| Literature DB >> 24974181 |
Jie Zhang1, Christina Grek1, Zhi-Wei Ye1, Yefim Manevich1, Kenneth D Tew2, Danyelle M Townsend3.
Abstract
Glutathione S-transferase P (GSTP) is one member of the GST superfamily that is prevalently expressed in mammals. Known to possess catalytic activity through deprotonating glutathione allowing formation of thioether bonds with electrophilic substrates, more recent discoveries have broadened our understanding of the biological roles of this protein. In addition to catalytic detoxification, other properties so far ascribed to GSTP include chaperone functions, regulation of nitric oxide pathways, regulation of a variety of kinase signaling pathways, and participation in the forward reaction of protein S-glutathionylation. The expression of GSTP has been linked with cancer and other human pathologies and more recently even with drug addiction. With respect to human health, polymorphic variants of GSTP may determine individual susceptibility to oxidative stress and/or be critical in the design and development of drugs that have used redox pathways as a discovery platform.Entities:
Keywords: Allelic variants; Cysteine; Glutathione; Glutathione S-transferase; Kinase signaling; Nitric oxide; Nitrosylation; Peroxiredoxins; Protein–protein interactions; Sulfur
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Year: 2014 PMID: 24974181 PMCID: PMC5079281 DOI: 10.1016/B978-0-12-420117-0.00004-9
Source DB: PubMed Journal: Adv Cancer Res ISSN: 0065-230X Impact factor: 6.242