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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 Nishiya, T. Articles by Ikeda, Y. Search for Related Content PubMed PubMed Citation Articles by Nishiya, T. Articles by Ikeda, Y. Related Collections Hemostasis, Thrombosis, and Vascular Biology Cell Adhesion and Motility Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  Blood, 1 July 2002, Vol. 100, No. 1, pp. 136-142 HEMOSTASIS, THROMBOSIS, AND VASCULAR BIOLOGY Reconstitution of adhesive properties of human platelets in liposomes carrying both recombinant glycoproteins Ia/IIa and Ib under flow conditions: specific synergy of receptor-ligand interactions Takako Nishiya, Mie Kainoh, Mitsuru Murata, Makoto Handa, and Yasuo Ikeda From the Department of Internal Medicine and Blood Center, Keio University, Tokyo, Japan; and Toray Industries, Kanagawa, Japan. Liposomes carrying both recombinant glycoprotein Ia/IIa (rGPIa/IIa) and Ib (rGPIb) (rGPIa/IIa-Ib-liposomes) instantaneously and irreversibly adhered to the collagen surface in the presence of soluble von Willebrand factor (VWF) at high shear rates, in marked contrast with translocation of liposomes carrying rGPIb alone on the VWF surface. In the absence of soluble VWF, the adhesion of rGPIa/IIa-Ib-liposomes to the collagen surface decreased with increasing shear rates, similar to liposomes carrying rGPIa/IIa alone. While adhesion of liposomes with exofacial rGPIa/IIa and rGPIb densities of 2.17 × 103 and 1.00 × 104 molecules per particle, respectively, was efficient at high shear rates, reduction in rGPIb density to 5.27 × 103 molecules per particle resulted in decreased adhesion even in the presence of soluble VWF. A 50% reduction in the exofacial rGPIa/IIa density resulted in a marked decrease in the adhesive ability of the liposomes at all shear rates tested. The inhibitory effect of antibody against GPIb (GUR83-35) on liposome adhesion was greater at higher shear rates. Further, the anti-GPIa antibody (Gi9) inhibited liposome adhesion more than GUR83-35 at all shear rates tested. These results suggest that the rGPIa/IIa-collagen interaction dominates the adhesion of rGPIa/IIa-Ib-liposomes to the collagen surface at low shear rates, while the rGPIa/IIa-collagen and rGPIb-VWF interaction complements each other, and they synergistically provide the needed functional integration required for liposome adhesion at high shear rates. This study thus has confirmed for the first time the proposed mechanisms of platelet adhesion to the collagen surface under flow conditions using the liposome system. © 2002 by The American Society of Hematology.   CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: P. R.-M. Siljander, S. Hamaia, A. R. Peachey, D. A. Slatter, P. A. Smethurst, W. H. Ouwehand, C. G. Knight, and R. W. Farndale Integrin Activation State Determines Selectivity for Novel Recognition Sites in Fibrillar Collagens J. Biol. Chem., November 12, 2004; 279(46): 47763 - 47772. [Abstract] [Full Text] [PDF] P. R.-M. Siljander, I. C. A. Munnix, P. A. Smethurst, H. Deckmyn, T. Lindhout, W. H. Ouwehand, R. W. Farndale, and J. W. M. Heemskerk Platelet receptor interplay regulates collagen-induced thrombus formation in flowing human blood Blood, February 15, 2004; 103(4): 1333 - 1341. [Abstract] [Full Text] [PDF]

	Copyright © 2002 by American Society of Hematology         Online ISSN: 1528-0020