Abstract
BackgroundThe incidence of Achilles tendinopathy is high and underlying etiology as well as biochemical and morphological pathology associated with the disease is largely unknown. The aim of the present study was to describe biochemical and morphological differences in chronic Achilles tendinopathy. The expressions of growth factors, inflammatory mediators and tendon morphology were determined in both chronically diseased and healthy tendon parts.MethodsThirty Achilles tendinopathy patients were randomized to an expression-study (n = 16) or a structural-study (n = 14). Biopsies from two areas in the Achilles tendon were taken and structural parameters: fibril density, fibril size, volume fraction of cells and the nucleus/cytoplasm ratio of cells were determined. Further gene expressions of various genes were analyzed.ResultsSignificantly smaller collagen fibrils and a higher volume fraction of cells were observed in the tendinopathic region of the tendon. Markers for collagen and its synthesis collagen 1, collagen 3, fibronectin, tenascin-c, transforming growth factor-β fibromodulin, and markers of collagen breakdown matrix metalloproteinase-2, matrix metalloproteinase-9 and metallopeptidase inhibitor-2 were significantly increased in the tendinopathic region. No altered expressions of markers for fibrillogenesis, inflammation or wound healing were observed.ConclusionThe present study indicates that an increased expression of factors stimulating the turnover of connective tissue is present in the diseased part of tendinopathic tendons, associated with an increased number of cells in the injured area as well as an increased number of smaller and thinner fibrils in the diseased tendon region. As no fibrillogenesis, inflammation or wound healing could be detected, the present data supports the notion that tendinopathy is an ongoing degenerative process.Trial registrationCurrent Controlled Trials ISRCTN20896880
Highlights
The incidence of Achilles tendinopathy is high and underlying etiology as well as biochemical and morphological pathology associated with the disease is largely unknown
Structural composition of the tendon The density, volume fraction and mean area of the collagen fibrils were measured in biopsies from 14 of the tendinopathy patients (Table 1)
The density of collagen fibrils was found to be significantly higher and the mean area of the collagen fibrils was significantly smaller in tendinopathic tendon region compared to that of healthy control region, a trend towards significant difference was found in volume fraction (Table 1)
Summary
The incidence of Achilles tendinopathy is high and underlying etiology as well as biochemical and morphological pathology associated with the disease is largely unknown. The aim of the present study was to describe biochemical and morphological differences in chronic Achilles tendinopathy. Tendons connect muscle to bone and enable transmission of forces from contracting muscle to bone, resulting in joint movement They possess the ability to adapt to changes in loading [1] and studies have shown that collagen synthesis is increased as a result of both acute exercise [2,3] and prolonged physical training [4]. Taking the aforementioned limitations into account, current data concerning local biochemical differences within tendinopathic tendons, seem to indicate that an altered expression of collagen [20], proteoglycans [21] and matrix metalloproteinases [16,22] exists in tendinopathic tendons. Analyses of local biochemical differences together with morphological differences are lacking
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
