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Blood, Vol. 94 No. 11 (December 1), 1999:
pp. 3633-3643
Human Signal-Regulatory Protein Is Expressed on Normal, But Not on
Subsets of Leukemic Myeloid Cells and Mediates Cellular Adhesion
Involving Its Counterreceptor CD47
Martina Seiffert,
Charles Cant,
Zhengjun Chen,
Irene Rappold,
Wolfram Brugger,
Lothar Kanz,
Eric J. Brown,
Axel Ullrich, and
Hans-Jörg Bühring
From the University of Tübingen, the Department of Internal
Medicine II, the Division of Hematology, Immunology, and Oncology,
Tübingen, Germany; the Max-Planck-Institute for Biochemistry, the
Department of Molecular Biology, Martinsried, Germany; and the
University of California, Program in Microbial Pathogenesis and Host
Defence, San Francisco, CA.
Signal-regulatory proteins (SIRPs) comprise a novel transmembrane
glycoprotein family involved in the negative regulation of receptor
tyrosine kinase-coupled signaling pathways. To analyze the expression
and function of SIRPs, we prepared soluble recombinant fusion proteins
of the extracellular regions of SIRP 1 and SIRP2, as well as a
variety of monoclonal antibodies (MoAbs) against these domains. The
antibodies reacted predominantly with monocytes, granulocytes,
dendritic cells, and their precursors, as well as with bone marrow
CD34+, AC133+, CD90+
hematopoietic stem/progenitor cells. In contrast, SIRP expression was
absent or significantly reduced on the majority of myeloid blasts from
patients with acute myeloid leukemia (AML) or chronic myeloid leukemia
(CML). Functional studies showed that the extracellular domains of
SIRP1 and SIRP2 support adhesion of a number of primary hematopoietic cells and cell lines. This interaction could be blocked
by 4 of 7 SIRP1-reactive MoAbs. In addition, SIRP1 and SIRP2
competed for the same cell binding site, suggesting a common widely
expressed SIRP ligand. In an approach to identify this molecule, MoAbs
were generated against the SIRP-binding cell line CCRF-CEM, and MoAb
CC2C6 was selected because of its capacity to inhibit cell binding to
SIRP1. Further analysis showed that this antibody recognized CD47, a
ubiquitously expressed plasma membrane protein previously implicated in
integrin function, host defense action, and neutrophil migration. In
this study, we identify CD47 as the extracellular ligand for human SIRP
and show that these two counterreceptors are involved in cellular adhesion.
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