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Originally published In Press as doi:10.1074/jbc.M002334200 on August 29, 2000

J. Biol. Chem., Vol. 275, Issue 48, 37984-37992, December 1, 2000
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CD47, a Ligand for the Macrophage Fusion Receptor, Participates in Macrophage Multinucleation*

Xin HanDagger , Hyacinth SterlingDagger , Yongmei Chen§, Charles SaginarioDagger , Eric J. Brown, William A. Frazier||, Frederik P. Lindberg§**, and Agnès VigneryDagger **Dagger Dagger

From the Dagger  Yale University School of Medicine, Departments of Cell Biology and Orthopaedics and Rehabilitation, New Haven, Connecticut 06510, the § Washington University School of Medicine, Division of Infectious Diseases, St. Louis, Missouri 63110, the  University of California, San Francisco, Center for Host/Pathogen Interactions, San Francisco, California 94143, and the || Washington University School of Medicine, Department of Biochemistry, St. Louis, Missouri 63110

The macrophage fusion receptor (MFR), also called P84/BIT/SIRPalpha /SHPS-1, is a transmembrane glycoprotein that belongs to the superfamily of immunoglobulins. Previously, we showed that MFR expression is highly induced at the onset of fusion in macrophages, and that MFR appears to play a role in macrophage-macrophage adhesion/fusion leading to multinucleation. The recent finding that IAP/CD47 acts as a ligand for MFR led us to hypothesize that it interacts with CD47 at the onset of cell-cell fusion. CD47 is a transmembrane glycoprotein, which, like MFR, belongs to the superfamily of immunoglobulins. We show that macrophages express the hemopoietic form of CD47, the expression of which is induced at the onset of fusion, but to a lower level than MFR. A glutathione S-transferase CD47 fusion protein engineered to contain the extracellular domain of CD47, binds macrophages, associates with MFR, and prevents multinucleation. CD47 and MFR associate via their amino-terminal immunoglobulin variable domain. Of the nine monoclonal antibodies raised against the extracellular domain of CD47, three block fusion, as well as MFR-CD47 interaction, whereas the others have no effect. Together, these data suggest that CD47 is involved in macrophage multinucleation by virtue of interacting with MFR during adhesion/fusion.

* This work was supported by National Institutes of Health Grants DE12110 (to A. V.) and GM57573-01 (to F. P. L.) and by a grant from Monsanto to Washington University (to F. P. L.).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.

** These authors made equal contributions to this work.

Dagger Dagger To whom correspondence should be addressed: Dept. of Orthopaedics and Rehabilitation, Yale University School of Medicine, 333 Cedar St., New Haven, CT 06510. Tel.: 203-785-5968; Fax: 203-737-2701; E-mail: agnes.vignery@yale.edu.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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