Skip to main content
SLU:s publikationsdatabas (SLUpub)

Forskningsartikel2014Vetenskapligt granskadÖppen tillgång

Fibrin binds to collagen and provides a bridge for alpha V beta 3 integrin-dependent contraction of collagen gels

Reyhani, Vahid; Seddigh, Pegah; Guss, Bengt; Gustafsson, Renata; Rask, Lars; Rubin, Kristofer


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.


collagen type I; fibrin; gel contraction; interface matrix; protein binding

Publicerad i

Biochemical Journal
2014, Volym: 462, sidor: 113-123

    Globala målen

    SDG3 God hälsa och välbefinnande

    UKÄ forskningsämne

    Mikrobiologi inom det medicinska området

    Publikationens identifierare


    Permanent länk till denna sida (URI)