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Prepublished online as a Blood First Edition Paper on July 12, 2002; DOI 10.1182/blood-2002-03-0787. This Article Full Text Full Text (PDF) All Versions of this Article: 2002-03-0787v1 100/9/3374    most recent Alert me when this article is cited Alert me if a correction is posted Citation Map 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 Nakamura, K. Articles by Coggeshall, K. M. Search for Related Content PubMed PubMed Citation Articles by Nakamura, K. Articles by Coggeshall, K. M. Related Collections Phagocytes Signal Transduction Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  Blood, 1 November 2002, Vol. 100, No. 9, pp. 3374-3382 PHAGOCYTES The Src homology 2 domain-containing inositol 5-phosphatase negatively regulates Fc receptor-mediated phagocytosis through immunoreceptor tyrosine-based activation motif-bearing phagocytic receptors Koji Nakamura, Alexander Malykhin, and K. Mark Coggeshall From The Oklahoma Medical Research Foundation, Program in Immunobiology and Cancer, Oklahoma City, OK. Molecular mechanisms by which the Src homology 2 domain-containing inositol 5-phosphatase (SHIP) negatively regulates phagocytosis in macrophages are unclear. We addressed the issue using bone marrow-derived macrophages from FcR- or SHIP-deficient mice. Phagocytic activities of macrophages from FcRII(b)/ and SHIP/ mice were enhanced to a similar extent, relative to those from wild type. However, calcium influx was only marginally affected in FcRII(b)/, but greatly enhanced in SHIP/ macrophages. Furthermore, SHIP was phosphorylated on tyrosine residues upon FcR aggregation even in macrophages from FcRII(b)/ mice or upon clustering of a chimeric receptor containing CD8 and the immunoreceptor tyrosine-based activation motif (ITAM)-bearing -chain or human-restricted FcRIIa. These findings indicate that, unlike B cells, SHIP is efficiently phosphorylated in the absence of an immunoreceptor tyrosine-based inhibition motif (ITIM)-bearing receptor. We further demonstrate that SHIP directly bound to phosphorylated peptides derived from FcRIIa with a high affinity, comparable to that of FcRII(b). Lastly, FcRIIa-mediated phagocytosis was significantly enhanced in THP-1 cells overexpressing dominant-negative form of SHIP in the absence of FcRII(b). These results indicate that SHIP negatively regulates FcR-mediated phagocytosis through all ITAM-containing IgG receptors using a molecular mechanism distinct from that in B cells. © 2002 by The American Society of Hematology.   CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: L. A. Kamen, J. Levinsohn, A. Cadwallader, S. Tridandapani, and J. A. Swanson SHIP-1 Increases Early Oxidative Burst and Regulates Phagosome Maturation in Macrophages J. Immunol., June 1, 2008; 180(11): 7497 - 7505. [Abstract] [Full Text] [PDF] C. Canetti, C. H. Serezani, R. G. Atrasz, E. S. White, D. M. Aronoff, and M. Peters-Golden Activation of Phosphatase and Tensin Homolog on Chromosome 10 Mediates the Inhibition of Fc{gamma}R Phagocytosis by Prostaglandin E2 in Alveolar Macrophages J. Immunol., December 15, 2007; 179(12): 8350 - 8356. [Abstract] [Full Text] [PDF] K. A. Horan, K.-i. Watanabe, A. M. Kong, C. G. Bailey, J. E. 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