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Disturbed platelet aggregation to collagen associated with an antibody
against an 85- to 90-Kd platelet glycoprotein in a patient with prolonged
bleeding time
H Deckmyn, E Van Houtte and J Vermylen
Center for Thrombosis and Vascular Research, K.U. Leuven, Belgium.
We studied a 5-year-old girl presenting with a markedly prolonged bleeding
time. Her platelets were refractory to collagen stimulation, but the
response to other agonists was normal. There were no coagulation
abnormalities as measured by standard tests. Two- dimensional
electrophoresis showed no abnormalities of the patient's platelet membrane
glycoproteins. When the patient's plasma or purified plasma IgG was mixed
with normal platelets, collagen-induced platelet aggregation was blocked.
Western blotting showed the presence of an antibody in the patient's plasma
directed against a protein of molecular weight 85 to 90 Kd under both
reducing and nonreducing conditions. This protein comigrated with
glycoprotein (GP) IV immunoprecipitated by OKM5 from 125I-labeled
platelets. Immunoprecipitation of 125I-labeled normal platelet
glycoproteins with the patient's IgGs also yielded an 85- to 90-Kd protein
that migrated on the diagonal following nonreduced/reduced two-dimensional
sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE).
Despite similarities in electrophoretic behavior, the antigen was not
demonstrated to be GPIV, since purified GPIV was not recognized by the
antibody.
Volume 79,
Issue 6,
pp. 1466-1471,
03/15/1992
Copyright © 1992 by The American Society of Hematology
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