Cyclopentenone prostaglandins with dienone structure promote cross-linking of the chemoresistance-inducing enzyme glutathione transferase P1-1

Molecular Pharmacology
Francisco J Sánchez-GómezDolores Pérez-Sala

Abstract

Glutathione transferase P1-1 (GSTP1-1) plays crucial roles in cancer chemoprevention and chemoresistance and is a key target for anticancer drug development. Oxidative stress or inhibitor-induced GSTP1-1 oligomerization leads to the activation of stress cascades and apoptosis in various tumor cells. Therefore, bivalent glutathione transferase (GST) inhibitors with the potential to interact with GST dimers are been sought as pharmacological and/or therapeutic agents. Here we have characterized GSTP1-1 oligomerization in response to various endogenous and exogenous agents. Ethacrynic acid, a classic GSTP1-1 inhibitor, 4-hydroxy-nonenal, hydrogen peroxide, and diamide all induced reversible GSTP1-1 oligomerization in Jurkat leukemia cells through the formation of disulphide bonds involving Cys47 and/or Cys101, as suggested by reducing and nonreducing SDS-polyacrylamide gel electrophoresis analysis of cysteine to serine mutants. Remarkably, the electrophilic prostanoid 15-deoxy-Δ(12,14)-prostaglandin J(2) (15d-PGJ(2)) induced irreversible GSTP1-1 oligomerization, specifically involving Cys101, a residue present in the human but not in the murine enzyme. 15d-PGJ(2)-induced GSTP1-1 cross-linking required the prostaglandin (PG) dienon...Continue Reading

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Citations

Jun 19, 2013·Journal of Proteomics·Rosário M DominguesCorinne M Spickett
Mar 1, 2011·Drug Metabolism Reviews·Kenneth D Tew, Danyelle M Townsend
Mar 13, 2012·Cancer Letters·Beatriz Díez-Dacal, Dolores Pérez-Sala
Jun 15, 2015·Redox Biology·Giancarlo AldiniDolores Pérez-Sala
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Dec 1, 2017·Antioxidants & Redox Signaling·María A Pajares, Dolores Pérez-Sala
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Mar 7, 2021·Antioxidants·Álvaro Viedma-PoyatosDolores Pérez-Sala
Jun 15, 2019·Free Radical Biology & Medicine·Sofia DuarteDolores Pérez-Sala

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