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Collagen-platelet interactions: evidence for a direct interaction of
collagen with platelet GPIa/IIa and an indirect interaction with platelet
GPIIb/IIIa mediated by adhesive proteins
BS Coller, JH Beer, LE Scudder and MH Steinberg
Department of Medicine, State University of New York Stony Brook 11794.
Using intact human platelets as the immunogen and a functional,
collagen-coated bead agglutination assay, we have produced a murine
monoclonal antibody (6F1) that blocks the interaction between platelets and
collagen in the presence of Mg++. 6F1 affinity-purified the platelet
glycoprotein Ia/IIa complex, and approximately 800 molecules of 6F1 bound
per platelet at saturation. 6F1 nearly completely inhibited
collagen-induced platelet aggregation and inhibited platelet adhesion to
collagen by greater than 95% when plasma proteins were absent. Antibody
10E5, which blocks the binding of adhesive glycoproteins to GPIIb/IIIa,
produced only minor inhibition (approximately 25%) of adhesion under the
same circumstances. In contrast, when tested in platelet-rich plasma (PRP),
6F1 had only a minor effect on collagen-induced platelet aggregation,
prolonging the lag phase but not the slope or maximum aggregation.
Similarly, when collagen was precoated with plasma, 6F1 caused less
inhibition of platelet adhesion (53%) than without the precoating (greater
than 95%). Antibody 10E5 inhibited this adhesion by 32%, and the
combination of 6F1 and 10E5 was more effective than either alone,
inhibiting it by 90%. Time course studies of platelet agglutination of
collagen-coated beads using PRP containing physiologic concentrations of
divalent cations showed early inhibition by 6F1, indicating that the
GPIa/IIa receptor operates in this environment. With more prolonged
incubation, however, 6F1 was less effective; this later agglutination could
be partially prevented by adding 10E5 or PGE1 to the 6F1. These data
support a model wherein collagen can directly interact with GPIa/IIa and
can indirectly interact with GPIIb/IIIa via intermediary adhesive proteins.
The physiological significance of these interactions, and potential
interactions with other receptors, remains to be established.
Volume 74,
Issue 1,
pp. 182-192,
07/01/1989
Copyright © 1989 by The American Society of Hematology
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