Biology:GSTA2

Glutathione S-transferase A2 is an enzyme that in humans is encoded by the GSTA2 gene.^[1]

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-transferase 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]

References

↑ ^1.0 ^1.1 "Entrez Gene: GSTA2 glutathione S-transferase A2". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2939.

"Isolation and characterization of the human glutathione S-transferase A2 subunit gene.". Arch. Biochem. Biophys. 298 (2): 747–52. 1992. doi:10.1016/0003-9861(92)90475-C. PMID 1329668.
"Heterologous expression of recombinant human glutathione transferase A1-1 from a hepatoma cell line.". Protein Expr. Purif. 3 (1): 80–4. 1992. doi:10.1016/1046-5928(92)90060-A. PMID 1330133.
"Cloning, sequencing and characterization of the human alpha glutathione S-transferase gene corresponding to the cDNA clone pGTH2.". Biochem. J. 285 (3): 925–8. 1992. doi:10.1042/bj2850925. PMID 1497629.
"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 (2): 383–8. 1992. doi:10.1042/bj2860383. PMID 1530570.
"The human glutathione S-transferases: comparison of isoenzyme expression in normal and astrocytoma brain.". Biochim. Biophys. Acta 1139 (3): 222–8. 1992. doi:10.1016/0925-4439(92)90138-D. PMID 1627661.
"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. 1990. doi:10.1042/bj2640437. PMID 2604726.
"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. 1987. doi:10.1073/pnas.84.8.2377. PMID 3031680.
"The basic glutathione S-transferases from human livers are products of separate genes.". Biochem. Biophys. Res. Commun. 145 (1): 474–81. 1987. doi:10.1016/0006-291X(87)91345-3. PMID 3036131.
"Human glutathione S-transferases. The Ha multigene family encodes products of different but overlapping substrate specificities.". J. Biol. Chem. 263 (26): 12797–800. 1988. PMID 3138230.
"Nucleotide sequence of the human liver glutathione S-transferase subunit 1 cDNA.". Biochem. Soc. Trans. 15 (4): 734–6. 1988. doi:10.1042/bst0150734. PMID 3678589.
"Human liver glutathione S-transferases: complete primary sequence of an Ha subunit cDNA.". Biochem. Biophys. Res. Commun. 141 (1): 229–37. 1987. doi:10.1016/S0006-291X(86)80358-8. PMID 3800996.
"Identification of heterogeneous and microheterogeneous subunits of glutathione S-transferase in rat liver cytosol.". Arch. Biochem. Biophys. 242 (1): 104–11. 1985. doi:10.1016/0003-9861(85)90484-9. PMID 3901925.
"A surface mutant (G82R) of a human alpha-glutathione S-transferase shows decreased thermal stability and a new mode of molecular association in the crystal.". Proteins 20 (3): 259–63. 1995. doi:10.1002/prot.340200306. PMID 7892174.
"Immunohistochemical localization of glutathione S-transferases in human lung.". Cancer Res. 53 (23): 5643–8. 1994. PMID 8242618.
"Structure and organization of the human alpha class glutathione S-transferase genes and related pseudogenes.". Genomics 18 (3): 680–6. 1994. doi:10.1016/S0888-7543(05)80373-8. PMID 8307579.
"Characterization of two novel subunits of the alpha-class glutathione S-transferases of human liver.". Biochim. Biophys. Acta 1161 (2–3): 333–6. 1993. doi:10.1016/0167-4838(93)90234-i. PMID 8431482.
"Subunit diversity and tissue distribution of human glutathione S-transferases: interpretations based on electrospray ionization-MS and peptide sequence-specific antisera". Biochem. J. 325 (2): 481–6. 1997. doi:10.1042/bj3250481. PMID 9230131.
"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. 2000. PMID 10676639.
"Polymorphism of human Alpha class glutathione transferases". Pharmacogenetics 11 (7): 609–17. 2001. doi:10.1097/00008571-200110000-00007. PMID 11668220.
"Effect of polymorphism in the human glutathione S-transferase A1 promoter on hepatic GSTA1 and GSTA2 expression". Pharmacogenetics 11 (8): 663–9. 2002. doi:10.1097/00008571-200111000-00004. PMID 11692074.