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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 (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 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 Related Article in Blood Online Social Bookmarking                   What's this? Submitted September 3, 2003 Accepted November 11, 2003 P-selectin anchors newly released ultra-large 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, Jose A Lopez, and Jing-Fei Dong* Department of Medicine, Baylor College of Medicine, Houston, TX, USA Institute of Bioengineering and Biosciences, Rice University, Houston, TX, USA Department of Biochemistry and Molecular Biology, Monash University, Parkville, VIC, Australia * Corresponding author; email: jfdong{at}bcm.tmc.edu. Von Willebrand factor (VWF) newly released from endothelial cells is ultra-large (UL) and hyper-reactive. If released directly into plasma, it can spontaneously aggregate platelets, resulting in systemic thrombosis. This disastrous consequence is prevented by ADAMTS-13 metalloprotease, which cleaves ULVWF into smaller, less active forms. We previously showed that ULVWF, upon release from endothelial cells, forms extremely long string-like structures. ADAMTS-13 cleaves these strings under flow more than 1000-fold faster than it does under static conditions. As ULVWF tethering to the endothelial surface appears to be important for its rapid proteolysis, we investigated two molecules for their potential to anchor the ULVWF strings: P-selectin and integrin v3. Several lines of evidence indicate that P-selectin anchors ULVWF to endothelium. First, CHO cells expressing P-selectin specifically adhered to immobilized ULVWF and ULVWF-coated beads adhered to immobilized P-selectin under static and flow conditions. Second, a monoclonal anti-VWF antibody coimmunoprecipitates P-selectin from endothelial cells, but only after histamine stimulation. The formation of ULVWF strings is blocked by either a polyclonal P-selectin antibody or by soluble P-selectin, but not by a v3 antibody, RGDS peptide, or heparin. The strength of the minimal ULVWF-P-selectin bond determined using optical tweezers was 7.2 pN. Immunostaining of cultured, histamine-stimulated endothelium showed that P-selectin expression appears in clusters predominantly along the ULVWF strings. We therefore conclude that P-selectin may anchor ULVWF strings to endothelial cells and facilitate their cleavage by ADAMTS-13. 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: 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. 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