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Prepublished online as a Blood First Edition Paper on June 12, 2003; DOI 10.1182/blood-2003-01-0204. This Article Full Text Full Text (PDF) All Versions of this Article: 2003-01-0204v1 102/7/2466    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 Moen, J. L. Articles by Lord, S. T. Search for Related Content PubMed PubMed Citation Articles by Moen, J. L. Articles by Lord, S. T. Related Collections Hemostasis, Thrombosis, and Vascular Biology Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  Blood, 1 October 2003, Vol. 102, No. 7, pp. 2466-2471 HEMOSTASIS, THROMBOSIS, AND VASCULAR BIOLOGY Recombinant BArg14His fibrinogen implies participation of N-terminus of B chain in desA fibrin polymerization Jennifer L. Moen, Oleg V. Gorkun, John W. Weisel, and Susan T. Lord From the Department of Chemistry and the Department of Pathology and Laboratory Medicine, University of North Carolina at Chapel Hill; and the Department of Cell and Developmental Biology, University of Pennsylvania School of Medicine, Philadelphia. We synthesized BArg14His fibrinogen with histidine substituted for arginine at the B thrombin-cleavage site. This substitution led to a 300-fold decrease in the rate of thrombin-catalyzed fibrinopeptide B (FpB, B 1-14) release, whereas the rate of FpA release was normal with either thrombin or the FpA-specific enzyme, batroxobin. Both thrombin- and batroxobincatalyzed polymerization of BArg14His fibrinogen were significantly impaired, with a longer lag time, slower rate of lateral aggregation, and decreased final turbidity. Moreover, desA monomer polymerization was similarly impaired, demonstrating that the histidine substitution itself, and not the lack of FpB cleavage, caused the abnormal polymerization of BArg14His fibrin. Scanning electron microscopy showed BArg14His fibrin fibers were thinner than normal (BArg14His, approximately 70 nm; normal, approximately 100 nm; P < .0001), as expected from the decreased final turbidity. We conclude that the N-terminus of the B chain is involved in the lateral aggregation of normal desAprotofibrils and that the ArgHis substitution disrupts these interactions in BArg14His fibrinogen. (Blood. 2003;102:2466-2471) CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: M. Nakayama-Hamada, A. Suzuki, H. Furukawa, R. Yamada, and K. Yamamoto Citrullinated Fibrinogen Inhibits Thrombin-catalysed Fibrin Polymerization J. Biochem., September 1, 2008; 144(3): 393 - 398. [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]

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