Fibrin binds to collagen and provides a bridge for alpha V beta 3 integrin-dependent contraction of collagen gels
(2014) In Biochemical Journal 462. p.113-123- 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... (More)
- 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. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/4659530
- author
- Reyhani, Vahid ; Seddigh, Pegah ; Guss, Bengt ; Gustafsson, Renata LU ; Rask, Lars and Rubin, Kristofer LU
- organization
- publishing date
- 2014
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- collagen type I, fibrin, gel contraction, interface matrix, protein, binding
- in
- Biochemical Journal
- volume
- 462
- pages
- 113 - 123
- publisher
- Portland Press
- external identifiers
-
- wos:000340218100010
- scopus:84904613293
- pmid:24840544
- ISSN
- 0264-6021
- DOI
- 10.1042/BJ20140201
- language
- English
- LU publication?
- yes
- id
- 467207df-fcde-4590-a41e-a3a545eac5d7 (old id 4659530)
- date added to LUP
- 2016-04-01 14:42:15
- date last changed
- 2022-03-22 01:29:38
@article{467207df-fcde-4590-a41e-a3a545eac5d7,
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.}},
author = {{Reyhani, Vahid and Seddigh, Pegah and Guss, Bengt and Gustafsson, Renata and Rask, Lars and Rubin, Kristofer}},
issn = {{0264-6021}},
keywords = {{collagen type I; fibrin; gel contraction; interface matrix; protein; binding}},
language = {{eng}},
pages = {{113--123}},
publisher = {{Portland Press}},
series = {{Biochemical Journal}},
title = {{Fibrin binds to collagen and provides a bridge for alpha V beta 3 integrin-dependent contraction of collagen gels}},
url = {{http://dx.doi.org/10.1042/BJ20140201}},
doi = {{10.1042/BJ20140201}},
volume = {{462}},
year = {{2014}},
}