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

Dörmann, D; Clemetson, JM; Navdaev, A; Kehrel, BE; Clemetson, KJ (2001). Alboaggregin A activates platelets by a mechanism involving glycoprotein VI as well as glycoprotein Ib. Blood, 97(4), pp. 929-36. Washington, D.C.: American Society of Hematology 10.1182/blood.V97.4.929

Full text not available from this repository. (Request a copy)

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.

Item Type:	Journal Article (Original Article)
Division/Institute:	04 Faculty of Medicine > Pre-clinic Human Medicine > Theodor Kocher Institute
UniBE Contributor:	Clemetson, Kenneth John
ISSN:	0006-4971
ISBN:	11159519
Publisher:	American Society of Hematology
Language:	English
Submitter:	Factscience Import
Date Deposited:	04 Oct 2013 14:52
Last Modified:	05 Dec 2022 14:16
Publisher DOI:	10.1182/blood.V97.4.929
PubMed ID:	11159519
Web of Science ID:	000166867200019
URI:	https://boris.unibe.ch/id/eprint/22201 (FactScience: 32256)