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Heterogeneity of drug-dependent platelet antigens and their antibodies in
quinine- and quinidine-induced thrombocytopenia: involvement of
glycoproteins Ib, IIb, IIIa, and IX
SL Pfueller, RA Bilston, D Logan, JM Gibson and BG Firkin
Department of Medicine, Monash University Medical School, Prahran,
Victoria, Australia.
The molecular nature of platelet receptors for quinine- and quinidine-
dependent antiplatelet antibodies (Q.Ab and Qd.Ab) was studied by
immunoblotting. One Q.Ab caused quinine-dependent IgG binding to platelet
proteins with molecular weights (mol wts) of 174 Kd and 93 Kd and another
to only a 93-Kd protein. A third Q.Ab caused binding to 174- , 140-, 93-,
and 57-Kd proteins, while a fourth Q.Ab and a Qd.Ab caused IgG binding to
174- and 18-Kd proteins. Using platelets from patients with Glanzmann's
thrombasthenia or Bernard Soulier syndrome and purified GPIIIa, these
proteins were shown to be GPIb, GPIIb, GPIIIa, GPIX, and an unidentified
57-Kd protein missing in Bernard Soulier syndrome. Binding to the 93-Kd
protein was independent of the PIA1 antigen. Absorption of one Q.Ab with
Glanzmann's thrombasthenia platelets revealed different populations of
antibodies with different specificities within the one patient. Thus Q.Ab
and Qd.Ab are heterogeneous and may be directed toward different epitopes
on major platelet glycoproteins.
Volume 72,
Issue 4,
pp. 1155-1162,
10/01/1988
Copyright © 1988 by The American Society of Hematology

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