GSTM2

GSTM2
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1HNA, 1HNB, 1HNC, 1XW5, 1YKC, 2AB6, 2C4J, 2GTU, 3GTU, 3GUR
Identifiers
Aliases	GSTM2 , GST4, GSTM, GSTM2-2, GTHMUS, glutathione S-transferase mu 2 (muscle), glutathione S-transferase mu 2
External IDs	OMIM: 138380 MGI: 1915562 HomoloGene: 41816 GeneCards: GSTM2
Gene location (Human) Chr. Chromosome 1 (human) [1] Band 1p13.3 Start 109,668,022 bp [1] End 109,709,551 bp [1]
Gene location (Mouse) Chr. Chromosome 3 (mouse) [2] Band 3|3 F2.3 Start 107,833,650 bp [2] End 107,839,133 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in right uterine tube fundus pituitary gland tibial nerve vagina anterior pituitary prostate canal of the cervix skin of abdomen left uterine tube Top expressed in interventricular septum left lobe of liver lens right ventricle ganglionic eminence testicle adrenal gland duodenum myocardium of ventricle seminiferous tubule More reference expression data BioGPS n/a
Gene ontology Molecular function transferase activity protein homodimerization activity glutathione binding protein binding enzyme binding signaling receptor binding glutathione peroxidase activity glutathione transferase activity Cellular component cytoplasm cytosol sarcoplasmic reticulum extracellular exosome intercellular bridge Biological process xenobiotic catabolic process glutathione metabolic process regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion negative regulation of ryanodine-sensitive calcium-release channel activity positive regulation of ryanodine-sensitive calcium-release channel activity cellular detoxification of nitrogen compound nitrobenzene metabolic process cellular response to caffeine metabolism regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum relaxation of cardiac muscle glutathione derivative biosynthetic process regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion cellular oxidant detoxification linoleic acid metabolic process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 2946 68312 Ensembl ENSG00000213366 ENSMUSG00000004035 UniProt P28161 Q80W21 RefSeq (mRNA) NM_001142368 NM_000848 NM_026672 NM_001356351 RefSeq (protein) NP_000839 NP_001135840 NP_080948 NP_001343280 Location (UCSC) Chr 1: 109.67 – 109.71 Mb Chr 3: 107.83 – 107.84 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Glutathione S-transferase Mu 2 is an enzyme that in humans is encoded by the GSTM2 gene. ^{[5] [6] [7]}

Cytosolic and membrane-bound forms of glutathione S-transferase are encoded by two distinct supergene families. At present, eight distinct classes of the soluble cytoplasmic mammalian glutathione S-transferases have been identified: alpha, kappa, mu, omega, pi, sigma, theta and zeta.

This gene encodes a glutathione S-transferase that belongs to the mu class. The mu class of enzymes functions in the detoxification of electrophilic compounds, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress, by conjugation with glutathione. The genes encoding the mu class of enzymes are organized in a gene cluster on chromosome 1p13.3 and are known to be highly polymorphic. These genetic variations can change an individual's susceptibility to carcinogens and toxins as well as affect the toxicity and efficacy of certain drugs. ^[7]

References

1. GRCh38: Ensembl release 89: ENSG00000213366 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000004035 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Vorachek WR, Pearson WR, Rule GS (Jun 1991). "Cloning, expression, and characterization of a class-mu glutathione transferase from human muscle, the product of the GST4 locus". Proc Natl Acad Sci U S A. 88 (10): 4443–7. Bibcode:1991PNAS...88.4443V. doi: 10.1073/pnas.88.10.4443 . PMC   51676 . PMID   2034681.
6. Campbell E, Takahashi Y, Abramovitz M, Peretz M, Listowsky I (Jul 1990). "A distinct human testis and brain mu-class glutathione S-transferase. Molecular cloning and characterization of a form present even in individuals lacking hepatic type mu isoenzymes". J Biol Chem. 265 (16): 9188–93. doi: 10.1016/S0021-9258(19)38830-1 . PMID   2345169.
7. "Entrez Gene: GSTM2 glutathione S-transferase M2 (muscle)".

Further reading

• Bogaards JJ, van Ommen B, van Bladeren PJ (1992). "Purification and characterization of eight glutathione S-transferase isoenzymes of hamster. Comparison of subunit composition of enzymes from liver, kidney, testis, pancreas and trachea". Biochem. J. 286. ( Pt 2) (2): 383–8. doi:10.1042/bj2860383. PMC   1132909 . PMID   1530570.
• Dawson SJ, White LA (1992). "Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin". J. Infect. 24 (3): 317–20. doi:10.1016/S0163-4453(05)80037-4. PMID   1602151.
• Taylor JB, Oliver J, Sherrington R, Pemble SE (1991). "Structure of human glutathione S-transferase class Mu genes". Biochem. J. 274. ( Pt 2) (2): 587–93. doi:10.1042/bj2740587. PMC   1150179 . PMID   2006920.
• Laisney V, Nguyen Van Cong, Gross MS, Frezal J (1985). "Human genes for glutathione S-transferases". Hum. Genet. 68 (3): 221–7. doi:10.1007/BF00418392. PMID   6500576. S2CID   39589156.
• Raghunathan S, Chandross RJ, Kretsinger RH, et al. (1994). "Crystal structure of human class mu glutathione transferase GSTM2-2. Effects of lattice packing on conformational heterogeneity". J. Mol. Biol. 238 (5): 815–32. doi:10.1006/jmbi.1994.1336. PMID   8182750.
• Anttila S, Hirvonen A, Vainio H, et al. (1994). "Immunohistochemical localization of glutathione S-transferases in human lung". Cancer Res. 53 (23): 5643–8. PMID   8242618.
• Pearson WR, Vorachek WR, Xu SJ, et al. (1993). "Identification of class-mu glutathione transferase genes GSTM1-GSTM5 on human chromosome 1p13". Am. J. Hum. Genet. 53 (1): 220–33. PMC   1682241 . PMID   8317488.
• Ross VL, Board PG (1993). "Molecular cloning and heterologous expression of an alternatively spliced human Mu class glutathione S-transferase transcript". Biochem. J. 294. ( Pt 2) (2): 373–80. doi:10.1042/bj2940373. PMC   1134464 . PMID   8373352.
• Baez S, Segura-Aguilar J, Widersten M, et al. (1997). "Glutathione transferases catalyse the detoxication of oxidized metabolites (o-quinones) of catecholamines and may serve as an antioxidant system preventing degenerative cellular processes". Biochem. J. 324. ( Pt 1) (Pt 1): 25–8. doi:10.1042/bj3240025. PMC   1218396 . PMID   9164836.
• Xu S, Wang Y, Roe B, Pearson WR (1998). "Characterization of the human class Mu glutathione S-transferase gene cluster and the GSTM1 deletion". J. Biol. Chem. 273 (6): 3517–27. doi: 10.1074/jbc.273.6.3517 . PMID   9452477.
• Patskovska LN, Fedorov AA, Patskovsky YV, et al. (1998). "Expression, crystallization and preliminary X-ray analysis of ligand-free human glutathione S-transferase M2-2". Acta Crystallogr. D. 54 (Pt 3): 458–60. Bibcode:1998AcCrD..54..458P. doi:10.1107/S0907444997011190. PMID   9761928.
• Coles BF, Anderson KE, Doerge DR, et al. (2000). "Quantitative analysis of interindividual variation of glutathione S-transferase expression in human pancreas and the ambiguity of correlating genotype with phenotype". Cancer Res. 60 (3): 573–9. PMID   10676639.
• Luo JK, Hornby JA, Wallace LA, et al. (2003). "Impact of domain interchange on conformational stability and equilibrium folding of chimeric class micro glutathione transferases". Protein Sci. 11 (9): 2208–17. doi:10.1110/ps.0208002. PMC   2373595 . PMID   12192076.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi: 10.1073/pnas.242603899 . PMC   139241 . PMID   12477932.
• Ivarsson Y, Mackey AJ, Edalat M, et al. (2003). "Identification of residues in glutathione transferase capable of driving functional diversification in evolution. A novel approach to protein redesign". J. Biol. Chem. 278 (10): 8733–8. doi: 10.1074/jbc.M211776200 . PMID   12486119.
• De Maria F, Pedersen JZ, Caccuri AM, et al. (2004). "The specific interaction of dinitrosyl-diglutathionyl-iron complex, a natural NO carrier, with the glutathione transferase superfamily: suggestion for an evolutionary pressure in the direction of the storage of nitric oxide". J. Biol. Chem. 278 (43): 42283–93. doi: 10.1074/jbc.M305568200 . PMID   12871945.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC   528928 . PMID   15489334.
• Weng MW, Hsiao YM, Chiou HL, et al. (2005). "Alleviation of benzo[a]pyrene-diolepoxide-DNA damage in human lung carcinoma by glutathione S-transferase M2". DNA Repair (Amst.). 4 (4): 493–502. doi:10.1016/j.dnarep.2004.12.006. PMID   15725629.