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Prepublished online as a Blood First Edition Paper on February 13, 2003; DOI 10.1182/blood-2002-08-2548. This Article Full Text (PDF) All Versions of this Article: 2002-08-2548v1 101/12/5033    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 Lee, T.-H. Articles by Yu, D.-Y. Search for Related Content PubMed PubMed Citation Articles by Lee, T.-H. Articles by Yu, D.-Y. Social Bookmarking                   What's this? Submitted August 20, 2002 Accepted February 6, 2003 Peroxiredoxin II is essential for sustaining life span of erythrocytes in mice Tae-Hoon Lee, Sun-Uk Kim, Seong-Lan Yu, Sue Hee Kim, Do-sim Park, Hyung-Bae Moon, Sohee Dho, Ki-Sun Kwon, Hyun jeong Kwon, Ying-Hao Han, Sangkyun Jeong, Sang Won Kang, Hee-Sup Shin, Kyung-Kwang Lee, Sue Goo Rhee, and Dae-Yeul Yu* Laboratory of Development & Differentiation, Korea Research Institute of Bioscience and Biotechnology, Daejeon, Korea, Republic of Departments of Pathology and Laboratory Medicine, Wonkwang University, Iksan, Korea, Republic of Proteome Research Laboratory, Korea Research Institute of Bioscience and Biotechnology, Daejeon, Korea, Republic of Center for Cell Signaling Research, Ewha Womans University, Seoul, Korea, Republic of National Creative Research Initiatives Center for Calcium and Learning, Korea Institute of Science and Technology, Seoul, Korea, Republic of Laboratory of Cell Signaling, NHLBI, NIH, Bethesda, MD, USA * Corresponding author; email: dyyu10{at}kribb.re.kr. Peroxiredoxins (Prxs) are a family of antioxidant proteins that reduce peroxide levels by using reducing agents like thioredoxin. These proteins were characterized to have a number of cellular functions, including, cell proliferation and differentiation, and protects specific proteins from oxidative damage. However, the physiological roles of the peroxiredoxins have not been determined. To clarify the physiological relevance of this protein type, we generated a mouse model deficient in Prx II, which is abundantly expressed in all types of cells. The Prx II-/- mice were healthy in appearance and fertile. However, they had splenomegaly caused by the congestion of red pulp with hemosiderin accumulation. Heinz bodies were detected in their peripheral blood, and morphologically abnormal cells were elevated in the dense RBC fractions, which contained markedly higher levels of reactive oxygen species (ROS). The Prx II-/- mice had significantly decreased hematocrit levels, but increased reticulocyte counts and erythropoietin levels, indicative of a compensatory action to maintain hematological homeostasis in the mice. In addition, a labeling experiment with the thiol modifying reagent BIAM in Prx II-/- mice revealed that a variety of RBC proteins were highly oxidized. Our results suggest that Prx II-/- mice have hemolytic anemia, and that Prx II plays a major role in protecting RBCs from oxidative stress in mice. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: Y. Zhang, Y. Ikeno, W. Qi, A. Chaudhuri, Y. Li, A. Bokov, S. R. Thorpe, J. W. Baynes, C. Epstein, A. Richardson, et al. 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