroxylysine, 148, 149
Hyperglycemia, 110, 142
Hypoglycemia, 64, 76, 160
Histamine, 34, 49, 57
HOMA-IR, 107,110
Homeostatic, 123, 125, 126
Homocysteine, 49, 67
Hormone, 4, 9, 13, 33, 52, 68, 83, 108, 118, 124,
133, 149, 161, 187
HPLC, 84
Restless leg syndrome, 68, 159
IGF-1, 34,
Immuno, 58, 60, 182
Infertility, 62
Insomnia (insomnia), 52
Insulin resistance, 55, 84, 103, 109, 110, 111, 128,
133
Insulin, 13, 23, 45, 53, 84, 103, 108, 110, 111, 118,
124, 131, 162, 190
Intolerance, 88, 108, 167
Ischemia, 70, 117, 118
İzak Karasu, 143
Appetite, 16, 36, 51, 53, 69, 83, 122, 128, 132
Caffeine, 158, 160, 182
Calories, 4, 6, 28, 100, 129, 132, 197
Heart, 49, 50, 60, 65, 84, 97, 116, 118, 142, 182, 200
Blood sugar, 51, 54, 76, 83, 84, 105, 109
Cancer, 55, 67, 84, 107, 151, 152, 182, 189
Liver, 25, 43, 48, 50, 55, 59, 67, 76, 97
Carboxyl, 41
Carbon, 41, 43
Carbohydrate, 1, 4, 6, 7, 39, 43, 53, 122, 169, 171,
190, 197
Cardiovascular, 84, 105, 138, 182
Carnitine, 13, 49, 186
fiber, 13
Synthesis, 48, 186
construction, 186
Muscle, 50, 54, 76, 108, 132, 137, 138, 165, 188. 190
Catabolic, 46, 58, 70, 82-84, 141
Kazin, 43, 159, 160, 168
Cachexia, 131
Kcal, 4, 5, 6, 25, 84, 85, 105, 112, 165
Chemotherapy, 56, 59, 131
Keratin, 10, 11, 39, 42, 56
Ketjenic, 44, 54
Restrictive amino acids, 23, 26, 194
Kininurenic acid, 165
Kininurenin, 163, 165
Clinical study, 87, 97 167, 187, 198
Codon, 19, 48
Cocaine, 126, 160
Collagen, 9, 11, 12, 18, 50, 59, 60, 65, 138, 148, 182
Complication, 36, 105, 108, 110, 152
Cortisone, 13
Creatine, 1, 13, 49, 61, 64, 181, 186
Chronic fatigue, 51, 61, 68, 159, 165
Xenobiotic, 4
Sulfur, 11, 45, 48
L-Dopa, 69
L-Alanine, 10, 16, 44, 64, 76, 186, 188, 197
L-Arginine, 10, 60, 63, 85, 153, 188, 197
L-Asparagine, 10, 44, 75
L-Aspartic acid, 10, 12, 15, 44, 56, 74, 85, 158, 197
L-isoleucine, 7, 10, 12, 16, 44, 54, 85, 106, 162, 169,
173
L-Phenylalanine, 7, 10, 12, 41, 44, 56, 68, 85, 106,
133, 160, 169, 196
L-Glutamic acid, 10, 12, 16, 20, 44, 64, 72, 85, 110,
158, 196
L-Glutamine, 10, 15, 42, 44, 69, 70, 85, 153, 160,
196
L-Histidine, 7, 10, 12, 42, 44, 57, 86, 169
L-Lysine, 10, 13, 23, 28, 30, 44, 51, 110, 169, 188,
194
Lleysin, 7, 10, 12, 16, 23, 44, 54, 85, 106, 153
L-Methionine, 7, 10, 12, 20, 44, 59, 66, 85
L-Prolin, 10, 12, 16, 44, 65, 85, 86, 197
L-Serine, 10, 12, 44, 59, 64, 66, 85, 174
L-Cysteine, 10, 12, 27, 44, 66, 131, 169
L-Tyrosine, 10, 12, 13, 44, 55, 68, 85, 106, 133, 160,
163, 166, 172
L-Threonine, 7, 10, 12, 44, 59, 85, 169
L-Tryptophan, 7, 10, 14, 44, 52, 53, 85, 128, 158, 162,
166
L-Valine, 7, 10, 12, 16, 20, 44, 54, 85, 106, 162, 173
Laboratory, 84, 86, 181
Lactate, 117, 141
LC-MS / MS, 84
Leptin, 13, 124, 126, 131
Libido, 156, 159, 182
Fiber, 4, 11, 141
Linoleic acid (omega-6), 7, 39
Linolenic acid (omega-3), 7, 39
Lipoprotein, 12
Lohusa, 167, 169, 170, 171
depression, 167, 168, 169
sadness, 167, 168, 169
sherbet, 169
Substance dependency, 126, 127, 159, 161
Major depression, 162, 164, 167, 170
Macrovascular, 110
Melatonin, 14, 34, 52, 128, 161, 181, 199
Menopause, 53
Menopause, 97, 138, 159
Metabolic, 4, 7, 16, 24, 25, 50, 70, 83, 97, 106, 129,
132
Metabolite, 84, 86, 93, 106, 129, 151, 186
Metabolism, 10, 13, 25, 42, 49, 61, 68, 76, 122,
163, 165
Metchnikoff, 143
Methyl, 48, 49, 171, 182, 186, 160
Fruit, 3, 26, 29, 43, 45, 87, 124
Microvascular, 105, 110
Mineral, 1-7, 24, 39, 87, 88, 93
Mitochondria, 129, 138, 140, 141, 142
Myosin, 11
Mood, 72
mTOR, 130, 131, 188, 189
Murchinson, 16
Mutation, 20
Nicotine, 34, 53, 118
Nitrogen, 7, 33, 34, 41, 42, 70
Starch, 159, 160, 161
NO (nitric oxide), 60, 63
Noradrenaline, 14, 48, 68, 128, 133, 158, 200
Neurotransmitter, 9, 14, 33, 64, 66, 70, 122, 126,
127, 133, 156, 157, 158, 159-161, 164, 174
Nucleus accumbens, 125, 126
Nucleotide, 4, 15, 19, 73, 118
Obesity, 121, 128, 131, 133, 161, 190
Obsessive-compulsive disorder, 162
Oxygen, 7, 41, 45, 57, 116, 117, 118, 141, 200
Ornithine, 61, 62, 85, 186, 187
Autism, 159, 160, 163, 173
Reward, 60, 125, 126, 128, 133, 143
Estrogen, 13, 168
Parkinson, 58, 68, 69, 159
Peptide, 9, 10, 14, 186, 187, 188
Performance, 50, 54, 62, 171, 182, 186, 187, 200
Personalized, 93
Pyrimidine, 15
Predictive, 93
Precursor, 67, 157, 159, 164
Premenstrual syndrome, 52, 56, 159
Preventive, 93
Protein, 18, 19, 24, 25, 27, 30, 100, 169, 172, 185,
187-199
Purine, 15, 43
Restaurant, 36, 73
S-adenosylmethionine (SAM), 48
Sarcopenia, 97, 137, 138, 139, 140, 142, 192
Vegetables, 3, 26-31, 39, 45, 50, 71, 149
Free radical, 49, 67, 140
Serotonin, 34, 52, 53, 125, 127, 128, 158, 159, 161,
169, 199
Sitrulin, 61, 62, 63, 86, 186
Soy, 64, 75, 186, 187, 196
Sports, 50, 51, 108, 128, 129, 167, 179, 180, 185, 186,
187, 190, 192, 194, 200
Steroid, 13, 55, 59, 63, 182, 187
Stoichiometry, 98
Stress, 16, 24, 33, 53, 55, 58, 68, 83, 110, 127, 128,
140, 142, 156, 163, 200
Water, 1, 4, 9, 39, 43, 123,
Supplement, 69, 181, 185, 186
Sulfur, 28, 29, 30, 31, 45, 48,
Milk, 1, 30, 40, 43, 50, 54, 57, 69, 72, 170
Sugar, 4, 6, 8, 9, 15, 21, 33, 43, 54, 65, 76, 105, 109,
122, 124, 126, 142, 159, 197
Cereal, 3, 26, 28, 30, 48, 50, 54, 66
Reinforcements 26, 59, 68, 87, 100, 108, 109, 111, 118,
129, 134, 152, 182, 183, 189, 194
Taurin, 45, 48, 64, 85, 158, 162, 172
Treatment was 24, 39, 47, 51, 53, 58, 62, 67, 69, 82, 93, 97,
105, 122, 128, 131, 152, 159, 162, 170
TEKHARF, 104
Tendon, 11, 33, 50, 65, 182, 189
Testosterone, 13, 188
Diagnosis, 82, 86, 90, 92, 97, 151, 159, 164
Thyroid, 68, 133
Titin, 10
Seed, 26, 27, 48, 56, 74
Toxin, 14, 67, 71, 158
Transferrin, 12
Trauma, 24, 40, 55, 60, 158, 192
Triglyceride, 43, 51, 118, 142
TURDEP, 103, 104, 105
Tobacco, 159, 160, 161
Umami, 73
Exciter (exciter), 15, 72, 74, 126, 156, 196
Urea, 1, 12
Uric acid, 43, 160, 165
Vegan, 24, 30, 49, 54
Vegetarian, 25, 30, 50, 51
Virus, 51, 62, 163
Vitamin, 52, 53, 57, 65, 69, 76, 84, 87, 124, 130,
148, 162, 180, 185, 196
Body composition, 1, 16, 83, 138
Whey, 186, 187, 191, 196, 197, 198
Oils, 2, 4, 5-7, 33, 35, 43, 64, 132, 190
essential, 2, 6-7, 39, 88, 124, 148, 190
Side chain, 41, 45, 47
The soothing (inhibitor), 72, 156, 173
Yogurt, 31, 52, 143
Abandonment, 161
Eggs, 1, 27, 30, 43, 45, 48, 50, 52, 60, 65, 69,
72, 100, 149
Slimming, 127, 130, 152
I give my infinite thanks to my beloved wife Semra and my son Alp who have not lost their support in the emergence of the book .