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This Article Full Text Full Text (PDF) 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 Motta, G. Articles by Schmaier, A. H. Search for Related Content PubMed PubMed Citation Articles by Motta, G. Articles by Schmaier, A. H. Related Collections Hemostasis, Thrombosis, and Vascular Biology Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  High Molecular Weight Kininogen Regulates Prekallikrein Assembly and Activation on Endothelial Cells: A Novel Mechanism for Contact Activation Guacyara Motta, Rasmus Rojkjaer, Ahmed A.K. Hasan, Douglas B. Cines, and Alvin H. Schmaier From the Division of Hematology and Oncology, Department of Internal Medicine, University of Michigan, Ann Arbor, MI; the Department of Biochemistry, Escola Paulista de Medicina (UNIFESP), São Paulo, Brazil; and the Department of Pathology and Laboratory Medicine, University of Pennsylvania, Philadelphia, PA. The consequences of assembling the contact system of proteins on the surface of vascular cells has received little study. We asked whether assembly of these proteins on the surface of cultured human endothelial cells (HUVECs) results in the activation of prekallikrein (PK) and its dependent pathways. Biotinylated PK binds specifically and reversibly to HUVECs in the presence of high molecular weight kininogen (HK) (apparent Kd of 23 ± 11 nmol/L, Bmax of 1.7 ± 0.5 × 107 sites per cell [mean ± SD, n = 5 experiments]). Cell-associated PK is rapidly converted to kallikrein. Surprisingly, the activation of cell-associated HKPK complexes is entirely independent of exogenous factor XII (Km = 30 nmol/L, Vmax = 12 ± 3 pmol/L/min in the absence v Km = 20 nmol/L, Vmax = 9.2 ± 2.1 pmol/L/min in the presence of factor XII). Rather, kallikrein formation is mediated by an endothelial cell-associated, thiol protease. Cell-associated HK is proteolyzed during the course of prekallikrein activation, releasing kallikrein from the surface. Furthermore, activation of PK bound to HK on HUVECs promotes kallikrein-dependent activation of pro-urokinase, resulting in the formation of plasmin. These results indicate the existence of a previously undescribed, factor XII-independent pathway for contact factor activation on HUVECs that regulates the production of bradykinin and may contribute to cell-associated plasminogen activation in vivo. Blood, Vol. 91 No. 2 (January 15), 1998: pp. 516-528 © 1998 by The American Society of Hematology. 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