Journal
BIOCHEMICAL JOURNAL
Volume 462, Issue -, Pages 113-123Publisher
PORTLAND PRESS LTD
DOI: 10.1042/BJ20140201
Keywords
collagen type I; fibrin; gel contraction; interface matrix; protein binding
Categories
Funding
- Swedish Cancer Foundation [CAN 2010/720]
- Swedish Science Council [521-2011-2625]
- Alfred Osterlunds Stiftelse (Sweden)
- Koch's stiftelse (Sweden)
- Uppsala University
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The functional significance of fibrin deposits typically seen in inflammatory lesions, carcinomas and in healing wounds is not fully understood. In the present study, we demonstrate that fibrinogen/fibrin specifically bound to native Col I (collagen type I) and used the Col I fibre network as a base to provide a functional interface matrix that connects cells to the Col I fibres through alpha V beta 3 integrins. This allowed murine myoblast C2C12 cells to contract the collagenous composite gel via alpha V beta 3 integrin. We show that fibrinogen specifically bound to immobilized native Col I at the site known to bind matrix metalloproteinase-1, discoidin domain receptor-2 and fibronectin, and that binding had no effect on Col I fibrillation. A specific competitive inhibitor blocking the Col-I-binding site for fibrinogen abolished the organization of fibrin into discernable fibrils, as well as the C2C12-mediated contraction of Col I gels. Our data show that fibrin can function as a linkage protein between Col I fibres and cells, and suggest that fibrin at inflammatory sites indirectly connects alpha V beta 3 integrins to Col I fibres and thereby promotes cell-mediated contraction of collagenous tissue structures.
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