Glutathione<i>S</i>-transferase (GST) inhibitors

Abstract

The glutathione S-transferases (GSTs; EC 2.5.1.18) comprise a family of widely distributed Phase II detoxication enzymes that catalyse the conjugation of a broad variety of reactive electrophiles to the nucleophilic sulfur atom of the major intracellular thiol, the tripeptide glutathione. The diverse functions, including catalytic GSH conjugation, passive ligandin-type binding and modulation of signal transduction, may be selectively targeted by different inhibitors. GST inhibitors are emerging as promising therapeautic agents for managing the development of resistance amongst anticancer agents. In diagnostic medicine, as well as in antiparasitic drug development, GST inhibitors are important lead molecules. In this review, the important molecules known for their GST inhibition together with potential therapeutic uses are summarised.