Functions of glutathione

When it is in reduced state, cysteine thiol gives the other unstable molecules a reducing equivalent, such as reactive oxygen species.After an electron given, glutathione becomes lively, so it is easy to form oxidized glutathione (GSSG) with other active glutathione. Because the content of glutathione is quite high in intracellular (up to 5mM in liver), this reaction may occur. GSSG can be reduced by glutathione reductase and re-generated the GSH.

In healthy cells and tissues, more than 90% of the pharmaceutical raw materials glutathione reduced form (GSH) exists, the remaining less than 10% of the oxidation state (GSSG) exists. GSSG using / GSH the ratio of increase is a sign of oxygen partial pressure increased. Glutathione has multiple functions, it is a major endogenous antioxidant produced by the cells directly involved in free radicals and reactive oxygen compounds in the same time maintaining exogenous antioxidants such as vitamins C and E to restore the state (active state) exists. It controls the cycle of NO, NO cycle life is critical, if not controlled will be a problem. It is used in metabolic reactions and biochemical reactions, such as DNA synthesis and repair, protein synthesis, prostaglandin chia seed synthesis, amino acid transport and enzyme activation. Therefore, the impact of the state of the glutathione system can be any system in the body, especially the immune system, nervous system, gastrointestinal system and lungs.

In the conjugate reaction and reduction, GSH is considered to be the enzyme substrate in the cytosolic, microsomal and mitochondrial glutathione S-transferase catalyzed. However, it can also participate in the non-enzyme conjugate and a number of chemical substances. For the case of NAPQI, when the GSH due to overdose of acetaminophen (paracetamol) is depleted, the reactive cytochrome P450 paracetamol (in the United States known as the retreat hot net) formation of the active metabolite will become toxic, this time, glutathione overdose is an important antidote. Glutathione and NAPQI is conjugated to its detoxification. In this case, it protects the cell protein thiol or sulfhydryl covalent change; all the GSH is depleted, NAPQI response and cell protein in this process, kill cells. The most commonly used treatment to deal with an overdose of this painkiller is the use of N-acetyl-L-cysteine (usually in a spray form), it is cell processing of L-cysteine, and used for GSH in re synthesis.

Glutathione involved in the synthesis of leukotrienes, and as a cofactor for glutathione peroxidase. As important hydrophilic molecules, lipophilic metabolites and toxins become a part of the bile, GSH hepatic biotransformation to be added to those toxic substances and metabolites. Glutathione the same for A and B two acid detoxification is necessary, consists of two acid is a metabolic byproduct.

In the cosmetics industry, glutathione becomes one melanin inhibitor. In some countries like Japan and Philippines, the products are called as whitening soaps. In the response of tyrosinase and levodopa, glutathione strongly inhibit the synthesis of melanin through stopping the combination between levodopa and tyrosinase. After the content of tyrosinase increases, inhibition of melanin synthesis is reversed. Although the syntheses of melanin are gathered within an hour, this concentration can be inhibited by the glutathione. These results suggest that GSH inhibit melanin synthesis and accumulation in blocking the function of levodopa.Source:http://www.cospcn.com