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J. Biol. Chem., Vol. 278, Issue 39, 37146-37153, September 26, 2003
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From the
Commissariat à l'Energie Atomique-Laboratoire de Bioénergétique Cellulaire et Pathologique, EA 2943, Département Réponses et Dynamique Cellulaire/BioEnergétique Cellulaire et Pathologique-Grenoble, 17 rue des martyrs, F-38054 Grenoble Cedex 9, France and ¶Laboratoire de Spectrométrie de Masse Bio-Organique, Unité Mixte de recherche CNRS 7509, Ecole de Chimie, Polymères et Matériaux, 25 rue Becquerel, 67002 Strasbourg Cedex, France
Peroxiredoxins (prx) are redox enzymes using an activated cysteine as their active site. This activated cysteine can be easily overoxidized to cysteine sulfinic acid or cysteine sulfonic acid, especially under oxidative stress conditions. The regeneration of peroxiredoxins after a short, intense oxidative stress was studied, using a proteomics approach. Important differences in regeneration speed were found, prx2 being the fastest regenerated protein, followed by prx1, whereas prx3 and prx6 were regenerated very slowly. Further study of the mechanism of this regeneration by pulse-chase experiments using stable isotope labeling and cycloheximide demonstrated that the fast-regenerating peroxiredoxins are regenerated at least in part by a retroreduction mechanism. This demonstrates that the overoxidation can be reversible under certain conditions. The pathway of this retroreduction and the reasons explaining the various regeneration speeds of the peroxiredoxins remain to be elucidated.
Received for publication, May 16, 2003 , and in revised form, July 7, 2003.
* The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
These two authors contributed equally to this work.
|| To whom correspondence should be addressed: DRDC/BECP, CEA-Grenoble, 17 rue des martyrs, F-38054 Grenoble Cedex 9, France. Tel.: 33-438-78-32-12; Fax: 33-438-78-51-87; E-mail: Thierry.rabilloud{at}cea.fr.
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