Mammalian cytosolic glutathione transferases

• Type: Another Publication in an International Scientific Journal
• Date: 2008

Authors

Daniel F A R Dourado (Author) Other; Pedro Alexandrino Fernandes (Author) FCUP; Maria Joao Ramos (Author) FCUP

Journal

Title: CURRENT PROTEIN & PEPTIDE SCIENCE

Vol. 9

Pages: 325-337

ISSN: 1389-2037

Publisher: Bentham Science

Indexing

ISI Web of Knowledge - 59 Citations

Scopus - 66 Citations

Scientific classification

FOS: Natural sciences > Biological sciences

Other information

Authenticus ID: P-003-X6F

DOI: 10.2174/138920308785132677

Abstract (EN): 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 Parkinson's, Alzheimer's, 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.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 13