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Current Protein & Peptide Science

Editor-in-Chief

ISSN (Print): 1389-2037
ISSN (Online): 1875-5550

Mammalian Cytosolic Glutathione Transferases

Author(s): Daniel F.A.R. Dourado, Pedro Alexandrino Fernandes and Maria Joao Ramos

Volume 9, Issue 4, 2008

Page: [325 - 337] Pages: 13

DOI: 10.2174/138920308785132677

Price: $65

Abstract

Glutathione Transferases (GSTs) are crucial enzymes in the cell detoxification process catalyzing the nucleophilic attack of glutathione (GSH) on toxic electrophilic substrates and producing a less dangerous compound. GSTs studies are of great importance since they have been implicated in the development of drug resistance in tumoral cells and are related to human diseases such as Parkinsons, Alzheimers, atherosclerois, liver cirrhosis, aging and cataract formation. In this review we start by providing an evolutionary perspective of the mammalian cytosolic GSTs known to date. Later on we focus on the more abundant classes alpha, mu and pi and their structure, catalysis, metabolic associated functions, drug resistance relation and inhibition methods. Finally, we introduce the recent insights on the GST class zeta from a metabolic perspective.

Keywords: Glutathione S-tranferase (GST), Glutathione (GSH), Glutathione S-transferase (GST) classes alpha, mu, pi and zeta, catalysis, metabolism of endogenous compounds, tumorogenesis, inhibition methods


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