Pleiotropic Functions of Glutathione S-Transferase P
| Autor: | Yefim Manevich, Danyelle M. Townsend, Christina L. Grek, Zhi-Wei Ye, Kenneth D. Tew, Jie Zhang |
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| Rok vydání: | 2014 |
| Předmět: |
Ligands
Nitric Oxide medicine.disease_cause Gene Expression Regulation Enzymologic Article Protein–protein interaction Nitric oxide Mice chemistry.chemical_compound Neoplasms medicine Animals Homeostasis Humans Alleles biology Nitrosylation Peroxiredoxins Glutathione Gene Expression Regulation Neoplastic Oxidative Stress Glutathione S-transferase Glutathione S-Transferase pi Biochemistry chemistry Chaperone (protein) biology.protein Nitric Oxide Synthase Reactive Oxygen Species Oxidation-Reduction Oxidative stress Signal Transduction Cysteine |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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