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

被引：61
作者：
Dörmann, D
Clemetson, JM
Navdaev, A
Kehrel, BE
Clemetson, KJ
机构：
[1] Univ Bern, Theodor Kocher Inst, CH-3012 Bern, Switzerland
[2] Univ Munster, Klin & Poliklin Anasthesiol & Operat Intens Med E, D-4400 Munster, Germany
来源：
BLOOD | 2001年 / 97卷 / 04期
关键词：
D O I：
10.1182/blood.V97.4.929
中图分类号：
R5 [内科学];
学科分类号：
1002 ; 100201 ;
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 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. (C) 2001 by The American Society of Hematology.
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页码：929 / 936
页数：8
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