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Blood, 15 March 2004, Vol. 103, No. 6, pp. 2150-2156. Prepublished online as a Blood First Edition Paper on November 20, 2003; DOI 10.1182/blood-2003-08-2956. This Article Full Text Full Text (PDF) All Versions of this Article: 2003-08-2956v1 103/6/2150    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 Padilla, A. Articles by Dong, J.-F. Search for Related Content PubMed PubMed Citation Articles by Padilla, A. Articles by Dong, J.-F. Related Collections Hemostasis, Thrombosis, and Vascular Biology Cell Adhesion and Motility Related Article in Blood Online Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  HEMOSTASIS, THROMBOSIS, AND VASCULAR BIOLOGY P-selectin anchors newly released ultralarge von Willebrand factor multimers to the endothelial cell surface Arnoldo Padilla, Joel L. Moake, Aubrey Bernardo, Chalmette Ball, Yongtao Wang, Maneesh Arya, Leticia Nolasco, Nancy Turner, Michael C. Berndt, Bahman Anvari, José A. López, and Jing-Fei Dong From the Section of Thrombosis Research, Department of Medicine, Baylor College of Medicine, Houston, TX; Institute of Bioengineering and Biosciences, Rice University, Houston, TX; Department of Biochemistry and Molecular Biology, Monash University, Victoria, Australia. von Willebrand factor (VWF) released from endothelium is ultralarge (UL) and hyperreactive. If released directly into plasma, it can spontaneously aggregate platelets, resulting in systemic thrombosis. This disastrous consequence is prevented by the ADAMTS13 (ADisintegrin and Metalloprotease with ThromboSpondin motif) cleavage of ULVWF into smaller, less active forms. We previously showed that ULVWF, on release, forms extremely long stringlike structures. ADAMTS13 cleaves these strings under flow significantly faster than it does under static conditions. As ULVWF tethering to endothelium is important for its rapid proteolysis, we investigated 2 molecules for their potential to anchor the ULVWF strings: P-selectin and integrin v3. We demonstrated that P-selectin anchors ULVWF to endothelium by several means. First, Chinese hamster ovary (CHO) cells expressing P-selectin specifically adhered to immobilized ULVWF and ULVWF-coated beads to immobilized P-selectin. Second, an anti-VWF antibody coimmunoprecipitates P-selectin from the histamine-activated endothelial cells. Third, P-selectin antibody or soluble P-selectin, but not a v3 antibody, RGDS peptide, or heparin, blocked the formation of ULVWF strings. Fourth, P-selectin expression was in clusters predominantly along the ULVWF strings. Finally, the strength of the minimal ULVWF–P-selectin bond was measured to be 7.2 pN. We, therefore, conclude that P-selectin may anchor ULVWF strings to endothelial cells and facilitate their cleavage by ADAMTS13. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? Related Article in Blood Online: P-selectin and VWF tie the knot Paul S. Frenette Blood 2004 103: 1979-1980. [Full Text] [PDF] This article has been cited by other articles: 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] J. Huang, R. Roth, J. E. Heuser, and J. E. 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