Glutathione Transferases as Targets for Cancer Therapy

ISSN: 1875-5992 (Online)
ISSN: 1871-5206 (Print)


Volume 16, 12 Issues, 2016


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Anti-Cancer Agents in Medicinal Chemistry

Formerly: Current Medicinal Chemistry - Anti-Cancer Agents

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  • 27th of 59 in Chemistry, Medicinal

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Editor-in-Chief:
Michelle Prudhomme
Universite Blaise Pascal - C.N.R.S
Aubiere Cedex
France


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Glutathione Transferases as Targets for Cancer Therapy



Anti-Cancer Agents in Medicinal Chemistry, 9(7): 763-777.

Author(s): Paolo Ruzza, Antonio Rosato, Carlo Riccardo Rossi, Maura Floreani and Luigi Quintieri.

Affiliation: Institute of Biomolecular Chemistry of CNR, Padova Unit, Via F. Marzolo 1, I-35131 Padova, Italy.

Abstract

Besides catalyzing the inactivation of various electrophile-producing anticancer agents via conjugation to the tripeptide glutathione, some cytosolic proteins belonging to the glutathione transferase (formerly glutatione-S-transferase; GST) superfamily are emerging as negative modulators of stress/drug-induced cell apoptosis through the interaction with specific signaling kinases. In addition, 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 GSTactivated cytotoxic prodrugs. In the present review we discuss the current structural and pharmacological knowledge of both types of GST-targeting compounds.

Keywords:

GST inhibitors, GST-activated prodrugs, cancer chemotherapy, anticancer drug resistance.



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Article Details

Volume: 9
Issue Number: 7
First Page: 763
Last Page: 777
Page Count: 15
DOI: 10.2174/187152009789056895
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