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Fibronectin fragments cause release and degradation of collagen-binding molecules from equine explant cultures.

Johnson, Anna LU ; Smith, Roger; Saxne, Tore LU ; Hickery, Mark and Heinegård, Dick LU (2004) In Osteoarthritis and Cartilage 12(2). p.149-159
Abstract
OBJECTIVE: Previous experiments have shown that addition of fragmented fibronectin can induce cartilage chondrolysis. In this study we investigated the fate of the collagen- and cell-binding molecules Cartilage oligomeric matrix protein (COMP) and chondroadherin. DESIGN: Equine articular cartilage explants were stimulated with the C-terminal and the N-terminal heparin-binding fragments of fibronectin respectively, and the conditioned media were analysed by both quantitative (ELISA) and qualitative (mass spectrometry, Western blots) methods. RESULTS: Both COMP and chondroadherin were released in a dose-dependent manner upon stimulation with the Hep II (C-terminal heparin-binding) fragment of fibronectin. The kinetics of release for the two... (More)
OBJECTIVE: Previous experiments have shown that addition of fragmented fibronectin can induce cartilage chondrolysis. In this study we investigated the fate of the collagen- and cell-binding molecules Cartilage oligomeric matrix protein (COMP) and chondroadherin. DESIGN: Equine articular cartilage explants were stimulated with the C-terminal and the N-terminal heparin-binding fragments of fibronectin respectively, and the conditioned media were analysed by both quantitative (ELISA) and qualitative (mass spectrometry, Western blots) methods. RESULTS: Both COMP and chondroadherin were released in a dose-dependent manner upon stimulation with the Hep II (C-terminal heparin-binding) fragment of fibronectin. The kinetics of release for the two components differed. Moreover, COMP was degraded while no fragments of chondroadherin could be detected. Stimulation with Hep II also induced production of nitric oxide in a dose-dependent manner. We compared effects of the Hep II fragment with that of Hep I (the N-terminal heparin-binding fragment of fibronectin) and found that while Hep I did indeed elicit release of COMP and chondroadherin, the response was less potent, and production of nitric oxide was negligible. The responses to both fragments were elicited within 24h. CONCLUSIONS: We suggest that the events described here may be early, critical stages in cartilage destruction preceding collagen destruction. (Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Chondrolysis, Chondroadherin, Fibronectin fragment, Cartilage oligomeric matrix protein
in
Osteoarthritis and Cartilage
volume
12
issue
2
pages
149 - 159
publisher
Elsevier
external identifiers
  • pmid:14723874
  • wos:000188844000007
  • scopus:0842323826
ISSN
1063-4584
DOI
10.1016/j.joca.2003.10.008
language
English
LU publication?
yes
id
924c750d-abe4-4b4a-a502-fb2b2d67d91c (old id 120126)
alternative location
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=14723874&dopt=Abstract
date added to LUP
2007-07-16 09:54:59
date last changed
2017-01-01 05:10:47
@article{924c750d-abe4-4b4a-a502-fb2b2d67d91c,
  abstract     = {OBJECTIVE: Previous experiments have shown that addition of fragmented fibronectin can induce cartilage chondrolysis. In this study we investigated the fate of the collagen- and cell-binding molecules Cartilage oligomeric matrix protein (COMP) and chondroadherin. DESIGN: Equine articular cartilage explants were stimulated with the C-terminal and the N-terminal heparin-binding fragments of fibronectin respectively, and the conditioned media were analysed by both quantitative (ELISA) and qualitative (mass spectrometry, Western blots) methods. RESULTS: Both COMP and chondroadherin were released in a dose-dependent manner upon stimulation with the Hep II (C-terminal heparin-binding) fragment of fibronectin. The kinetics of release for the two components differed. Moreover, COMP was degraded while no fragments of chondroadherin could be detected. Stimulation with Hep II also induced production of nitric oxide in a dose-dependent manner. We compared effects of the Hep II fragment with that of Hep I (the N-terminal heparin-binding fragment of fibronectin) and found that while Hep I did indeed elicit release of COMP and chondroadherin, the response was less potent, and production of nitric oxide was negligible. The responses to both fragments were elicited within 24h. CONCLUSIONS: We suggest that the events described here may be early, critical stages in cartilage destruction preceding collagen destruction.},
  author       = {Johnson, Anna and Smith, Roger and Saxne, Tore and Hickery, Mark and Heinegård, Dick},
  issn         = {1063-4584},
  keyword      = {Chondrolysis,Chondroadherin,Fibronectin fragment,Cartilage oligomeric matrix protein},
  language     = {eng},
  number       = {2},
  pages        = {149--159},
  publisher    = {Elsevier},
  series       = {Osteoarthritis and Cartilage},
  title        = {Fibronectin fragments cause release and degradation of collagen-binding molecules from equine explant cultures.},
  url          = {http://dx.doi.org/10.1016/j.joca.2003.10.008},
  volume       = {12},
  year         = {2004},
}