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Lookup NU author(s): Dr William Shingleton,
Emeritus Professor Drew Rowan,
Emeritus Professor Tim Cawston
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Retinoic acid (RetA) and interleukin-1 alpha (IL-l) together can induce a reproducible release of proteoglycan fragments from bovine nasal cartilage in culture. However, release of collagen fragments with either agent alone is often variable. In this study over 70% of the total collagen was released from bovine nasal cartilage in culture by day 14 when RetA and IL-l were combined. This release was accompanied by the appearance of collagenolytic activity in the culture medium that cleaved collagen specifically at the 1/4/3/4 position. Tissue inhibitor of metalloproteinases (TIMP) activity was present at day 7 but low or absent in media from resorbing tissue at day 14. The breakdown of cartilage collagen could be prevented by the addition of BB-94, a specific metalloproteinase inhibitor. These results suggest that RetA promotes the early release of TIMP from the tissue and that IL-l stimulates pro-collagenase secretion which, when activated, exceeds the local concentration of TIMP. Th us in the later stages of culture collagen destruction occurs. Both MMP-1 and MMP-13 were detected and appear to be involved in IL-l + RetA induced bovine cartilage destruction. However, for the first time, we also present evidence to suggest that MMP-13 is the predominant collagenase in this system. I. Cell. Biochem. 79.519-531, 2000. (C) 2000 Wiley-Lisa Inc.
Author(s): Shingleton WD, Ellis AJ, Rowan AD, Cawston TE
Publication type: Article
Publication status: Published
Journal: Journal of Cellular Biochemistry
ISSN (print): 0730-2312
ISSN (electronic): 1097-4644
Publisher: John Wiley & Sons, Inc.
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