Fibrin binds to collagen and provides a bridge for αVβ3 integrin-dependent contraction of collagen gels
| العنوان: | Fibrin binds to collagen and provides a bridge for αVβ3 integrin-dependent contraction of collagen gels |
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| المؤلفون: | Renata Gustafsson, Kristofer Rubin, Vahid Reyhani, Pegah Seddigh, Bengt Guss, Lars Rask |
| المصدر: | Biochemical Journal |
| بيانات النشر: | Portland Press Ltd., 2014. |
| سنة النشر: | 2014 |
| مصطلحات موضوعية: | interface matrix, collagen type I, Integrin, c-RGD, cyclic RGD, SPR, surface plasmon resonance, protein binding, Fibril, Biochemistry, Collagen Type I, DMEM, Dulbecco’s modified Eagle’s medium, PDGF, platelet-derived growth factor, Fibrin, Cell Line, Extracellular matrix, Mice, Thrombin, medicine, Animals, gel contraction, fibrin, Molecular Biology, Cells, Cultured, Col I, collagen type I, Integrin alphaVbeta3, biology, Chemistry, PAE, porcine aortic endothelial, PBS-T, 0.05% Tween 20 in PBS, CNE, collagen-binding protein from Steptococcus equi, Cell Biology, Molecular biology, Extracellular Matrix, ECM, extracellular matrix, Cell biology, Fibronectin, biology.protein, PAR, protease-activated receptor, Gels, Discoidin domain, Research Article, medicine.drug |
| الوصف: | 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 αVβ3 integrins. This allowed murine myoblast C2C12 cells to contract the collagenous composite gel via αVβ3 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 αVβ3 integrins to Col I fibres and thereby promotes cell-mediated contraction of collagenous tissue structures. The putative functions of extravascular fibrin in pathologies are poorly characterized. We show that fibrinogen binds specifically to a defined protein-binding site of the native collagen. Through this binding, fibrin provides an interface matrix allowing αVβ3 integrin-mediated collagen gel contraction. |
| تدمد: | 1470-8728 0264-6021 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d0f54b9fb3b20574f372e176621b9eed https://doi.org/10.1042/bj20140201 |
| حقوق: | OPEN |
| رقم الأكسشن: | edsair.doi.dedup.....d0f54b9fb3b20574f372e176621b9eed |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 14708728 02646021 |
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