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Effects of OKM5, a monoclonal antibody to glycoprotein IV, on platelet
aggregation and thrombospondin surface expression [see comments]
ML Aiken, MH Ginsberg, V Byers-Ward and EF Plow
Department of Biochemistry, University of Texas Health Science Center,
Tyler.
The monoclonal antibody, OKM5, recognizes an 88-Kd monocyte membrane
protein and also binds to the platelet membrane protein, GPIV (GPIIIb,
CD36). In this study, we have found that the OKM5 target epitope is present
at approximately 12,000 copies per platelet and that interaction with the
antibody has both stimulatory and inhibitory effects on platelet function.
In the absence of other stimuli, OKM5 induced platelet aggregation,
secretion, and expression of fibrinogen receptors. These stimulatory
responses required intact antibody as F(ab')2 fragments were not active but
blocked the stimulatory activity of the intact antibody. In contrast,
exposure of platelets to OKM5 followed by another strong stimulus such as
thrombin resulted in a marked suppression of fibrinogen, fibronectin, and
von Willebrand factor binding to the cells. This effect was not noted when
a weak stimulus, adenosine diphosphate, was the second agonist. At OKM5
concentrations that interfered with fibrinogen binding to thrombin-
stimulated platelets by 80% to 90%, platelet binding of exogenous
thrombospondin, or surface expression of endogenous thrombospondin was not
affected. The inhibitory effect of OKM5 on fibrinogen binding to
thrombin-stimulated platelets was related to the formation of massive
platelet aggregates in the samples. These results show that interaction of
OKM5 with its target antigen on platelets can elicit diverse functional
responses from the cells.
Volume 76,
Issue 12,
pp. 2501-2509,
12/15/1990
Copyright © 1990 by The American Society of Hematology
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