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This Article Full Text (PDF) 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 Kessler, C. M. Articles by Gralnick, H. R. Search for Related Content PubMed PubMed Citation Articles by Kessler, C. M. Articles by Gralnick, H. R. Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  Collagen-factor VIII/von Willebrand factor protein interaction CM Kessler, CM Floyd, ME Rick, DM Krizek, SL Lee and HR Gralnick Factor VIII/von Willebrand factor (FVIII/vWF) protein interaction with collagen was studied by incubating plasma or purified FVIII/vWF with purified type I fibrillar collagen. Collagen adsorbed FVIII/vWF activities in a similar time and concentration-dependent manner from normal plasma, plasmas from classical and variant type von Willebrand's disease (vWD), and from purified FVIII/vWF. Incubation with denatured collagen or fibrin, produced in the presence or absence of fibronectin, showed no adsorption of FVIII/vWF. Examination of the multimeric structure of the remaining unadsorbed FVIII/vWF protein by agarose gel electrophoresis and autoradiography showed that the largest multimers had been adsorbed to the collagen. Studies of the adsorbed FVIII/vWF protein when eluted from collagen showed that it complemented the alterations in multimeric structure observed in the supernatants following collagen exposure. The multimeric structure of normal plasma following collagen adsorption resembled that of unadsorbed type IIb plasma; however, the collagen-adsorbed normal plasma did not produce enhanced ristocetin-induced platelet aggregation ( RIPA ). This phenomenon, therefore, must not be due solely to absence of large multimers from type IIb FVIII/vWF protein. The adsorbed multimers of FVIII/vWF protein may act as a subendothelial collagen-platelet bridge to promote primary hemostasis. Volume 63, Issue 6, pp. 1291-1298, 06/01/1984 Copyright © 1984 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: Y.-P. Wu, H. H.F.I. van Breugel, H. Lankhof, R. J. Wise, R. I. Handin, P. G. de Groot, and J. J. Sixma Platelet Adhesion to Multimeric and Dimeric von Willebrand Factor and to Collagen Type III Preincubated With von Willebrand Factor Arterioscler. Thromb. Vasc. Biol., May 1, 1996; 16(5): 611 - 620. [Abstract] [Full Text]

	Copyright © 1984 by American Society of Hematology         Online ISSN: 1528-0020