Glutathione (Reduced) (GSH)

Glutathione (GSH) is a vital tripeptide consisting of glutamate, cysteine, and glycine, serving as the primary low-molecular-weight thiol and antioxidant in eukaryotic cells (PubChem CID 124886). It plays a critical role in maintaining cellular redox homeostasis by scavenging reactive oxygen species and acting as a cofactor for various enzymes, including glutathione peroxidases and glutathione S-transferases (PubMed: 22549109). In clinical contexts, GSH is central to the detoxification of drugs like acetaminophen; its depletion leads to oxidative stress and cell death, particularly in the liver (StatPearls: Acetaminophen Toxicity). Conversely, many cancer cells overexpress GSH to resist the pro-oxidant effects of chemotherapy and radiation, making the GSH biosynthetic pathway a target for chemosensitization (PubMed: 28263956). Therapeutic interventions include the use of N-acetylcysteine to boost GSH levels in cases of poisoning or respiratory disease, and inhibitors like buthionine sulfoximine to deplete the pool in experimental oncology.

Other names

L-Glutathionegamma-L-Glutamyl-L-cysteinylglycineReduced glutathioneGSH

Glutathione acts as a nucleophilic scavenger of reactive oxygen species and electrophilic xenobiotics, often catalyzed by glutathione peroxidases and glutathione S-transferases. Therapeutic modulation involves either replenishing the GSH pool via precursors to prevent oxidative damage or depleting it to overcome drug resistance in oncology.