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Blood, 15 June 2001, Vol. 97, No. 12, pp. 3989-3991
BRIEF REPORT
The snake venom toxin alboaggregin-A activates
glycoprotein VI
Naoki Asazuma,
Stuart J. Marshall,
Oscar Berlanga,
Daniel Snell,
Alastair W. Poole,
Michael C. Berndt,
Robert K. Andrews, and
Steve P. Watson
From the Department of Pharmacology, University of
Oxford, and the Department of Pharmacology, University of Bristol,
School of Medical Sciences, United Kingdom; and the Baker Medical
Research Institute, Melbourne, Australia.
The glycoprotein (GP)-Ib-IX-V receptor complex has recently been
reported to signal through a pathway similar to that used by the
collagen receptor GPVI, with a critical role described for the Fc
receptor -chain. The evidence for this was based in part on
studies with the GPIb -selective snake venom toxin, alboaggregin-A. In the present study, it is reported that alboaggregin-A has activity at the collagen receptor GPVI in addition to GPIb , and evidence is
provided that this contributes to protein tyrosine phosphorylation, shape change, and GPIIb-IIIa-dependent aggregation. This may
explain why responses to alboaggregin-A are distinct from those to von Willebrand factor- ristocetin.

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