rdf:type |
|
lifeskim:mentions |
umls-concept:C0007452,
umls-concept:C0009325,
umls-concept:C0021755,
umls-concept:C0033414,
umls-concept:C0040845,
umls-concept:C0225415,
umls-concept:C0243125,
umls-concept:C0331858,
umls-concept:C0699900,
umls-concept:C1157968,
umls-concept:C1314939,
umls-concept:C1704640,
umls-concept:C1706515,
umls-concept:C2931073
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pubmed:issue |
4
|
pubmed:dateCreated |
2000-12-8
|
pubmed:abstractText |
Retinoic acid (RetA) and interleukin-1alpha (IL-1) 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-1 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-1 stimulates pro-collagenase secretion which, when activated, exceeds the local concentration of TIMP. Thus in the later stages of culture collagen destruction occurs. Both MMP-1 and MMP-13 were detected and appear to be involved in IL-1 + 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.
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Collagen,
http://linkedlifedata.com/resource/pubmed/chemical/Collagenases,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-1,
http://linkedlifedata.com/resource/pubmed/chemical/Matrix Metalloproteinase 1,
http://linkedlifedata.com/resource/pubmed/chemical/Matrix Metalloproteinase 13,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Proteoglycans,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Tissue Inhibitor of...,
http://linkedlifedata.com/resource/pubmed/chemical/Tretinoin
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0730-2312
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pubmed:author |
|
pubmed:copyrightInfo |
Copyright 2000 Wiley-Liss, Inc.
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pubmed:issnType |
Print
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pubmed:day |
14
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pubmed:volume |
79
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
519-31
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:10996843-Animals,
pubmed-meshheading:10996843-Cartilage,
pubmed-meshheading:10996843-Cattle,
pubmed-meshheading:10996843-Cells, Cultured,
pubmed-meshheading:10996843-Chondrocytes,
pubmed-meshheading:10996843-Collagen,
pubmed-meshheading:10996843-Collagenases,
pubmed-meshheading:10996843-Drug Synergism,
pubmed-meshheading:10996843-Interleukin-1,
pubmed-meshheading:10996843-Matrix Metalloproteinase 1,
pubmed-meshheading:10996843-Matrix Metalloproteinase 13,
pubmed-meshheading:10996843-Peptide Fragments,
pubmed-meshheading:10996843-Proteoglycans,
pubmed-meshheading:10996843-RNA, Messenger,
pubmed-meshheading:10996843-Tissue Inhibitor of Metalloproteinase-1,
pubmed-meshheading:10996843-Tretinoin
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pubmed:year |
2000
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pubmed:articleTitle |
Retinoic acid combines with interleukin-1 to promote the degradation of collagen from bovine nasal cartilage: matrix metalloproteinases-1 and -13 are involved in cartilage collagen breakdown.
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pubmed:affiliation |
Department of Rheumatology, The Medical School, Unviersity of Newcastle upon Tyne, United Kingdom. W.D.Shingleton@ncl.ac.uk
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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