Mechanical properties and collagen cross-linking of the patellar tendon in old and young men

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Mechanical properties and collagen cross-linking of the patellar tendon in old and young men. / Couppé, C; Hansen, P; Kongsgaard, M; Kovanen, V; Suetta, C; Aagaard, P; Kjaer, M; Magnusson, S P.

In: Journal of Applied Physiology, Vol. 107, No. 3, 2009, p. 880-6.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Couppé, C, Hansen, P, Kongsgaard, M, Kovanen, V, Suetta, C, Aagaard, P, Kjaer, M & Magnusson, SP 2009, 'Mechanical properties and collagen cross-linking of the patellar tendon in old and young men', Journal of Applied Physiology, vol. 107, no. 3, pp. 880-6. https://doi.org/10.1152/japplphysiol.00291.2009

APA

Couppé, C., Hansen, P., Kongsgaard, M., Kovanen, V., Suetta, C., Aagaard, P., Kjaer, M., & Magnusson, S. P. (2009). Mechanical properties and collagen cross-linking of the patellar tendon in old and young men. Journal of Applied Physiology, 107(3), 880-6. https://doi.org/10.1152/japplphysiol.00291.2009

Vancouver

Couppé C, Hansen P, Kongsgaard M, Kovanen V, Suetta C, Aagaard P et al. Mechanical properties and collagen cross-linking of the patellar tendon in old and young men. Journal of Applied Physiology. 2009;107(3):880-6. https://doi.org/10.1152/japplphysiol.00291.2009

Author

Couppé, C ; Hansen, P ; Kongsgaard, M ; Kovanen, V ; Suetta, C ; Aagaard, P ; Kjaer, M ; Magnusson, S P. / Mechanical properties and collagen cross-linking of the patellar tendon in old and young men. In: Journal of Applied Physiology. 2009 ; Vol. 107, No. 3. pp. 880-6.

Bibtex

@article{af1863a0367c11df8ed1000ea68e967b,
title = "Mechanical properties and collagen cross-linking of the patellar tendon in old and young men",
abstract = "Age-related loss in muscle mass and strength impairs daily life function in the elderly. However, it remains unknown whether tendon properties also deteriorate with age. Cross-linking of collagen molecules provides structural integrity to the tendon fibrils and has been shown to change with age in animals but has never been examined in humans in vivo. In this study, we examined the mechanical properties and pyridinoline and pentosidine cross-link and collagen concentrations of the patellar tendon in vivo in old (OM) and young men (YM). Seven OM (67 +/- 3 years, 86 +/- 10 kg) and 10 YM (27 +/- 2 years, 81 +/- 8 kg) with a similar physical activity level (OM 5 +/- 6 h/wk, YM 5 +/- 2 h/wk) were examined. MRI was used to assess whole tendon dimensions. Tendon mechanical properties were assessed with the use of simultaneous force and ultrasonographic measurements during ramped isometric contractions. Percutaneous tendon biopsies were taken and analyzed for hydroxylysyl pyridinoline (HP), lysyl pyridinoline (LP), pentosidine, and collagen concentrations. We found no significant differences in the dimensions or mechanical properties of the tendon between OM and YM. Collagen concentrations were lower in OM than in YM (0.49 +/- 0.27 vs. 0.73 +/- 0.14 mg/mg dry wt; P < 0.05). HP concentrations were higher in OM than in YM (898 +/- 172 vs. 645 +/- 183 mmol/mol; P < 0.05). LP concentrations were higher in OM than in YM (49 +/- 38 vs. 16 +/- 8 mmol/mol; P < 0.01), and pentosidine concentrations were higher in OM than in YM (73 +/- 13 vs. 11 +/- 2 mmol/mol; P < 0.01). These cross-sectional data raise the possibility that age may not appreciably influence the dimensions or mechanical properties of the human patellar tendon in vivo. Collagen concentration was reduced, whereas both enzymatic and nonenzymatic cross-linking of concentration was elevated in OM vs. in YM, which may be a mechanism to maintain the mechanical properties of tendon with aging.",
author = "C Coupp{\'e} and P Hansen and M Kongsgaard and V Kovanen and C Suetta and P Aagaard and M Kjaer and Magnusson, {S P}",
note = "Keywords: Adult; Aged; Aging; Amino Acids; Arginine; Arm; Biomechanics; Biopsy; Collagen; Glycosylation End Products, Advanced; Humans; Hydroxyproline; Knee; Lysine; Male; Movement; Muscle, Skeletal; Patellar Ligament; Protein-Lysine 6-Oxidase",
year = "2009",
doi = "10.1152/japplphysiol.00291.2009",
language = "English",
volume = "107",
pages = "880--6",
journal = "Journal of Applied Physiology",
issn = "8750-7587",
publisher = "American Physiological Society",
number = "3",

}

RIS

TY - JOUR

T1 - Mechanical properties and collagen cross-linking of the patellar tendon in old and young men

AU - Couppé, C

AU - Hansen, P

AU - Kongsgaard, M

AU - Kovanen, V

AU - Suetta, C

AU - Aagaard, P

AU - Kjaer, M

AU - Magnusson, S P

N1 - Keywords: Adult; Aged; Aging; Amino Acids; Arginine; Arm; Biomechanics; Biopsy; Collagen; Glycosylation End Products, Advanced; Humans; Hydroxyproline; Knee; Lysine; Male; Movement; Muscle, Skeletal; Patellar Ligament; Protein-Lysine 6-Oxidase

PY - 2009

Y1 - 2009

N2 - Age-related loss in muscle mass and strength impairs daily life function in the elderly. However, it remains unknown whether tendon properties also deteriorate with age. Cross-linking of collagen molecules provides structural integrity to the tendon fibrils and has been shown to change with age in animals but has never been examined in humans in vivo. In this study, we examined the mechanical properties and pyridinoline and pentosidine cross-link and collagen concentrations of the patellar tendon in vivo in old (OM) and young men (YM). Seven OM (67 +/- 3 years, 86 +/- 10 kg) and 10 YM (27 +/- 2 years, 81 +/- 8 kg) with a similar physical activity level (OM 5 +/- 6 h/wk, YM 5 +/- 2 h/wk) were examined. MRI was used to assess whole tendon dimensions. Tendon mechanical properties were assessed with the use of simultaneous force and ultrasonographic measurements during ramped isometric contractions. Percutaneous tendon biopsies were taken and analyzed for hydroxylysyl pyridinoline (HP), lysyl pyridinoline (LP), pentosidine, and collagen concentrations. We found no significant differences in the dimensions or mechanical properties of the tendon between OM and YM. Collagen concentrations were lower in OM than in YM (0.49 +/- 0.27 vs. 0.73 +/- 0.14 mg/mg dry wt; P < 0.05). HP concentrations were higher in OM than in YM (898 +/- 172 vs. 645 +/- 183 mmol/mol; P < 0.05). LP concentrations were higher in OM than in YM (49 +/- 38 vs. 16 +/- 8 mmol/mol; P < 0.01), and pentosidine concentrations were higher in OM than in YM (73 +/- 13 vs. 11 +/- 2 mmol/mol; P < 0.01). These cross-sectional data raise the possibility that age may not appreciably influence the dimensions or mechanical properties of the human patellar tendon in vivo. Collagen concentration was reduced, whereas both enzymatic and nonenzymatic cross-linking of concentration was elevated in OM vs. in YM, which may be a mechanism to maintain the mechanical properties of tendon with aging.

AB - Age-related loss in muscle mass and strength impairs daily life function in the elderly. However, it remains unknown whether tendon properties also deteriorate with age. Cross-linking of collagen molecules provides structural integrity to the tendon fibrils and has been shown to change with age in animals but has never been examined in humans in vivo. In this study, we examined the mechanical properties and pyridinoline and pentosidine cross-link and collagen concentrations of the patellar tendon in vivo in old (OM) and young men (YM). Seven OM (67 +/- 3 years, 86 +/- 10 kg) and 10 YM (27 +/- 2 years, 81 +/- 8 kg) with a similar physical activity level (OM 5 +/- 6 h/wk, YM 5 +/- 2 h/wk) were examined. MRI was used to assess whole tendon dimensions. Tendon mechanical properties were assessed with the use of simultaneous force and ultrasonographic measurements during ramped isometric contractions. Percutaneous tendon biopsies were taken and analyzed for hydroxylysyl pyridinoline (HP), lysyl pyridinoline (LP), pentosidine, and collagen concentrations. We found no significant differences in the dimensions or mechanical properties of the tendon between OM and YM. Collagen concentrations were lower in OM than in YM (0.49 +/- 0.27 vs. 0.73 +/- 0.14 mg/mg dry wt; P < 0.05). HP concentrations were higher in OM than in YM (898 +/- 172 vs. 645 +/- 183 mmol/mol; P < 0.05). LP concentrations were higher in OM than in YM (49 +/- 38 vs. 16 +/- 8 mmol/mol; P < 0.01), and pentosidine concentrations were higher in OM than in YM (73 +/- 13 vs. 11 +/- 2 mmol/mol; P < 0.01). These cross-sectional data raise the possibility that age may not appreciably influence the dimensions or mechanical properties of the human patellar tendon in vivo. Collagen concentration was reduced, whereas both enzymatic and nonenzymatic cross-linking of concentration was elevated in OM vs. in YM, which may be a mechanism to maintain the mechanical properties of tendon with aging.

U2 - 10.1152/japplphysiol.00291.2009

DO - 10.1152/japplphysiol.00291.2009

M3 - Journal article

C2 - 19556458

VL - 107

SP - 880

EP - 886

JO - Journal of Applied Physiology

JF - Journal of Applied Physiology

SN - 8750-7587

IS - 3

ER -

ID: 18788573