GSTA1

From Wikipedia, the free encyclopedia


Glutathione S-transferase A1
PDB rendering based on 1ags.
Available structures: 1ags, 1gsd, 1gse, 1gsf, 1guh, 1k3l, 1k3o, 1k3y, 1pkw, 1pkz, 1pl1, 1pl2, 1tdi, 1usb, 1xwg, 1ydk
Identifiers
Symbol(s) GSTA1; GST2; GSTA1-1; GTH1; MGC131939
External IDs OMIM: 138359 HomoloGene: 69229
RNA expression pattern

More reference expression data
Orthologs
Human Mouse
Entrez 2938 n/a
Ensembl ENSG00000187919 n/a
Uniprot P08263 n/a
Refseq NM_145740 (mRNA)
NP_665683 (protein)		 n/a (mRNA)
n/a (protein)
Location Chr 6: 52.76 - 52.78 Mb n/a
Pubmed search [1] n/a

Glutathione S-transferase A1, also known as GSTA1, is a human gene.

Cytosolic and membrane-bound forms of glutathione S-transferase are encoded by two distinct supergene families. These enzymes function in the detoxification of electrophilic compounds, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress, by conjugation with glutathione. The genes encoding these enzymes 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 some drugs. 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-tranferase belonging to the alpha class. The alpha class genes, located in a cluster mapped to chromosome 6, are the most abundantly expressed glutathione S-transferases in liver. In addition to metabolizing bilirubin and certain anti-cancer drugs in the liver, the alpha class of these enzymes exhibit glutathione peroxidase activity thereby protecting the cells from reactive oxygen species and the products of peroxidation.[1]

[edit] References

  1. ^ Entrez Gene: GSTA1 glutathione S-transferase A1.

[edit] Further reading

  • Morel F, Schulz WA, Sies H (1995). "Gene structure and regulation of expression of human glutathione S-transferases alpha.". Biol. Chem. Hoppe-Seyler 375 (10): 641–9. PMID 7888077. 
  • Stenberg G, Björnestedt R, Mannervik B (1992). "Heterologous expression of recombinant human glutathione transferase A1-1 from a hepatoma cell line.". Protein Expr. Purif. 3 (1): 80–4. PMID 1330133. 
  • 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. 
  • Rozen F, Nguyen T, Pickett CB (1992). "Isolation and characterization of a human glutathione S-transferase Ha1 subunit gene.". Arch. Biochem. Biophys. 292 (2): 589–93. PMID 1731620. 
  • Board PG, Mannervik B (1991). "The contribution of the C-terminal sequence to the catalytic activity of GST2, a human alpha-class glutathione transferase.". Biochem. J. 275 ( Pt 1): 171–4. PMID 2018473. 
  • Hayes JD, Kerr LA, Cronshaw AD (1990). "Evidence that glutathione S-transferases B1B1 and B2B2 are the products of separate genes and that their expression in human liver is subject to inter-individual variation. Molecular relationships between the B1 and B2 subunits and other Alpha class glutathione S-transferases.". Biochem. J. 264 (2): 437–45. PMID 2604726. 
  • Board PG, Webb GC (1987). "Isolation of a cDNA clone and localization of human glutathione S-transferase 2 genes to chromosome band 6p12.". Proc. Natl. Acad. Sci. U.S.A. 84 (8): 2377–81. PMID 3031680. 
  • Rhoads DM, Zarlengo RP, Tu CP (1987). "The basic glutathione S-transferases from human livers are products of separate genes.". Biochem. Biophys. Res. Commun. 145 (1): 474–81. PMID 3036131. 
  • Chow NW, Whang-Peng J, Kao-Shan CS, et al. (1988). "Human glutathione S-transferases. The Ha multigene family encodes products of different but overlapping substrate specificities.". J. Biol. Chem. 263 (26): 12797–800. PMID 3138230. 
  • Tu CP, Qian B (1988). "Nucleotide sequence of the human liver glutathione S-transferase subunit 1 cDNA.". Biochem. Soc. Trans. 15 (4): 734–6. PMID 3678589. 
  • Tu CP, Qian B (1987). "Human liver glutathione S-transferases: complete primary sequence of an Ha subunit cDNA.". Biochem. Biophys. Res. Commun. 141 (1): 229–37. PMID 3800996. 
  • Suzuki T, Smith S, Board PG (1994). "Structure and function of the 5' flanking sequences of the human alpha class glutathione S-transferase genes.". Biochem. Biophys. Res. Commun. 200 (3): 1665–71. doi:10.1006/bbrc.1994.1643. PMID 8185623. 
  • 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. 
  • Suzuki T, Johnston PN, Board PG (1994). "Structure and organization of the human alpha class glutathione S-transferase genes and related pseudogenes.". Genomics 18 (3): 680–6. PMID 8307579. 
  • Sinning I, Kleywegt GJ, Cowan SW, et al. (1993). "Structure determination and refinement of human alpha class glutathione transferase A1-1, and a comparison with the Mu and Pi class enzymes.". J. Mol. Biol. 232 (1): 192–212. PMID 8331657. 
  • Ahmad H, Singhal SS, Saxena M, Awasthi YC (1993). "Characterization of two novel subunits of the alpha-class glutathione S-transferases of human liver.". Biochim. Biophys. Acta 1161 (2-3): 333–6. PMID 8431482. 
  • Cameron AD, Sinning I, L'Hermite G, et al. (1996). "Structural analysis of human alpha-class glutathione transferase A1-1 in the apo-form and in complexes with ethacrynic acid and its glutathione conjugate.". Structure 3 (7): 717–27. PMID 8591048. 
  • Mulder TP, Peters WH, Court DA, Jansen JB (1996). "Sandwich ELISA for glutathione S-transferase Alpha 1-1: plasma concentrations in controls and in patients with gastrointestinal disorders.". Clin. Chem. 42 (3): 416–9. PMID 8598105. 
  • Mücher G, Becker J, Knapp M, et al. (1998). "Fine mapping of the autosomal recessive polycystic kidney disease locus (PKHD1) and the genes MUT, RDS, CSNK2 beta, and GSTA1 at 6p21.1-p12.". Genomics 48 (1): 40–5. doi:10.1006/geno.1997.5145. PMID 9503014. 
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