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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 (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 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. Social Bookmarking                   What's this? Submitted March 13, 2002 Accepted June 17, 2002 The Src homology 2 domain-containing inositol 5-phosphatase (SHIP) negatively regulates Fc receptor-mediated phagocytosis through ITAM-bearing phagocytic receptors Koji Nakamura, Alexander Malykhin, and K. Mark Coggeshall* Immunobiology & Cancer, Oklahoma Medical Research Foundation, Oklahoma City, OK, USA * Corresponding author; email: mark-coggeshall{at}omrf.ouhsc.edu. 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 ITAM-bearing -chain or human-restricted FcRIIa. These findings indicate that, unlike B cells, SHIP is efficiently phosphorylated in the absence of an 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 over-expressing 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. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: J. Covert, A. J. 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Shibuya, S. Yamazaki, S. Tahara-Hanaoka, S.-i. Honda, M. Osawa, A. Kuroiwa, Y. Matsuda, D. G. Tenen, et al. Paired Activating and Inhibitory Immunoglobulin-like Receptors, MAIR-I and MAIR-II, Regulate Mast Cell and Macrophage Activation J. Exp. Med., July 21, 2003; 198(2): 223 - 233. [Abstract] [Full Text] [PDF] A. R. Crow, S. Song, J. Freedman, C. D. Helgason, R. K. Humphries, K. A. Siminovitch, and A. H. Lazarus IVIg-mediated amelioration of murine ITP via Fc{gamma}RIIB is independent of SHIP1, SHP-1, and Btk activity Blood, July 15, 2003; 102(2): 558 - 560. [Abstract] [Full Text] [PDF] R. A. Pengal, L. P. Ganesan, H. Fang, C. B. Marsh, C. L. Anderson, and S. Tridandapani SHIP-2 Inositol Phosphatase Is Inducibly Expressed in Human Monocytes and Serves to Regulate Fc{gamma} Receptor-mediated Signaling J. Biol. Chem., June 13, 2003; 278(25): 22657 - 22663. [Abstract] [Full Text] [PDF]

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