GSTA1 (glutathione S-transferase alpha 1) is a cytosolic enzyme that catalyzes glutathione conjugation of electrophilic compounds, including xenobiotics, carcinogens, and endogenous metabolites 1. It facilitates glutathione conjugation of prostaglandins A2 and J2, exhibits glutathione-dependent peroxidase activity toward oxidized linoleic acid metabolites, and catalyzes steroid isomerization in hormone biosynthesis. GSTA1 expression is regulated by promoter SNPs showing significant population-specific variation, with particular variants affecting transcriptional activity 1. Clinically, GSTA1 has multiple disease associations: elevated expression suppresses ferroptosis and mediates sorafenib resistance in hepatocellular carcinoma through a CTNNB1-dependent pathway 2; the BB genotype increases colorectal cancer risk, particularly in Caucasians 3; the -69C/T polymorphism associates with gestational hypertension 4 and asthma susceptibility 5; and expression is notably increased in proliferative inflammatory atrophy of the prostate, suggesting response to oxidative stress 6. However, GSTA1 polymorphisms show no significant association with bladder cancer susceptibility 7. These findings indicate GSTA1's critical role in detoxification, redox homeostasis, and disease pathogenesis across multiple organ systems.