Change in proteoglycan metabolism is a characteristic of human patellar tendinopathy

Article


Parkinson, John, Samiric, Tom, Ilic, Mirna Z., Cook, Jill, Feller, Julian A. and Handley, Christopher J.. 2010. "Change in proteoglycan metabolism is a characteristic of human patellar tendinopathy." Arthritis and Rheumatology. 62 (10), pp. 3028-3035. https://doi.org/10.1002/art.27587
Article Title

Change in proteoglycan metabolism is a characteristic of human patellar tendinopathy

ERA Journal ID15730
Article CategoryArticle
AuthorsParkinson, John (Author), Samiric, Tom (Author), Ilic, Mirna Z. (Author), Cook, Jill (Author), Feller, Julian A. (Author) and Handley, Christopher J. (Author)
Journal TitleArthritis and Rheumatology
Journal Citation62 (10), pp. 3028-3035
Number of Pages8
Year2010
Place of PublicationHoboken, NJ. USA
ISSN0004-3591
0893-7524
1529-0131
2326-5191
2326-5205
Digital Object Identifier (DOI)https://doi.org/10.1002/art.27587
Web Address (URL)http://onlinelibrary.wiley.com/doi/10.1002/art.27587/abstract
Abstract

Objective. To determine differences in the metabolism of proteoglycans and the gene expression of proteinases and their inhibitors between patellar tendons exhibiting chronic overuse tendinopathy and normal patellar tendons in humans.
Methods. Rates of loss and synthesis of proteoglycans were determined. Radiolabeled and total proteoglycans retained in and lost from the tissue were analyzed by fluorography and Western blotting. Levels of messenger RNA for matrix metalloproteinase 1(MMP-1), MMP-2, MMP-3, MMP-9, MMP-13,
ADAMTS-1, ADAMTS-4, ADAMTS-5, tissue inhibitor of metalloproteinases 1 (TIMP-1), TIMP-2, TIMP-3, and TIMP-4 were determined in fresh tissue.
Results. The rate of loss of 35S-labeled proteoglycans was greater in abnormal tendons, as was the rate of synthesis of proteoglycans. Fluorography and Western blotting revealed the presence of greater amounts of large proteoglycans (aggrecan and versican) in abnormal tendons, and these proteoglycans were rapidly lost from the matrix of abnormal tendons. There was no significant difference in the expression of ADAMTS-1, ADAMTS-4, ADAMTS-5, MMP-1, MMP-2, MMP-3, MMP-13, TIMP-2, TIMP-3, or TIMP-4. There was a
significant increase in the expression of MMP-9 and TIMP-1 in abnormal tendons.
Conclusion. Our findings suggest that a change in the proteoglycan content of the extracellular matrix in abnormal tendons results from the altered metabolism of the cells, reflected in the enhanced synthesis of the large proteoglycans aggrecan and versican, and does not appear to result from changes at the level of gene expression.

Keywordsgene expression profiling; human tissue; nucleotide sequence; patella tendon; protein degradation; protein expression; protein metabolism; protein synthesis; repetitive strain injury; tendinitis
ANZSRC Field of Research 2020310103. Cell metabolism
320223. Rheumatology and arthritis
320601. Gene and molecular therapy
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Byline AffiliationsLa Trobe University
Deakin University
Institution of OriginUniversity of Southern Queensland
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