Glutathione S-transferase omega-1 (GSTO1)

Glutathione S-transferase omega-1 (GSTO1) is a cytosolic enzyme of the omega class of glutathione S-transferases involved in redox regulation, detoxification of xenobiotics, and defense against oxidative stress[2][4][8]. Unlike other GSTs, GSTO1 has a cysteine residue at its active site and primarily catalyzes thioltransferase, dehydroascorbate reductase, and monomethylarsonic acid reductase activities[1][2][4]. GSTO1 modulates protein glutathionylation, regulates key inflammatory and oxidative stress pathways, and has been implicated in the pathogenesis of cancer, neurodegenerative diseases (such as Alzheimer's and Parkinson's), atherosclerosis, and ALS[4][6][9]. It is the target of specific covalent small-molecule inhibitors under preclinical investigation for anti-inflammatory and anti-cancer effects[1][4]. GSTO1 polymorphisms (notably Ala140Asp) have been associated with disease susceptibility and prognosis in neurodegeneration and cardiovascular disease[3][6][9].

Other names

Glutathione S-transferase omega 1-1GSTTLP28GSTO-1GSTO 1-1MMA(V) reductaseSPG-RGSTTLp28P28Glutathione-dependent dehydroascorbate reductaseMonomethylarsonic acid reductaseS-(Phenacyl)glutathione reductaseHEL-S-21epididymis secretory protein Li 21glutathione-S-transferase like

Covalent inhibition of active site cysteine (by chloroacetamide-containing small-molecule inhibitors); Modulation of redox regulation and glutathionylation status of signaling proteins; Inhibition of pro-inflammatory signaling pathways (e.g., LPS-induced TLR4 pathway)