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Glutathione S-transferase alpha 2 (GSTA2) is an enzyme belonging to the alpha class of the glutathione S-transferase family, predominantly expressed in the liver and involved in cellular defense against toxins and oxidative stress by catalyzing the conjugation of glutathione to a broad range of electrophilic compounds. GSTA2 expression is regulated by genetic polymorphisms and stress-responsive factors, and it contributes to detoxification processes, antioxidant defense, and the regulation of cell survival and apoptotic pathways. It plays roles in cancer progression, particularly hepatocellular carcinoma, and in protection against neurodegenerative and oxidative injuries, making it both a promising therapeutic target and a disease biomarker[1][2][3][4][5].
GSTA2's mechanism of action primarily involves the conjugation of glutathione to electrophilic substrates, serving as a key enzyme in phase II metabolism. It also contributes to the reduction of reactive oxygen species and peroxidation damage through its glutathione peroxidase activity, and has been shown to inhibit apoptosis in various cellular models, including cancer and neuronal cells.
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