The prevention of collagen breakdown in bovine nasal cartilage by TIMP, TIMP-2 and a low molecular weight synthetic inhibitor
Autor: | A.J. Ellis, E.K. Powell, V.A. Curry, T.E. Cawston |
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Rok vydání: | 1994 |
Předmět: |
Biophysics
Dose dependence Connective tissue Matrix metalloproteinase Matrix Metalloproteinase Inhibitors Nose Biochemistry Culture Techniques medicine Animals Nasal cartilages Molecular Biology Glycoproteins Metalloproteinase Tissue Inhibitor of Metalloproteinase-2 biology Chemistry Cartilage Proteins Tissue Inhibitor of Metalloproteinases Cell Biology Molecular biology Peptide Fragments medicine.anatomical_structure Proteoglycan Collagen breakdown biology.protein Cattle Collagen Interleukin-1 |
Zdroj: | Biochemical and biophysical research communications. 201(1) |
ISSN: | 0006-291X |
Popis: | Interleukin-1 stimulated bovine nasal cartilage fragments were cultured in the presence and absence of various metalloproteinase inhibitors. Tissue inhibitor of metalloproteinases (TIMP) and tissue inhibitor of metalloproteinases-2 (TIMP-2) completely blocked the release of collagen from the cartilage but were unable to prevent the release of proteoglycan. Similarly, a low molecular weight synthetic inhibitor (BB87) inhibited collagen release in a dose dependent manner, but was unable to inhibit proteoglycan release at the same concentrations. Significantly greater concentrations of inhibitor than those required to block collagen release did, however, block proteoglycan release. These results indicate that the therapeutic use of naturally occurring or synthetic inhibitors may provide a means of modifying the destruction of connective tissue proteins occurring in the arthritides and other connective tissue pathologies. |
Databáze: | OpenAIRE |
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