Changes in the composition of the extracellular matrix in patellar tendinopathy

Article


Samiric, Tom, Parkinson, John, Ilic, Mirna Z., Cook, Jill, Feller, Julian A. and Handley, Christopher J.. 2009. "Changes in the composition of the extracellular matrix in patellar tendinopathy ." Matrix Biology. 28 (4), pp. 230-236. https://doi.org/10.1016/j.matbio.2009.04.001
Article Title

Changes in the composition of the extracellular matrix in patellar tendinopathy

ERA Journal ID2067
Article CategoryArticle
AuthorsSamiric, Tom (Author), Parkinson, John (Author), Ilic, Mirna Z. (Author), Cook, Jill (Author), Feller, Julian A. (Author) and Handley, Christopher J. (Author)
Journal TitleMatrix Biology
Journal Citation28 (4), pp. 230-236
Number of Pages7
Year2009
Place of PublicationAmsterdam, Netherlands
ISSN0945-053X
1569-1802
Digital Object Identifier (DOI)https://doi.org/10.1016/j.matbio.2009.04.001
Abstract

Objective: To compare the chemical levels and mRNA expression of proteoglycan and collagen in normal human patellar tendons and tendons exhibiting chronic overuse tendinopathy. Methods: Sulfated glycosaminoglycan and hydroxyproline content were investigated by spectrophotometric measurement using papain-digested samples. Deglycosylated proteoglycan core proteins were analysed by Western blot using specific antibodies. Total mRNA isolated from samples of frozen tendons was assayed by relative quantitative RT-PCR for decorin, biglycan, fibromodulin, versican, aggrecan, and collagens Type I, II and III and normalised to glyceraldehyde-3-phosphate dehydrogenase. Results: There was a significant increase in sulfated glycosaminoglycan content in pathologic tendons compared to normal. This was attributed to an increased deposition of the large aggregating proteoglycans versican and aggrecan and the small proteoglycans biglycan and fibromodulin, but not decorin. Aggrecan and versican were extensively degraded in both normal and pathologic tendons, biglycan was more fragmented in the pathologic tendons while predominantly intact fibromodulin and decorin were present in normal and pathologic tendons. There was a greater range in total collagen content but no change in the level of total collagen in pathologic tendons. There were no significant differences between the pathologic and normal tendon for all genes, however p values close to 0.05 indicated a trend in downregulation of Type I collagen and fibromodulin, and upregulation in versican and Type III genes in pathologic tissue. Conclusion: The changes in proteoglycan and collagen levels observed in patellar tendinopathy appear to be primarily due to changes in the metabolic turnover of these macromolecules. Changes in the expression of these macromolecules may not play a major role in this process.

Keywordscollagen; patellar tendinopathy; proteoglycans; tendon
ANZSRC Field of Research 2020420701. Biomechanics
320216. Orthopaedics
320603. Medical molecular engineering of nucleic acids and proteins
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Byline AffiliationsLa Trobe University
Deakin University
Institution of OriginUniversity of Southern Queensland
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