GSTM2

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Glutathione S-transferase M2 (muscle)
PDB rendering based on 1hna.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Identifiers
Symbols GSTM2 ; GST4; GSTM; GSTM2-2; GTHMUS; MGC117303
External IDs Template:OMIM5 Template:MGI HomoloGene41816
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

Glutathione S-transferase M2 (muscle), also known as GSTM2, is a human gene.[1]

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.[1]

References

  1. 1.0 1.1 "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): 383–8. PMID 1530570.
  • Dawson SJ, White LA (1992). "Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin". J. Infect. 24 (3): 317–20. 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): 587–93. PMID 2006920.
  • Vorachek WR, Pearson WR, Rule GS (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. PMID 2034681.
  • Campbell E, Takahashi Y, Abramovitz M; et al. (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. PMID 2345169.
  • Laisney V, Nguyen Van Cong , Gross MS, Frezal J (1985). "Human genes for glutathione S-transferases". Hum. Genet. 68 (3): 221–7. PMID 6500576.
  • 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. 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): 373–80. 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): 25–8. 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. 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 Biol. Crystallogr. 54 (Pt 3): 458–60. 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. 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. doi:10.1073/pnas.242603899. 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. 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.

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