Mechanical properties and collagen cross-linking of the patellar tendon in old and young men.
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.
Couppé
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Institute of Sports Medicine, Bispebjerg Hospital and Center for Healthy Aging, Faculty of Health Sciences, University of Copenhagen, 2400 Copenhagen NV, Denmark.
Hansen
P
P
Kongsgaard
M
M
Kovanen
V
V
Suetta
C
C
Aagaard
P
P
Kjaer
M
M
Magnusson
S P
SP
D000328:Adult; D000368:Aged; D000375:Aging / Q000502:physiology*; D000596:Amino Acids / Q000737:chemistry; D001120:Arginine / Q000031:analogs & derivatives / Q000378:metabolism; D001132:Arm / Q000502:physiology; D001696:Biomechanical Phenomena; D001706:Biopsy; D003094:Collagen / Q000737:chemistry* / Q000502:physiology*; D017127:Glycation End Products, Advanced / Q000378:metabolism; D006801:Humans; D006909:Hydroxyproline / Q000378:metabolism; D007717:Knee / Q000502:physiology; D008239:Lysine / Q000031:analogs & derivatives / Q000378:metabolism; D008297:Male; D009068:Movement / Q000502:physiology; D018482:Muscle, Skeletal / Q000033:anatomy & histology / Q000737:chemistry / Q000378:metabolism; D017847:Patellar Ligament / Q000033:anatomy & histology / Q000737:chemistry* / Q000502:physiology*; D008249:Protein-Lysine 6-Oxidase / Q000378:metabolism
D000596:Amino Acids; D017127:Glycation End Products, Advanced; C015484:pyridinoline; D003094:Collagen; D001120:Arginine; C062187:pentosidine; D008249:Protein-Lysine 6-Oxidase; D008239:Lysine; D006909:Hydroxyproline