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Papers In Press, published online ahead of print January 15, 2002
Department of Pathology and Laboratory Medicine, Emory University, Atlanta, GA 30322
Corresponding Author: yliu3{at}emory.edu
Recent studies have demonstrated that CD47 plays an important role in regulating human neutrophil (PMN) chemotaxis. Two ligands for CD47, thrombospondin and SIRP
J. Biol. Chem, 10.1074/jbc.M109720200
Submitted on October 9, 2001
Revised on January 11, 2002
Accepted on January 14, 2002
Signal regulatory protein (SIRP
), a cellular ligand for CD47, regulates PMN transmigration
, 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 SIRP1 directly binds to the IgV 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 mAbs. 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 mAbs inhibited PMN transmigration by markedly different kinetics. Results of signal transduction experiments suggested differential regulation of PMN migration by SIRP versus CD47 by PI3 kinase and tyrosine kinases, respectively. Immunoprecipitation followed by western blotting after SDS-PAGE under non-reducing 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 SIRP-dependent and SIRP-independent mechanisms.
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