The Prxs (peroxiredoxins) are a family of cysteine-dependent peroxidases that decompose hydrogen peroxide. Prxs become hyperoxidized when a sulfenic acid formed during the catalytic cycle reacts with hydrogen peroxide. In the present study, Western blot methodology was developed to quantify hyperoxidation of individual 2-Cys Prxs in cells. It revealed that Prx 1 and 2 were hyperoxidized at lower doses of hydrogen peroxide than would be predicted from in vitro data, suggesting intracellular factors that promote hyperoxidation. In contrast, mitochondrial Prx 3 was considerably more resistant to hyperoxidation. The concentration of Prx 3 was estimated at 125 μM in the mitochondrial matrix of Jurkat T-lymphoma cells. Although the local cellular environment could influence susceptibility, purified Prx 3 was also more resistant to hyperoxidation, suggesting that despite having C-terminal motifs similar to sensitive eukaryote Prxs, other structural features must contribute to the innate resilience of Prx 3 to hyperoxidation.
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July 2009
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Research Article|
June 12 2009
Mitochondrial peroxiredoxin 3 is more resilient to hyperoxidation than cytoplasmic peroxiredoxins Available to Purchase
Andrew G. Cox;
Andrew G. Cox
*Free Radical Research Group and National Research Centre for Growth and Development, Department of Pathology, University of Otago, Christchurch, New Zealand
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Andree G. Pearson;
Andree G. Pearson
*Free Radical Research Group and National Research Centre for Growth and Development, Department of Pathology, University of Otago, Christchurch, New Zealand
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Juliet M. Pullar;
Juliet M. Pullar
*Free Radical Research Group and National Research Centre for Growth and Development, Department of Pathology, University of Otago, Christchurch, New Zealand
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Thomas J. Jönsson;
Thomas J. Jönsson
†Center for Structural Biology and Department of Biochemistry, Wake Forest University School of Medicine, Winston-Salem, NC, U.S.A.
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W. Todd Lowther;
W. Todd Lowther
†Center for Structural Biology and Department of Biochemistry, Wake Forest University School of Medicine, Winston-Salem, NC, U.S.A.
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Christine C. Winterbourn;
Christine C. Winterbourn
*Free Radical Research Group and National Research Centre for Growth and Development, Department of Pathology, University of Otago, Christchurch, New Zealand
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Mark B. Hampton
Mark B. Hampton
1
*Free Radical Research Group and National Research Centre for Growth and Development, Department of Pathology, University of Otago, Christchurch, New Zealand
1To whom correspondence should be addressed (email [email protected]).
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Publisher: Portland Press Ltd
Received:
February 11 2009
Revision Received:
April 07 2009
Accepted:
April 08 2009
Accepted Manuscript online:
April 08 2009
Online ISSN: 1470-8728
Print ISSN: 0264-6021
© The Authors Journal compilation © 2009 Biochemical Society
2009
Biochem J (2009) 421 (1): 51–58.
Article history
Received:
February 11 2009
Revision Received:
April 07 2009
Accepted:
April 08 2009
Accepted Manuscript online:
April 08 2009
Citation
Andrew G. Cox, Andree G. Pearson, Juliet M. Pullar, Thomas J. Jönsson, W. Todd Lowther, Christine C. Winterbourn, Mark B. Hampton; Mitochondrial peroxiredoxin 3 is more resilient to hyperoxidation than cytoplasmic peroxiredoxins. Biochem J 1 July 2009; 421 (1): 51–58. doi: https://doi.org/10.1042/BJ20090242
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