Achilles Tendinosis

Mos, Marieke de; El, B. van; DeGroot, Jeroen; Jahr, Holger; Schie, Hans T. M. van; Arkel, Ewoud R. van; Tol, H. T. M. van; Heijboer, Rien; Osch, Gerjo J. V. M. van; Verhaar, Jan A N

doi:10.1177/0363546507301885

Cited by 133 publications

(60 citation statements)

References 42 publications

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“…The extremes of this relationship may cause a loss of mechanical function, which may be related to the subtle degradation of ECM components, notably those involved in cross-linking and/or stabilisation of the tendon structure [121], such as minor collagens including Col V as well as proteoglycans. In contrast, a lower level of MMP-3 expression compared to normal tissue samples has been reported in human tendon displaying pathological characteristics [100,117,[122][123][124]. These observations may represent a failure of the normal matrix remodelling process [125].…”

Section: Functionmentioning

confidence: 93%

Genetic Variation, Protein Composition and Potential Influences on Tendon Properties in Humans

Foster¹

2012

TOSMJ

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Sequence variations in genes that code for proteins involved in homeostatic processes within tendons may influence tendon mechanical properties. Since variants of the four genes COL5A1, TNC, MMP3 and GDF5 have been implicated in the aetiopathogenesis of tendinopathies, which is ultimately characterised by abnormal structural and regulatory processes, sequence variations in these four genes may also influence how the tendon functions mechanically, even in the absence of tendinopathy. For example, two reports of association between variation in the COL5A1 gene and measures of flexibility complement reported associations between genotype and incidence of tendinopathy. Non-genetic factors such as age, body mass and physical activity status influence risk of tendon injury and physical performance potential independently from genomics, and also in gene-environment interactions. However, these non-genetic factors are often not considered in genetic association studies, probably due to their retrospective nature. Further research examining COL5A1, TNC, MMP3 and GDF5, as well as other genes that may influence the maintenance of tendon homeostasis such as COL1A1 which regulates the production of collagen type 1, the most abundant structural component of tendon is encouraged. Establishing the genetic basis of tendon properties in asymptomatic populations may advance understanding of some aspects relevant to physical performance and of the aetiology of tendinopathies. To improve understanding, accurate and reproducible assessments of tendon properties are required. However, no valid and reliable assessments of tendon properties, such as those involving in vivo ultrasound imaging techniques, have yet been applied to genetic association studies in humans.

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Section: Functionmentioning

confidence: 93%

Genetic Variation, Protein Composition and Potential Influences on Tendon Properties in Humans

Foster¹

2012

TOSMJ

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Section: Methodsmentioning

confidence: 99%

“…MMPs 1 and 13 were selected as they are known to be active against fibrillar collagens, including the predominant collagen type I 1, 28, 29, 30. MMP‐3 was selected as it degrades other minor proteins in tendon matrix, including collagens III, IV, IX, and X, and also proteoglycans and elastin 28, 29, 30, 31, 32, 33. The C1,2C (or COL 2 3/4C short) antibody detects the carboxy terminus of fragmented type I and II collagen, cleaved by collagenases MMP‐1, MMP‐8 or MMP‐13 21, 34, 35, 36, 37…”

Section: Methodsmentioning

confidence: 99%

Tendon extracellular matrix damage, degradation and inflammation in response to in vitro overload exercise

Spiesz

Thorpe

Chaudhry

et al. 2015

Journal Orthopaedic Research

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The role of inflammation in tendon injury is uncertain and a topic of current interest. In vitro studies of tendon accelerated overload damage can serve as a valuable source of information on the early stages of tendinopathy. Viable fascicle bundles from bovine flexor tendons were subjected to cyclic uniaxial loading from 1–10% strain. Immuno‐staining for inflammatory markers and matrix degradation markers was performed on the samples after mechanical testing. Loaded samples exhibited visible extracellular matrix damage, with disrupted collagen fibers and fiber kinks, and notable damage to the interfascicular matrix. Inflammatory markers COX‐2 and IL‐6 were only expressed in the cyclically loaded samples. Collagen degradation markers MMP‐1 and C1,2C were colocalized in many areas, with staining occurring in the interfascicular matrix or the fascicular tenocytes. These markers were present in control samples, but staining became increasingly intense with loading. Little MMP‐3 or MMP‐13 was evident in control sections. In loaded samples, some sections showed intense staining of these markers, again localized to interfascicular regions. This study suggests that inflammatory markers may be expressed rapidly after tendon overload exercise. Interestingly, both inflammation and damage‐induced matrix remodeling seem to be concentrated in, or in the vicinity of, the highly cellular interfascicular matrix. © 2015 The Authors. Journal of Orthopaedic Research Published by Wiley Periodicals, Inc. J Orthop Res 33:889–897, 2015.

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“…Focal histopathological changes have been documented in the region of the overused tendon, including collagen disorganization, increased cellularity, cell rounding and neovascularisation (de Mos et al, 2009). Further it has been shown that expression of both collagen type I, collagen type III, matrix metalloproteinases and other ECM proteins is higher in tendinopathic than in healthy tendon (de Mos et al, 2007, Jones et al, 2006) and that the tissue content of several proteins like versican and aggrecan is upregulated in tendinopathy (Parkinson et al, 2010). Whether or not tendinopathy is associated with inflammatory activity is debated (Millar et al, 2009, Pingel et al, 2013a) and may depend upon the chronicity of the condition.…”

Section: Introductionmentioning

confidence: 99%

3‐D ultrastructure and collagen composition of healthy and overloaded human tendon: evidence of tenocyte and matrix buckling

et al. 2014

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Achilles tendinopathies display focal tissue thickening with pain and ultrasonography changes. Whilst complete rupture might be expected to induce changes in tissue organization and protein composition, little is known about the consequences of non-rupture-associated tendinopathies, especially with regards to changes in the content of collagen type I and III (the major collagens in tendon) and changes in tendon fibroblast (tenocyte) shape and organization of the extracellular matrix. To gain new insights, we took biopsies from the tendinopathic region and flanking healthy region of Achilles tendons of six individuals with clinically diagnosed tendinopathy who had no evidence of cholesterol, uric acid and amyloid accumulation. Biochemical analysis of collagen III/I ratio were performed on all six individuals and electron microscope analysis using transmission electron microscopy and serial block face-scanning electron microscopy were made on two individuals. In the tendinopathic regions, compared to the flanking healthy tissue, we observed 1) an increase in the ratio of collagen III:I proteins, 2) buckling of the collagen fascicles in the extracellular matrix, 3) buckling of tenocytes and their nuclei, and 4) an increase in the ratio small:large diameter collagen fibrils. In summary, load-induced non-rupture tendinopathy in humans is associated with localized biochemical changes, a shift from large to small diameter fibrils, buckling of the tendon extracellular matrix, and buckling of the cells and their nuclei.

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Achilles Tendinosis

Abstract: Although tendon tissue directly adjacent to an Achilles tendinosis lesion looks macroscopically healthy, histological and biochemical degenerative changes in adjacent tissue are evident, which may have implications for surgical interventions.

Cited by 133 publications

References 42 publications

Genetic Variation, Protein Composition and Potential Influences on Tendon Properties in Humans

Genetic Variation, Protein Composition and Potential Influences on Tendon Properties in Humans

Tendon extracellular matrix damage, degradation and inflammation in response to in vitro overload exercise

3‐D ultrastructure and collagen composition of healthy and overloaded human tendon: evidence of tenocyte and matrix buckling

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