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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 Savage, B. Articles by Ruggeri, Z. M. Search for Related Content PubMed PubMed Citation Articles by Savage, B. Articles by Ruggeri, Z. M. Related Collections Hemostasis, Thrombosis, and Vascular Biology Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  Blood, Vol. 94 No. 8 (October 15), 1999: pp. 2704-2715 Influence of Fibrillar Collagen Structure on the Mechanisms of Platelet Thrombus Formation Under Flow Brian Savage, Mark H. Ginsberg, and Zaverio M. Ruggeri From the Roon Research Center for Arteriosclerosis and Thrombosis, Division of Experimental Hemostasis and Thrombosis, Departments of Molecular and Experimental Medicine and of Vascular Biology, The Scripps Research Institute, La Jolla, CA. We have used real-time video microscopy to study the mechanisms of platelet adhesion to type I collagen fibrils of distinct structure exposed to flowing blood. Electron microscopy analysis by surface replication demonstrated morphological differences between acid-insoluble fibrils, displaying a regularly repeating striated pattern (banded collagen), and acid-soluble fibrils generated by pepsin treatment of insoluble collagen, smaller in size with a helical configuration (nonbanded collagen). These structural differences proved to be related to the role of platelet integrin 21 in stabilizing adhesion to collagen under a variety of flow conditions. Blocking 21 function with a monoclonal antibody had no effect on platelet adhesion to insoluble type I collagen coated at high density on a glass surface, whereas there was an absolute dependence of 21 function for the initial permanent arrest of platelets and subsequent thrombus formation on pepsin-solubilized type I collagen under the same conditions. In contrast, reconstituted, banded fibrils prepared from pepsin-solubilized type I collagen supported platelet adhesion and thrombus development even when platelet 21 function was blocked, a process that was greatly accelerated by pre-exposure of this substrate to autologous plasma under flow. These results implicate a collagen receptor(s) on platelets other than 21 that can selectively engage domains in banded, but not nonbanded type I collagen when 21 function is blocked. In addition, collagen structure may regulate the extent and affinity of the binding under flow of plasma components such as von Willebrand factor and/or other IIb3 ligands. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: M. A. Cejas, W. A. Kinney, C. Chen, J. G. Vinter, H. R. Almond Jr., K. M. Balss, C. A. Maryanoff, U. Schmidt, M. Breslav, A. Mahan, et al. Thrombogenic collagen-mimetic peptides: Self-assembly of triple helix-based fibrils driven by hydrophobic interactions PNAS, June 24, 2008; 105(25): 8513 - 8518. [Abstract] [Full Text] [PDF] E. Calvo, F. Tokumasu, O. Marinotti, J.-L. Villeval, J. M. C. Ribeiro, and I. M. B. Francischetti Aegyptin, a Novel Mosquito Salivary Gland Protein, Specifically Binds to Collagen and Prevents Its Interaction with Platelet Glycoprotein VI, Integrin {alpha}2beta1, and von Willebrand Factor J. Biol. Chem., September 14, 2007; 282(37): 26928 - 26938. 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