Glycine is an essential amino acid
Glycine should be added to the list of essential amino acids, because, although the metabolism can manufacture it, this capacity is much lower than what is required. The metabolic needs of glucose exceed 15 per year, while the metabolic capacity of its synthesis is between 2 and 3 grams; therefore, the diet must obligatorily cover this deficit, like that of any essential amino acid. Glycine should be considered as an essential amino acid, and really the most essential of all, which requires more of it in the diet than any other. However, a normal diet only contains about 2 grams of glycine; there is, therefore, a daily deficit of at least 10 grams that is widespread in the human population, and in all large animals (from 35 kg of weight).
The persistent lack of glycine over the years will inevitably lead to several metabolic pathways working in precarious conditions due to lack of material. The main process affected is the synthesis of collagen, which spends more than 90% of the available glycine. The deficient synthesis of collagen causes that its renewal is not done properly, and from there can arise many health problems that are related to a weakness of the mechanical system of the body. Many diseases traditionally considered degenerative, such as osteoarthritis, osteoporosis, weakness of joints, propensity to physical injuries, broken bones, ankle sprains, etc., are rather deficiency diseases, due to the lack of glycine, in the same way as Scurvy, which had all the appearance of being a degenerative disease, and turned out to be a deficiency disease due to the lack of vitamin C.
Apart from the problems related to the mechanical structure of the body, glycine is used in many other metabolic processes, for the synthesis of hemoglobin, creatine, for the elimination of cholesterol, etc., and in principle, the lack of glycine can condition that all these processes, or some of them do not work properly. The lack of glycine can, therefore have many other health impacts, all important, such as anemia, muscle weakness, muscular dystrophies, excess cholesterol, and many others, which could be resolved by increasing the daily intake of glycine as a nutritional supplement.
The results obtained in the nutritional program that we have carried out have shown that the daily intake of glycine in the calculated doses helps to solve and prevent the aforementioned problems. We have begun to communicate these results to the scientific community through the corresponding patent applications in the United States and the European Union, in a doctoral thesis and in several congresses.
Glutamine is an amino acid that is part of the proteins of mammals. However, you will wonder what is the function of this amino acid in the organism.
Well, although glutamine is not an essential amino acid, it is the most abundant of the organism and intervenes in different bodily functions. For this reason, it is of great importance in human nutrition, to such an extent that it is consumed as a nutritional supplement. Hence, it is interesting that you know what are the effects of glutamine on health.
I will tell you that, among the main benefits of glutamine for the organism, the following stand out:
• Increase muscle mass. In fact, L-glutamine acts at the muscular level, enhancing muscle formation and preventing muscle degradation. That is why, in both powder and capsules, it is used as a supplement to gain muscle. This has led to suppose that glutamine is fattening, which is not true since what is increased is not fat but muscle mass.
• Increase energy. On the other hand glutamine is used to stimulate the formation of reserve energy in the body, which is very beneficial for athletes.
• Helps to cope with stress. Glutamine is also useful to deal with situations of traumatic stress on the organism, since this amino acid allows a better and faster recovery.
• Prevents the malabsorption of nutrients. Likewise, this organic compound maintains and promotes the integrity of the intestinal mucosa, preventing the malabsorption of nutrients.
• Improve defenses. Even, they are attributed benefits for the treatment of certain diseases such as Crhon's disease, and improves the defenses and reduces intestinal damage.
• Relieves arthritis. Lastly, glutamine is useful for the treatment of arthritis, reducing inflammation and pain in the joint.
As you can see, this amino acid has very beneficial effects for health.
The following uses are based on tradition, scientific theories or limited research. They have often not been fully tested in humans and their safety and efficacy have not always been proven. Some of these conditions are potentially serious and should be evaluated by a qualified medical provider. There could be other proposed uses that are not listed below.
Aging, antibacterial, anti-inflammatory, antimicrobial, antioxidant, antiviral, bodybuilding, bowel health, cancer, cognitive function, depression, diabetes, fat burning, fracture healing, gastrointestinal disorders, gastrointestinal difficulties (induced by anti-inflammatory drugs non-steroidal), reduced healing time, hyperglycemia (high blood sugar), irritable bowel syndrome, keratitis (inflammation of the eyes), longevity, measles, mood stimulant, mucositis due to cancer treatment, nerves, osteoporosis, rheumatoid arthritis, skin conditions, xerostomia (dry mouth).
The following uses in humans or animals have been tested. The safety and efficacy of these have not always been demonstrated. Some of these conditions are potentially serious and should be evaluated by a qualified medical provider.
• Colitis (C) Preliminary evidence suggests that bovine colostrum may be effective in improving gastrointestinal health. More studies are needed in this area.
• Diarrhea (C) Bovine colostrum may be effective for the improvement of gastrointestinal health. Preliminary evidence suggests that colostrum inhibits the adhesion or activity of certain bacteria to intestinal cells, which may help in the treatment of diarrhea. Additional studies are required in this area.
• Improvement of performance in physical exercise (C) Although human studies are currently contradictory, bovine colostrum could be effective for improving performance in physical exercise. Additional studies are needed in this area to be able to make a firm recommendation.
• Immune function (C) Bovine colostrum contains immunoglobulins or antibodies that are released into the bloodstream in response to infections. These immunoglobulins could help improve the functions of the immune system. More evidence is required before a firm recommendation can be made.
• Immune system deficiencies (cryptosporidiosis) (C) Cryptosporidium parvum is a parasite that could cause severe and debilitating diarrhea in patients with AIDS. Preliminary evidence suggests a potential benefit of bovine colostrum in this area. However, additional studies are needed before a firm recommendation can be made.
• Infections (rotavirus) (C) Bovine colostrum, which is high in antibodies to certain viruses such as rotavirus, may help prevent diarrhea associated with rotavirus. Additional studies are needed in this area.
• Helicobacter pylori infection (C) According to preliminary studies, the use of bovine colostrum seems not to be beneficial in H. pylori infection. Additional studies are needed before a firm recommendation can be made.
• Multiple sclerosis Bovine colostrum has been used for multiple sclerosis, although preliminary results indicate no benefit. Additional studies are required in this area.
• Oral hygiene Bovine colostrum has shown potential for immunological stimulation and may be useful in oral hygiene products. Currently, there is not enough evidence available to make recommendations for or against the use of colostrum for this purpose.
• Sore throat Bovine colostrum has shown potential for immunological stimulation and could be useful in the treatment of sore throat. Currently there is not enough evidence available to make recommendations for or against the use of colostrum for this purpose.
• Post-surgical recovery Bovine colostrum has been studied in individuals who are going to undergo coronary bypass surgeries, but none were found benefit. Additional studies are required before a firm recommendation can be made.
• Infections of the upper respiratory tract Bovine colostrum has shown potential for immunological stimulation. However, preliminary evidence has shown no benefit in treating long-lasting upper respiratory tract infections, although this colostrum may reduce symptoms. Additional studies are needed before a firm recommendation can be made.
Health professionals who have formal instruction practice many complementary techniques, in accordance with the standards of national organizations. However, this is not the universal case; There may be adverse effects. Due to limited existing research, in some cases there is only little information available on the safety of the treatment.
It should be avoided in individuals with known allergy or hypersensitivity to dairy products.
Synthesis of cysteine. The cysteine beta synthetase catalyzes the superior reaction and the cystathionine gamma-lyase catalyzes the inferior reaction. In animals, biosynthesis begins with the amino acid serine. Sulfur is derived from methionine that is converted to homocysteine by the intermediate S-adenosylmethionine. After this, cystathionine beta-synthetase combines homocysteine and serine to form the asymmetric thioether cystathionine. The enzyme cystathionine gamma-lyase converts cystathionine to cysteine and alpha-ketobutyrate. In plants and bacteria, the biosynthesis of cysteine also starts from serine, which is converted to O-acetyl-serine by the action of the enzyme serine acetyltransferase (EC 18.104.22.168). The enzyme O-acetylserine (thiol) -liase ((OAS-TL; EC 22.214.171.124), using sulfur in the form of hydrogen sulfide, converts this ester into cysteine by displacement of acetate.
The thiol group of cysteine is nucleophilic and easily oxidizable. The reactivity increases when the thiol is ionized and the cysteine residues in proteins have pH values close to neutrality, so thiols are often found in reactive form in the cell. Due to its high reactivity, the thiol group of cysteine has numerous biological functions. Antioxidant glutathione precursor.
Due to the ability of thiols to undergo redox reactions, cysteine has antioxidant properties. These antioxidant properties of cysteine are mostly expressed in tripeptide glutathione that are produced in both humans and other organisms. The systematic availability of oral glutathione (GSH) is insignificant, therefore it must be biosynthesized from the amino acids that constitute it such as cysteine, glycine and glutamic acid. Glutamic acid and glycine are found abundantly in most western diets, so the availability of cysteine may be the limiting substrate. Disulfide bridges
Disulfide bridges have an important role in the assembly and stability of some proteins, normally proteins secreted into the extracellular medium. Since most cell compartments are reduced media, disulfide bridges are generally unstable in the cytosol, except for a few exceptions that we see below. Protein disulfide bridges are formed by the oxidation of thiol groups of cysteine residues. The other amino acids that also contain sulfur, such as methionine, can not form disulfide bridges. Very aggressive oxidants convert the cysteine into the corresponding sulfuric acid and sulphonic acid. Cysteine residues have a valuable role in cross-linked proteins, since they increase the rigidity of the proteins and also confers proteolytic resistance. Within the cell, the disulfide bridges between cysteine residues act as a support in the secondary structure of polypeptides. Insulin is an example of proteins with cross-linked cysteines, where two separate chains of peptides are connected by a pair of disulfide bridges. The disulfide isomerase proteins catalyze the formation of disulfide bridges; the cell transfers dehydroascorbic acid to the endoplasmic reticulum. In nature, cysteines are, in general, oxidized to cystines, with their only function being nucleophilic. Cystine (in neutral form) is derived from two molecules of cysteine. Forming a disulfide bridge.
Precursors of iron-sulfur groups
Cysteine is an important source of sulfur in human metabolism. Sulfur from the iron-sulfur and nitrogen groups is extracted from cysteine and becomes alanine during the process. Union to the metallic ion.
Apart from the iron-sulfur-proteins, many other metal cofactors in enzymes are bonds for the thiol substituent of the cysteine residues. Examples of this are zinc in the zinc fingers and alcohol dehydrogenase; copper in cuprous blue proteins, iron in cytochrome P450; and nickel in the [NiFe] -hydrogenase. The thiol group also has great affinity for heavy metals, so proteins that contain cysteine such as metallothionine will bind metals such as mercury, lead and strong cadmium. Post-translational modifications.
Apart from its oxidation to cystine, cysteine participates in numerous post-translational modifications. The nucleophilic thiol group allows cysteine to conjugate other groups, such as in prenylation, ubiquitin ligases transfer ubiquitin to its pendants, proteins and to caspases that participate in proteolysis in the apoptotic cycle. Inteins (protein introns) normally act as an aid to catalytic cysteine. These roles of cysteine are typical limited to the intracellular medium, where the medium is reduced and the cysteine is not oxidized in cystine. Alpha-lipoic acid
R / S-LA and RLA are available as nutritional supplements in the United States in the form of capsules, tablets and aqueous liquids, and have been marketed as antioxidants (For example, it helps the regeneration of vitamin C and E, therefore says that it is a good antioxidant) .63 This label has recently been questioned.3 In Japan, LA is marketed mainly as a product that helps to lose weight and as an energy supplement. The relationships between supplemental doses and therapeutic doses have not been clearly defined. Lipoic acid is not an essential nutrient, it has not been established by the "Recommended Daily Allowance" (RDA). In Germany, LA is approved as an anti-diabetes drug comorbidities since 1966 and is available by prescription.
LA is also used for various cases, such as liver or kidney diseases.
Some studies have indicated that LA can be beneficial for the heart or kidneys of hypertensive people, which is indicative that it is a great antioxidant. On the other hand, LA may increase, according to some studies, the synthesis of glutathione (an important intracellular antioxidant) by increasing the expression of γ-glutamylcysteine of ligase (GCL), the limitation of the enzyme's speed in the synthesis of glutathione and by increasing the cellular uptake of cysteine, an amino acid necessary for the synthesis of glutathione.
-According to the "American Cancer Society", "there is no reliable scientific evidence at this time to say that lipoic acid prevents the development or expansion of cancer." Despite this there are some studies that claim that lipoic acid can inhibit the proliferation of some tumors (such as breast or colon cancer). On the other hand, other studies say that it can be harmful for various types of cancer such as the one mentioned above, colon cancer. Therefore, it is said that the evidence is not enough to ensure that LA acts against cancer. -For peripheral diabetic neuropathy, intravenous administration of alpha-lipoic acid leads to short-term improvement, but there is no great evidence of a significant benefit when taken orally.
-A literary review, using studies available since January 2008, failed to find randomized controlled trials using lipoic acid for the treatment of dementia. Due to the lack of evidence, the use of lipoic acid could not be supported for the treatment of any of the forms of dementia.67 Despite this, there are studies that indicate the possibility that lipoic acid is a treatment option for the patient. Alzheimer's and other dementias.
-There is a slight evidence that lipoic acid can help to control the burning mouth syndrome, although some studies have also indicated that for the treatment of the syndrome it is necessary to complement the lipoic acid with psychological treatment. -There is no evidence that alpha lipoic acid helps people with mitochondrial disorders.
-There is limited evidence that lipoic acid may have potential as a drug for the treatment of multiple sclerosis.
Glutathione is not an essential nutrient, since it can be synthesized from the amino acids L-cysteine, L-glutamic acid and glycine. The sulfhydryl (thiol), group (SH) of cysteine, serves as an electron donor and is responsible for the biological activity of glutathione. The provision of this amino acid is the limiting factor in the synthesis of glutathione in cells because cysteine is rare in food products. On the other hand, if released, like the free amino acid, cysteine is toxic and spontaneously catabolizes in the gastrointestinal tract and the blood plasma. Glutathione is synthesized in two steps dependent on adenosine triphosphate:
• First, gamma-glutamylcysteine is synthesized from L-glutamate and cysteine through the enzyme gamma-glutamylcysteine synthetase (also known as Ligase glutamate-cysteine (GCL) ligase). This reaction is the limiting step in the synthesis of glutathione.
• Secondly, glycine is added to the C-terminal of gamma-glutamylcysteine through the enzyme glutathione synthetase. In animals and insects glutamate cysteine ligase (GCL) is a heterodimeric enzyme composed of a catalyst (GCLC) and modulating subunit (GCLM). The GCLC constitutes all the enzymatic activity, while the GCLM increases the catalytic efficiency of the GCLC. Mice lacking GCLC (ie, all new GSH synthesis) die before birth. Mice lacking GCLM do not demonstrate phenotype, but exhibit a marked decrease in GSH and greater sensitivity to toxics. Although all cells in the human body are capable of synthesizing glutathione, the synthesis of glutathione in the liver has been shown to be essential. After birth, mice with GCLC-induced genetic loss (ie, GSH synthesis) only in the liver die within 1 month of birth.
Glutamate cysteine ligase from plants (GCL) is a sensitive homodimeric redox enzyme, conserved in the plant kingdom. In an oxidizing environment intermolecular disulfide bridges are formed and the enzyme changes to the active dimeric state. The mean critical potential of the cysteine parella is - 318 mV.
In addition to the redox control is the GCL enzyme inhibited by GSH. The GCL is exclusively located in the plastids and the glutathione synthetase is in the plastids and the cytosol, therefore they are GSH and gamma-glutamylcisteína exported from the plastids. The two biosynthesis of glutathione enzymes are essential in plants. The route of glutathione biosynthesis is found in some bacteria, such as cyanobacteria and proteobacteria, but it is absent in many other bacteria. Most eukaryotes synthesize glutathione, including humans, but some do not, such as legumes, Entamoeba and Giardia.
In the reduced state, the thiol group of cysteine is capable of donating a reduction equivalent (H + + e-) to other unstable molecules, such as reactive oxygen species. When donating an electron, glutathione becomes reactive, but it quickly combines with another reactive glutathione to form glutathione disulfide (GSSG). This reaction is possible because glutathione is found in a relatively high proportion in cells (up to 5 mM in hepatocytes). GSH can be regenerated from GSSG by means of the enzyme glutathione reductase.
In healthy cells and tissues, more than 90% of total glutathione is in the reduced form (GSH) and less than 10% is in the disulfide form (GSSG). An increase in the ratio between GSSG and GSH is considered an indication of oxidative stress. Glutathione has multiple functions:
1. It is the largest endogenous antioxidant produced by the cells, participating directly in the neutralization of free radicals and reactive oxygen compounds, as well as in the maintenance of exogenous antioxidants, for example vitamins C and E, in their reduced forms (active ).
2. Through direct conjugation, it detoxifies many xenobiotics (foreign compounds) and carcinogens, both organic and inorganic. 3. It is essential for the immune system to be able to exert its full potential, for example, in the modulation of the presentation of antigens to lymphocytes, which influences the production of cytokines and the type of response (cellular or humoral) that is develops, is able to increase the proliferation of lymphocytes, which increases the magnitude of the response, also increase the elimination activity of cytotoxic T cells and NK cells, and the regulation of apoptosis, thus maintaining control of the immune response.
4. It plays a fundamental role in numerous metabolic and biochemical reactions such as DNA synthesis and repair, protein synthesis, prostaglandin synthesis, amino acid transport and enzyme activation. Therefore, all systems of the organism can be affected by the state of the glutathione system, especially the immune system, the nervous system, the gastrointestinal system and the lungs.
Supplementation has been difficult, since research suggests that oral glutathione is not well absorbed through the gastrointestinal tract. In a study of the acute oral administration of a very large dose (3 grams) of glutathione, Witschi and coworkers found that "it is not possible to increase the circulation of glutathione to a clinically beneficial degree with the oral administration of a single dose of glutathione. 3 g of glutathione However, at the end of the 70s, doctors Israil Brekhman (one of the parents of the adaptogens) and Raimundo Torres Díaz, created some compositions currently called "Reactor-20" and "Riendol", which make Glutathione through the "alveolar-pulmonary" route, which is equivalent to a vein injection since these products pass immediately into the bloodstream and the positive effects are much higher than those that are administered orally, since in The "digestive-intestinal" function loses a lot of the components, these two doctors (Brekhman and Torres) were the creators of the Immunotherapy-Adaptogens-Cubans in 1977.
However, plasma and liver concentrations of glutathione can be raised by oral administration of S-adenosyl-methionine (SAM) 242526 Cysteine-rich glutathione precursors include N-acetylcysteine (NAC) 2728 and undenatured serum protein, and these supplements have been shown to increase the glutathione content of the cell. N-acetylcysteine is available as a medication and as a generic supplement. Alpha lipoic acid has also been shown to restore intracellular glutathione.3738 Melatonin has been shown to stimulate a related enzyme, glutathione peroxidase, 39 and silymarin, a component of Silybum marianum (milk thistle), has also been shown to be able to to replenish glutathione levels. Of all these methods, the two methods that are most investigated for efficacy in increasing intracellular glutathione are variants of cysteine. N acetyl cysteine, which is a drug on the fight against drugs, and the consolidated cysteine as found in the nutraceuticals of undenatured whey protein, has been shown to be effective in increasing glutathione values.
Glutathione is an intracellular component strongly regulated and limited in its production due to the inhibition of negative feedback of its own synthesis through the enzyme gamma-synthetase glutamylcysteine, thus greatly reducing any possibility of overdose to a minimum. The increase of glutathione is a strategy to cope with the states of glutathione deficiency, high oxidative stress, immune deficiency, and overload of xenobiotics in which glutathione plays a role in the detoxification of the xenobiotics in question. The states of glutathione deficiency include, but are not limited to: HIV / AIDS, chemistry and infectious hepatitis, prostate cancer and other cancers, cataracts, Alzheimer's, Parkinson's, chronic obstructive pulmonary disease, asthma, radiation poisoning , states of malnutrition, arduous physical stress, aging, and has been associated with optimal immune sub-response. Many clinical pathologies are associated with oxidative stress and are detailed in numerous medical references. The level of low glutathione is also strongly involved in the wear and negative nitrogen balance, in particular, seen in cancer, AIDS, sepsis, trauma, burns and even sports overtraining. Oral administration of N-acetyl cysteine (NAC), a prodrug used to increase glutathione levels after an acetaminophen overdose, increases glutathione levels in patients infected with HIV and has been associated with longer survival of these.
The concentrations of glutathione in tumor cells are high and this may be an important factor in resistance to chemotherapy. Preliminary studies have shown that the state of antioxidants can affect the tolerance of children with lymphoblastic leukemia to chemotherapy. Other supplements (including TRAUMEEL S, glutamine, vitamin E, Immunocal and Glutacal, developed by pharmaceutical PiSA researchers) can help reduce the gastrointestinal toxicity of chemotherapy and radiation. Also the Immunotherapics-Adaptogens-Cubans developed in Cuba in the late 70s by doctors Israil Brekhman and Raimundo Torres Díaz (which are drugs currently authorized by Brussels for the entire European Community and very used by the Association of People Affected by Chemotherapies and Radioterapia www.asociacionafectados.com) are the ones with the highest content of Glutathione worldwide, since it also incorporates the precursors (Cysteine, Glycine and Glutamic Acid) and those that have more than 30 years of tests on the human being. Either way more conclusive evidence is necessary.
An in vitro test was carried out in 5 patients who had breast cancer with metastasis, one with pancreatic cancer and one with liver cancer, 30g of a concentrate of cow's milk serum was administered daily for 6 months. The study showed that at concentrations at which the whey concentrate induces the synthesis of glutathione in normal cells, it also caused a depletion and inhibition of glutathione in cancer cells. This indicated that the whey concentrate used can lower glutathione levels in tumor cells and make them more vulnerable to chemotherapy.