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J. Biol. Chem., Vol. 281, Issue 50, 38208-38216, December 15, 2006

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Decorin Modulates Fibrin Assembly and Structure^*

Tracey A. Dugan¹, Vivian W.-C. Yang, David J. McQuillan^¶, and Magnus Höök²

From the Center for Extracellular Matrix Biology, Institute of Biosciences and Technology, Texas A&M Health Science Center, Houston, Texas 77030, the Graduate Institute of Biomedical Materials, Taipei Medical University, Taipei 110, Taiwan, and the ^¶LifeCell Corporation, Branchburg, New Jersey 08876

Emerging evidence indicates that fibrin clotting is regulated by different external factors. We demonstrated recently that decorin, a regulator of collagen fibrillogenesis and transforming growth factor- activity, binds to the D regions of fibrinogen (Dugan, T.A., Yang, V. W.-C., McQuillan, D.J., and Höök, M. (2003) J. Biol. Chem. 278, 13655–13662). We now report that the decorin-fibrinogen interaction alters the assembly, structure, and clearance of fibrin fibers. Relative to fibrinogen, substoichiometric amounts of decorin core protein modulated clotting, whereas an excess of an active decorin peptide was necessary for similar activity. These concentration-dependent effects suggest that decorin bound to the D regions sterically modulates fibrin assembly. Scanning electron microscopy images of fibrin clotted in the presence of increasing concentrations of decorin core protein showed progressively decreasing fiber diameter. The sequestration of Zn²⁺ ions from the N-terminal fibrinogen-binding region abrogated decorin incorporation into the fibrin network. Compared with linear thicker fibrin fibers, the curving thin fibers formed with decorin underwent accelerated tissue-type plasminogen activator-dependent fibrinolysis. Collectively, these data demonstrate that decorin can regulate fibrin organization and reveal a novel mechanism by which extracellular matrix components can participate in hemostasis, thrombosis, and wound repair.

Received for publication, July 31, 2006 , and in revised form, October 4, 2006.

^* This work was supported by National Institutes of Health Grants AR042919 and AI020624 (to M. H.). The acquisition of the field emission scanning electron microscope used in this work was supported by National Science Foundation Grant DBI-0116835. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ Present address: Baylor College of Medicine, Houston, TX 77030.

² To whom correspondence should be addressed: Center for Extracellular Matrix Biology, Inst. of Biosciences and Technology, Texas A&M Health Science Center, 2121 W. Holcombe Blvd., Houston, TX 77030. Tel.: 713-677-7552; Fax: 713-677-7576; E-mail: mhook{at}ibt.tamhsc.edu.

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