- Lifts your mood
- Improves learning abilities
- Builds self esteem
- Keeps your brain fit
- Keeps your body fit and able
- Boost mental health
jueves, 29 de mayo de 2014
Excercise Benefits
miércoles, 4 de julio de 2012
Cysteine
Cysteine (abbreviated as Cys or C) is an α-amino acid with the chemical formula HO2CCH (NH2) CH2SH. Unaminoácido is not essential, which means that can be synthesized by humans. The codons encoding cysteine and are UGC UGU. The part of the chain where the cysteine is the thiol is nonpolar and thus cysteine are usually classified as a hydrophobic amino acid. The thiol side chain is often involved in enzymatic reactions, acting as a nucleophile. The thiol is susceptible to oxidation to yield the disulfide bridges of cysteine derivatives that have an important structural role in many proteins. Cysteine is also called cystine, but the latter is a dimer of two cysteines via a disulfide bridge.Content
Precursor of glutathione.
Food source
Although it is classified as a nonessential amino acid, in some cases, the cysteine may be essential for infants, elderly and people with certain metabolic diseases or suffering from malabsorption syndromes. Cysteine is normally synthesized by the body within normal physiological conditions, provided that sufficient hayametionina. Cysteine is potentially toxic and is catabolized in the digestive tract and blood plasma. Cysteine securely travels through the gastrointestinal tract and plasma and is rapidly reduced to the two cysteine molecules to enter the cell. Cysteine is the most high-protein foods, such as:
Animal Resources: pork, stuffed chicken, turkey, duck, sausage, eggs, milk, cottage cheese, yogurt.Plant resources: red peppers, garlic, onions, broccoli, Brussels sprouts, granola, wheat germ.Like other amino acids cysteine has an amphoteric character.(R)-cysteine (left) (S)-Cysteine (right) at a neutral pH zwitterion ionic.
Industrial source
L-Cysteine was obtained industrially by hydrolysis of hair keratin. But now the main route of obtaining this is by fermentation using a mutant of E. Coli. Wacker Chemie introduced a route from tiazonilos substituents. By this route the L-Cysteine is produced by hydrolysis of the racemic mixture of 2-amino-Δ2-tiazolin-4-carboxylico using thiazolinophilum Pseudomonas.
BiosynthesisSynthesis of cysteine.
Cysteine synthetase catalyzes the reaction beta upper and cystathionine gamma-lyase catalyzes the reaction below.In animals, the biosynthesis starts with the amino acid serine. The sulfur is derived from lametionina which is converted into homocysteine via the intermediate S-adenosilmetionina.Tras that the cystathionine beta-synthase combines homocysteine and serine to form cystathionine asymmetric thioether. The enzyme cystathionine gamma-lyase converts cystathionine to cysteine and alpha-ketobutirato. Plant and bacterial cysteine biosynthesis starts also from passing serine O-acetylserine become by action of the enzyme serine acetyltransferase (EC 2.3.1.30). The enzyme O-acetylserine (thiol)-lyase ((OAS-TL, EC 2.5.1.47), using sulfur as hydrogen sulfide, converts cysteine ester by displacement of the acetate.
Biological functionsThe thiol group of cysteine is nucleophilic and easily oxidized. The reactivity increases when the thiol is ionized and the cysteine residues in proteins have pH values near neutrality, as often found in a reactive thiols in the cell. Due to its high reactivity, the thiol group of cysteine has numerous biological functions.Antioxidant glutathione precursorDue to the ability of thiols undergo redox reactions, cysteine has antioxidant properties. These antioxidant properties of cysteine are mainly expressed in glutathione tripeptides that occur in humans and other organisms. Systemic availability of oral glutathione (GSH) is negligible, this must be biosynthesized from the amino acids that constitute 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.DisulfideDisulfide bridges play an important role in the assembly and stability of some proteins normally secreted proteins into the extracellular medium. Since most cell compartments are reduced means, the disulfide bridges are generally unstable in the cytosol, with certain exceptions we see below.Protein disulfide bridges are formed by oxidation of thiol groups of cysteine residues. The other amino acids also contain sulfur, such as methionine can not form disulfide bridges. Very aggressive oxidants convert cysteine into the corresponding acid and sulfonic acid sulfánico. Cysteine residues have a valuable role in cross-linked proteins, as it increases the rigidity of proteins and confers resistance to proteolytic. Within the cell, the disulfide bridges between cysteine residues support acting in the secondary structure of polypeptides. Insulin is an example of crosslinked protein with cysteines, wherein two separate peptide chains are connected by a pair of bridges disulfuros.Las protein disulfide isomerases catalyze the formation of disulfide bridges itself, the cell transfers dehydroascorbic acid into the endoplasmic reticulum. In nature, the cysteines are generally oxidized to cystine their only function is nucleophilic.Figure 2: Cystine (as neutral) is derived from two molecules of cysteine. Forming a disulfide bridge.Group precursors iron-sulfurCysteine is an important source of sulfur in human metabolism. Sulfur from the iron-sulfur groups and nitrogenases is extracted from cysteine and alanine passes into the process.Metal ion bindingApart from the iron-sulfur-proteins, many other metal cofactors of enzymes are unions for the substituent of the thiol of the cysteine residues. Examples include zinc in zinc finger and alcohol dehydrogenase, the blue copper proteins cuprous, iron in cytochrome P450 and nickel in [NiFe]-hydrogenase. The thiol group also has high affinity to heavy metals, so that cysteine-containing proteins such as metallothionein linking metals such as [[mercury], lead and cadmiofuerte.Posttranslational modificationsApart from its oxidation to cystine, cysteine participates in numerous posttranslational modifications. The nucleophilic thiol group of cysteine conjugate allows other groups, such as the prenylation, ubiquitin ligases transferring ubiquitin to its pendant, proteins and caspases involved in apoptotic proteolysis in the cycle. The inteínas (protein introns) normally act to help the catalytic cysteine. These papers are typically limited to cysteine intracellular environment, where the medium is reduced and cysteine is not oxidized cystine.Other metabolitesThe product of decarboxylation of cysteine cysteamine is a biogenic amine that is a fundamental component of coenzyme A. The product of transamination of cysteine is the mercaptopyruvate, which can be degraded to pyruvate or reduced by various routes mercaptolactato possible, depending on the organism. Many microorganisms and plants cyanide anions attached by nucleophilic substitution with the sulfhydryl to give as product cyanoalanine, which can be hydrolyzed to aspartate. The sulfur of cysteine can be methylated to get a homologue of methionine called S-methyl.
Precursor of glutathione.
Food source
Although it is classified as a nonessential amino acid, in some cases, the cysteine may be essential for infants, elderly and people with certain metabolic diseases or suffering from malabsorption syndromes. Cysteine is normally synthesized by the body within normal physiological conditions, provided that sufficient hayametionina. Cysteine is potentially toxic and is catabolized in the digestive tract and blood plasma. Cysteine securely travels through the gastrointestinal tract and plasma and is rapidly reduced to the two cysteine molecules to enter the cell. Cysteine is the most high-protein foods, such as:
Animal Resources: pork, stuffed chicken, turkey, duck, sausage, eggs, milk, cottage cheese, yogurt.Plant resources: red peppers, garlic, onions, broccoli, Brussels sprouts, granola, wheat germ.Like other amino acids cysteine has an amphoteric character.(R)-cysteine (left) (S)-Cysteine (right) at a neutral pH zwitterion ionic.
Industrial source
L-Cysteine was obtained industrially by hydrolysis of hair keratin. But now the main route of obtaining this is by fermentation using a mutant of E. Coli. Wacker Chemie introduced a route from tiazonilos substituents. By this route the L-Cysteine is produced by hydrolysis of the racemic mixture of 2-amino-Δ2-tiazolin-4-carboxylico using thiazolinophilum Pseudomonas.
BiosynthesisSynthesis of cysteine.
Cysteine synthetase catalyzes the reaction beta upper and cystathionine gamma-lyase catalyzes the reaction below.In animals, the biosynthesis starts with the amino acid serine. The sulfur is derived from lametionina which is converted into homocysteine via the intermediate S-adenosilmetionina.Tras that the cystathionine beta-synthase combines homocysteine and serine to form cystathionine asymmetric thioether. The enzyme cystathionine gamma-lyase converts cystathionine to cysteine and alpha-ketobutirato. Plant and bacterial cysteine biosynthesis starts also from passing serine O-acetylserine become by action of the enzyme serine acetyltransferase (EC 2.3.1.30). The enzyme O-acetylserine (thiol)-lyase ((OAS-TL, EC 2.5.1.47), using sulfur as hydrogen sulfide, converts cysteine ester by displacement of the acetate.
Biological functionsThe thiol group of cysteine is nucleophilic and easily oxidized. The reactivity increases when the thiol is ionized and the cysteine residues in proteins have pH values near neutrality, as often found in a reactive thiols in the cell. Due to its high reactivity, the thiol group of cysteine has numerous biological functions.Antioxidant glutathione precursorDue to the ability of thiols undergo redox reactions, cysteine has antioxidant properties. These antioxidant properties of cysteine are mainly expressed in glutathione tripeptides that occur in humans and other organisms. Systemic availability of oral glutathione (GSH) is negligible, this must be biosynthesized from the amino acids that constitute 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.DisulfideDisulfide bridges play an important role in the assembly and stability of some proteins normally secreted proteins into the extracellular medium. Since most cell compartments are reduced means, the disulfide bridges are generally unstable in the cytosol, with certain exceptions we see below.Protein disulfide bridges are formed by oxidation of thiol groups of cysteine residues. The other amino acids also contain sulfur, such as methionine can not form disulfide bridges. Very aggressive oxidants convert cysteine into the corresponding acid and sulfonic acid sulfánico. Cysteine residues have a valuable role in cross-linked proteins, as it increases the rigidity of proteins and confers resistance to proteolytic. Within the cell, the disulfide bridges between cysteine residues support acting in the secondary structure of polypeptides. Insulin is an example of crosslinked protein with cysteines, wherein two separate peptide chains are connected by a pair of bridges disulfuros.Las protein disulfide isomerases catalyze the formation of disulfide bridges itself, the cell transfers dehydroascorbic acid into the endoplasmic reticulum. In nature, the cysteines are generally oxidized to cystine their only function is nucleophilic.Figure 2: Cystine (as neutral) is derived from two molecules of cysteine. Forming a disulfide bridge.Group precursors iron-sulfurCysteine is an important source of sulfur in human metabolism. Sulfur from the iron-sulfur groups and nitrogenases is extracted from cysteine and alanine passes into the process.Metal ion bindingApart from the iron-sulfur-proteins, many other metal cofactors of enzymes are unions for the substituent of the thiol of the cysteine residues. Examples include zinc in zinc finger and alcohol dehydrogenase, the blue copper proteins cuprous, iron in cytochrome P450 and nickel in [NiFe]-hydrogenase. The thiol group also has high affinity to heavy metals, so that cysteine-containing proteins such as metallothionein linking metals such as [[mercury], lead and cadmiofuerte.Posttranslational modificationsApart from its oxidation to cystine, cysteine participates in numerous posttranslational modifications. The nucleophilic thiol group of cysteine conjugate allows other groups, such as the prenylation, ubiquitin ligases transferring ubiquitin to its pendant, proteins and caspases involved in apoptotic proteolysis in the cycle. The inteínas (protein introns) normally act to help the catalytic cysteine. These papers are typically limited to cysteine intracellular environment, where the medium is reduced and cysteine is not oxidized cystine.Other metabolitesThe product of decarboxylation of cysteine cysteamine is a biogenic amine that is a fundamental component of coenzyme A. The product of transamination of cysteine is the mercaptopyruvate, which can be degraded to pyruvate or reduced by various routes mercaptolactato possible, depending on the organism. Many microorganisms and plants cyanide anions attached by nucleophilic substitution with the sulfhydryl to give as product cyanoalanine, which can be hydrolyzed to aspartate. The sulfur of cysteine can be methylated to get a homologue of methionine called S-methyl.
CellGevity Side Effects, and Max GXL and MaxOne
Max International products have no side effects and can interact with medications. As the process of toxin extraction occurs within the cell, many people experience detox symptoms directly related to this process.
The typical reaction to this process to expel toxins, involves a cold-like symptoms, but not limited only to this, you can also include headache, sore throat, feeling of fever, muscle aches and fatigue. These symptoms do not occur in all individuals, but rather those who are intoxicated and full of free radicals.
For those going through the process of detox after using MaxGXL, CellGevity MaxOne and is recommended to lower the dose is taken with sufficient water, food and gradually increase the daily dose but never stop using them.
In some people, detox symptoms may not occur may not occur until after several weeks or months. And for those exposed to toxins, bacteria and / or viruses often symptoms may recur until the supplement Maximise the cell level, since it is a cleansing process within the cell. If this happens again it is recommended that lower the dose level that reduce symptoms and increase gradually to the normal dose.
It is very important to understand that the body uses water as the primary means to expel all these toxins. For this reason, it is recommended that you take 1/2 oz. of water per pound of body weight. The goal is to exercise our patience and understand that once our cells are free of toxins will work optimally. The perfect combination for our cells are CellGevity, Max N-Fuze and Max Atp.
Glutathione and the Immune System
Glutathione and the Immune System
It is surprising how many people still believe that you get the flu from taking cold or leave the house with wet hair. It is common knowledge that is a fact that flu is a contagious and transmissible. Although many think so, do not get sick of influenza expose to cold air. These beliefs are deeply ingrained in our culture. However, the reality is that we get sick of the flu when you are exposed directly to the virus that causes this disease.
Some people tend to blame their flu to the fact of being very stressed, overworked, or have done too much exercise. These people are closer to the truth. Because although these factors alone do not cause the flu, if we become more susceptible to contracting the virus. In striving for more and stressed, these people lower their immune resources and suffer for it - the virus overcomes her defenses. Most doctor visits are the result of the immune system has failed to deal with a specific threat. The good news is that the immune system can be improved.
Very few people realize this, even those who are always concerned with their welfare. Many of us know how to care for our heart and muscles, but very few will pay attention to our immune system, although this represents our first line of defense against all infections and destructive attacks. To maintain a good immune response should do regular exercise (45-60 minutes 3 times per week), eating regularly and varied, maintaining an ideal weight, sleep on a regular basis (8 hours for young adults, less for people seniors), supplement their diet with vitamins, minerals and micronutrients, to avoid unnecessary stress, and, although it sounds funny, laugh a lot. We should also avoid exposure to radiation and toxins, abuse of snuff, alcohol and caffeine, as well as unnecessary use of antibiotics and steroids.
The immune defense system is extraordinarily sophisticated. Microscopic examination of any part of the body immune system shows dealing with microorganisms such as bacteria, parasites and fungi, and that's just within the body. The environment which we take the air we breathe and the water and the food we eat are also saturated with microorganisms. It's amazing that we survive in spite of all this.
Usually, only consulted a doctor once said that a disease control over us. Often, the doctor launches an attack strategy with antibiotics, antiviral compounds, or chemotherapy, trying to eliminate the invaders. Despite the side effects, this offensive strategy has proved highly effective treatment. It is the best way we've found to fight the war.
However, it is preferable to avoid war, after all, the battlefield is our body. Even when drugs win the battle, the damage remains. Side effects of drugs and the after-effects of chemotherapy can be described as random destruction resulting in the deaths of many innocents. We can not overemphasize the importance of defensive strategy - preventive medicine to stop the invaders before they are established in the body and thus avoids conflict. An immune system to optimal performance is undoubtedly the best prevention. We can achieve this type of operation nurturing and nourishing our immune system the same way we feed the rest of our body.
The Immune Response
The immune response search, identify, and attack microorganisms, allergens, cancer cells and dead tissue, which together are known as antigens. The reaction of the body is known as antigenic response.
When a pathogen enters the bloodstream and activate immune cells. Different types of cells such as polymorphonuclear cells that form the pus. These huge cells simply surround and digest pathogens. Lymphocytes smaller and more sophisticated, are responsible for the pathogen to adapt a specific defense for them.
B cells identify pathogens and mark them for the T lymphocyte attack. Helper T cells alert the immune cells to these are added to the battle, killer T cells kill the intruder, and suppressor T cells are responsible for turning off the immune response once the job is done.
However, the healthy immune response can be compromised, ie, tends to deteriorate. You may find too few immune cells, the cells themselves may be incompetent, or may be defeated by a pathogen more powerful than them. In most cases, the side of adaptive immune system can identify and subsequently remember the chemical signature of a particular pathogen and is capable of dealing with the next time you have to face it. This leads to a full or partial immunity. For example, you can only get smallpox again in life.
The immune system is impressive but not infallible. Sometimes it can react to threats as if they were not, and normal mechanisms as if they attack the body. We want our immune response protects us against infections, ignore harmless substances, accept organs have been transplanted, not attack our own bodies and protect us against carcinogens and tumor growth. We want to avoid recurrent infections, allergic reactions to harmless substances, rejection of transplanted organs that have been, autoimmune disease in which the body attacks its own systems, and cancer.
The two least desirable immune responses are autoimmune diseases and allergies. In an autoimmune disease the body mistakes normal tissue with a foreign antigen and attack him, leading to the destruction of healthy tissue. In the case of allergies, the immune system mistakes a harmless substance with harmful and responds with aggressive reaction, and sometimes fatal. Some autoimmune diseases are:
• Lupus
• Myasthenia Gravis
• Chronic Fatigue Syndrome
• Rheumatoid Arthritis
• Multiple Sclerosis
• Polymyositis
• Escloeroderma
• Lou Gehrig's Disease
• Grave's Disease
• Crohn's Disease
The Immune System and Glutathione
Our count of polymorphonuclear cells and lymphocytes in the previous section covers only part of the immune system. B-cell lymphocytes comprise 10% of lymphocytes circulating in the body, and work to release immunoglobulins to attack and destroy invading pathogens. Approximately 80% of lymphocytes in the body are T cells When these cells are disturbed, the doors open to infection and health is compromised. For example, the Human Immunodeficiency Virus (HIV) destroys helper T cells and leaves cut off killer T cells and powerless. As a result, invading microorganisms which normally dissipate body are capable of causing severe infections that characterize AIDS.
Glutathione plays a crucial role in the functioning of immune cells. Dr. Gustavo Bounous, a leading expert in the study of glutathione says, "The limiting factor in the proper activity of our cells is the availability of glutathione." This concept is clearly evident in the Human Immunodeficiency Virus or HIV-the cause AIDS.
In essence, AIDS is a dysfunction of T cell lymphocytes Patients suffering from this disease usually show low levels of glutathione, especially in the count of glutathione in T cell lymphocytes Several studies have shown that GSH levels may be indicators that show the possibilities of survival and quality of life of AIDS patients.
The growth and healthy cell activity is directly dependent on the availability of GSH. The experimental reduction of GSH levels showed severely diminish the ability of immune cells to fight pathogens which leaves the door open to disease. In several studies, either glutathione intracellular levels correspond directly to the effectiveness of the immune response. In a way, GSH is a type of food for the immune system.
In some autoimmune diseases such as rheumatoid arthritis, lupus (SLE) and in the normal process of aging, T-cell lymphocytes show a poor immune response to invading antigens. Additionally, these chronic inflammatory conditions have been associated with low levels of glutathione in the blood serum and red blood cells.
A lymphocyte is attacking a pathogen by releasing a powerful chemical oxidant such as peroxide, and lymphocyte protects itself with neutralizing glutathione. Also, the cells must replicate themselves over and over again (monoclonal expansion) to attack the pathogen population as a whole. This process requires the use of additional oxygen and the release of oxidants. To achieve an efficient and continuous replication requires the use of GSH to counteract the effects of oxidation. So the fight infection consumes GSH in two ways-by using it to stabilize free radicals and to produce immune cells. This is apparent in acute infections such as bacterial pneumonia. In chronic infections such as hepatitis C or AIDS, wasting in GSH levels is even more pronounced. Recent studies have shown that elevated levels of GSH allows the immune system deal with these infections more effectively.
Dr. Gustavo Bounous and his team of researchers from McGill University measured the immune response in animals who were fed protein isolate rich in glutathione precursors (which was later called Immunocal). These animals showed both intracellular GSH levels higher, as a more effective response to immune threats. Interestingly, other animals who were fed a similar protein to casein did not benefit from the same way.
So the protective activity of glutathione has two functions, strengthens the immune cell function and also functions as an antioxidant within them.
An alarming number of bacterial infections resistant to antibiotics such as disease that eats away the skin, vancomycin-resistant enterococci, and methicillin-resistant staph have come to our hospitals and communities. Some health professionals believe that the causative virus such as AIDS and Hepatitis C are just the tip of the iceberg, and that a new wave of emerging pathogens is underway. Ancient evils, such as tuberculosis, which are believed to have been eradicated have returned with greater force and are no longer susceptible to treatments that previously worked to counter them. The strengthening our GSH levels is a convenient way to prepare to defend against these threats evident.
Conclusion
The immune system uses various types of cells to fight infections and other threats and growth and healthy functioning of these cells depends on the availability of GSH. Glutathione is found in the center of all immunological processes and having low GSH levels is common in many diseases, especially AIDS which is characterized by a severely compromised immune system.Raising and maintaining GSH levels can minimize the risk of these diseases. Although only people who are severely ill show a deficiency in GSH levels, those with stable health may also benefit from supplementation of GSH, especially in these days when we are so exposed as never before to environmental toxins and drug-resistant bacteria.Undoubtedly, the best form of preventive medicine is an immune system in optimal performance and the best way to optimize this system by feeding GSH to provide the body with the precursors for synthesis. -Dr. Jewel
It is surprising how many people still believe that you get the flu from taking cold or leave the house with wet hair. It is common knowledge that is a fact that flu is a contagious and transmissible. Although many think so, do not get sick of influenza expose to cold air. These beliefs are deeply ingrained in our culture. However, the reality is that we get sick of the flu when you are exposed directly to the virus that causes this disease.
Some people tend to blame their flu to the fact of being very stressed, overworked, or have done too much exercise. These people are closer to the truth. Because although these factors alone do not cause the flu, if we become more susceptible to contracting the virus. In striving for more and stressed, these people lower their immune resources and suffer for it - the virus overcomes her defenses. Most doctor visits are the result of the immune system has failed to deal with a specific threat. The good news is that the immune system can be improved.
Very few people realize this, even those who are always concerned with their welfare. Many of us know how to care for our heart and muscles, but very few will pay attention to our immune system, although this represents our first line of defense against all infections and destructive attacks. To maintain a good immune response should do regular exercise (45-60 minutes 3 times per week), eating regularly and varied, maintaining an ideal weight, sleep on a regular basis (8 hours for young adults, less for people seniors), supplement their diet with vitamins, minerals and micronutrients, to avoid unnecessary stress, and, although it sounds funny, laugh a lot. We should also avoid exposure to radiation and toxins, abuse of snuff, alcohol and caffeine, as well as unnecessary use of antibiotics and steroids.
The immune defense system is extraordinarily sophisticated. Microscopic examination of any part of the body immune system shows dealing with microorganisms such as bacteria, parasites and fungi, and that's just within the body. The environment which we take the air we breathe and the water and the food we eat are also saturated with microorganisms. It's amazing that we survive in spite of all this.
Usually, only consulted a doctor once said that a disease control over us. Often, the doctor launches an attack strategy with antibiotics, antiviral compounds, or chemotherapy, trying to eliminate the invaders. Despite the side effects, this offensive strategy has proved highly effective treatment. It is the best way we've found to fight the war.
However, it is preferable to avoid war, after all, the battlefield is our body. Even when drugs win the battle, the damage remains. Side effects of drugs and the after-effects of chemotherapy can be described as random destruction resulting in the deaths of many innocents. We can not overemphasize the importance of defensive strategy - preventive medicine to stop the invaders before they are established in the body and thus avoids conflict. An immune system to optimal performance is undoubtedly the best prevention. We can achieve this type of operation nurturing and nourishing our immune system the same way we feed the rest of our body.
The Immune Response
The immune response search, identify, and attack microorganisms, allergens, cancer cells and dead tissue, which together are known as antigens. The reaction of the body is known as antigenic response.
When a pathogen enters the bloodstream and activate immune cells. Different types of cells such as polymorphonuclear cells that form the pus. These huge cells simply surround and digest pathogens. Lymphocytes smaller and more sophisticated, are responsible for the pathogen to adapt a specific defense for them.
B cells identify pathogens and mark them for the T lymphocyte attack. Helper T cells alert the immune cells to these are added to the battle, killer T cells kill the intruder, and suppressor T cells are responsible for turning off the immune response once the job is done.
However, the healthy immune response can be compromised, ie, tends to deteriorate. You may find too few immune cells, the cells themselves may be incompetent, or may be defeated by a pathogen more powerful than them. In most cases, the side of adaptive immune system can identify and subsequently remember the chemical signature of a particular pathogen and is capable of dealing with the next time you have to face it. This leads to a full or partial immunity. For example, you can only get smallpox again in life.
The immune system is impressive but not infallible. Sometimes it can react to threats as if they were not, and normal mechanisms as if they attack the body. We want our immune response protects us against infections, ignore harmless substances, accept organs have been transplanted, not attack our own bodies and protect us against carcinogens and tumor growth. We want to avoid recurrent infections, allergic reactions to harmless substances, rejection of transplanted organs that have been, autoimmune disease in which the body attacks its own systems, and cancer.
The two least desirable immune responses are autoimmune diseases and allergies. In an autoimmune disease the body mistakes normal tissue with a foreign antigen and attack him, leading to the destruction of healthy tissue. In the case of allergies, the immune system mistakes a harmless substance with harmful and responds with aggressive reaction, and sometimes fatal. Some autoimmune diseases are:
• Lupus
• Myasthenia Gravis
• Chronic Fatigue Syndrome
• Rheumatoid Arthritis
• Multiple Sclerosis
• Polymyositis
• Escloeroderma
• Lou Gehrig's Disease
• Grave's Disease
• Crohn's Disease
The Immune System and Glutathione
Our count of polymorphonuclear cells and lymphocytes in the previous section covers only part of the immune system. B-cell lymphocytes comprise 10% of lymphocytes circulating in the body, and work to release immunoglobulins to attack and destroy invading pathogens. Approximately 80% of lymphocytes in the body are T cells When these cells are disturbed, the doors open to infection and health is compromised. For example, the Human Immunodeficiency Virus (HIV) destroys helper T cells and leaves cut off killer T cells and powerless. As a result, invading microorganisms which normally dissipate body are capable of causing severe infections that characterize AIDS.
Glutathione plays a crucial role in the functioning of immune cells. Dr. Gustavo Bounous, a leading expert in the study of glutathione says, "The limiting factor in the proper activity of our cells is the availability of glutathione." This concept is clearly evident in the Human Immunodeficiency Virus or HIV-the cause AIDS.
In essence, AIDS is a dysfunction of T cell lymphocytes Patients suffering from this disease usually show low levels of glutathione, especially in the count of glutathione in T cell lymphocytes Several studies have shown that GSH levels may be indicators that show the possibilities of survival and quality of life of AIDS patients.
The growth and healthy cell activity is directly dependent on the availability of GSH. The experimental reduction of GSH levels showed severely diminish the ability of immune cells to fight pathogens which leaves the door open to disease. In several studies, either glutathione intracellular levels correspond directly to the effectiveness of the immune response. In a way, GSH is a type of food for the immune system.
In some autoimmune diseases such as rheumatoid arthritis, lupus (SLE) and in the normal process of aging, T-cell lymphocytes show a poor immune response to invading antigens. Additionally, these chronic inflammatory conditions have been associated with low levels of glutathione in the blood serum and red blood cells.
A lymphocyte is attacking a pathogen by releasing a powerful chemical oxidant such as peroxide, and lymphocyte protects itself with neutralizing glutathione. Also, the cells must replicate themselves over and over again (monoclonal expansion) to attack the pathogen population as a whole. This process requires the use of additional oxygen and the release of oxidants. To achieve an efficient and continuous replication requires the use of GSH to counteract the effects of oxidation. So the fight infection consumes GSH in two ways-by using it to stabilize free radicals and to produce immune cells. This is apparent in acute infections such as bacterial pneumonia. In chronic infections such as hepatitis C or AIDS, wasting in GSH levels is even more pronounced. Recent studies have shown that elevated levels of GSH allows the immune system deal with these infections more effectively.
Dr. Gustavo Bounous and his team of researchers from McGill University measured the immune response in animals who were fed protein isolate rich in glutathione precursors (which was later called Immunocal). These animals showed both intracellular GSH levels higher, as a more effective response to immune threats. Interestingly, other animals who were fed a similar protein to casein did not benefit from the same way.
So the protective activity of glutathione has two functions, strengthens the immune cell function and also functions as an antioxidant within them.
An alarming number of bacterial infections resistant to antibiotics such as disease that eats away the skin, vancomycin-resistant enterococci, and methicillin-resistant staph have come to our hospitals and communities. Some health professionals believe that the causative virus such as AIDS and Hepatitis C are just the tip of the iceberg, and that a new wave of emerging pathogens is underway. Ancient evils, such as tuberculosis, which are believed to have been eradicated have returned with greater force and are no longer susceptible to treatments that previously worked to counter them. The strengthening our GSH levels is a convenient way to prepare to defend against these threats evident.
Conclusion
The immune system uses various types of cells to fight infections and other threats and growth and healthy functioning of these cells depends on the availability of GSH. Glutathione is found in the center of all immunological processes and having low GSH levels is common in many diseases, especially AIDS which is characterized by a severely compromised immune system.Raising and maintaining GSH levels can minimize the risk of these diseases. Although only people who are severely ill show a deficiency in GSH levels, those with stable health may also benefit from supplementation of GSH, especially in these days when we are so exposed as never before to environmental toxins and drug-resistant bacteria.Undoubtedly, the best form of preventive medicine is an immune system in optimal performance and the best way to optimize this system by feeding GSH to provide the body with the precursors for synthesis. -Dr. Jewel
Role of Glutathione
Glutathione is a tripeptide which is processed intracellularly from its constituent amino acids: L glutamate, L-cysteine and glycine. The group of the sulfhydryl (SH) (thiol) of cysteine is responsible for the biological activity of glutathione. The limiting factor in glutathione synthesis is the supply of this amino acid in cells whose presence in food is very difficult to achieve. The disulphide bond in the cysteine is resistant to pepsin and trypsin but can be broken by heat, with low pH or by mechanical stress releasing unlinked cysteine. When subjected to heat or violent mechanical processes (inherent to most extraction processes), the fragile bonds between peptides bisulfates break and the bioavailability of cysteine decreases considerably. Glutathione is a highly regulated intracellular constituent and its production is limited by the negative feedback inhibition of its own synthesis by the enzyme synthetase glutamylcystine range, thereby minimizing any possibility of overdose. Write to saludymax@gmail.com
Glutathione plays multiple roles:1. Is the main endogenous antioxidant produced by the cells participating directly in the neutralization of free radicals and reactive oxygen compounds, as well as maintaining exogenous antioxidants such as vitamins C and E in their reduced forms (active).2. Through direct conjugation, it detoxifies various xenobiotics (foreign compounds) and carcinogens, both organic and inorganic. Write to saludymax@gmail.com.
It is essential for the immune system works to its full potential, ie, (1) modulating antigen presentation to lymphocytes and therefore influences the production of cytokines and the type of response (cellular or humoral) that develops , (2) enhances lymphocyte proliferation and thus increases the magnitude of response, (3) enhances the killing activity of cytotoxic T cells and NK (4) regulating apoptosis, thereby maintaining control of the immune response. Write to saludymax@gmail.com.
Plays a fundamental role in numerous metabolic and biochemical reactions such as synthesis and DNA repair synthesis of proteins, amino acid transport and activation of the enzymes. Therefore, each system of our body can be affected by the state of glutathione system, especially the immune system, nervous system, gastrointestinal system and lungs.
Glutathione plays multiple roles:1. Is the main endogenous antioxidant produced by the cells participating directly in the neutralization of free radicals and reactive oxygen compounds, as well as maintaining exogenous antioxidants such as vitamins C and E in their reduced forms (active).2. Through direct conjugation, it detoxifies various xenobiotics (foreign compounds) and carcinogens, both organic and inorganic. Write to saludymax@gmail.com.
It is essential for the immune system works to its full potential, ie, (1) modulating antigen presentation to lymphocytes and therefore influences the production of cytokines and the type of response (cellular or humoral) that develops , (2) enhances lymphocyte proliferation and thus increases the magnitude of response, (3) enhances the killing activity of cytotoxic T cells and NK (4) regulating apoptosis, thereby maintaining control of the immune response. Write to saludymax@gmail.com.
Plays a fundamental role in numerous metabolic and biochemical reactions such as synthesis and DNA repair synthesis of proteins, amino acid transport and activation of the enzymes. Therefore, each system of our body can be affected by the state of glutathione system, especially the immune system, nervous system, gastrointestinal system and lungs.
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