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Deficiency of intact thrombospondin and membrane glycoprotein Ia in
platelets with defective collagen-induced aggregation and spontaneous loss
of disorder
B Kehrel, L Balleisen, R Kokott, R Mesters, W Stenzinger, KJ Clemetson and J van de Loo
Institute of Arteriosclerosis Research, University of Munster, FRG.
Platelets from a patient with a severe lifelong bleeding tendency, which
later spontaneously disappeared, lacked intact thrombospondin and
glycoprotein (GP) Ia. Before disappearance of the bleeding disorder,
results of coagulation studies and platelet aggregation in response to
adenosine diphosphate (ADP), arachidonic acid, thrombin, A23187,
epinephrine, and ristocetin were normal. In contrast, aggregation only
occurred in the presence of collagen or wheat germ agglutinin at unusually
high doses of these agonists. The platelets adhered normally to purified
bovine and human type I collagen, and they did not spread in the presence
of methylated type I collagen. No collagen-induced clot retraction was
observed. Two-dimensional gel electrophoretic analyses of platelet proteins
and immunologic studies showed that intact thrombospondin and GP Ia were
absent. Aggregation in response to collagen could be restored by adding
thrombospondin. Disappearance of the bleeding tendency occurred at the
onset of menopause; subsequent analyses revealed that thrombospondin and GP
Ia were present in platelets and that collagen-induced platelet aggregation
was normal. These results suggest that both thrombospondin and GP Ia are
essential in collagen-induced platelet aggregation. The spontaneous
disappearance of the bleeding tendency may have been related to hormonal
influences.
Volume 71,
Issue 4,
pp. 1074-1078,
04/01/1988
Copyright © 1988 by The American Society of Hematology
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