Glutathione transferases as targets for cancer therapy

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

Research output: Contribution to journalArticlepeer-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 languageEnglish
Pages (from-to)763-777
Number of pages15
JournalAnti-Cancer Agents in Medicinal Chemistry
Volume9
Issue number7
DOIs
Publication statusPublished - 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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