Abstract：
:It has recently been shown that the ultralarge platelet-recruiting von Willebrand factor (VWF) strings formed immediately at exocytosis from endothelial cells may be anchored to the cell surface by interaction with the integral membrane protein P-selectin. This finding of a new binding partner for VWF immediately prompts the question which domains of VWF bind to P-selectin. We have exploited the fact that VWF expression in HEK293 cells triggers the formation of Weibel-Palade body-like structures that can recruit P-selectin. A suitably modified version of this assay using coexpressed truncations of VWF, together with P-selectin variants in HEK293 cells, allowed us to determine which domains of VWF would recruit P-selectin within a physiologically appropriate intracellular environment. Confirming the results of such a cellular assay by conventional coimmunoprecipitation, we concluded that the lumenal domain of P-selectin interacts with the D'-D3 domains of VWF.
journal_name
Bloodjournal_title
Bloodauthors
Michaux G,Pullen TJ,Haberichter SL,Cutler DFdoi
10.1182/blood-2005-09-3635subject
Has Abstractpub_date
2006-05-15 00:00:00pages
3922-4issue
10eissn
0006-4971issn
1528-0020pii
2005-09-3635journal_volume
107pub_type
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