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Mutations of the dimerization site of glycoprotein (GP) VI result in abolished expression.

Authors :
Navarro, Stefano
Vögtle, Timo
Groß, Nina
Preu, Julia
Englert, Maximilian
Nieswandt, Bernhard
Bösl, Michael R.
Stegner, David
Source :
Thrombosis Research. Dec2023, Vol. 232, p89-92. 4p.
Publication Year :
2023

Abstract

[Display omitted] • Here, we aimed to study the role of Glycoprotein VI (GPVI) dimerization in platelet activation in vivo. • The previously identified putative dimerization site of GPVI was mutated to disrupt the GPVI dimerization on the platelet surface. • Two different mutations of the GPVI dimerization site resulted in a loss of GPVI surface abundance in vivo. • Multivalent ligands (fibrillar collagen) of GPVI can elicit platelet activation also at very low GPVI density levels. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
00493848
Volume :
232
Database :
Academic Search Index
Journal :
Thrombosis Research
Publication Type :
Academic Journal
Accession number :
173808639
Full Text :
https://doi.org/10.1016/j.thromres.2023.10.016