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(Received for publication, April 1, 1997)
From the Department of Biochemistry and Molecular Biophysics,
Washington University School of Medicine,
St. Louis, Missouri 63110
Integrin-associated protein (IAP or CD47) is a
receptor for the cell/platelet-binding domain (CBD) of thrombospondin-1
(TS1), the most abundant protein of platelet
Volume 272, Number 23,
Issue of June 6, 1997
pp. 14740-14746
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
IIb
3
granules. Although it associates with IIb
3, IAP has no known function in platelets. TS1, the CBD, and an IAP agonist peptide (4N1K) from the CBD of TS1
activate the platelet integrin IIb3, resulting in platelet spreading on immobilized fibrinogen, stimulation of platelet
aggregation, and enhanced tyrosine phosphorylation of focal adhesion
kinase. Furthermore, 4N1K peptide selectively stimulates the
phosphorylation of LYN and SYK and their association with FAK. The
phosphorylation of SYK is blocked by pertussis toxin, implicating a
Gi-like heterotrimeric G protein. IAP solublized from
membranes of unstimulated platelets binds specifically to an affinity
column of 4N1K peptide. Both IIb and 3 integrin subunits and
c-Src bind along with IAP. This complex of proteins is also detected
with immunoprecipitation. Activation of platelets with the agonist
peptide 4N1K results in the association of FAK with the IAP-IIb3
complex. Thus an important function of TS1 in platelets is that of a
secreted costimulator of IIb3 whose unique properties result in
its localization to the platelet surface and the fibrin clot.
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