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Blood, 1 April 2001, Vol. 97, No. 7, pp. 2159-2164
RED CELLS
Integrin-associated protein is an adhesion receptor on sickle red
blood cells for immobilized thrombospondin
Julia E. Brittain,
Kathryn
J. Mlinar,
Christopher S. Anderson,
Eugene P. Orringer, and
Leslie V. Parise
From the Departments of Pharmacology and Medicine,
School of Medicine, Center for Thrombosis and Hemostasis and Lineberger
Comprehensive Cancer Center, The University of North Carolina at Chapel
Hill.
The adhesive protein thrombospondin (TSP) potentially
mediates sickle (SS) red blood cell (RBC) adhesion to the blood vessel wall, thereby contributing to vaso-occlusive crises in sickle cell
disease. We previously reported that SS RBCs bind to immobilized TSP
under flow conditions, whereas normal (AA) red cells do not. However,
the SS RBC receptors that mediate this interaction are largely unknown.
Here it is reported that integrin-associated protein (IAP), or CD47,
mediates the adhesion of these cells to immobilized TSP under both flow
and static conditions. A peptide derived from the C-terminal IAP
binding site of TSP also supports sickle cell adhesion; adhesion to
this peptide or to TSP is inhibited specifically by the anti-IAP
monoclonal antibody, 1F7. Furthermore, these data suggest that IAP on
SS RBCs is structurally different from that expressed on AA RBCs but
that IAP expression levels do not vary between AA and SS RBCs. This
structural difference may contribute to the enhanced adhesion of SS
RBCs to immobilized TSP. These results identify IAP as a TSP receptor
on SS RBCs and suggest that this receptor and its binding site within
TSP represent potential therapeutic targets to decrease
vaso-occlusion.
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