GSTP1
GSTP1 | |||||||||||||||||||||||||||||||||||||||||||||||||||
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Identifiers | |||||||||||||||||||||||||||||||||||||||||||||||||||
Aliases | GSTP1, DFN7, FAEES3, GST3, GSTP, HEL-S-22, PI, glutathione S-transferase pi 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||
External IDs | OMIM: 134660; MGI: 3782108; HomoloGene: 660; GeneCards: GSTP1; OMA:GSTP1 - orthologs | ||||||||||||||||||||||||||||||||||||||||||||||||||
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Glutathione S-transferase P is an enzyme that in humans is encoded by the GSTP1 gene.[4][5]
Function
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.[6]
Interactions
GSTP1 has been shown to interact with Fanconi anemia, complementation group C[7][8] and MAPK8.[9]
GST-Pi is expressed in many human tissues, particularly in the biliary tree, renal distal convoluted tubules and lungs.[10]
Possible drug target
Triple-negative breast cancer cells rely on glutathione-S-transferase Pi1, and inhibitors are being studied.[11] Piperlongumine has been found to silence the gene.[12]
References
- ^ a b c GRCh38: Ensembl release 89: ENSG00000084207 – Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ Bora PS, Bora NS, Wu XL, Lange LG (October 1991). "Molecular cloning, sequencing, and expression of human myocardial fatty acid ethyl ester synthase-III cDNA". J. Biol. Chem. 266 (25): 16774–7. doi:10.1016/S0021-9258(18)55367-9. PMID 1885604.
- ^ Smith CM, Bora PS, Bora NS, Jones C, Gerhard DS (November 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. PMID 7587384.
- ^ "Entrez Gene: GSTP1 glutathione S-transferase pi".
- ^ Cumming RC, Lightfoot J, Beard K, Youssoufian H, O'Brien PJ, Buchwald M (July 2001). "Fanconi anemia group C protein prevents apoptosis in hematopoietic cells through redox regulation of GSTP1". Nat. Med. 7 (7): 814–20. doi:10.1038/89937. PMID 11433346. S2CID 35177844.
- ^ Reuter TY, Medhurst AL, Waisfisz Q, Zhi Y, Herterich S, Hoehn H, Gross HJ, Joenje H, Hoatlin ME, Mathew CG, Huber PA (October 2003). "Yeast two-hybrid screens imply involvement of Fanconi anemia proteins in transcription regulation, cell signaling, oxidative metabolism, and cellular transport". Exp. Cell Res. 289 (2): 211–21. doi:10.1016/S0014-4827(03)00261-1. PMID 14499622.
- ^ Wang T, Arifoglu P, Ronai Z, Tew KD (15 June 2001). "Glutathione S-transferase P1-1 (GSTP1-1) inhibits c-Jun N-terminal kinase (JNK1) signaling through interaction with the C terminus". J. Biol. Chem. 276 (24): 20999–1003. doi:10.1074/jbc.M101355200. PMID 11279197.
- ^ Terrier, P; Townsend, AJ; Coindre, JM; Triche, TJ; Cowan, KH (October 1990). "An immunohistochemical study of pi class glutathione S-transferase expression in normal human tissue". The American Journal of Pathology. 137 (4): 845–53. PMC 1877535. PMID 1977319.
- ^ Triple-negative breast cancer target is found. May 2016
- ^ "Researchers uncover mechanism for cancer-killing properties of pepper plant".
Further reading
- Strange RC, Fryer AA (1999). "The glutathione S-transferases: influence of polymorphism on cancer susceptibility". IARC Sci. Publ. (148): 231–49. PMID 10493261.
- 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. PMID 17404387.
- 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. PMID 17409824.
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- 10gs: HUMAN GLUTATHIONE S-TRANSFERASE P1-1, COMPLEX WITH TER117
- 11gs: GLUTATHIONE S-TRANSFERASE COMPLEXED WITH ETHACRYNIC ACID-GLUTATHIONE CONJUGATE (FORM II)
- 12gs: GLUTATHIONE S-TRANSFERASE COMPLEXED WITH S-NONYL-GLUTATHIONE
- 13gs: GLUTATHIONE S-TRANSFERASE COMPLEXED WITH SULFASALAZINE
- 14gs: GLUTATHIONE S-TRANSFERASE P1-1 APO FORM 1
- 16gs: GLUTATHIONE S-TRANSFERASE P1-1 APO FORM 3
- 17gs: GLUTATHIONE S-TRANSFERASE P1-1
- 18gs: GLUTATHIONE S-TRANSFERASE P1-1 COMPLEXED WITH 1-(S-GLUTATHIONYL)-2,4-DINITROBENZENE
- 19gs: GLUTATHIONE S-TRANSFERASE P1-1
- 1aqv: GLUTATHIONE S-TRANSFERASE IN COMPLEX WITH P-BROMOBENZYLGLUTATHIONE
- 1aqw: GLUTATHIONE S-TRANSFERASE IN COMPLEX WITH GLUTATHIONE
- 1aqx: GLUTATHIONE S-TRANSFERASE IN COMPLEX WITH MEISENHEIMER COMPLEX
- 1eog: CRYSTAL STRUCTURE OF PI CLASS GLUTATHIONE TRANSFERASE
- 1eoh: GLUTATHIONE TRANSFERASE P1-1
- 1gss: THREE-DIMENSIONAL STRUCTURE OF CLASS PI GLUTATHIONE S-TRANSFERASE FROM HUMAN PLACENTA IN COMPLEX WITH S-HEXYLGLUTATHIONE AT 2.8 ANGSTROMS RESOLUTION
- 1kbn: Glutathione transferase mutant
- 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
- 1md3: A folding mutant of human class pi glutathione transferase, created by mutating glycine 146 of the wild-type protein to alanine
- 1md4: A folding mutant of human class pi glutathione transferase, created by mutating glycine 146 of the wild-type protein to valine
- 1pgt: CRYSTAL STRUCTURE OF HUMAN GLUTATHIONE S-TRANSFERASE P1-1[V104] COMPLEXED WITH S-HEXYLGLUTATHIONE
- 1px6: A folding mutant of human class pi glutathione transferase, created by mutating aspartate 153 of the wild-type protein to asparagine
- 1px7: A folding mutant of human class pi glutathione transferase, created by mutating aspartate 153 of the wild-type protein to glutamate
- 1zgn: Crystal Structure of the Glutathione Transferase Pi in Complex with Dinitrosyl-diglutathionyl Iron Complex
- 20gs: GLUTATHIONE S-TRANSFERASE P1-1 COMPLEXED WITH CIBACRON BLUE
- 21gs:
- 22gs: HUMAN GLUTATHIONE S-TRANSFERASE P1-1 Y49F MUTANT
- 2a2r: Crystal Structure of Glutathione Transferase Pi in complex with S-nitrosoglutathione
- 2a2s: Crystal Structure of Human Glutathione Transferase in complex with S-nitrosoglutathione in the absence of reducing agent
- 2gss: HUMAN GLUTATHIONE S-TRANSFERASE P1-1 IN COMPLEX WITH ETHACRYNIC ACID
- 2j9h: CRYSTAL STRUCTURE OF HUMAN GLUTATHIONE-S-TRANSFERASE P1-1 CYS-FREE MUTANT IN COMPLEX WITH S-HEXYLGLUTATHIONE AT 2.4 A RESOLUTION
- 2pgt: CRYSTAL STRUCTURE OF HUMAN GLUTATHIONE S-TRANSFERASE P1-1[V104] COMPLEXED WITH (9R,10R)-9-(S-GLUTATHIONYL)-10-HYDROXY-9,10-DIHYDROPHENANTHRENE
- 3gss: HUMAN GLUTATHIONE S-TRANSFERASE P1-1 IN COMPLEX WITH ETHACRYNIC ACID-GLUTATHIONE CONJUGATE
- 3pgt: CRYSTAL STRUCTURE OF HGSTP1-1[I104] COMPLEXED WITH THE GSH CONJUGATE OF (+)-ANTI-BPDE
- 4gss: HUMAN GLUTATHIONE S-TRANSFERASE P1-1 Y108F MUTANT
- 4pgt: CRYSTAL STRUCTURE OF HGSTP1-1[V104] COMPLEXED WITH THE GSH CONJUGATE OF (+)-ANTI-BPDE
- 5gss: HUMAN GLUTATHIONE S-TRANSFERASE P1-1, COMPLEX WITH GLUTATHIONE
- 6gss: HUMAN GLUTATHIONE S-TRANSFERASE P1-1, COMPLEX WITH GLUTATHIONE
- 7gss: HUMAN GLUTATHIONE S-TRANSFERASE P1-1, COMPLEX WITH GLUTATHIONE
- 8gss: HUMAN GLUTATHIONE S-TRANSFERASE P1-1, COMPLEX WITH GLUTATHIONE
- 9gss: HUMAN GLUTATHIONE S-TRANSFERASE P1-1, COMPLEX WITH S-HEXYL GLUTATHIONE
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