Glutathione S-transferase Mu 1

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Glutathione S-transferase M1
PDB rendering based on 1gtu.
Available structures: 1gtu, 1xw6, 1xwk, 1yj6, 2f3m
Identifiers
Symbol(s) GSTM1; GST1; GSTM1-1; GSTM1a-1a; GSTM1b-1b; GTH4; GTM1; H-B; MGC26563; MU; MU-1
External IDs OMIM: 138350 MGI95861 HomoloGene84561
RNA expression pattern

More reference expression data

Orthologs
Human Mouse
Entrez 2944 14863
Ensembl ENSG00000134184 n/a
Uniprot P09488 n/a
Refseq NM_000561 (mRNA)
NP_000552 (protein)
NM_008183 (mRNA)
NP_032209 (protein)
Location Chr 1: 110.03 - 110.04 Mb n/a
Pubmed search [1] [2]

Glutathione S-transferase Mu 1 (gene name GSTM1) is a human glutathione S-transferase.

Cytosolic and membrane-bound forms of glutathione S-transferase are encoded by two distinct supergene families. 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 cytoplasmic glutathione S-transferase that belongs to the mu class. The mu class of enzymes functions in the detoxification of electrophilic compounds, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress, by conjugation with glutathione. The genes encoding the mu class of enzymes are organized in a gene cluster on chromosome 1p13.3 and 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 certain drugs. Null mutations of this class mu gene have been linked with an increase in a number of cancers, likely due to an increased susceptibility to environmental toxins and carcinogens. Multiple protein isoforms are encoded by transcript variants of this gene.[1]

[edit] References

[edit] Further reading

  • Engel LS, Taioli E, Pfeiffer R, et al. (2002). "Pooled analysis and meta-analysis of glutathione S-transferase M1 and bladder cancer: a HuGE review.". Am. J. Epidemiol. 156 (2): 95–109. PMID 12117698. 
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