Glutathione S-transferases (GSTs) are a family of enzymes that play an important role in detoxification by catalyzing the conjugation of many hydrophobic and electrophilic compounds with reduced glutathione. Based on their biochemical, immunologic, and structural properties, the soluble GSTs are categorized into four main classes: alpha, mu, pi, and theta. The glutathione S-transferase pi gene (GSTP1) is a polymorphic gene encoding active, functionally different GSTP1 variant proteins that are thought to function in xenobiotic metabolism and play a role in susceptibility to cancer, and other diseases.[3]
GST-Pi is expressed in many human tissues, particularly in the biliary tree and renal distal convoluted tubules.It the most common gene alteration in ca prostate (hyper methylation)[7]
↑Bora PS, Bora NS, Wu XL, Lange LG (Oct 1991). "Molecular cloning, sequencing, and expression of human myocardial fatty acid ethyl ester synthase-III cDNA". J. Biol. Chem. 266 (25): 16774–7. PMID1885604.
↑Smith CM, Bora PS, Bora NS, Jones C, Gerhard DS (Nov 1995). "Genetic and radiation-reduced somatic cell hybrid sublocalization of the human GSTP1 gene". Cytogenet. Cell Genet. 71 (3): 235–9. doi:10.1159/000134117. PMID7587384.
Strange RC, Fryer AA (1999). "The glutathione S-transferases: influence of polymorphism on cancer susceptibility". IARC Sci. Publ. (148): 231–49. PMID10493261.
Kellen E, Hemelt M, Broberg K, Golka K, Kristensen VN, Hung RJ, Matullo G, Mittal RD, Porru S, Povey A, Schulz WA, Shen J, Buntinx F, Zeegers MP, Taioli E (2007). "Pooled analysis and meta-analysis of the glutathione S-transferase P1 Ile 105Val polymorphism and bladder cancer: a HuGE-GSEC review". Am. J. Epidemiol. 165 (11): 1221–30. doi:10.1093/aje/kwm003. PMID17404387.
Sekine I, Minna JD, Nishio K, Tamura T, Saijo N (2006). "A literature review of molecular markers predictive of clinical response to cytotoxic chemotherapy in patients with lung cancer". J Thorac Oncol. 1 (1): 31–7. doi:10.1097/01243894-200601000-00008. PMID17409824.
1gss: THREE-DIMENSIONAL STRUCTURE OF CLASS PI GLUTATHIONE S-TRANSFERASE FROM HUMAN PLACENTA IN COMPLEX WITH S-HEXYLGLUTATHIONE AT 2.8 ANGSTROMS RESOLUTION
1lbk: Crystal structure of a recombinant glutathione transferase, created by replacing the last seven residues of each subunit of the human class pi isoenzyme with the additional C-terminal helix of human class alpha isoenzyme