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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 (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 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 Related Letter in Blood Online Social Bookmarking                   What's this?  Previous Article  |  Next Article  Submitted January 21, 2005 Accepted June 10, 2005 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 DiOrio, and Laurie Stojanovic Department of Biomedical Sciences, Marquette University, Milwaukee, WI, USA The Blood Research Institute, Milwaukee, WI, USA Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, MO, USA Department of Chemistry, Cleveland State University, Cleveland, OH, USA Baxter Healthcare Corporation, Round Lake, IL, USA * Corresponding author; email: kevin.siebenlist{at}marquette.edu. 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 differs 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. 1) 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 FPA 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. 2) Cross-linking of fibrin chains was virtually the same for both types of fibrin. 3) 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. 4) Fibrinolysis of fibrin 2 was delayed compared to fibrin 1. Altogether, differences between fibrins 1 and 2 structure and function 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: S. Uitte de Willige, K. F. Standeven, H. Philippou, and R. A. S. Ariens The pleiotropic role of the fibrinogen {gamma}' chain in hemostasis Blood, November 5, 2009; 114(19): 3994 - 4001. [Abstract] [Full Text] [PDF] 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. 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