Abstract
The glycoprotein (GP)-lb-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 γ-chain. The evidence for this was based in part on studies with the GPlbα-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 GPlbα, and evidence is provided that this contributes to protein tyrosine phosphorylation, shape change, and GPlb-llla-dependent aggregation. This may explain why responses to alboaggregin-A are distinct from those to von Willebrand factor-ristocetin.
Original language | English |
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Pages (from-to) | 3989-3991 |
Number of pages | 3 |
Journal | Blood |
Volume | 97 |
Issue number | 12 |
DOIs | |
Publication status | Published - 15 Jun 2001 |
Externally published | Yes |