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Blood, 12 February 2009, Vol. 113, No. 7, pp. 1589-1597. Prepublished online as a Blood First Edition Paper on October 16, 2008; DOI 10.1182/blood-2008-05-158584. This Article Full Text Full Text (PDF) Supplemental Figures All Versions of this Article: blood-2008-05-158584v1 113/7/1589    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 Huang, J. Articles by Sadler, J. E. Search for Related Content PubMed PubMed Citation Articles by Huang, J. Articles by Sadler, J. E. Related Collections Vascular Biology Related Article in Blood Online Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  VASCULAR BIOLOGY Integrin vβ3 on human endothelial cells binds von Willebrand factor strings under fluid shear stress Jing Huang1, Robyn Roth2, John E. Heuser2, and J. Evan Sadler1 1 Departments of Medicine, Biochemistry and Molecular Biophysics, and Howard Hughes Medical Institute, and 2 Department of Cell Biology, Washington University School of Medicine, St Louis, MO Acutely secreted von Willebrand factor (VWF) multimers adhere to endothelial cells, support platelet adhesion, and may induce microvascular thrombosis. Immunofluorescence microscopy of live human umbilical vein endothelial cells showed that VWF multimers rapidly formed strings several hundred micrometers long on the cell surface after stimulation with histamine. Unexpectedly, only a subset of VWF strings supported platelet binding, which depended on platelet glycoprotein Ib. Electron microscopy showed that VWF strings often consisted of bundles and networks of VWF multimers, and each string was tethered to the cell surface by a limited number of sites. Several approaches implicated P-selectin and integrin vβ3 in anchoring VWF strings. An RGDS peptide or a function-blocking antibody to integrin vβ3 reduced the number of VWF strings formed. In addition, integrin v decorated the VWF strings by immunofluorescence microscopy. Furthermore, lentiviral transduction of shRNA against the v subunit reduced the expression of cell-surface integrin vβ3 and impaired the ability of endothelial cells to retain VWF strings. Soluble P-selectin reduced the number of platelet-decorated VWF strings in the absence of Ca2+ and Mg2+ but had no effect in the presence of these cations. These results indicate that VWF strings bind specifically to integrin vβ3 on human endothelial cells. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? Related Article in Blood Online: Fishing for platelets Daniel F. Cutler Blood 2009 113: 1397-1398. [Full Text] [PDF] This article has been cited by other articles: A. N. Vomund and E. M. Majerus ADAMTS13 Bound to Endothelial Cells Exhibits Enhanced Cleavage of von Willebrand Factor J. Biol. Chem., November 6, 2009; 284(45): 30925 - 30932. [Abstract] [Full Text] [PDF] S. F. De Meyer, H. Deckmyn, and K. Vanhoorelbeke von Willebrand factor to the rescue Blood, May 21, 2009; 113(21): 5049 - 5057. [Abstract] [Full Text] [PDF] D. F. Cutler Fishing for platelets Blood, February 12, 2009; 113(7): 1397 - 1398. [Full Text] [PDF]

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