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Pharmaceutics 2013, 5(2), 220-231; doi:10.3390/pharmaceutics5020220
Review

Glutathione Transferase (GST)-Activated Prodrugs

*  and
Institute of Biomolecular Chemistry of CNR, Padova Unit, Via Marzolo 1, Padova 35131, Italy
* Author to whom correspondence should be addressed.
Received: 28 February 2013 / Revised: 21 March 2013 / Accepted: 22 March 2013 / Published: 2 April 2013
(This article belongs to the Special Issue Prodrugs)
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Abstract

Glutathione transferase (formerly GST) catalyzes the inactivation of various electrophile-producing anticancer agents via conjugation to the tripeptide glutathione. Moreover, several data link the overexpression of some GSTs, in particular GSTP1-1, to both natural and acquired resistance to various structurally unrelated anticancer drugs. Tumor overexpression of these proteins has provided a rationale for the search of GST inhibitors and GST activated cytotoxic prodrugs. In the present review we discuss the current structural and pharmacological knowledge of GST-activated cytotoxic compounds.
Keywords: glutatione transferase; glutathione; anticancer prodrugs glutatione transferase; glutathione; anticancer prodrugs
This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

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Ruzza, P.; Calderan, A. Glutathione Transferase (GST)-Activated Prodrugs. Pharmaceutics 2013, 5, 220-231.

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