| First Author | Reyhani V | Year | 2014 |
| Journal | Biochem J | Volume | 462 |
| Issue | 1 | Pages | 113-23 |
| PubMed ID | 24840544 | Mgi Jnum | J:215243 |
| Mgi Id | MGI:5604950 | Doi | 10.1042/BJ20140201 |
| Citation | Reyhani V, et al. (2014) Fibrin binds to collagen and provides a bridge for alphaVbeta3 integrin-dependent contraction of collagen gels. Biochem J 462(1):113-23 |
| abstractText | 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 alphaVbeta3 integrins. This allowed murine myoblast C2C12 cells to contract the collagenous composite gel via alphaVbeta3 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 alphaVbeta3 integrins to Col I fibres and thereby promotes cell-mediated contraction of collagenous tissue structures. |
