Source:http://linkedlifedata.com/resource/pubmed/id/18991091
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5
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pubmed:dateCreated |
2008-11-10
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pubmed:abstractText |
Recent studies have identified a range of interactions between type IX collagen and other cartilage matrix components. To determine the extent to which these interactions are important in maintaining the integrity of ageing articular cartilage, we analyzed an age range of normal healthy articular cartilage samples by Western blotting, immunohistochemical, and PCR analyses. Reduced levels of type IX collagen were detected in post adolescence cartilage. Type IX collagen epitopes were evident throughout the matrix in all cartilage samples up to 19 years of age. Post adolescence, however, the pattern of immunoreactivity revealed territorial staining only. Type IX collagen expression at the transcriptional level is maintained at all ages. Type IX collagen fragments were extracted from young tissue, supporting the hypothesis that young cartilage is continually remodelled, while mature cartilage maintains relatively low levels of collagen turnover. Clearly the age changes we observed may have significant effects on the integrity of the tissue as the chondrocytes in ageing articular cartilage have limited capacity to turnover the interterritorial matrix. However, this study provides evidence that even in old age, the chondrocyte attempts to maintain its pericellular environment and hence its mechanical role. Therefore, the potential of type IX collagen to interact with other matrix components continues to be of importance in the territorial environment, and these interactions may have significant roles in mechanotransduction.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/COL9A1protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Collagen Type IX,
http://linkedlifedata.com/resource/pubmed/chemical/Cyanogen Bromide,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger
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pubmed:status |
MEDLINE
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pubmed:issn |
1607-8438
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:volume |
49
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
374-82
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pubmed:meshHeading |
pubmed-meshheading:18991091-Adolescent,
pubmed-meshheading:18991091-Adult,
pubmed-meshheading:18991091-Age Factors,
pubmed-meshheading:18991091-Aged,
pubmed-meshheading:18991091-Cartilage, Articular,
pubmed-meshheading:18991091-Child,
pubmed-meshheading:18991091-Collagen Type IX,
pubmed-meshheading:18991091-Cyanogen Bromide,
pubmed-meshheading:18991091-Extracellular Matrix,
pubmed-meshheading:18991091-Humans,
pubmed-meshheading:18991091-Middle Aged,
pubmed-meshheading:18991091-Peptides,
pubmed-meshheading:18991091-RNA, Messenger,
pubmed-meshheading:18991091-Young Adult
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pubmed:year |
2008
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pubmed:articleTitle |
Modification of the composition of articular cartilage collagen fibrils with increasing age.
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pubmed:affiliation |
Faculty of Veterinary Science, University of Liverpool, Liverpool, UK.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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