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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 LU ; Rask, Lars and Rubin, Kristofer LU (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)
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author
organization
publishing date
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 Limited
external identifiers
  • wos:000340218100010
  • scopus:84904613293
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
2014-10-01 07:23:42
date last changed
2017-09-03 04:21:28
@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},
  keyword      = {collagen type I,fibrin,gel contraction,interface matrix,protein,binding},
  language     = {eng},
  pages        = {113--123},
  publisher    = {Portland Press Limited},
  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},
  volume       = {462},
  year         = {2014},
}