3-D ultrastructure and collagen composition of healthy and overloaded human tendon: evidence of tenocyte and matrix buckling
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3-D ultrastructure and collagen composition of healthy and overloaded human tendon : evidence of tenocyte and matrix buckling. / Pingel, Jessica; Lu, Yinhui; Starborg, Tobias; Fredberg, Ulrich; Langberg, Henning; Nedergaard, Anders; Weis, Maryann; Eyre, David; Kjær, Michael; Kadler, Karl E.
I: Journal of Anatomy, Bind 224, Nr. 5, 09.02.2014, s. 548–555.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
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TY - JOUR
T1 - 3-D ultrastructure and collagen composition of healthy and overloaded human tendon
T2 - evidence of tenocyte and matrix buckling
AU - Pingel, Jessica
AU - Lu, Yinhui
AU - Starborg, Tobias
AU - Fredberg, Ulrich
AU - Langberg, Henning
AU - Nedergaard, Anders
AU - Weis, Maryann
AU - Eyre, David
AU - Kjær, Michael
AU - Kadler, Karl E
N1 - CURIS 2014 NEXS 402
PY - 2014/2/9
Y1 - 2014/2/9
N2 - 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 (ECM). 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 analyses 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 with the flanking healthy tissue, we observed: (i) an increase in the ratio of collagen III : I proteins; (ii) buckling of the collagen fascicles in the ECM; (iii) buckling of tenocytes and their nuclei; and (iv) an increase in the ratio of small-diameter : 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 ECM, and buckling of the cells and their nuclei.
AB - 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 (ECM). 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 analyses 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 with the flanking healthy tissue, we observed: (i) an increase in the ratio of collagen III : I proteins; (ii) buckling of the collagen fascicles in the ECM; (iii) buckling of tenocytes and their nuclei; and (iv) an increase in the ratio of small-diameter : 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 ECM, and buckling of the cells and their nuclei.
U2 - 10.1111/joa.12164
DO - 10.1111/joa.12164
M3 - Journal article
C2 - 24571576
VL - 224
SP - 548
EP - 555
JO - Journal of Anatomy
JF - Journal of Anatomy
SN - 0021-8782
IS - 5
ER -
ID: 101430712