Jump to content

Glutathione S-transferase A1

From Wikipedia, the free encyclopedia

This is an old revision of this page, as edited by OAbot (talk | contribs) at 03:33, 14 June 2020 (Open access bot: doi added to citation with #oabot.). The present address (URL) is a permanent link to this revision, which may differ significantly from the current revision.

GSTA1
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesGSTA1, GST2, GSTA1-1, GTH1, GST-epsilon, glutathione S-transferase alpha 1
External IDsOMIM: 138359; MGI: 95863; HomoloGene: 130684; GeneCards: GSTA1; OMA:GSTA1 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_145740
NM_001319059

NM_008182

RefSeq (protein)

NP_001305988
NP_665683

NP_032208

Location (UCSC)Chr 6: 52.79 – 52.8 MbChr 9: 78.24 – 78.26 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Glutathione S-transferase A1 is an enzyme that in humans is encoded by the GSTA1 gene.[5]

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 (hepatocytes) and kidney (proximal tubules). 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.[6]

Release of GST-A1 as an indication of cellular necrosis

Increases in serum and urinary GST-A1 have been found in association with hepatocyte and renal proximal tubular necrosis respectively and have potential for monitoring injury to these tissues.[7][8]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000243955Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000057933Ensembl, 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. ^ Mucher G, Becker J, Knapp M, Buttner R, Moser M, Rudnik-Schoneborn S, Somlo S, Germino G, Onuchic L, Avner E, Guay-Woodford L, Zerres K (Apr 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.
  6. ^ "Entrez Gene: GSTA1 glutathione S-transferase A1".
  7. ^ Knapen, MF; Mulder, TP; Bisseling, JG; Penders, RH; Peters, WH; Steegers, EA (January 1998). "Plasma glutathione S-transferase alpha 1-1: a more sensitive marker for hepatocellular damage than serum alanine aminotransferase in hypertensive disorders of pregnancy". American Journal of Obstetrics and Gynecology. 178 (1 Pt 1): 161–5. doi:10.1016/S0002-9378(98)70645-3. PMID 9465822.
  8. ^ Heemskerk, S; Pickkers, P; Bouw, MP; Draisma, A; van der Hoeven, JG; Peters, WH; Smits, P; Russel, FG; Masereeuw, R (July 2006). "Upregulation of renal inducible nitric oxide synthase during human endotoxemia and sepsis is associated with proximal tubule injury". Clinical Journal of the American Society of Nephrology. 1 (4): 853–62. doi:10.2215/cjn.00490206. PMID 17699297.

Further reading