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Related Collections Hemostasis, Thrombosis, and Vascular Biology Signal Transduction Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  Blood, 15 February 2001, Vol. 97, No. 4, pp. 929-936 HEMOSTASIS, THROMBOSIS, AND VASCULAR BIOLOGY Alboaggregin A activates platelets by a mechanism involving glycoprotein VI as well as glycoprotein Ib Dagmar Dörmann, Jeannine M. Clemetson, Alexei Navdaev, Beate E. Kehrel, and Kenneth J. Clemetson From the Theodor Kocher Institute, University of Berne, Berne, Switzerland; and the Klinik und Poliklinik für Anästhesiologie und Operative Intensivmedizin, Experimental and Clinical Haemostasis, University of Münster, Germany. 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 of tyrosine phosphorylation that were different from those of other GPIb agonists and suggested the presence of an additional receptor. In this study, the binding of biotinylated alboaggregin A to platelet lysates, as well as affinity chromatography evaluations of platelet lysates on an alboaggregin A-coated column, indicated that this other receptor is GPVI. Additional experiments with reagents that inhibit either GPIb or GPVI specifically supported this finding. These experiments also showed that both GPIb and GPVI have a role in the combined signaling and that the overall direction this takes can be influenced by inhibitors of one or the other receptor pathway. © 2001 by The American Society of Hematology.   CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: G. Pula, D. Crosby, J. Baker, and A. W. 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	Copyright © 2001 by American Society of Hematology         Online ISSN: 1528-0020