GSTA1

GSTA1

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

PBB_Summary
section_title =
summary_text = 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.cite web | title = Entrez Gene: GSTA1 glutathione S-transferase A1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2938| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Morel F, Schulz WA, Sies H |title=Gene structure and regulation of expression of human glutathione S-transferases alpha. |journal=Biol. Chem. Hoppe-Seyler |volume=375 |issue= 10 |pages= 641–9 |year= 1995 |pmid= 7888077 |doi=
*cite journal | author=Stenberg G, Björnestedt R, Mannervik B |title=Heterologous expression of recombinant human glutathione transferase A1-1 from a hepatoma cell line. |journal=Protein Expr. Purif. |volume=3 |issue= 1 |pages= 80–4 |year= 1992 |pmid= 1330133 |doi=
*cite journal | author=Bogaards JJ, van Ommen B, van Bladeren PJ |title=Purification and characterization of eight glutathione S-transferase isoenzymes of hamster. Comparison of subunit composition of enzymes from liver, kidney, testis, pancreas and trachea. |journal=Biochem. J. |volume=286 ( Pt 2) |issue= |pages= 383–8 |year= 1992 |pmid= 1530570 |doi=
*cite journal | author=Rozen F, Nguyen T, Pickett CB |title=Isolation and characterization of a human glutathione S-transferase Ha1 subunit gene. |journal=Arch. Biochem. Biophys. |volume=292 |issue= 2 |pages= 589–93 |year= 1992 |pmid= 1731620 |doi=
*cite journal | author=Board PG, Mannervik B |title=The contribution of the C-terminal sequence to the catalytic activity of GST2, a human alpha-class glutathione transferase. |journal=Biochem. J. |volume=275 ( Pt 1) |issue= |pages= 171–4 |year= 1991 |pmid= 2018473 |doi=
*cite journal | author=Hayes JD, Kerr LA, Cronshaw AD |title=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. |journal=Biochem. J. |volume=264 |issue= 2 |pages= 437–45 |year= 1990 |pmid= 2604726 |doi=
*cite journal | author=Board PG, Webb GC |title=Isolation of a cDNA clone and localization of human glutathione S-transferase 2 genes to chromosome band 6p12. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 8 |pages= 2377–81 |year= 1987 |pmid= 3031680 |doi=
*cite journal | author=Rhoads DM, Zarlengo RP, Tu CP |title=The basic glutathione S-transferases from human livers are products of separate genes. |journal=Biochem. Biophys. Res. Commun. |volume=145 |issue= 1 |pages= 474–81 |year= 1987 |pmid= 3036131 |doi=
*cite journal | author=Chow NW, Whang-Peng J, Kao-Shan CS, "et al." |title=Human glutathione S-transferases. The Ha multigene family encodes products of different but overlapping substrate specificities. |journal=J. Biol. Chem. |volume=263 |issue= 26 |pages= 12797–800 |year= 1988 |pmid= 3138230 |doi=
*cite journal | author=Tu CP, Qian B |title=Nucleotide sequence of the human liver glutathione S-transferase subunit 1 cDNA. |journal=Biochem. Soc. Trans. |volume=15 |issue= 4 |pages= 734–6 |year= 1988 |pmid= 3678589 |doi=
*cite journal | author=Tu CP, Qian B |title=Human liver glutathione S-transferases: complete primary sequence of an Ha subunit cDNA. |journal=Biochem. Biophys. Res. Commun. |volume=141 |issue= 1 |pages= 229–37 |year= 1987 |pmid= 3800996 |doi=
*cite journal | author=Suzuki T, Smith S, Board PG |title=Structure and function of the 5' flanking sequences of the human alpha class glutathione S-transferase genes. |journal=Biochem. Biophys. Res. Commun. |volume=200 |issue= 3 |pages= 1665–71 |year= 1994 |pmid= 8185623 |doi= 10.1006/bbrc.1994.1643
*cite journal | author=Anttila S, Hirvonen A, Vainio H, "et al." |title=Immunohistochemical localization of glutathione S-transferases in human lung. |journal=Cancer Res. |volume=53 |issue= 23 |pages= 5643–8 |year= 1994 |pmid= 8242618 |doi=
*cite journal | author=Suzuki T, Johnston PN, Board PG |title=Structure and organization of the human alpha class glutathione S-transferase genes and related pseudogenes. |journal=Genomics |volume=18 |issue= 3 |pages= 680–6 |year= 1994 |pmid= 8307579 |doi=
*cite journal | author=Sinning I, Kleywegt GJ, Cowan SW, "et al." |title=Structure determination and refinement of human alpha class glutathione transferase A1-1, and a comparison with the Mu and Pi class enzymes. |journal=J. Mol. Biol. |volume=232 |issue= 1 |pages= 192–212 |year= 1993 |pmid= 8331657 |doi=
*cite journal | author=Ahmad H, Singhal SS, Saxena M, Awasthi YC |title=Characterization of two novel subunits of the alpha-class glutathione S-transferases of human liver. |journal=Biochim. Biophys. Acta |volume=1161 |issue= 2-3 |pages= 333–6 |year= 1993 |pmid= 8431482 |doi=
*cite journal | author=Cameron AD, Sinning I, L'Hermite G, "et al." |title=Structural analysis of human alpha-class glutathione transferase A1-1 in the apo-form and in complexes with ethacrynic acid and its glutathione conjugate. |journal=Structure |volume=3 |issue= 7 |pages= 717–27 |year= 1996 |pmid= 8591048 |doi=
*cite journal | author=Mulder TP, Peters WH, Court DA, Jansen JB |title=Sandwich ELISA for glutathione S-transferase Alpha 1-1: plasma concentrations in controls and in patients with gastrointestinal disorders. |journal=Clin. Chem. |volume=42 |issue= 3 |pages= 416–9 |year= 1996 |pmid= 8598105 |doi=
*cite journal | author=Mücher G, Becker J, Knapp M, "et al." |title=Fine mapping of the autosomal recessive polycystic kidney disease locus (PKHD1) and the genes MUT, RDS, CSNK2 beta, and GSTA1 at 6p21.1-p12. |journal=Genomics |volume=48 |issue= 1 |pages= 40–5 |year= 1998 |pmid= 9503014 |doi= 10.1006/geno.1997.5145

PBB_Controls
update_page = yes
require_manual_inspection = no
update_protein_box = yes
update_summary = yes
update_citations = yes


Wikimedia Foundation. 2010.

Игры ⚽ Поможем написать реферат

Look at other dictionaries:

  • Aryl hydrocarbon receptor — AHR redirects here. For other uses, see Ahr (disambiguation). Aryl hydrocarbon receptor Identifiers Symbols AHR; External IDs …   Wikipedia

  • Glutathione S-transferase, C-terminal domain — Pfam box Symbol = GST C Name = Glutathione S transferase, C terminal domain width = caption = Pfam= PF00043 InterPro= IPR004046 SMART= Prosite = SCOP = 2gst TCDB = OPM family= 139 OPM protein= 1z9h PDB=PDB3|1gnwA:111 206 PDB3|1bx9A:111 206… …   Wikipedia

  • GSTA2 — Glutathione S transferase A2, also known as GSTA2, is a human gene.cite web | title = Entrez Gene: GSTA2 glutathione S transferase A2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene Cmd=ShowDetailView TermToSearch=2939| accessdate = ] PBB …   Wikipedia

  • Glutathion-S-Transferase — Enzymklassifikation EC, Kategorie …   Deutsch Wikipedia

  • Glutathiontransferase — Glutathion S Transferase Enzymklassifikation EC, Kategorie …   Deutsch Wikipedia

  • Interruptor endocrino — Un interruptor endocrino (también llamado disruptor endocrino o disruptor hormonal; en inglés son llamados endocrine disruptor o EDC, Endocrine Disrupting Chemicals) es una sustancia química, ajena al cuerpo humano o a la especie animal a la que… …   Wikipedia Español

Share the article and excerpts

Direct link
Do a right-click on the link above
and select “Copy Link”