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Bispebjerg Hospital - en del af Københavns Universitetshospital
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Evidence of structurally continuous collagen fibrils in tendons

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

Dokumenter

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  1. Effects of maturation and advanced glycation on tensile mechanics of collagen fibrils from rat tail and Achilles tendons

    Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

  1. Mechanical properties of human patellar tendon collagen fibrils. An exploratory study of aging and sex

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  2. Different training responses in elderly men and women following a prolonged muscle resistance training intervention

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  3. Mechanical properties and UTE-T2* in Patellar tendinopathy: The effect of load magnitude in exercise-based treatment

    Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

  4. Altered Triceps Surae Muscle-Tendon Unit Properties after 6 Months of Static Stretching

    Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

Vis graf over relationer

Tendons transmit muscle-generated force through an extracellular matrix of aligned collagen fibrils. The force applied by the muscle at one end of a microscopic fibril has to be transmitted through the macroscopic length of the tendon by mechanisms that are poorly understood. A key element in this structure-function relationship is the collagen fibril length. During embryogenesis short fibrils are produced but they grow rapidly with maturation. There is some controversy regarding fibril length in adult tendon, with mechanical data generally supporting discontinuity while structural investigations favor continuity. This study initially set out to trace the full length of individual fibrils in adult human tendons, using serial block face-scanning electron microscopy. But even with this advanced technique the required length could not be covered. Instead a statistical approach was used on a large volume of fibrils in shorter image stacks. Only a single end was observed after tracking 67.5mm of combined fibril lengths, in support of fibril continuity. To shed more light on this observation, the full length of a short tendon (mouse stapedius, 125μm) was investigated and continuity of individual fibrils was confirmed. In light of these results, possible mechanisms that could reconcile the opposing findings on fibril continuity are discussed.

STATEMENT OF SIGNIFICANCE: Connective tissues hold all parts of the body together and are mostly constructed from thin threads of the protein collagen (called fibrils). Connective tissues provide mechanical strength and one of the most demanding tissues in this regard are tendons, which transmit the forces generated by muscles. The length of the collagen fibrils is essential to the mechanical strength and to the type of damage the tissue may experience (slippage of short fibrils or breakage of longer ones). This in turn is important for understanding the repair processes after such damage occurs. Currently the issue of fibril length is contentious, but this study provides evidence that the fibrils are extremely long and likely continuous.

OriginalsprogEngelsk
TidsskriftActa Biomaterialia
Vol/bind50
Sider (fra-til)293-301
Antal sider9
ISSN1742-7061
DOI
StatusUdgivet - 1 mar. 2017

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