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Platelets deficient in glycoprotein IIIb aggregate normally to collagens
type I and III but not to collagen type V
B Kehrel, A Kronenberg, J Rauterberg, D Niesing-Bresch, U Niehues, J Kardoeus, B Schwippert, D Tschope, J van de Loo and KJ Clemetson
Department of Internal Medicine, University of Munster, Germany.
The aggregation of platelets induced by collagens is considered an
important step in primary hemostasis. Glycoprotein (GP) IIIb (GPIIIb, GPIV,
CD36) has been proposed as a blood platelet receptor for collagen.
Platelets from three healthy blood donors were shown to be clearly
deficient in GPIIIb. These platelets aggregated normally in response to
type I and III collagens. In addition, platelet factor 4,
beta-thromboglobulin, and adenosine triphosphate (ATP) secretion in
response to type I and III collagens was normal. The findings indicate that
GPIIIb is not the major, essential collagen receptor for type I and III
collagens. This would explain why all individuals with GPIIIb- deficient
platelets examined so far are healthy and, in particular, show no apparent
evidence of hemostatic problems. However, in contrast to control platelets,
no aggregation and impaired platelet factor 4, beta-thromboglobulin, and
ATP secretion was observed in response to type V collagen. Therefore, it is
postulated that for type V collagen- induced aggregation both GPIa/IIa and
GPIIIb are essential.
Volume 82,
Issue 11,
pp. 3364-3370,
12/01/1993
Copyright © 1993 by The American Society of Hematology
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