Sigma-class glutathione transferases

Flanagan, Jack U. and Smythe, Mark L. (2011) Sigma-class glutathione transferases. Drug Metabolism Reviews, 43 2: 194-214. doi:10.3109/03602532.2011.560157

Author Flanagan, Jack U.
Smythe, Mark L.
Title Sigma-class glutathione transferases
Journal name Drug Metabolism Reviews   Check publisher's open access policy
ISSN 0360-2532
Publication date 2011-05
Sub-type Article (original research)
DOI 10.3109/03602532.2011.560157
Volume 43
Issue 2
Start page 194
End page 214
Total pages 21
Place of publication New York, NY, U.S.A.
Publisher Informa Healthcare
Collection year 2012
Language eng
Formatted abstract
Mammalian cytosolic glutathione transferases (GSTs) can be grouped into seven classes. Of these, the sigma class is also widely distributed in nature, with isoforms found in both vertebrates and invertebrates. It contains examples of proteins that have evolved specialized functions, such as the cephalopod lens S-crystallins, the mammalian hematopoietic prostaglandin D2 synthase, and the helminth 28-kDa antigen. In mammals, the sigma-class GST has both anti- and proinflammatory functions, depending on the type of immune response, and an immunomodulatory function is also associated with the enzyme from helminth parasites. In the fly, it is associated with a specific detoxication activity toward lipid oxidation products. Mice genetically depleted of the sigma-class GST, or transgenically overexpressing it, have provided insight into the physiological roles of the GST. Inhibitors of the mammalian enzyme developed by structure-based methods are effective in controlling allergic response. This review covers the structure, function, and pharmacology of vertebrate and invertebrate GSTs.
Keyword Sigma
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2012 Collection
Institute for Molecular Bioscience - Publications
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Citation counts: TR Web of Science Citation Count  Cited 11 times in Thomson Reuters Web of Science Article | Citations
Scopus Citation Count Cited 12 times in Scopus Article | Citations
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Created: Tue, 24 Jan 2012, 13:57:01 EST by Susan Allen on behalf of Institute for Molecular Bioscience