Glutathione S-transferase Pi 1 (GSTP1) (GSTP1)

Glutathione S-transferase Pi 1 (GSTP1) is a member of the glutathione S-transferase (GST) family of enzymes, which play a critical role in the detoxification of electrophilic compounds by conjugating them with reduced glutathione [2, 4]. GSTP1 is particularly notable for its high expression in various human cancers, where it contributes to multi-drug resistance by neutralizing chemotherapeutic agents such as cisplatin and alkylating agents [7, 13]. Beyond its catalytic role, GSTP1 acts as a regulatory protein in cell signaling pathways, specifically by sequestering c-Jun N-terminal kinase (JNK) and preventing apoptosis under non-stressed conditions [4, 12]. This dual role makes GSTP1 an attractive therapeutic target; inhibitors like ezatiostat are designed to reverse drug resistance and stimulate hematopoiesis, while prodrugs like canfosfamide are engineered to be selectively activated by the enzyme within tumor cells [7, 17]. Additionally, the epigenetic silencing of the GSTP1 gene via promoter methylation is a well-recognized biomarker for the early detection and progression of prostate cancer [13, 17].

Other names

GSTP1-1Glutathione S-transferase PGST class-piGlutathione S-transferase-1GST-1Fatty acid ethyl ester synthaseFAEES

Inhibition of catalytic activity to reverse drug resistance; activation of cytotoxic prodrugs; modulation of JNK-mediated apoptosis.