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Blood, 15 October 2005, Vol. 106, No. 8, pp. 2730-2736. Prepublished online as a Blood First Edition Paper on July 7, 2005; DOI 10.1182/blood-2005-01-0240. This Article Full Text Full Text (PDF) All Versions of this Article: 2005-01-0240v1 106/8/2730    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 Siebenlist, K. R. Articles by Stojanovic, L. Search for Related Content PubMed PubMed Citation Articles by Siebenlist, K. R. Articles by Stojanovic, L. Related Collections Hemostasis, Thrombosis, and Vascular Biology Related Letter in Blood Online Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  HEMOSTASIS, THROMBOSIS, AND VASCULAR BIOLOGY Studies on the basis for the properties of fibrin produced from fibrinogen-containing ' chains Kevin R. Siebenlist, Michael W. Mosesson, Irene Hernandez, Leslie A. Bush, Enrico Di Cera, John R. Shainoff, James P. Di Orio, and Laurie Stojanovic From the Department of Biomedical Sciences, College of Health Sciences, Marquette University, Milwaukee, WI; The Blood Research Institute, Milwaukee, WI; Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, Saint Louis, MO; Department of Chemistry, Cleveland State University, Cleveland, OH; and Baxter Healthcare Corporation, Round Lake, IL. Human fibrinogen 1 is homodimeric with respect to its chains (`A-A'), whereas fibrinogen 2 molecules each contain one A (A1-411V) and one ' chain, which differ by containing a unique C-terminal sequence from '408 to 427L that binds thrombin and factor XIII. We investigated the structural and functional features of these fibrins and made several observations. First, thrombin-treated fibrinogen 2 produced finer, more branched clot networks than did fibrin 1. These known differences in network structure were attributable to delayed release of fibrinopeptide (FP) A from fibrinogen 2 by thrombin, which in turn was likely caused by allosteric changes at the thrombin catalytic site induced by thrombin exosite 2 binding to the ' chains. Second, cross-linking of fibrin chains was virtually the same for both types of fibrin. Third, the acceleratory effect of fibrin on thrombin-mediated XIII activation was more prominent with fibrin 1 than with fibrin 2, and this was also attributable to allosteric changes at the catalytic site induced by thrombin binding to ' chains. Fourth, fibrinolysis of fibrin 2 was delayed compared with fibrin 1. Altogether, differences between the structure and function of fibrins 1 and 2 are attributable to the effects of thrombin binding to ' chains. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? Related Letter in Blood Online: Fibrinogen containing ' chains David H. Farrell and Kevin R. Siebenlist Blood 2006 107: 3011-3012. [Full Text] [PDF] This article has been cited by other articles: J. C. Fredenburgh, A. R. Stafford, B. A. Leslie, and J. I. Weitz Bivalent Binding to {gamma}A/{gamma}'-Fibrin Engages Both Exosites of Thrombin and Protects It from Inhibition by the Antithrombin-Heparin Complex J. Biol. Chem., February 1, 2008; 283(5): 2470 - 2477. [Abstract] [Full Text] [PDF] R. L. Davis, M. W. Mosesson, B. A. Kerlin, J. A. Canner, F. B. Ruymann, and S. O. Brennan Fibrinogen Columbus: a novel gamma Gly200Val mutation causing hypofibrinogenemia in a family with associated thrombophilia Haematologica, August 1, 2007; 92(8): 1151 - 1152. [Abstract] [Full Text] [PDF] J.P. Collet, Y. Allali, C. Lesty, M.L. Tanguy, J. Silvain, A. Ankri, B. Blanchet, R. Dumaine, J. Gianetti, L. Payot, et al. Altered Fibrin Architecture Is Associated With Hypofibrinolysis and Premature Coronary Atherothrombosis Arterioscler. Thromb. Vasc. Biol., November 1, 2006; 26(11): 2567 - 2573. [Abstract] [Full Text] [PDF] S. Kani, F. Terasawa, K. Yamauchi, M. Tozuka, and N. Okumura Analysis of fibrinogen variants at {gamma}387Ile shows that the side chain of {gamma}387 and the tertiary structure of the {gamma}C-terminal tail are important not only for assembly and secretion of fibrinogen but also for lateral aggregation of protofibrils and XIIIa-catalyzed {gamma}-{gamma} dimer formation Blood, September 15, 2006; 108(6): 1887 - 1894. [Abstract] [Full Text] [PDF] D. H. Farrell and K. R. Siebenlist Fibrinogen containing {gamma}' chains. Blood, April 1, 2006; 107(7): 3011 - 3012. [Full Text] [PDF] S. Uitte de Willige, M. C. H. de Visser, J. J. Houwing-Duistermaat, F. R. Rosendaal, H. L. Vos, and R. M. Bertina Genetic variation in the fibrinogen gamma gene increases the risk for deep venous thrombosis by reducing plasma fibrinogen {gamma}' levels Blood, December 15, 2005; 106(13): 4176 - 4183. [Abstract] [Full Text] [PDF]

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