Normally there is no reaction. (A few patients feel slightly itchy.) This disease is mostly caused by the skin due to poor perspiration, long time high temperature and high humidity, breeding pathogenic bacteria. Patients are mostly adolescent males who exercise a lot and are more prone to flare-ups during the summer months. In the cold winter, the skin sweats less, and the body of most of those who suffer from the disease recovers on its own. In fact, the key to this disease lies in the endocrine and keep the skin dry. It is necessary for you to give Mixi-Chun Cream?
Amino acids are linked by peptide bonds to become peptides and proteins. Amino acids, peptides and proteins are the basic components of the tissues and cells of organic living organisms and play an important role in life activities.
Some amino acids not only form proteins, but also participate in some special metabolic reactions and exhibit some important characteristics.
(1) Lysine
(2) Lysine is the most important amino acid in the world. Lysine
Lysine is an alkaline essential amino acid. It is called the first limiting amino acid because the content of lysine in cereals is very low, and it is easily destroyed during processing.
Lysine can regulate the metabolic balance of the human body. Lysine provides a structural component for the synthesis of carnitine, which leads to the synthesis of fatty acids in cells. Adding a small amount of lysine to food can stimulate the secretion of pepsin and gastric acid, increase the effectiveness of gastric juice secretion, enhance appetite, and promote the growth and development of young children. Lysine can also improve the absorption of calcium and its accumulation in the body, accelerating bone growth. Lack of lysine can cause anorexia and nutritional anemia due to insufficient gastric juices, resulting in central nervous system obstruction and poor development.
Lysine can also be used in medicine as an adjuvant to diuretics, in the treatment of lead poisoning caused by the reduction of chloride in the blood, and can also be used with acidic drugs (e.g., salicylic acid, etc.) to produce salts to alleviate the adverse effects of the combination of methionine can inhibit the severe hypertensive disease.
Herpes simplex virus is the cause of herpes labialis, herpes pyoderma, and genital herpes, while its close genus, herpes zoster virus, is the causative agent of chickenpox, herpes zoster, and infectious mononucleosis. Research published in 1979 by the Lilly Research Laboratory in Indianapolis showed that lysine supplementation accelerated recovery from herpes infections and inhibited their recurrence.
Long-term use of lysine antagonizes another amino acid, arginine, which promotes the growth of herpes viruses.
(2)? Methionine
Methionine is a sulfur-containing essential amino acid that is closely related to the metabolism of various sulfur-containing compounds in living organisms. When methionine is deficient, it can cause loss of appetite, slowed growth or lack of weight gain, enlarged kidneys, and iron buildup in the liver, eventually leading to liver necrosis or fibrosis.
Methionine can also use its methyl group to methylate toxic substances or drugs and play a role in detoxification. Therefore, methionine can be used to prevent and control liver diseases such as chronic or acute hepatitis and cirrhosis, and can also be used to alleviate the toxic reactions of harmful substances such as arsenic, trichloromethane, carbon tetrachloride, benzene, pyridine and quinoline.
(3) ? Tryptophan
Tryptophan can be converted to produce 5-hydroxytryptophan, an important neurotransmitter in the human brain, and 5-hydroxytryptophan has the effect of neutralizing adrenaline and norepinephrine, and can improve the duration of sleep. When the level of 5-hydroxytryptophan in the brain is lowered, animals show abnormal behavior, delusional hallucinations and insomnia. In addition, 5-hydroxytryptophan has a strong vasoconstrictor effect and is found in many tissues, including platelets and intestinal mucosal cells, and is released by the body to stop bleeding after injury. Tryptophan is often used in medicine as an anti-smothering agent, anti-spasmodic agent, gastric secretion regulator, gastric mucous membrane protector, and strong anti-coma agent.
(4)? Valine, leucine, isoleucine and threonine
Valine, leucine and isoleucine are all branched-chain amino acids, and all are essential amino acids. When valine is deficient, the central nervous system of rats becomes dysfunctional, resulting in tremors in the limbs. By dissecting and slicing the brain tissue, it is found that there is degeneration of red nucleus cells, and patients with advanced cirrhosis are prone to form hyperinsulinemia due to the damage of liver function, resulting in the reduction of branched-chain amino acids in the blood, and the ratio of branched-chain amino acids and aromatic amino acids decreases to 1.0-1.5 from 3.0-3.5 in normal people. Therefore, it is often used in the treatment of hepatic failure by injecting branched-chain amino acids, such as valine, etc. In addition, it can also be used as the injection of valine in the treatment of hepatic failure, which can be used as a medicine for the treatment of liver failure. In addition, it can also be used as a therapeutic agent to accelerate the healing of wounds.
Leucine can be used in the diagnosis and treatment of sudden hyperglycemia in children, and can also be used as a dizziness treatment agent and nutritional tonic. Isoleucine is used in the treatment of nervous disorders, loss of appetite, and anemia, and is important in muscle protein metabolism.
Threonine is one of the essential amino acids and is involved in fat metabolism; hepatic steatosis occurs when threonine is deficient.
(5)? Aspartic acid and asparagine
Aspartic acid promotes the tricarboxylic acid cycle through the deamination of oxaloacetic acid, so it is an important component of the tricarboxylic acid cycle. Aspartic acid is also closely related to the ornithine cycle and plays a part in converting ammonia in the blood to urea for excretion. At the same time, aspartic acid is a raw material for the synthesis of nucleic acid precursors such as orotate.
Aspartic acid is usually used in the form of salts such as calcium, magnesium, potassium or iron. This is because these metals, when combined with aspartic acid, can enter the cell through the cell membrane via the active transport route. A mixture of potassium and magnesium aspartate salts is mainly used to combat fatigue and is used clinically in the treatment of heart disease, liver disease, diabetes and other diseases. Potassium aspartate is used in the treatment of hypokalemia, and iron salts are used in the treatment of anemia.
The proliferation of different cancer cells requires the consumption of large amounts of a specific amino acid. The search for analogs of this amino acid, metabolic antagonists, is considered an effective means of treating cancer. Asparaginase prevents the proliferation of cancer cells (leukemia) that require asparagine. An analog of asparagine, S-carbamoyl-cysteine, has been tested in animal studies and shown to be effective against leukemia. At present, there are more than 10 kinds of amino acid anticancer substances, such as N-acetyl-L-phenylalanine, N-acetyl-L-valine, etc., and the inhibition rate of some of them on cancer cells can be as high as 95% or more. The inhibition rate of some of them on cancer cells can be as high as 95% or more.
(6) Cysteine, cysteine, cysteine
(7) Cystine and cysteine
Cystine and cysteine are sulfur-containing non-essential amino acids, which can reduce the body's need for methionine. Cystine is indispensable for the formation of skin, accelerates the recovery of burn wounds and chemical protection against radiation damage, and stimulates the increase of red and white blood cells.
The sulfhydryl group (-SH) carried by cysteine has many physiological effects, relieves the degree of toxicity of toxic substances or toxic drugs (phenol, benzene, naphthalene, cyanide ions), and has a preventive effect on radiation. N-acetyl-L-cysteine, a derivative of cysteine, has the effect of lowering viscosity due to the action of sulfhydryl groups, and can be used as a mucolytic agent for preventing and treating difficulties in coughing up sputum in bronchitis. In addition, cysteine promotes hair growth and is used in the treatment of alopecia. Other derivatives, such as L-cysteine methyl ester hydrochloride, are used in the treatment of bronchitis and exudative inflammation of the nasal mucosa.
(7)? Glycine
Glycine is the simplest amino acid, which can be produced by the loss of a carbon from serine. Glycine is involved in the synthesis of purines, porphyrins, creatine, and glyoxalate, which contributes to the hereditary disease oxaluria by producing oxalic acid from its oxidation. In addition, glycine binds to a wide variety of substances that are excreted in bile or urine. In addition, glycine provides a nitrogen source for non-essential amino acids and improves the tolerance of amino acid injections in the body. The use of glycine together with glutamic acid and alanine is effective in the prevention and treatment of prostatic hypertrophy complications, urinary disorders, frequent urination and residual urination.
(8)? Histidine
Histidine is a non-essential amino acid for adults, but an essential amino acid for young children. When a small amount of histidine is added to the diet of patients with chronic uremia, the rate of amino acid incorporation into hemoglobin increases, and nephrogenic anemia is reduced, so histidine is also an essential amino acid for patients with uremia.
The imidazole group of histidine can form ligand compounds with Fe2+ or other metal ions to promote iron absorption, and thus can be used to prevent anemia. Histidine can reduce the acidity of gastric juice, ease the pain of gastrointestinal surgery, reduce vomiting and heartburn during pregnancy, inhibit the digestive tract ulcers caused by vegetative nervous tension, and is also effective in allergic diseases such as asthma. In addition, histidine can dilate blood vessels, lower blood pressure, clinically used in angina pectoris, cardiac insufficiency and other diseases. Rheumatoid arthritis patients with a significant reduction in blood histidine content, the use of histidine found that their grip strength, walking and blood sedimentation indicators have improved.
Histidine decarboxylates to form histamine under the action of histidine decarboxylase. Histamine has a strong vasodilatory effect and is associated with a variety of allergic reactions and inflammation. In addition, histamine stimulates pepsin and gastric acid.
(9)? Glutamic acid
Glutamic acid and aspartic acid have the role of excitatory transmitter, they are the highest content of amino acids in the central nervous system of mammals, and their excitatory effect is limited to the center. When the glutamate content reaches 9%, as long as the increase of 10-15 mol of glutamate can produce excitatory effects on cortical neurons. Therefore, glutamate is essential for the improvement and maintenance of brain function.
Glutamate is decarboxylated by glutamic acid decarboxylase to form gamma-aminobutyric acid (GABA), which is a substance present in brain tissue that inhibits central nervous system excitability, and affects cellular metabolism and cellular function when the level of GABA decreases.
Many derivatives of glutamic acid, such as dimethylaminoethanol acetylglutamic acid, are used clinically to treat movement disorders, memory disorders, and encephalitis caused by cerebral vascular disorders. γ-aminobutyric acid is effective in memory disorders, speech disorders, paralysis, and hypertension, and γ-amino beta-hydroxybutyric acid is effective in localized paralysis. -hydroxybutyric acid is effective in local paralysis, memory disorders, speech disorders, instinctive renal hypertension, epilepsy and mental retardation.
Glutamic acid, like aspartic acid, is closely related to the tricarboxylic acid cycle and is used in the treatment of hepatic coma. Glutamine, an amide derivative of glutamic acid, has a significant effect on gastric ulcers because the amino group of glutamine is transferred to glucose to produce glucosamine, a component of mucin in the mucous epithelial tissue of the digestive apparatus.
(10)? Serine, alanine and proline
Serine is the precursor for the synthesis of purine, thymine and choline, and alanine plays an important role in the process of protein synthesis in vivo, which is metabolized in vivo through the deamination of ketoacids to produce sugar according to the pathway of glucose metabolism. The pyrrole ring in the proline molecule is structurally related to hemoglobin. Hydroxyproline is a component of collagen. An imbalance in the concentration of proline and hydroxyproline in the body causes a reduction in the toughness of teeth, cartilage in bones and ligamentous tissue. Proline derivatives have antihypertensive effects in combination with diuretics.
Bull? Sulfuric acid
Taurine is a constituent of taurine.
Taurine is commonly found in animal milk, brain and heart, and is most abundant in muscle, where it exists in free form and does not participate in protein metabolism. It is found only in algae, but not in higher plants. Taurine is metabolized from cysteine in the body.
Deficiencies in taurine can affect growth, vision, and the normal development of the heart and brain.
Bacterial infections can also lead to taurine deficiency and changes in the retinal electroretinogram in the fundus of the eye due to the depletion of taurine by bacterial growth, and taurine supplementation can lead to improvement in the fundus of the eye due to the limited synthesis of taurine in humans.
Dairy products contain low levels of taurine. In poultry, the taurine content of black poultry meat is higher than that of white meat. Seafood and poultry, livestock, seafood in the highest taurine content, such as oysters, clams and mussels in the taurine can be as high as 400mg/100g or more, while the heating and cooking of its taurine content has no effect. Everyday foods, including grains, fruits and vegetables, do not contain taurine.
Sperm? Taurine
(a)? Arginine is a component of the ornithine cycle and has an extremely important physiological function. Eating more arginine can increase the activity of arginase in the liver, which helps to convert ammonia in the blood into urea and excrete it. Therefore, arginine is effective in diseases such as hyperammonemia and liver dysfunction.
Arginine is a double amino acid, although it is not an essential amino acid for adults, but in some cases, such as immature body development or under severe stress conditions, if the body is deficient in arginine, the body will not be able to maintain positive nitrogen balance and normal physiological functions. In patients, arginine deficiency can lead to high blood ammonia and even coma. If an infant is congenitally deficient in some of the enzymes of the urea cycle, arginine is also necessary for it to maintain its normal growth and development.
Arginine's important metabolic function is to promote wound healing, it can promote the synthesis of collagen tissue, so it can repair wounds. An increase in arginase activity was observed in the wound secretion, which also indicated that the need for arginine in the vicinity of the wound was greatly increased. Arginine can promote the microcirculation around the wound and promote early wound healing.
Arginine's immunomodulatory function prevents thymus degeneration, especially after injury, and supplementation increases thymus weight and promotes the growth of lymphocytes in the thymus.
Arginine supplementation can also reduce the size of tumor-bearing animals, lower the rate of tumor metastasis, and increase the survival time and survival rate of animals.
In the immune system, the vitality of phagocytes in addition to lymphocytes is also related to arginine. Adding arginine can activate their enzyme system and make them more capable of killing target cells such as tumor cells or bacteria.
Dr. Zheng Jianxian, professor at South China University of Technology
Amino acids and human health
Amino acids are the most basic substances that make up the proteins of living organisms and are related to the activities of life, and they are the basic units of the protein molecules in living organisms, which have a close relationship with the life activities of living organisms. It has a special physiological function in the antibody, is one of the indispensable nutrients in the organism.
One of the basic substances that make up the human body, the material basis of life
1. One of the most basic substances that make up the human body
The most basic substances that make up the human body, there are proteins, lipids, carbohydrates, inorganic salts, vitamins, water and dietary fiber and so on.
As the basic unit of protein molecules, amino acids are undoubtedly one of the most basic substances in the human body.
There are more than 20 kinds of amino acids in the human body, they are: tryptophan, methionine, threonine, valine, lysine, histidine, leucine, isoleucine, alanine, phenylalanine, cystine, cysteine, arginine, glycine, serine, tyrosine, 3.5.iodo-tyrosine, glutamate, aspartate, proline, hydroxyproline, arginine, citrulline, urea and so on. Tyrosine, 3.5. These amino acids are found in nature and can be synthesized in plants, but not in the human body. Eight of these amino acids cannot be synthesized by the human body and must be supplied by food, and are called "essential amino acids". These eight essential amino acids are: tryptophan, threonine, methionine, valine, lysine, leucine, isoleucine, and phenylalanine. The others are "non-essential amino acids". Histidine can be synthesized in the body, but the rate of synthesis is not sufficient to meet the body's needs, so some people also classify it as an "essential amino acid". Cystine, tyrosine, arginine, serine and glycine are classified as "semi-essential amino acids" because they can be synthesized in the body, but their synthetic raw materials are essential amino acids, and cystine can replace 80% to 90% of methionine, and tyrosine can replace 70% to 75% of phenylalanine. Phenylalanine, play the role of essential amino acids, the above amino acids are divided into "essential amino acids", "semi-essential amino acids" and "non-essential amino acids" 3 categories, according to its nutritional function. Functions; such as its metabolic pathway in the body can be divided into "ketogenic amino acids" and "sugar amino acids"; according to its chemical properties can be divided into neutral amino acids, acidic amino acids and alkaline amino acids, most of the amino acids belong to the neutral.
2. The material basis of life metabolism
The generation, existence and demise of life, none of which is related to protein, as Engels said: "Protein is the material basis of life, life is a form of protein existence." If there is a lack of protein in the human body, the lower body quality, developmental delays, resistance to weaken, anemia and weakness, the heavier formed edema, and even life-threatening. Once the loss of protein, life will no longer exist, so some people call protein as "the carrier of life". It can be said that it is the first element of life.
The basic unit of protein is amino acid. If the human body lacks any one of the essential amino acids, it can lead to abnormal physiological functions, affecting the normal metabolism of antibodies, and finally lead to disease. Similarly, if the human body lacks certain non-essential amino acids, it will produce antibody metabolism disorders. Arginine and citrulline are very important for the formation of urea; insufficient intake of cystine will cause insulin decrease and blood sugar increase. The need for cystine and arginine increases dramatically after trauma, and if they are deficient, protein synthesis will not be successful even if there is sufficient calorie intake. In short, amino acids can play the following roles in the human body through metabolism: ① synthesize tissue proteins; ② turn into acids, hormones, antibodies, creatine and other ammonia-containing substances; ③ transformed into carbohydrates and fats; ④ oxidized into carbon dioxide and water and urea, generating energy. Therefore, the presence of amino acids in the human body, not only provides an important raw material for the synthesis of proteins, but also for the promotion of growth, normal metabolism, and maintenance of life provides the material basis. If the human body lacks or reduces one of them, the normal life metabolism of the human body will be impaired, and even lead to the occurrence of various diseases or the termination of life activities. This shows that amino acids in human life activities in the human body appears to be how much need.
Second, the status and role of food nutrition
Human beings in order to survive the need to ingest food, in order to maintain the normal physiology of the antibody, biochemistry, immune function, as well as growth and development, metabolism and other life activities, food in the body through digestion, absorption, metabolism, and to promote the antibody growth, development, wisdom and fitness, anti-degeneration disease prevention and prolong the life of a comprehensive process known as nutrition. The active ingredients in food are called nutrients.
As the human body's most basic substances of protein, lipids, carbohydrates, inorganic salts (i.e., minerals, including macronutrients and trace elements), vitamins, water and dietary fiber, but also the body's need for nutrients. They have their own unique nutritional function in the body, but in the metabolic process and closely linked, *** with the participation, promote and regulate life activities. The body through the food and external links, to maintain the relative constancy of the internal environment, and complete the unity and balance of the internal and external environment.
What is the role of amino acids in these nutrients?
1. Protein digestion and absorption in the body is accomplished through amino acids
As the first element of nutrition in the body of protein, its role in food nutrition is obvious, but it can not be utilized directly in the body, but through the amino acid molecules into a small molecule after being used. That is, it is not directly absorbed in the gastrointestinal tract of the human body, but is absorbed in the small intestine and enters the liver along the hepatic portal vein after breaking down the high molecular proteins into low molecular peptides or amino acids in the gastrointestinal tract through the action of many kinds of digestive enzymes. Part of the amino acids are decomposed or synthesized into proteins in the liver; the other part of the amino acids continue to be distributed with the blood to various tissues and organs, where they are selected for the synthesis of various specific tissue proteins. Under normal circumstances, amino acids enter the bloodstream at almost the same rate as they leave the bloodstream, so the amino acid content in the blood of normal people is fairly constant. For example, the content of amino nitrogen is 4-6 milligrams per 100 milliliters of plasma and 6.5-9.6 milligrams per 100 milliliters of blood cells. After a full meal of protein, a large amount of amino acid is absorbed, and the level of amino acid in the blood rises temporarily, but after 6-7 hours, the level returns to normal. This indicates that amino acid metabolism in the body is in dynamic balance, with blood amino acids as its balance hub, and the liver is an important regulator of blood amino acids. Therefore, food proteins are digested and decomposed into amino acids, which are absorbed by the body and utilized by the antibodies to synthesize their own proteins. The body's need for protein is actually a need for amino acids.
2.2 Nitrogen balance
When the quality and quantity of protein in the daily diet are appropriate, the amount of nitrogen ingested is equal to the amount of nitrogen excreted by the feces, urine and skin, which is called the total nitrogen balance. In fact, it is the balance between the continuous synthesis and decomposition of protein and amino acids. Normal human daily protein intake should be kept within a certain range, and the body can still regulate protein metabolism to maintain nitrogen balance when the intake is suddenly increased or decreased. If excessive protein is consumed, the body's ability to regulate protein metabolism is exceeded, and the homeostatic mechanism will be disrupted. If the body does not eat protein at all, the tissue proteins will still be decomposed and the negative nitrogen balance will continue to occur, which will eventually lead to the death of the antibody if no timely measures are taken to correct the situation.
3. Transformation into sugar or fat
The a-keto acid produced by amino acid catabolism is metabolized along the sugar or lipid pathway with different characteristics. a-keto acid can be synthesized as a new amino acid, transformed into sugar or fat, or oxidized and decomposed into CO2 and H2O by the tricarboxylic acid cycle, and releases energy. energy.
4. Involved in the composition of enzymes, hormones, some vitamins
Enzymes are chemically proteins (amino acid molecules), such as amylase, pepsin, cholinesterase, carbonic anhydrase, aminotransferase and so on. Nitrogen-containing hormones are composed of proteins or their derivatives, such as growth hormone, thyroid-stimulating hormone, adrenaline, insulin, enteric fluid-stimulating hormone. Some vitamins are converted from amino acids or combined with proteins. Enzymes, hormones, vitamins in the regulation of physiological functions, catalyzing the metabolic process plays a very important role.
5. The human body's essential amino acid requirements
The adult essential amino acid requirements are about 20% of the protein requirements, -37%.
Three, in the medical application
Amino acids in medicine is mainly used to prepare compound amino acid infusion, but also used as therapeutic drugs and for the synthesis of peptide drugs. At present, there are more than 100 kinds of amino acids used in medicine, including 20 kinds of amino acids constituting proteins and more than 100 kinds of amino acids constituting non-proteins.
The compound preparation composed of many kinds of amino acids occupies a very important position in modern intravenous nutritional infusion and "elemental diet" therapy, which plays a positive role in maintaining the nutrition of the critically ill patients and rescuing the patients' lives, and has become one of the indispensable medicinal varieties in modern medical treatment.
Glutamic acid, arginine, aspartic acid, cystine, L-dopa and other amino acids act individually to treat a number of diseases, mainly used in the treatment of liver disease, gastrointestinal disease, cerebral disease, cardiovascular disease, respiratory disease, as well as used to improve muscle vitality, pediatric nutrition and detoxification. In addition, amino acid derivatives have shown promise in the treatment of cancer.
Four, and the relationship between aging
The elderly if the body lacks protein decomposition is more and slower synthesis. Therefore, in general, the elderly need more protein than young adults, and the demand for methionine, lysine is also higher than young adults. 60 years old or older should consume about 70 grams of protein per day,? And the requirements of the protein contains a complete range of essential amino acids and appropriate ratios, so that high-quality protein, prolong life.
Yu Chuanlong (China Medical Science and Technology Publishing)
Amino acids and health in old age
The U.S. space shuttle Discovery sent the world's oldest astronaut (77 years old) Glenn into space. This day is known as the greatest day for the elderly and attracts the most attention. In his twilight years, Glenn went back into space to help medical science. One important study is the biology of protein breakdown in the elderly and amino acids in the human body. Amino acids and the health of the elderly should be studied not only on Earth, but also in space. This is because amino acids are so important to the longevity and aging of the elderly. Why is it important? The following is an explanation. 1. Physiological changes and amino acids in old age
It is generally recognized that people enter old age when they are over 60 years old. The physiological and nutritional status of the elderly changes as they age. Protein changes in the elderly body is summarized in two: one is the synthesis, synthesis of tissue proteins and a variety of active substances; the second is the decomposition, the decomposition of tissue proteins, the production of energy, the production of waste. For infants and adolescents during the growth period, synthesis is greater than catabolism, and thus the body grows gradually; for adults in general, synthesis is equal to catabolism, and thus the body weight is relatively stable. For the elderly, protein metabolism in the aging process is mainly catabolic, anabolic metabolism is gradually slow, the body's protein is gradually consumed, often showing a negative nitrogen balance. For example, the synthesis of hemoglobin decreases, so anemia is a common geriatric disease; due to the role of enzymes and the decline of small intestine function, protein absorption process is not sufficiently decomposed, the body peptides increase, free amino acids decrease. Due to the low renal function of the elderly, the reabsorption of amino acids is affected, and due to the decline in liver function, the utilization of peptides is also reduced. Recent studies have reported that the plasma amino acid (val, leuc, tyrosine, lysine, methionine, serine, alanine) content of the elderly is lower than that of the middle-aged and young people under the same nutritional conditions, especially the branched-chain amino acids (val, leuc, and isoleucine) are shown to be insufficient. It is believed that high concentrations of branched-chain amino acids have the effect of providing synthesis, and when supplemented with branched-chain amino acids, they can provide energy through the production of adenosine triphosphate (ATP), reduce proteolysis, and enhance protein synthesis through the promotion of insulin secretion. Branched-chain amino acids have been used in clinics to maintain nitrogen balance and promote protein synthesis. Domestic special amino acids have been used in liver disease, kidney disease and children.
Since the absorption or utilization of amino acids. Due to aging and affect the immune function, changes in immune activity also affect the function of other organs, such as infections, cancer, immune complex disease, autoimmune disease, amyloidosis incidence in the old age are higher, easy to cause aging disease and death.
2. Amino acids and longevity
In order to promote the health of the elderly, such as anti-aging, improve body resistance, promote the function of the immune mechanism, the need for food rich in trace elements or sugar. However, the material basis of immunity is protein, and none of the human immune substances are not composed of protein. For example, immunoglobulins, antibodies, antigens, complements, etc., and even white blood cells, lymphocytes and phagocytes contain more than 90% of proteins in their cells. Therefore, if the body is not deficient in proteins or amino acids, the above mentioned micronutrients and polysaccharides will work. If there is a deficiency, no matter how much is used, they will not work. With advances in nutrition and biochemistry, new research has shown that supplementation of certain non-essential amino acids, although synthesized by the human body, are susceptible to deficiencies under conditions of severe stress (including stress, anxiety, and burden of thought) or certain diseases. If deficiencies occur, they can have harmful effects on the human body. These amino acids are called conditionally essential amino acids. These are called conditionally essential amino acids, such as taurine, arginine and glutamine.
Deficiencies in essential amino acids under normal conditions can reduce the humoral immune response. For example, in tryptophan-deficient rats, IgG and IgM receptors are inhibited, and when tryptophan is reintroduced, normal antibody production can be maintained; phenylalanine and tyrosine deficiencies inhibit the immune cells of rats from responding to tumor cells; and deficiencies of methionine and cystine can cause impaired antibody synthesis. It has been proved that the balance of amino acids also has this unfavorable effect. Therefore, essential amino acids play an important role in immunity, and in order to prolong the life span of the elderly, it is necessary to improve immunity and pay attention to the supply of essential amino acids. Currently, the essential amino acids related to longevity are the most popularly researched ones:
Taurine: The source of taurine in the human body is either self-synthesis or dietary intake. Taurine biosynthesis from methionine by sulfation into cystine, and by cystine synthesis, which after a series of enzymatic reactions, many higher animals, including humans have lost the ability to synthesize enough taurine to maintain the overall level of taurine in the body, the need for dietary intake of taurine in order to meet the needs of the body. The role of taurine in the aging of the central nervous system has been reported; the degenerative changes of the nervous system in old age are one of the most complex and profound processes in the whole body system, and the aging of the central nervous system has obvious changes in morphology or biochemical level, and there are aging changes in the synthesis, release, reabsorption, and transport mechanisms of monoamines and amino acid neurotransmitters. Lipofuscin is a characteristic substance in the aging process, and the increase of lipofuscin in the brain is one of the signs of neurological aging. When the cytoplasm of neurons accumulates a large amount of lipofuscin, the nucleus of the cell and the cytoplasm of the cell will be deformed by the pressure, which affects the normal metabolism of neurons. In aging, the content of lipofuscin in tissues increases significantly, and taurine can decrease and increase the activity of superoxide dismutase (SOD), and inhibit the modification of low-density lipoprotein (LDL) by malondialdehyde (MDA), a product of lipid peroxidation. Meanwhile, the reaction products of taurine and glucose showed strong antioxidant effects, and prevented the oxidation of egg yolk lecithin into lipid peroxides, thus having significant anti-aging effects.
Arginine: Although arginine is not an essential amino acid, it is a conditionally essential amino acid because it cannot maintain nitrogen homeostasis and normal physiological functions under severe stress (such as disease or injury) or when arginine is deficient. It has been theorized that arginine is essential for the enzymatic pathway of nitric oxide (NO) reaction with citrulline. The main biochemical effect of NO or endothelium-derived relaxing factor is to stimulate the body to increase cyclic guanosine levels in phagocytes and to stimulate the production of interleukin to regulate bacterial phagocytosis by macrophages. The NO enzyme system associated with arginine is also found in endothelial cells of blood vessels, brain tissue and kupffer cells of the liver, and it leads to hormone secretion in these organs and tissues, thus contributing to immune function. In order to improve the immunity of the elderly can also be used amino acid injection.
Glutamine: It is a non-essential amino acid under normal conditions, but under stressful conditions such as intense exercise, injury, infection, etc., it can be used to enhance the immune system.