Glutathione S-transferase A4, also known as GSTA4, is an enzyme which in humans is encoded by the GSTA4 gene.[3][4][5]

GSTA4
Available structures
PDBHuman UniProt search: PDBe RCSB
Identifiers
AliasesGSTA4, GSTA4-4, GTA4, glutathione S-transferase alpha 4
External IDsOMIM: 605450; HomoloGene: 55585; GeneCards: GSTA4; OMA:GSTA4 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001512

n/a

RefSeq (protein)

NP_001503

n/a

Location (UCSC)Chr 6: 52.98 – 53 Mbn/a
PubMed search[2]n/a
Wikidata
View/Edit Human

Function

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Cytosolic and membrane-bound forms of glutathione S-transferase are encoded by two distinct supergene families. These enzymes are involved in cellular defense against toxic, carcinogenic, and pharmacologically active electrophilic compounds. 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, which are located in a cluster on chromosome 6, are highly related and encode enzymes with glutathione peroxidase activity that function in the detoxification of lipid peroxidation products.[3]

GSTA4 shows very high activity with reactive carbonyl compounds such as alk-2-enals.[4] GSTA4 is highly effective in catalyzing the conjugate addition of reduced glutathione to 4-hydroxynonenal, an important product of peroxidative degradation of arachidonic acid and a commonly used biomarker for oxidative damage in tissue.[5]

Clinical significance

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Reactive electrophiles produced by oxidative metabolism have been linked to a number of degenerative diseases including Parkinson's disease, Alzheimer's disease, cataract formation, and atherosclerosis hence reduced expression of the GSTA4 enzyme may have pathophysiological consequences.[3] The expression of this gene is decreased drastically among burn and trauma victims.[citation needed]

References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000170899Ensembl, May 2017
  2. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  3. ^ a b c "Entrez Gene: GSTA4 glutathione S-transferase A4".
  4. ^ a b Board PG (March 1998). "Identification of cDNAs encoding two human alpha class glutathione transferases (GSTA3 and GSTA4) and the heterologous expression of GSTA4-4". Biochem. J. 330 (Pt 2): 827–31. doi:10.1042/bj3300827. PMC 1219212. PMID 9480897.
  5. ^ a b Hubatsch I, Ridderström M, Mannervik B (February 1998). "Human glutathione transferase A4-4: an alpha class enzyme with high catalytic efficiency in the conjugation of 4-hydroxynonenal and other genotoxic products of lipid peroxidation". Biochem. J. 330 (Pt 1): 175–9. doi:10.1042/bj3300175. PMC 1219124. PMID 9461507.

Further reading

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