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Blood, 1 December 2006, Vol. 108, No. 12, pp. 3746-3752. Prepublished online as a Blood First Edition Paper on August 22, 2006; DOI 10.1182/blood-2006-03-010322. This Article Full Text Full Text (PDF) Supplemental Videos All Versions of this Article: blood-2006-03-010322v1 108/12/3746    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 Pendu, R. Articles by Denis, C. V. Search for Related Content PubMed PubMed Citation Articles by Pendu, R. Articles by Denis, C. V. Related Collections Hemostasis, Thrombosis, and Vascular Biology Phagocytes Cell Adhesion and Motility Signal Transduction Free Research Articles Related Article in Blood Online Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  HEMOSTASIS, THROMBOSIS, AND VASCULAR BIOLOGY P-selectin glycoprotein ligand 1 and 2-integrins cooperate in the adhesion of leukocytes to von Willebrand factor Ronan Pendu, Virginie Terraube, Olivier D. Christophe, Carl G. Gahmberg, Philip G. de Groot, Peter J. Lenting, and Cecile V. Denis From the Laboratory for Thrombosis and Haemostasis, Department of Clinical Chemistry and Haematology, University Medical Center Utrecht, The Netherlands; Institut National de la Santé el de la Recherche Médicale (INSERM) U770, Le Kremlin-Bicêtre, France; Faculté de Médecine Paris-Sud, Université Paris-Sud 11, Le Kremlin-Bicêtre, France; and Department of Biological and Environmental Sciences, University of Helsinki, Finland. Von Willebrand factor (VWF) is an essential component of hemostasis. However, animal studies using VWF-deficient mice suggest that VWF may also contribute to inflammation. In the present study, we demonstrate that VWF was able to interact with polymorphonuclear leukocytes (PMNs) and monocytes under static and flow conditions. Adhesion under flow was dominated by short-lasting contact with resting PMNs, whereas adhesion of phorbol-12-myristate-13-acetate (PMA)–stimulated PMNs was characterized by firm adhesion. Transient binding of PMNs to VWF appeared to be mediated by P-selectin glycoprotein ligand-1 (PSGL-1). Moreover, recombinant PSGL-1 protein and cell surface–expressed PSGL-1 directly interacted with VWF. As for stable adhesion by PMA-stimulated PMNs, we observed that static adhesion and adhesion under flow were strongly inhibited (greater than 75%) by neutrophil-inhibitory factor, an inhibitor of 2-integrin function. In addition, the isolated I-domain of M2 bound to VWF, and cell lines expressing L2 or X2 adhered efficiently to VWF. Taken together, our data showed that VWF can function as an adhesive surface for various leukocyte subsets (monocytes, PMNs). Analogous to VWF-platelet interaction, VWF provided binding sites for leukocyte receptors involved in rolling (PSGL-1) and stable (2-integrins) adhesion. VWF is unique in its intrinsic capacity to combine the rolling and the stable adhesion step in the interaction with leukocytes. 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