title: Pleiotropic functions of glutathione S-transferase P.
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.
authors: Department of Cell and Molecular Pharmacology and Experimental Therapeutics, Medical University of South Carolina, Charleston, South Carolina, USA.
authors: Jie
authors: J
authors: Zhang
authors: Department of Cell and Molecular Pharmacology and Experimental Therapeutics, Medical University of South Carolina, Charleston, South Carolina, USA.
authors: Christina
authors: C
authors: Grek
authors: Department of Cell and Molecular Pharmacology and Experimental Therapeutics, Medical University of South Carolina, Charleston, South Carolina, USA.
authors: Zhi-Wei
authors: ZW
authors: Ye
authors: Department of Cell and Molecular Pharmacology and Experimental Therapeutics, Medical University of South Carolina, Charleston, South Carolina, USA.
authors: Yefim
authors: Y
authors: Manevich
authors: Professor and Chairman, Department of Cell and Molecular Pharmacology, John C. West Chair of Cancer Research, Medical University of South Carolina, Charleston, South Carolina, USA.
authors: Kenneth D
authors: KD
authors: Tew
authors: Department of Pharmaceutical and Biomedical Sciences, Medical University of South Carolina, Charleston, South Carolina, USA. Electronic address: townsed@musc.edu.
authors: Danyelle M
authors: DM
authors: Townsend
mesh_terms: D000483:Alleles; D000818:Animals; D015971:Gene Expression Regulation, Enzymologic; D015972:Gene Expression Regulation, Neoplastic; D005978:Glutathione / Q000737:chemistry; D051549:Glutathione S-Transferase pi / Q000502:physiology*; D006706:Homeostasis; D006801:Humans; D008024:Ligands; D051379:Mice; D009369:Neoplasms / Q000378:metabolism; D009569:Nitric Oxide / Q000737:chemistry; D019001:Nitric Oxide Synthase / Q000378:metabolism; D010084:Oxidation-Reduction; D018384:Oxidative Stress; D054464:Peroxiredoxins / Q000737:chemistry; D017382:Reactive Oxygen Species / Q000378:metabolism; D015398:Signal Transduction
chemical_list: D008024:Ligands; D017382:Reactive Oxygen Species; D009569:Nitric Oxide; D054464:Peroxiredoxins; D019001:Nitric Oxide Synthase; C496556:GSTP1 protein, human; D051549:Glutathione S-Transferase pi; C496557:Gstp1 protein, mouse; D005978:Glutathione
keywords: Allelic variants; Cysteine; Glutathione; Glutathione S-transferase; Kinase signaling; Nitric oxide; Nitrosylation; Peroxiredoxins; Protein–protein interactions; Sulfur