What is Glutathione?
Glutathione (GSH) is an endogenous tripeptide composed of three amino acids that occurs naturally in cells. It plays a role as a skin lightener, in human metabolites, in Escherichia coli metabolites, in mouse metabolites, as an anti-aging agent, antioxidant, and cofactor.
Glutathione is a tripeptide composed of three amino acids, cysteine, glycine, and glutamate, which exist in the cell in two forms: reduced and oxidized, and is a very powerful antioxidant. It serves as one of the main antioxidant defense systems in living organisms and plays a critical role in maintaining cellular redox balance.
Glutathione is an antioxidant that directly scavenges various oxidants such as superoxide anion, hydroxyl radical, nitric oxide, and carbon radicals. It is a cofactor for many antioxidants. It plays a role in the regeneration of vitamin C and vitamin E. It neutralizes free radicals produced by chemical toxins of liver metabolism. It is involved in the transport of mercury from cells and the brain. It is crucial for the regulation of cellular proliferation and apoptosis, as well as for mitochondrial function and mitochondrial DNA formation.
Glutathione actively participates in many biological processes such as oxidative stress responses, detoxification mechanisms, and the regulation of cellular homeostasis. In the field of research, glutathione is an important reference peptide frequently used in the study of antioxidant mechanisms, modeling of cellular stress responses, and redox biochemistry studies.
Structure
Glutathione has a unique peptide structure containing a γ-glutamyl bond. This structural feature distinguishes it from classical peptides and forms the basis of its biological activity. The molecule can undergo transformation between reduced (GSH) and oxidized (GSSG) forms.
Molecular Sequence: γ-L-Glutamyl – L-Cysteine – Glycine
The thiol (-SH) group of the cysteine amino acid in this sequence is the main determinant of glutathione's antioxidant properties.
Biological Identification: H-ꝩGlu-Cys-Gly-OH
Molecular Formula: C₁₀H₁₇N₃O₆S
Molecular Weight: 307.33 g/mol
PubChem CID: 124886
CAS Number: 70-18-8
Synonyms:
• Reduced Glutathione
• GSH
• L-Glutathione reduced,
• γ-L-Glutamyl-L-cysteinyl-glycine
MeSH (Medical Subject Headings) Pharmacological Classification
• Antioxidants
• Detoxifying Agents
Glutathione is a tripeptide with numerous biological roles in cells.
• It conjugates with drugs and xenobiotics (especially via glutathione S-transferases), making these compounds more water-soluble and facilitating their excretion.
• It acts as a cofactor or auxiliary molecule in some enzymatic reactions.
• It contributes to the proper folding and maintenance of protein functions by playing a role in the rearrangement of protein disulfide bonds.
• It reduces peroxides and reactive oxygen species, thus playing an important role in the control of cellular oxidative stress.
ATC Code:
V Drugs Used for Different Purposes
V03 All Other Therapeutic Products
V03A All Other Therapeutic Products
V03AB Antidotes
V03AB32 Glutathione
Mechanism of Action
Human metabolite: Glutathione is naturally synthesized in human cells and plays an active role in metabolic processes.
Escherichia coli metabolite: Glutathione is a molecule that is also biosynthesized and used in bacteria such as E. coli. Therefore, it is used as a reference in recombinant and biotechnological studies.
Mouse metabolite: Since glutathione is found as an endogenous metabolite in animals, it is studied in experimental animal models (e.g., mice).
Glutathione (GSH) participates in leukotriene synthesis and is a cofactor for the enzyme glutathione peroxidase. It also plays a role in the hepatic biotransformation and detoxification process; it acts as a hydrophilic molecule that is added to other lipophilic toxins or wastes prior to entering biliary excretion. It participates in the detoxification of methylglyoxal, a toxic by-product of metabolism, mediated by glyoxalase enzymes. Glyoxalase I catalyzes the conversion of methylglyoxal and reduced glutathione to S-D-Lactoyl-glutathione. Glyoxalase II catalyzes the conversion of S-D-Lactoyl Glutathione to Reduced Glutathione and D-lactate. Glyoxalase I catalyzes the conversion of methylglyoxal and reduced glutathione to S-D-Lactoyl-glutathione. Glyoxalase II catalyzes the conversion of S-D-Lactoyl Glutathione to Reduced Glutathione and D-lactate. GSH is a cofactor of conjugation and reduction reactions that are catalyzed by glutathione S-transferase enzymes expressed in the cytosol, microsomes, and mitochondria. However, it is capable of participating in non-enzymatic conjugation with some chemicals, as it is hypothesized to do to a significant extent with n-acetyl-p-benzoquinone imine (NAPQI), the reactive cytochrome P450 reactive metabolite formed by toxic overdose of acetaminophen. Glutathione in this capacity binds to NAPQI as a suicide substrate and in the process detoxifies it, taking the place of cellular protein sulfhydryl groups which would otherwise be toxically adducted. The preferred medical treatment to an overdose of this nature, whose efficacy has been consistently supported in literature, is the administration (usually in atomized form) of N-acetylcysteine, which is used by cells to replace spent GSSG and allow a usable GSH pool.
A The glutathione information in this library is provided for research use only and does not constitute a claim for clinical or therapeutic use.
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References
https://pubchem.ncbi.nlm.nih.gov/compound/Glutathione
