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Antioxid Redox Signal. 2011 Feb 15;14(4):725-30. doi: 10.1089/ars.2010.3717. Epub 2010 Dec 17.

Is overoxidation of peroxiredoxin physiologically significant?

Author information

1
Department of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, Michigan 48109, USA.

Abstract

Eukaryotic peroxiredoxins are highly susceptible to sulfinic acid formation. This overoxidation, which is thought to convert peroxiredoxins into chaperones, can be reversed by sulfiredoxins. Several organisms, including Caenorhabditis elegans, lack sulfiredoxins but encode sestrins, proteins proposed to be functionally equivalent. We induced peroxiredoxin overoxidation in C. elegans with a short peroxide pulse. We found that reduction of overoxidized peroxiredoxin 2 (PRDX-2) was extremely slow and sestrin-independent, strongly implying that worms lack an efficient repair system. Analysis of PRDX-2's overoxidation status during C. elegans lifespan revealed no accumulation of overoxidized PRDX-2 at any point, questioning whether PRDX-2 overoxidation in worms is physiologically relevant.

PMID:
20964547
PMCID:
PMC3021361
DOI:
10.1089/ars.2010.3717
[Indexed for MEDLINE]
Free PMC Article

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