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Originally published In Press as doi:10.1074/jbc.M109720200 on January 15, 2002

J. Biol. Chem., Vol. 277, Issue 12, 10028-10036, March 22, 2002
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Signal Regulatory Protein (SIRPalpha ), a Cellular Ligand for CD47, Regulates Neutrophil Transmigration*

Yuan LiuDagger §, Hans-Jörg Bühring, Ke ZenDagger , Stephanie L. BurstDagger , Frederick J. SchnellDagger , Ifor R. WilliamsDagger , and Charles A. ParkosDagger

From the Dagger  Division of Gastrointestinal Pathology, Department of Pathology and Laboratory Medicine, Emory University, Atlanta, Georgia 30322 and the  Division of Hematology, Immunology and Oncology, Department of Internal Medicine II, University of Tübingen, 72076 Tübingen, Germany

Recent studies have demonstrated that CD47 plays an important role in regulating human neutrophil (PMN) chemotaxis. Two ligands for CD47, thrombospondin and SIRPalpha , have been described. However, it is not known if SIRP-CD47 interactions play a role in regulating PMN migration. In this study, we show that SIRPalpha 1 directly binds to the immunoglobulin variable domain loop of purified human CD47 and that such SIRP-CD47 interactions regulate PMN transmigration. Specifically, PMN migration across both human epithelial monolayers and collagen-coated filters was partially inhibited by anti-SIRP monoclonal antibodies. Similar kinetics of inhibition were observed for PMN transmigration in the presence of soluble, recombinant CD47 consisting of the SIRP-binding loop. In contrast, anti-CD47 monoclonal antibodies inhibited PMN transmigration by markedly different kinetics. Results of signal transduction experiments suggested differential regulation of PMN migration by SIRP versus CD47 by phosphatidylinositol 3-kinase and tyrosine kinases, respectively. Immunoprecipitation followed by Western blotting after SDS-PAGE under nonreducing conditions suggested that several SIRP protein species may be present in PMN. Stimulation of PMN with fMLP resulted in increased surface expression of these SIRP proteins, consistent with the existence of intracellular pools. Taken together, these results demonstrate that PMN migration is regulated by CD47 through SIRPalpha -dependent and SIRPalpha -independent mechanisms.

* This work was supported in part by National Institutes of Health Grants DK10013 (to Y. L.), HL60540, HL54229 (to C. A. P.), and AR44268 (to I. R. W.) and by a Biomedical Sciences grant from the Arthritis Foundation (to C. A. P.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ To whom correspondence should be addressed: Dept. of Pathology and Laboratory Medicine, Whitehead Biomedical Bldg., Rm. 115, Emory University, 615 Michael St., Atlanta, GA 30322. Tel.: 404-727-8665; Fax: 404-727-3321; E-mail: yliu3@emory.edu.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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