Dörmann D Clemetson JM Navdaev A Kehrel BE Clemetson KJ 2001 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. application/pdf https://sonar.ch/global/documents/41665 eng info:eu-repo/semantics/altIdentifier/doi/10.1182/blood.v97.4.929 info:eu-repo/semantics/altIdentifier/pmid/11159519 info:eu-repo/semantics/openAccess Blood. - 2001 Adaptor Proteins, Signal Transducing Adult Annexin A5 Biotinylation Blood Coagulation Blood Platelets Carrier Proteins Chromatography, Affinity Crotalid Venoms Cytoplasmic Granules Humans Immunoglobulin Fab Fragments Isoenzymes Lectins, C-Type Membrane Proteins Phospholipase C gamma Phosphoproteins Phosphorylation Platelet Activation Platelet Adhesiveness Platelet Glycoprotein GPIb-IX Complex Platelet Membrane Glycoproteins Protein Binding Protein Processing, Post-Translational Proteins Receptors, IgG Signal Transduction Type C Phospholipases Viper Venoms Alboaggregin A activates platelets by a mechanism involving glycoprotein VI as well as glycoprotein Ib. http://purl.org/coar/resource_type/c_6501