Age-Related Changes in the Pyridinoline Content of Guinea Pigs Cartilage and Achilles Tendon Collagen.

Regular sport practice could prevent age-related changes in tendinous tissues. The purpose of the study was to investigate the effect of regular badminton practice on patellar and Achilles tendon mechanical properties in senior competitive badminton players (>35 years old) and to compare the results with physically active people matched by age. One hundred ninety-two badminton players and 193 physically active people were divided by age into four groups, between 35 and 44 (U45), between 45 and 54 (U55), between 55 and 64 (U65), and over 65 (O65) years old. A LogiqS8 transducer in elastography mode and a MyotonPRO myotonometer were used to assess patellar and Achilles mechanical properties. Achilles tendon stiffness was higher in the control group than the badminton players for the U45, U55, and O65 age groups (p < .01). Also, the elastography index was higher in the control group than the badminton players for the U45, U55, U65, and O65 age groups (p < .05). In conclusion, regular badminton practice could prevent the decline in mechanical properties of the patellar and Achilles tendons.

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AGE RELATED CHANGES IN ULTRASTRUCTURE AND BIOMECHANICAL PROPERTIES OF SLOW AND FAST MUSCLE TENDON IN RABBIT ACHILLES TENDON

Medicine & Science in Sports & Exercise ◽

10.1249/00005768-199505001-01240 ◽

1995 ◽

Vol 27 (Supplement) ◽

pp. S221

Author(s):

Y. Nakagawa ◽

N. Yamamoto ◽

K. Hayashi ◽

K. Nagashima

Keyword(s):

Achilles Tendon ◽

Biomechanical Properties ◽

Fast Muscle ◽

Age Related ◽

Age Related Changes

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The Effect of L-Ascorbic Acid on Age-Related Changes of Pyridinoline in Cartilage Collagen of Guinea Pigs.

Journal of Nutritional Science and Vitaminology ◽

10.3177/jnsv.44.217 ◽

1998 ◽

Vol 44 (2) ◽

pp. 217-224 ◽

Cited By ~ 4

Author(s):

Mihyan KIM ◽

Megumi OTSUKA ◽

Eriko SHIMAMURA ◽

Nobuhiko ARAKAWA

Keyword(s):

Ascorbic Acid ◽

Guinea Pigs ◽

Age Related ◽

Age Related Changes

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Age-related changes in the physical properties, cross-linking, and glycation of collagen from mouse tail tendon

Journal of Biological Chemistry ◽

10.1074/jbc.ra119.011031 ◽

2020 ◽

Vol 295 (31) ◽

pp. 10562-10571 ◽

Cited By ~ 4

Author(s):

Melanie Stammers ◽

Irina M. Ivanova ◽

Izabella S. Niewczas ◽

Anne Segonds-Pichon ◽

Matthew Streeter ◽

...

Keyword(s):

The Other ◽

Cross Linking ◽

Structural Protein ◽

Cross Link ◽

Age Related ◽

Cross Links ◽

Tail Tendon ◽

Collagen Cross Linking ◽

Age Related Changes ◽

Tendon Collagen

Collagen is a structural protein whose internal cross-linking critically determines the properties and functions of connective tissue. Knowing how the cross-linking of collagen changes with age is key to understanding why the mechanical properties of tissues change over a lifetime. The current scientific consensus is that collagen cross-linking increases with age and that this increase leads to tendon stiffening. Here, we show that this view should be reconsidered. Using MS-based analyses, we demonstrated that during aging of healthy C57BL/6 mice, the overall levels of collagen cross-linking in tail tendon decreased with age. However, the levels of lysine glycation in collagen, which is not considered a cross-link, increased dramatically with age. We found that in 16-week-old diabetic db/db mice, glycation reaches levels similar to those observed in 98-week-old C57BL/6 mice, while the other cross-links typical of tendon collagen either decreased or remained the same as those observed in 20-week-old WT mice. These results, combined with findings from mechanical testing of tendons from these mice, indicate that overall collagen cross-linking in mouse tendon decreases with age. Our findings also reveal that lysine glycation appears to be an important factor that contributes to tendon stiffening with age and in diabetes.

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