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Blood, 1 January 2006, Vol. 107, No. 1, pp. 341-348. Prepublished online as a Blood First Edition Paper on September 1, 2005; DOI 10.1182/blood-2005-05-1896. This Article Full Text (PDF) Supplemental Table and Figure All Versions of this Article: 2005-05-1896v1 107/1/341    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 Ishikawa-Sekigami, T. Articles by Nojima, Y. Search for Related Content PubMed PubMed Citation Articles by Ishikawa-Sekigami, T. Articles by Nojima, Y. Social Bookmarking                   What's this?  Previous Article  |  Next Article  Submitted May 10, 2005 Accepted August 20, 2005 SHPS-1 promotes the survival of circulating erythrocytes through inhibition of phagocytosis by splenic macrophages Tomomi Ishikawa-Sekigami, Yoriaki Kaneko, Hideki Okazawa, Takeshi Tomizawa, Jun Okajo, Yasuyuki Saito, Chie Okuzawa, Minako Sugawara-Yokoo, Uichi Nishiyama, Hiroshi Ohnishi, Takashi Matozaki*, and Yoshihisa Nojima Department of Medicine and Clinical Science, Gunma University Graduate School of Medicine, Maebashi, Gunma, Japan Laboratory of Biosignal Sciences, Institute for Molecular and Cellular Regulation, Gunma University, Maebashi, Gunma, Japan Pharmaceutical Development Laboratories, Kirin Brewery Co. Ltd., Takasaki, Gunma, Japan * Corresponding author; email: matozaki{at}showa.gunma-u.ac.jp. The life span of circulating red blood cells (RBCs) produced in bone marrow is determined by their elimination through phagocytosis by splenic macrophages. The mechanism by which RBCs elimination is regulated has remained unclear, however. The surface glycoprotein SHPS-1, a member of the immunoglobulin superfamily, is abundant in macrophages. We have now examined the regulation of RBCs turnover with the use of mice that express a mutant form of SHPS-1 lacking most of its cytoplasmic region. The mutant mice manifested mild anemia as well as splenomegaly characterized by expansion of the red pulp. The numbers of erythroid precursor cells in the spleen and of circulating reticulocytes were also increased in the mutant mice. In contrast, the half-life of circulating RBCs was reduced in these animals, and the rate of clearance of injected opsonized RBCs from the peripheral circulation was increased in association with their incorporation into splenic macrophages. Phagocytosis of opsonized RBCs by splenic macrophages from mutant mice in vitro was also increased compared with that observed with wild-type macrophages. These results suggest that SHPS-1 negatively regulates the phagocytosis of RBCs by splenic macrophages, thereby determining both the life span of individual RBCs and the number of circulating erythrocytes. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: H. Sadakata, H. Okazawa, T. Sato, Y. Supriatna, H. Ohnishi, S. Kusakari, Y. Murata, T. Ito, U. Nishiyama, T. Minegishi, et al. SAP-1 is a microvillus-specific protein tyrosine phosphatase that modulates intestinal tumorigenesis Genes Cells, March 1, 2009; 14(3): 295 - 308. [Abstract] [Full Text] [PDF] M. Kobayashi, H. Ohnishi, H. Okazawa, Y. Murata, Y. Hayashi, H. Kobayashi, T. Kitamura, and T. Matozaki Expression of Src Homology 2 Domain-Containing Protein Tyrosine Phosphatase Substrate-1 in Pancreatic {beta}-Cells and Its Role in Promotion of Insulin Secretion and Protection against Diabetes Endocrinology, November 1, 2008; 149(11): 5662 - 5669. [Abstract] [Full Text] [PDF] S. Kusakari, H. Ohnishi, F.-J. Jin, Y. Kaneko, T. Murata, Y. Murata, H. Okazawa, and T. Matozaki Trans-endocytosis of CD47 and SHPS-1 and its role in regulation of the CD47-SHPS-1 system J. Cell Sci., April 15, 2008; 121(8): 1213 - 1223. [Abstract] [Full Text] [PDF] A. Miyake, Y. Murata, H. Okazawa, H. Ikeda, Y. Niwayama, H. Ohnishi, Y. Hirata, and T. Matozaki Negative regulation by SHPS-1 of Toll-like receptor-dependent proinflammatory cytokine production in macrophages. Genes Cells, February 1, 2008; 13(2): 209 - 219. [Abstract] [Full Text] [PDF] M. L. Johansen and E. J. Brown Dual Regulation of SIRP{alpha} Phosphorylation by Integrins and CD47 J. Biol. Chem., August 17, 2007; 282(33): 24219 - 24230. [Abstract] [Full Text] [PDF] T. Tomizawa, Y. Kaneko, Y. Kaneko, Y. Saito, H. Ohnishi, J. Okajo, C. Okuzawa, T. Ishikawa-Sekigami, Y. Murata, H. Okazawa, et al. Resistance to Experimental Autoimmune Encephalomyelitis and Impaired T Cell Priming by Dendritic Cells in Src Homology 2 Domain-Containing Protein Tyrosine Phosphatase Substrate-1 Mutant Mice J. Immunol., July 15, 2007; 179(2): 869 - 877. [Abstract] [Full Text] [PDF] J. Okajo, Y. Kaneko, Y. Murata, T. Tomizawa, C. Okuzawa, Y. Saito, Y. Kaneko, T. Ishikawa-Sekigami, H. Okazawa, H. Ohnishi, et al. Regulation by Src Homology 2 Domain-Containing Protein Tyrosine Phosphatase Substrate-1 of {alpha}-Galactosylceramide-Induced Antimetastatic Activity and Th1 and Th2 Responses of NKT Cells J. Immunol., May 15, 2007; 178(10): 6164 - 6172. [Abstract] [Full Text] [PDF] H. Ikeda, H. Okazawa, H. Ohnishi, Y. Murata, P.-A. Oldenborg, and T. Matozaki Mutational analysis of the mechanism of negative regulation by SRC homology 2 domain-containing protein tyrosine phosphatase substrate-1 of phagocytosis in macrophages. J. Immunol., September 1, 2006; 177(5): 3123 - 3132. [Abstract] [Full Text] [PDF]

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