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Blood, 1 December 2005, Vol. 106, No. 12, pp. 3824-3830. Prepublished online as a Blood First Edition Paper on August 9, 2005; DOI 10.1182/blood-2005-05-2150. This Article Full Text Full Text (PDF) All Versions of this Article: 2005-05-2150v1 106/12/3824    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 Collet, J.-P. Articles by Weisel, J. W. Search for Related Content PubMed PubMed Citation Articles by Collet, J.-P. Articles by Weisel, J. W. Related Collections Hemostasis, Thrombosis, and Vascular Biology Related Article in Blood Online Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  HEMOSTASIS, THROMBOSIS, AND VASCULAR BIOLOGY The C domains of fibrinogen affect the structure of the fibrin clot, its physical properties, and its susceptibility to fibrinolysis Jean-Philippe Collet, Jennifer L. Moen, Yuri I. Veklich, Oleg V. Gorkun, Susan T. Lord, Gilles Montalescot, and John W. Weisel From the Institut de Cardiologie, Hôpital Pitié-Salpêtrière, Assistance Publique Hôpitaux de Paris, France; the Department of Cell and Developmental Biology, University of Pennsylvania School of Medicine, Philadelphia; and the Department of Pathology and Laboratory Medicine, University of North Carolina, Chapel Hill. The functions of the C domains of fibrinogen in clotting and fibrinolysis, which have long been enigmatic, were determined using recombinant fibrinogen truncated at A chain residue 251. Scanning electron microscopy and confocal microscopy revealed that the fibers of 251 clots were thinner and denser, with more branch points than fibers of control clots. Consistent with these results, the permeability of 251 clots was nearly half that of control clots. Together, these results suggest that in normal clot formation, the C domains enhance lateral aggregation to produce thicker fibers. The viscoelastic properties of 251 fibrin clots differed markedly from control clots; 251 clots were much less stiff and showed more plastic deformation, indicating that interactions between the C domains in normal clots play a major role in determining the clot's mechanical properties. Comparing factor XIIIa cross-linked 251 and control clots showed that chain cross-linking had a significant effect on clot stiffness. Plasmin-catalyzed lysis of 251 clots, monitored with both macroscopic and microscopic methods, was faster than lysis of control clots. In conclusion, these studies provide the first definitive evidence that the C domains play an important role in determining the structure and biophysical properties of clots and their susceptibility to fibrinolysis. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? Related Article in Blood Online: Another fibrin C scene unmasked Dennis K. Galanakis Blood 2005 106: 3680. [Full Text] [PDF] This article has been cited by other articles: C. Karlsson, M. Morgelin, M. Collin, R. Lood, M.-L. Andersson, A. Schmidtchen, L. Bjorck, and I.-M. Frick SufA - a bacterial enzyme that cleaves fibrinogen and blocks fibrin network formation Microbiology, January 1, 2009; 155(1): 238 - 248. [Abstract] [Full Text] [PDF] R. A. Campbell, K. A. Overmyer, C. R. Bagnell, and A. S. Wolberg Cellular Procoagulant Activity Dictates Clot Structure and Stability as a Function of Distance From the Cell Surface Arterioscler Thromb Vasc Biol, December 1, 2008; 28(12): 2247 - 2254. [Abstract] [Full Text] [PDF] J. Suntharalingam, K. Goldsmith, V. van Marion, L. Long, C. M. Treacy, F. Dudbridge, M. R. Toshner, J. Pepke-Zaba, J. C. J. Eikenboom, and N. W. Morrell Fibrinogen A{alpha} Thr312Ala polymorphism is associated with chronic thromboembolic pulmonary hypertension Eur. Respir. J., April 1, 2008; 31(4): 736 - 741. [Abstract] [Full Text] [PDF] R. Ajjan, B. C. B. Lim, K. F. Standeven, R. Harrand, S. Dolling, F. Phoenix, R. Greaves, R. H. Abou-Saleh, S. Connell, D. A. M. Smith, et al. Common variation in the C-terminal region of the fibrinogen -chain: effects on fibrin structure, fibrinolysis and clot rigidity Blood, January 15, 2008; 111(2): 643 - 650. [Abstract] [Full Text] [PDF] K. F. Standeven, A. M. Carter, P. J. Grant, J. W. Weisel, I. Chernysh, L. Masova, S. T. Lord, and R. A. S. Ariens Functional analysis of fibrin {gamma}-chain cross-linking by activated factor XIII: determination of a cross-linking pattern that maximizes clot stiffness Blood, August 1, 2007; 110(3): 902 - 907. [Abstract] [Full Text] [PDF] R. I. Litvinov, O. V. Gorkun, D. K. Galanakis, S. Yakovlev, L. Medved, H. Shuman, and J. W. Weisel Polymerization of fibrin: direct observation and quantification of individual B:b knob-hole interactions Blood, January 1, 2007; 109(1): 130 - 138. [Abstract] [Full Text] [PDF] A. Silveira and A. Hamsten Fibrin gel architecture influences endogenous fibrinolysis and may promote coronary artery disease. Arterioscler Thromb Vasc Biol, November 1, 2006; 26(11): 2419 - 2420. [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]

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