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Blood, 15 March 2007, Vol. 109, No. 6, pp. 2611-2617. Prepublished online as a Blood First Edition Paper on November 14, 2006; DOI 10.1182/blood-2006-09-048728. This Article Full Text (PDF) All Versions of this Article: blood-2006-09-048728v1 109/6/2611    most recent Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Rights and Permissions Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Low, F. M. Articles by Winterbourn, C. C. Search for Related Content PubMed PubMed Citation Articles by Low, F. M. Articles by Winterbourn, C. C. Social Bookmarking                   What's this?  Previous Article  |  Next Article  Submitted September 25, 2006 Accepted November 1, 2006 Peroxiredoxin 2 functions as a non-catalytic scavenger of low level hydrogen peroxide in the erythrocyte Felicia M. Low, Mark B. Hampton, Alexander V. Peskin, and Christine C. Winterbourn* Christchurch School of Medicine & Health Sciences, University of Otago, New Zealand * Corresponding author; email: christine.winterbourn{at}chmeds.ac.nz. Peroxiredoxin 2 (Prx2), a thiol-dependent peroxidase, is the third most abundant protein in the erythrocyte, and its absence in knockout mice gives rise to hemolytic anemia. We have found that in human erythrocytes, Prx2 was extremely sensitive to oxidation by H2O2, as dimerization was observed after exposure of 5 x 106 cells/ml to 0.5 µM H2O2. In contrast to Prx2 in Jurkat T-lymphocytes, Prx2 was resistant to overoxidation (oxidation of the cysteine thiol to a sulfinic/sulfonic acid) in erythrocytes. Reduction of dimerized Prx2 in the erythrocyte occurred very slowly, with reversal occurring gradually over a 20 min period. Very low thioredoxin reductase activity was detected in hemolysates. We postulate that this limits the rate of Prx2 regeneration, and this inefficiency in recycling prevents the overoxidation of Prx2. We also found that Prx2 was oxidized by endogenously generated H2O2, which was mainly derived from hemoglobin autoxidation. Our results demonstrate that in the erythrocyte Prx2 is extremely efficient at scavenging H2O2 non-catalytically. Although it does not act as a classical antioxidant enzyme, its high concentration and substrate sensitivity enable it to handle low H2O2 concentrations efficiently. These unique redox properties may account for its non-redundant role in erythrocyte defense against oxidative stress. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: G. Manandhar, A. Miranda-Vizuete, J. R. Pedrajas, W. J. Krause, S. Zimmerman, M. Sutovsky, and P. Sutovsky Peroxiredoxin 2 and Peroxidase Enzymatic Activity of Mammalian Spermatozoa Biol Reprod, June 1, 2009; 80(6): 1168 - 1177. [Abstract] [Full Text] [PDF] T. Thum and J. Borlak LOX-1 Receptor Blockade Abrogates oxLDL-induced Oxidative DNA Damage and Prevents Activation of the Transcriptional Repressor Oct-1 in Human Coronary Arterial Endothelium J. Biol. Chem., July 11, 2008; 283(28): 19456 - 19464. [Abstract] [Full Text] [PDF] E. Schroder, J. P. Brennan, and P. Eaton Cardiac peroxiredoxins undergo complex modifications during cardiac oxidant stress Am J Physiol Heart Circ Physiol, July 1, 2008; 295(1): H425 - H433. [Abstract] [Full Text] [PDF] M. Reinartz, Z. Ding, U. Flogel, A. Godecke, and J. Schrader Nitrosative Stress Leads to Protein Glutathiolation, Increased S-Nitrosation, and Up-regulation of Peroxiredoxins in the Heart J. Biol. Chem., June 20, 2008; 283(25): 17440 - 17449. [Abstract] [Full Text] [PDF] K. Buchholz, R. H. Schirmer, J. K. Eubel, M. B. Akoachere, T. Dandekar, K. Becker, and S. Gromer Interactions of Methylene Blue with Human Disulfide Reductases and Their Orthologues from Plasmodium falciparum Antimicrob. Agents Chemother., January 1, 2008; 52(1): 183 - 191. [Abstract] [Full Text] [PDF] J. Fang, T. Nakamura, D.-H. Cho, Z. Gu, and S. A. Lipton S-nitrosylation of peroxiredoxin 2 promotes oxidative stress-induced neuronal cell death in Parkinson's disease PNAS, November 20, 2007; 104(47): 18742 - 18747. [Abstract] [Full Text] [PDF] T. R. Hurd, T. A. Prime, M. E. Harbour, K. S. Lilley, and M. P. Murphy Detection of Reactive Oxygen Species-sensitive Thiol Proteins by Redox Difference Gel Electrophoresis: IMPLICATIONS FOR MITOCHONDRIAL REDOX SIGNALING J. Biol. Chem., July 27, 2007; 282(30): 22040 - 22051. [Abstract] [Full Text] [PDF] A. V. Peskin, F. M. Low, L. N. Paton, G. J. Maghzal, M. B. Hampton, and C. C. Winterbourn The High Reactivity of Peroxiredoxin 2 with H2O2 Is Not Reflected in Its Reaction with Other Oxidants and Thiol Reagents J. Biol. Chem., April 20, 2007; 282(16): 11885 - 11892. [Abstract] [Full Text] [PDF]

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