Glutathione S-transferase A1

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Glutathione S-transferase alpha 1
Human glutathione transferase (GST) A1-1 in complex with glutathione. PDB rendering based on 1pkw[1].
Available structures
PDB Ortholog search: PDBe, RCSB
Symbols GSTA1 ; GST2; GSTA1-1; GTH1
External IDs OMIM138359 HomoloGene130684 ChEMBL: 3409 GeneCards: GSTA1 Gene
EC number
RNA expression pattern
PBB GE GSTA1 203924 at tn.png
More reference expression data
Species Human Mouse
Entrez 2938 n/a
Ensembl ENSG00000243955 n/a
UniProt P08263 n/a
RefSeq (mRNA) NM_145740 n/a
RefSeq (protein) NP_665683 n/a
Location (UCSC) Chr 6:
52.61 – 52.63 Mb
PubMed search [1] n/a

Glutathione S-transferase A1 is an enzyme that in humans is encoded by the GSTA1 gene.[2]

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.[3]

Release of GST-A1 as an indication of cellular necrosis[edit]

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.[4][5]


  1. ^ Grahn, E.; Novotny, M.; Jakobsson, E.; Gustafsson, A.; Grehn, L.; Olin, B.; Madsen, D.; Wahlberg, M. R.; Mannervik, B.; Kleywegt, G. J. (2006). "New crystal structures of human glutathione transferase A1-1 shed light on glutathione binding and the conformation of the C-terminal helix". Acta Crystallographica Section D Biological Crystallography 62 (2): 197–207. doi:10.1107/S0907444905039296. PMID 16421451.  edit
  2. ^ 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. 
  3. ^ "Entrez Gene: GSTA1 glutathione S-transferase A1". 
  4. ^ 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. PMID 9465822. 
  5. ^ 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 : CJASN 1 (4): 853–62. doi:10.2215/cjn.00490206. PMID 17699297. 

Further reading[edit]