Reduced glutathione (GSH) (GSH)

Reduced glutathione (GSH) is a ubiquitous tripeptide (gamma-glutamyl-cysteinyl-glycine) that serves as the primary endogenous antioxidant in eukaryotic cells (PubChem CID 124886). It plays a critical role in maintaining the intracellular redox environment, protecting cellular components from oxidative damage by neutralizing reactive oxygen species (ROS) and free radicals (StatPearls, NBK557396). Beyond its antioxidant capacity, GSH is essential for the detoxification of xenobiotics through conjugation reactions and acts as a reservoir for cysteine (PMC4684116). In disease states, GSH depletion is linked to neurodegeneration, liver injury, and aging, while elevated GSH levels in cancer cells often contribute to chemotherapy resistance (PMC3549305). Therapeutic strategies involve either replenishing GSH levels using precursors like N-acetylcysteine to treat toxicity and oxidative stress or depleting GSH to sensitize tumor cells to treatment or induce ferroptosis (PMC6835862). The GSH redox state, defined by the ratio of GSH to its oxidized form (GSSG), is a key indicator of cellular health and a target for various pharmacological interventions.

Other names

L-Glutathionegamma-L-Glutamyl-L-cysteinylglycineGSHGlutathione

Reduced glutathione acts as a cofactor for glutathione peroxidase (GPx) to reduce hydrogen peroxide and lipid hydroperoxides, and as a substrate for glutathione S-transferases (GST) to conjugate and detoxify electrophilic xenobiotics (StatPearls, NBK557396). It also maintains protein thiol groups in their reduced state and directly scavenges reactive oxygen and nitrogen species (PMC4684116).