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.

In: Journal of Anatomy, Vol. 224, No. 5, 09.02.2014, p. 548–555.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Pingel, J, Lu, Y, Starborg, T, Fredberg, U, Langberg, H, Nedergaard, A, Weis, M, Eyre, D, Kjær, M & Kadler, KE 2014, '3-D ultrastructure and collagen composition of healthy and overloaded human tendon: evidence of tenocyte and matrix buckling', Journal of Anatomy, vol. 224, no. 5, pp. 548–555. https://doi.org/10.1111/joa.12164

APA

Pingel, J., Lu, Y., Starborg, T., Fredberg, U., Langberg, H., Nedergaard, A., ... Kadler, K. E. (2014). 3-D ultrastructure and collagen composition of healthy and overloaded human tendon: evidence of tenocyte and matrix buckling. Journal of Anatomy, 224(5), 548–555. https://doi.org/10.1111/joa.12164

Vancouver

Pingel J, Lu Y, Starborg T, Fredberg U, Langberg H, Nedergaard A et al. 3-D ultrastructure and collagen composition of healthy and overloaded human tendon: evidence of tenocyte and matrix buckling. Journal of Anatomy. 2014 Feb 9;224(5):548–555. https://doi.org/10.1111/joa.12164

Author

Pingel, Jessica ; Lu, Yinhui ; Starborg, Tobias ; Fredberg, Ulrich ; Langberg, Henning ; Nedergaard, Anders ; Weis, Maryann ; Eyre, David ; Kjær, Michael ; Kadler, Karl E. / 3-D ultrastructure and collagen composition of healthy and overloaded human tendon : evidence of tenocyte and matrix buckling. In: Journal of Anatomy. 2014 ; Vol. 224, No. 5. pp. 548–555.

Bibtex

@article{4d7d8c2bc704488f93cf0ef253ea6f93,
title = "3-D ultrastructure and collagen composition of healthy and overloaded human tendon: evidence of tenocyte and matrix buckling",
abstract = "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.",
author = "Jessica Pingel and Yinhui Lu and Tobias Starborg and Ulrich Fredberg and Henning Langberg and Anders Nedergaard and Maryann Weis and David Eyre and Michael Kj{\ae}r and Kadler, {Karl E}",
note = "CURIS 2014 NEXS 402",
year = "2014",
month = "2",
day = "9",
doi = "10.1111/joa.12164",
language = "English",
volume = "224",
pages = "548–555",
journal = "Journal of Anatomy",
issn = "0021-8782",
publisher = "Wiley-Blackwell",
number = "5",

}

RIS

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