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Ruzza, P. et al.

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

Glutathione transferases as targets for cancer therapy.

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.[1]

References

Glutathione transferases as targets for cancer therapy. Ruzza, P., Rosato, A., Rossi, C.R., Floreani, M., Quintieri, L. Anticancer. Agents. Med. Chem (2009) [Pubmed]

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