Abstract |
Interleukin-1 (IL-1) in combination with other cytokines can induce a reproducible release of collagen fragments from bovine nasal cartilage in culture. Over 70% of the total collagen is released by day 14 and this release is accompanied by the appearance of collagenolytic activity in the medium that cleaves collagen specifically at the one quarter/three quarter position. Interleukin-4 is able to prevent the release of collagen fragments from the tissue and this is accompanied by a reduced secretion and activation of collagenase (MMP-1) with an increase in tissue inhibitor of metalloproteinases-1 (TIMP-1). IL-4, especially in the presence of IL-1, increased TIMP secretion by bovine nasal cartilage in culture. These results suggest that IL-4 is able to specifically block cartilage collagen resorption by down-regulating the production of collagenase (MMP-1) and up-regulating TIMP-1 by chondrocytes within the cartilage.
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Authors | T E Cawston, A J Ellis, H Bigg, V Curry, E Lean, D Ward |
Journal | Biochimica et biophysica acta
(Biochim Biophys Acta)
Vol. 1314
Issue 3
Pg. 226-32
(Dec 12 1996)
ISSN: 0006-3002 [Print] Netherlands |
PMID | 8982276
(Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
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Chemical References |
- Cytokines
- Enzyme Precursors
- Glycoproteins
- Glycosaminoglycans
- Matrix Metalloproteinase Inhibitors
- Peptide Fragments
- Peptides
- Protease Inhibitors
- Tissue Inhibitor of Metalloproteinases
- Oncostatin M
- Interleukin-10
- Interleukin-4
- Collagen
- Collagenases
- procollagenase
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Topics |
- Animals
- Cattle
- Collagen
(metabolism)
- Collagenases
(metabolism)
- Cytokines
(pharmacology)
- Enzyme Precursors
(metabolism)
- Glycoproteins
(biosynthesis)
- Glycosaminoglycans
(metabolism)
- In Vitro Techniques
- Interleukin-10
(pharmacology)
- Interleukin-4
(pharmacology)
- Matrix Metalloproteinase Inhibitors
- Nasal Septum
(metabolism)
- Oncostatin M
- Peptide Fragments
(metabolism)
- Peptides
(pharmacology)
- Protease Inhibitors
- Tissue Inhibitor of Metalloproteinases
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