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Blood, 15 May 2006, Vol. 107, No. 10, pp. 3922-3924.
Prepublished online as a Blood First Edition Paper on January 17, 2006; DOI 10.1182/blood-2005-09-3635.
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HEMOSTASIS, THROMBOSIS, AND VASCULAR BIOLOGY Brief report
P-selectin binds to the D'-D3 domains of von Willebrand factor in Weibel-Palade bodies
Grégoire Michaux,
Timothy J. Pullen,
Sandra L. Haberichter, and
Daniel F. Cutler
From the Medical Research Council (MRC) Laboratory for Molecular Cell Biology, Cell Biology Unit and Department of Biochemistry, University College London, London, United Kingdom; the Department of Pediatrics, Medical College of Wisconsin, Milwaukee, WI; and the Children's Research Institute, Children's Hospital of Wisconsin, Blood Research Institute, Blood Center of Wisconsin, Milwaukee, WI.
It has recently been shown that the ultralarge plateletrecruiting 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 bodylike 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.

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