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Molecular and Cellular Biology, November 1998, p. 6213-6223, Vol. 18, No. 11
Department of Cell
Biology,1
Department of Medicine,
Received 26 March 1998/Returned for modification 15 July
1998/Accepted 31 July 1998
We had previously identified a macrophage surface protein whose
expression is highly induced, transient, and specific, as it is
restricted to actively fusing macrophages in vitro and in vivo. This
protein is recognized by monoclonal antibodies that block macrophage
fusion. We have now purified this protein and cloned its corresponding
cDNA. This protein belongs to the superfamily of immunoglobulins and is
similar to immune antigen receptors such as the T-cell receptor, B-cell
receptor, and viral receptors such as CD4. We have therefore named this
protein macrophage fusion receptor (MFR). We show that the
extracellular domain of MFR prevents fusion of macrophages in vitro and
therefore propose that MFR belongs to the fusion machinery of
macrophages. MFR is identical to SHPS-1 and BIT and is a homologue of
P84, SIRP
0270-7306/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
MFR, a Putative Receptor Mediating the Fusion of
Macrophages
, and MyD-1, all of which have been recently cloned and
implicated in cell signaling and cell-cell interaction events.
*
Corresponding author. Mailing address: Yale University
School of Medicine, Department of Orthopaedics and Rehabilitation, 333 Cedar St., New Haven, CT 06510. Phone: (203) 785-5968. Fax: (203)
737-2701. E-mail: agnes.vignery{at}yale.edu.
Molecular and Cellular Biology, November 1998, p. 6213-6223, Vol. 18, No. 11
0270-7306/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
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