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Role of botrocetin in platelet agglutination: formation of an activated
complex of botrocetin and von Willebrand factor
MS Read, SV Smith, MA Lamb and KM Brinkhous
Department of Pathology, University of North Carolina, Chapel Hill 27599.
Botrocetin (venom coagglutinin) induces binding of von Willebrand factor
(vWF) to platelet glycoprotein Ib (GPIb), resulting in platelet
agglutination. A mechanism whereby botrocetin causes vWF to change to an
active platelet-agglutinating form is proposed. Incubation of native vWF
with botrocetin yielded an increasingly active vWF with slower migration in
two-dimensional immunoelectrophoresis but with no apparent change in vWF
multimer pattern. The "activated" vWF eluted mainly in the void volume (Vo)
(Bio-Gel A-15m column chromatography). Botrocetin eluted in the included
volume (Vi). Vo peaks appeared to contain a vWF- botrocetin complex, based
on bioassays and immunoassays. 125I- Botrocetin mixed with vWF eluted in
two peaks: in the Vo, coincident with active vWF, and in the Vi. With von
Willebrand disease (vWD) plasma lacking vWF, 125I-Botrocetin eluted in the
Vi only. It did not bind to platelets without vWF. In aggregometric
studies, antibodies (Ab) against botrocetin, vWF, and GPIb prevented
botrocetin-induced platelet agglutination and caused dissolution of
preformed platelet agglutinates. Immunostaining of aggregates with
antibotrocetin Ab revealed a positive reaction. Botrocetin appears to act
in a two-step manner, first binding with vWF to form a complex, which then
binds to GPIb to cause agglutination. All three components, vWF,
botrocetin, and GPIb, appear to be required for maintenance of stable
platelet agglutinates.
Volume 74,
Issue 3,
pp. 1031-1035,
08/15/1989
Copyright © 1989 by The American Society of Hematology
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