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Semin Thromb Hemost 1998; 24(2): 169-174
DOI: 10.1055/s-2007-995837
Copyright © 1998 by Thieme Medical Publishers, Inc.

Fibrinogen Structure and Fibrin Clot Assembly

Michael W. Mosesson
  • From the University of Wisconsin Medical School, Milwaukee Clinical Campus, Sinai Samaritan Medical Center, Milwaukee, Wisconsin.
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Publication History

Publication Date:
06 February 2008 (online)

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Abstract

Fibrinogen is a complex multifunctional protein, which contains constitutive association sites (γXL, D:D, Da, Db) as well as cryptic sites that become exposed as a result of fibrinogen proteolysis by thrombin (EA, EB). Utilization of these sites by self-association (γXL or D:D) or by association with exposed complementary fibrin sites (Da:EA, Db:EB) produces an orderly process of molecular assembly to form linear and branched fibrils, concomitant with lateral fibril associations and factor XIIIa-mediated fibrin crosslinking that together result in the mature fibrin network.

Keywords:

Factor XIII - crosslinking - fibrinogen - fibrin - polymerization