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Echicetin: a snake venom protein that inhibits binding of von Willebrand
factor and alboaggregins to platelet glycoprotein Ib
M Peng, W Lu, L Beviglia, S Niewiarowski and EP Kirby
Department of Biochemistry, Temple University School of Medicine,
Philadelphia, PA.
Echicetin, a new protein isolated from Echis carinatus venom by reverse
phase and ion exchange chromatography specifically inhibited agglutination
of fixed platelets induced by several platelet glycoprotein Ib (GPIb)
agonists, such as bovine von Willebrand factor (vWF), alboaggregins, and
human vWF in the presence of botrocetin. Unlike alboaggregins, echicetin
bound to GPIb but did not induce agglutination of washed or fixed
platelets. In contrast to disintegrins, it did not block adenosine
5'-diphosphate (ADP)-induced platelet aggregation in the presence of
fibrinogen. The apparent molecular weight of echicetin measured on sodium
dodecyl sulfate (SDS) gel electrophoresis was 26 Kd under nonreducing
conditions. On reduction, echicetin showed 16 and 14-Kd subunits suggesting
that the molecule is a dimer. Reduced echicetin retained its binding
activity and its inhibitory effect on the agglutination of fixed platelets
induced by bovine vWF. 125I-echicetin bound to fixed platelets with high
affinity (kd = 30 +/- 1.8 nmol/L) at 45,000 +/- 2,400 binding sites per
platelet. The binding was selectively inhibited by a monoclonal antibody to
the 45-Kd N-terminal domain of platelet GPIb, but not by monoclonal
antibodies to other regions on GPIb. Binding of 125I-bovine vWF to fixed
platelets was strongly inhibited by echicetin. In contrast, bovine vWF
showed a much weaker inhibitory activity on binding of 125I-echicetin to
platelets. The half life of echicetin in blood was approximately 170
minutes with no detectable degradation. Echicetin significantly prolonged
the bleeding time of mice, suggesting that it may inhibit vWF binding to
GPIb in vivo as well as in vitro.
Volume 81,
Issue 9,
pp. 2321-2328,
05/01/1993
Copyright © 1993 by The American Society of Hematology
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