Glutathione (GSH) (GSH)

Glutathione is a vital tripeptide consisting of glutamate, cysteine, and glycine, serving as the most abundant low-molecular-weight thiol and primary endogenous antioxidant in mammalian cells (PubChem, CID 124886). It plays a fundamental role in maintaining cellular redox homeostasis by scavenging reactive oxygen species and acting as a cofactor for enzymes like glutathione peroxidase (NIH, StatPearls). Beyond its antioxidant capacity, glutathione is essential for the detoxification of xenobiotics and metabolic byproducts through conjugation reactions catalyzed by glutathione S-transferases (PubMed, PMID 24513447). In clinical contexts, glutathione levels are often dysregulated; for instance, depletion is associated with neurodegenerative conditions like Parkinson's disease and chronic liver injury, whereas elevated levels in malignant cells can confer resistance to chemotherapy and radiation (PubMed, PMID 11396606). Therapeutic interventions target this system either by replenishing the pool with precursors like N-acetylcysteine to treat toxicity or by depleting it to sensitize cancer cells to oxidative damage (PubMed, PMID 28263961).

Other names

L-gamma-glutamyl-L-cysteinyl-glycineReduced glutathioneEndogenous glutathione poolCellular redox system

Drugs modulate the glutathione pool by providing biosynthetic precursors (e.g., N-acetylcysteine), inhibiting rate-limiting enzymes like glutamate-cysteine ligase (e.g., buthionine sulfoximine), or inducing glutathione depletion through conjugation and export (e.g., acetaminophen or erastin-mediated ferroptosis induction).