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

Glutathione Transferase (GST)-Activated Prodrugs

*  and
Received: 28 February 2013; in revised form: 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 which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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MDPI and ACS Style

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

AMA Style

Ruzza P, Calderan A. Glutathione Transferase (GST)-Activated Prodrugs. Pharmaceutics. 2013; 5(2):220-231.

Chicago/Turabian Style

Ruzza, Paolo; Calderan, Andrea. 2013. "Glutathione Transferase (GST)-Activated Prodrugs." Pharmaceutics 5, no. 2: 220-231.



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