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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. This Article Full Text Full Text (PDF) Supplemental Figures All Versions of this Article: 2005-09-3635v1 107/10/3922    most recent Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Rights and Permissions Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Michaux, G. Articles by Cutler, D. F. Search for Related Content PubMed PubMed Citation Articles by Michaux, G. Articles by Cutler, D. F. Related Collections Hemostasis, Thrombosis, and Vascular Biology Cell Adhesion and Motility Brief Reports Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  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 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. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: V. Babich, L. Knipe, L. Hewlett, A. Meli, J. Dempster, M. J. Hannah, and T. Carter Differential Effect of Extracellular Acidosis on the Release and Dispersal of Soluble and Membrane Proteins Secreted from the Weibel-Palade Body J. Biol. Chem., May 1, 2009; 284(18): 12459 - 12468. [Abstract] [Full Text] [PDF] M. van den Biggelaar, A. B. Meijer, J. Voorberg, and K. Mertens Intracellular cotrafficking of factor VIII and von Willebrand factor type 2N variants to storage organelles Blood, March 26, 2009; 113(13): 3102 - 3109. [Abstract] [Full Text] [PDF] J. Huang, R. Roth, J. E. Heuser, and J. E. Sadler Integrin {alpha}v{beta}3 on human endothelial cells binds von Willebrand factor strings under fluid shear stress Blood, February 12, 2009; 113(7): 1589 - 1597. [Abstract] [Full Text] [PDF] V. Babich, A. Meli, L. Knipe, J. E. Dempster, P. Skehel, M. J. Hannah, and T. Carter Selective release of molecules from Weibel-Palade bodies during a lingering kiss Blood, June 1, 2008; 111(11): 5282 - 5290. [Abstract] [Full Text] [PDF] D. J. Metcalf, T. D. Nightingale, H. L. Zenner, W. W. Lui-Roberts, and D. F. Cutler Formation and function of Weibel-Palade bodies J. Cell Sci., January 1, 2008; 121(1): 19 - 27. [Abstract] [Full Text] [PDF]

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