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World J Gastroenterol. May 28, 2011; 17(20): 2552-2557
Published online May 28, 2011. doi: 10.3748/wjg.v17.i20.2552
Role of MGST1 in reactive intermediate-induced injury
Courtney S Schaffert
Courtney S Schaffert, Department of Biochemistry and Molecular Biology, University of Nebraska Medical Center, Omaha, NE 68198-5870, United States
Author contributions: Schaffert CS solely contributed to this review.
Correspondence to: Courtney S Schaffert, PhD, Department of Biochemistry and Molecular Biology, University of Nebraska Medical Center, Omaha, NE 68198-5870, United States. cschaffert@unmc.edu
Telephone: +1-402-5596647 Fax: +1-402-5596650
Received: March 17, 2011
Revised: April 15, 2011
Accepted: April 22, 2011
Published online: May 28, 2011
Abstract

Microsomal glutathione transferase (MGST1, EC 2.5.1.18) is a membrane bound glutathione transferase extensively studied for its ability to detoxify reactive intermediates, including metabolic electrophile intermediates and lipophilic hydroperoxides through its glutathione dependent transferase and peroxidase activities. It is expressed in high amounts in the liver, located both in the endoplasmic reticulum and the inner and outer mitochondrial membranes. This enzyme is activated by oxidative stress. Binding of GSH and modification of cysteine 49 (the oxidative stress sensor) has been shown to increase activation and induce conformational changes in the enzyme. These changes have either been shown to enhance the protective effect ascribed to this enzyme or have been shown to contribute to cell death through mitochondrial permeability transition pore formation. The purpose of this review is to elucidate how one enzyme found in two places in the cell subjected to the same conditions of oxidative stress could both help protect against and contribute to reactive oxygen species-induced liver injury.

Keywords: Microsomal glutathione transferase 1; Oxidative stress; Mitochondrial permeability transition; Glutathione; Liver injury