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Research article2014Peer reviewedOpen access

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

Abstract

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.

Keywords

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

Published in

Biochemical Journal
2014, Volume: 462, pages: 113-123 Publisher: PORTLAND PRESS LTD

    Sustainable Development Goals

    SDG3 Good health and well-being

    UKÄ Subject classification

    Microbiology
    Microbiology in the medical area

    Publication identifier

    DOI: https://doi.org/10.1042/BJ20140201

    Permanent link to this page (URI)

    https://res.slu.se/id/publ/63313