Glutathione S-transferase Mu 1 (GSTM1) (GSTM1)

Glutathione S-transferase Mu 1 (GSTM1) is a cytosolic enzyme belonging to the Mu class of the glutathione S-transferase superfamily, primarily responsible for the Phase II detoxification of electrophilic compounds [1, 6]. It catalyzes the conjugation of reduced glutathione to a wide array of exogenous and endogenous toxins, including environmental carcinogens, therapeutic drugs, and products of lipid peroxidation like 4-hydroxynonenal [1, 7]. Beyond its enzymatic role, GSTM1 functions as a regulatory protein by binding to and inhibiting apoptosis signal-regulating kinase 1 (ASK1), thereby modulating cellular responses to oxidative stress and inflammation [3, 12]. A common genetic polymorphism, the GSTM1 null genotype, results in a complete loss of enzyme activity and is present in approximately 30-50% of the human population, significantly influencing individual susceptibility to various cancers, chronic kidney disease, and hypertension [4, 9, 11]. In clinical oncology, GSTM1 is a key factor in chemoresistance, as its ability to detoxify certain chemotherapeutic agents can reduce treatment efficacy, making it a potential target for adjunctive therapy to sensitize tumors [10, 13]. Furthermore, GSTM1 status is increasingly recognized as a biomarker for precision medicine, particularly in tailoring antioxidant therapies for renal and cardiovascular health [1, 4].

Other names

GST1H-BMUMU-1GSTM1-1GSTM1a-1aGSTM1b-1bGTH4GTM1Glutathione S-transferase M1

Catalyzes the nucleophilic attack of reduced glutathione on electrophilic centers of various substrates to facilitate detoxification and excretion [6, 7]. It also acts as a non-catalytic regulator by sequestering signaling kinases such as ASK1 and MEKK1, thereby inhibiting stress-induced apoptotic pathways [1, 12].