Murine tendon function is adversely affected by aggrecan accumulation due to the knockout of ADAMTS5

Wang, Vincent; Bell, Rick; Thakore, Ruchir; Eyre, David R.; Galante, Jorge O.; Li, Jun; Sandy, John D.; Plaas, Anna

doi:10.1002/jor.21558

Cited by 51 publications

(61 citation statements)

References 26 publications

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“…The proteolytic processing of proteoglycans in tendons is evidently a normal process in healthy tendon,31 32 and recent evidence from ADAMTS-5−/− mice indicates that ADAMTS-5 aggrecanase activity is required for the maintenance of normal tendon structure and some biomechanical properties 33. Both the FDLT and Achilles tendons in the ADAMTS-5−/− mice showed increased aggrecan deposition, but the biomechanical changes observed differed between the two tendons 33…”

Section: Discussionmentioning

confidence: 99%

Changes in matrix protein biochemistry and the expression of mRNA encoding matrix proteins and metalloproteinases in posterior tibialis tendinopathy

et al. 2012

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ObjectivesAdult-acquired flat foot secondary to a dysfunctional posterior tibialis tendon (PTT) is often treated by surgical transfer of the flexor digitorum longus tendon (FDLT). In this study, the authors compared normal PTT, stage II dysfunctional PTT and replacement FDLT, aiming to define changes in collagen modification, glycosaminoglycan (GAG) and the expression of matrix and metalloproteinase mRNA.MethodsNormal PTTs were obtained from patients with no history of tendon problems. Samples of dysfunctional PTT and replacement FDLT tissue were obtained from patients undergoing surgical reconstruction. Tissue samples were analysed for total collagen and GAG, pentosidine and collagen cross-links. Total RNA was assayed for mRNA encoding matrix proteins and metalloproteinases, using real-time reverse transcription PCR. Differences between clinical groups were assessed using non-parametric statistics.ResultsDysfunctional PTT contained higher levels of GAG and lower levels of pentosidine than normal PTT or FDLT. In contrast, collagen in FDLT contained fewer ketoimine and more aldimine cross-links than either normal or dysfunctional PTT. mRNA encoding types I and III collagens, aggrecan, biglycan, matrix metalloproteinase (MMP)-2, -13 and -23, and a disintegrin and metalloproteinase (ADAM)-12L each showed increased levels in dysfunctional PTT compared with either normal PTT or (except MMP-13) FDLT. In contrast, MMP-3 and ADAM with thrombospondin domain (ADAMTS)-5 mRNA were lower in both dysfunctional PTT and FDLT than in normal PTT, while ADAMTS-1 mRNA was lower in dysfunctional PTT than in FDLT.ConclusionsStage II dysfunctional PTT shows biochemical and molecular changes consistent with a chronic remodelling of the extracellular matrix, rather than rupture, while the replacement FDLT resembles normal PTT in many, but not all, parameters.

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Section: Discussionmentioning

confidence: 99%

Changes in matrix protein biochemistry and the expression of mRNA encoding matrix proteins and metalloproteinases in posterior tibialis tendinopathy

et al. 2012

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“…The large aggregating proteoglycans such as versican and aggrecan are particularly prominent in the pericellular regions 25 , but also in compressive regions of tendon, for example where tendons wrap around joints 26 . Their role, increasing water content in these regions, provides resistance to compression 27 .…”

Section: Tendon Compositionmentioning

confidence: 99%

Tendon Functional Extracellular Matrix

Screen

Berk²,

Kadler

et al. 2015

Journal Orthopaedic Research

192

157

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This article is one of a series, summarising views expressed at the Orthopaedic Research Society New Frontiers in Tendon Research Conference. This particular article reviews the three workshops held under the “Functional Extracellular Matrix” stream. The workshops focused on the roles of the tendon extracellular matrix, such as performing the mechanical functions of tendon, creating the local cell environment and providing cellular cues. Tendon is a complex network of matrix and cells, and its biological functions are influenced by widely-varying extrinsic and intrinsic factors such as age, nutrition, exercise levels and biomechanics. Consequently, tendon adapts dynamically during development, ageing and injury. The workshop discussions identified research directions associated with understanding cell-matrix interactions to be of prime importance for developing novel strategies to target tendon healing or repair.

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“…decorin, fibromodulin, biglycan, lumican, aggrecan) in relatively small quantities, with types and amounts varying according to different species, ages and anatomical locations [11,[19][20][21]. In tendon, PGs have been found to play an important role in facilitating fibrillogenesis, regulating extracellular matrix assembly and modulating cellmatrix interaction [20,[22][23][24]. Properties of, and interactions between, structural components at different length scales of the hierarchical tendon organization are significant for providing adequate mechanical function in a variety of in vivo loading environments.…”

Section: Overview Of Tendon Structure and Compositionmentioning

confidence: 99%

Modelling approaches for evaluating multiscale tendon mechanics

Fang

Lake

2016

Interface Focus.

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Tendon exhibits anisotropic, inhomogeneous and viscoelastic mechanical properties that are determined by its complicated hierarchical structure and varying amounts/organization of different tissue constituents. Although extensive research has been conducted to use modelling approaches to interpret tendon structure–function relationships in combination with experimental data, many issues remain unclear (i.e. the role of minor components such as decorin, aggrecan and elastin), and the integration of mechanical analysis across different length scales has not been well applied to explore stress or strain transfer from macro- to microscale. This review outlines mathematical and computational models that have been used to understand tendon mechanics at different scales of the hierarchical organization. Model representations at the molecular, fibril and tissue levels are discussed, including formulations that follow phenomenological and microstructural approaches (which include evaluations of crimp, helical structure and the interaction between collagen fibrils and proteoglycans). Multiscale modelling approaches incorporating tendon features are suggested to be an advantageous methodology to understand further the physiological mechanical response of tendon and corresponding adaptation of properties owing to unique in vivo loading environments.

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Murine tendon function is adversely affected by aggrecan accumulation due to the knockout of ADAMTS5

Cited by 51 publications

References 26 publications

Changes in matrix protein biochemistry and the expression of mRNA encoding matrix proteins and metalloproteinases in posterior tibialis tendinopathy

Changes in matrix protein biochemistry and the expression of mRNA encoding matrix proteins and metalloproteinases in posterior tibialis tendinopathy

Tendon Functional Extracellular Matrix

Modelling approaches for evaluating multiscale tendon mechanics

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