Alboaggregin A activates platelets by a mechanism involving glycoprotein VI as well as glycoprotein Ib.

作者: Dagmar Dörmann , Jeannine M. Clemetson , Alexei Navdaev , Beate E. Kehrel , Kenneth J. Clemetson

DOI: 10.1182/BLOOD.V97.4.929

关键词:

摘要: The snake venom C-type lectin alboaggregin A (or 50-kd alboaggregin) from Trimeresurus albolabris was previously shown to be a platelet glycoprotein (GP) Ib agonist. However, investigations of the signal transduction induced in platelets showed patterns tyrosine phosphorylation that were different those other GPIb agonists and suggested presence an additional receptor. In this study, binding biotinylated lysates, as well affinity chromatography evaluations lysates on A-coated column, indicated receptor is GPVI. Additional experiments with reagents inhibit either or GPVI specifically supported finding. These also both have role combined signaling overall direction takes can influenced by inhibitors one pathway.

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