Glutathione S-transferase Pi 1 (GSTP1)

Glutathione S-transferase Pi 1 (GSTP1) is a widely expressed cytosolic phase II detoxification enzyme that catalyzes the conjugation of reduced glutathione to a variety of electrophilic and hydrophobic compounds, facilitating their detoxification and elimination[1][2][4][5]. It belongs to the Pi class of the glutathione S-transferase (GST) superfamily, with high expression in erythrocytes and many other tissues[2]. Beyond its detoxification activity, GSTP1 modulates signal transduction pathways by directly binding and inhibiting components such as c-Jun N-terminal kinase (JNK), thereby influencing cell survival, apoptosis, and drug response[3]. GSTP1 plays significant roles in cancer biology, both as a marker of tumor cells and as a mediator of resistance to chemotherapeutic drugs such as cisplatin. As a result, it is a therapeutic target in oncology where inhibitors (e.g., piperlongumine, ethacraplatin) are being developed or explored to overcome drug resistance or directly drive tumor cell death[1][3]. Polymorphisms in the GSTP1 gene are associated with varying cancer risk and treatment response, complicating its therapeutic targeting and making it a pharmacogenomic biomarker[1][2][4].

Other names

Glutathione S-transferase PiGSTPGST piGSTP1-1

Inhibition of enzymatic activity (by small molecule inhibitors), Reversal of drug resistance, Sensitization of tumor cells to chemotherapy