Glutathione transferases as targets for cancer therapy

Paolo Ruzza; Antonio Rosato; Carlo Riccardo Rossi; Maura Floreani; Luigi Quintieri

doi:10.2174/187152009789056895

Glutathione transferases as targets for cancer therapy

Paolo Ruzza, Antonio Rosato, Carlo Riccardo Rossi, Maura Floreani, Luigi Quintieri

Istituto Oncologico Veneto

Research output: Contribution to journal › Article › peer-review

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 GST-activated cytotoxic prodrugs. In the present review we discuss the current structural and pharmacological knowledge of both types of GST-targeting compounds.

Original language	English
Pages (from-to)	763-777
Number of pages	15
Journal	Anti-Cancer Agents in Medicinal Chemistry
Volume	9
Issue number	7
DOIs	https://doi.org/10.2174/187152009789056895
Publication status	Published - 2009

Keywords

Anticancer drug resistance
Cancer chemotherapy
GST inhibitors
GST-activated prodrugs

ASJC Scopus subject areas

Cancer Research
Molecular Medicine
Pharmacology

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title = "Glutathione transferases as targets for cancer therapy",

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 GST-activated cytotoxic prodrugs. In the present review we discuss the current structural and pharmacological knowledge of both types of GST-targeting compounds.",

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AU - Ruzza, Paolo

AU - Rosato, Antonio

AU - Rossi, Carlo Riccardo

AU - Floreani, Maura

AU - Quintieri, Luigi

PY - 2009

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AB - 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 GST-activated cytotoxic prodrugs. In the present review we discuss the current structural and pharmacological knowledge of both types of GST-targeting compounds.

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Glutathione transferases as targets for cancer therapy

Abstract

Keywords

ASJC Scopus subject areas

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