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Exercise modifies the age-related change in crimp pattern in the core region of the equine superficial digital flexor tendon.

作者信息

Patterson-Kane J C, Parry D A, Goodship A E, Firth E C

机构信息

Department of Veterinary Clinical Sciences, Massey University, Palmerston North, New Zealand.

出版信息

N Z Vet J. 1997 Aug;45(4):135-9. doi: 10.1080/00480169.1997.36013.

DOI:10.1080/00480169.1997.36013
PMID:16031973
Abstract

One of the current concepts with regard to equine superficial digital flexor tendonitis is that cumulative subclinical microscopic damage weakens the structure, predisposing the tendon to partial or complete rupture. This microtrauma is likely to affect the waveform or crimp of the collagen fibrils, which are the units of tensile strength. Collagen fibril crimp morphology characteristics were determined in superficial digital flexor tendons of 18 horses presented for necropsy. Horses were separated into exercised (n = 9) and non-exercised groups (n = 9), based on recent function. Five of the eight exercised horses below the age of 10 years showed a significantly lower crimp angle in the central region of the tendon in comparison with the periphery. Three of those five animals also showed a significantly lower crimp period length in the centre. No non-exercised horses in this age group showed such regional differences. Horses classified as non-exercised may have Horses classified as non-exercised may have undergone competitive galloping activity at an earlier age, implying that changes in central region crimp morphology did not occur at that time, or had reverted to normal values in the intervening period. A lower crimp angle in the core region in comparison with the periphery is abnormal in animals younger than 10 years, on the basis of previous data obtained from wild horses. It is hypothesised that imposed exercise regimens involving galloping modify the normal age-related reduction of crimp angle in the tendon core, probably as a result of the increased number of rapid high-strain cycles experienced by the collagen fibrils.

摘要

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