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Connective tissue research1997; 36(3); 253-260; doi: 10.3109/03008209709160225

An age-related study of morphology and cross-link composition of collagen fibrils in the digital flexor tendons of young thoroughbred horses.

Abstract: The superficial digital flexor tendon is the most commonly injured tendon in the racing Thoroughbred. Despite the clinical significance of this structure, only limited data exist regarding normal age-related morphology of the tensile units, the collagen fibrils. The age at which these collagen fibrils become mature in composition and structure may be of importance. Consequently, the association of age and collagen fibril crosslink composition, diameter distribution and crimp morphology in the superficial and deep digital flexor tendons of Thoroughbreds up to and including three years of age has been studied. Replacement of immature crosslinks, peaking of the collagen fibril mass-average diameter and collagen fibril index, and stabilization of collagen crimp morphology changes supported the hypothesis that both digital flexor tendons become mature in structure by two years of age.
Publication Date: 1997-01-01 PubMed ID: 9512893DOI: 10.3109/03008209709160225Google Scholar: Lookup
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  • Journal Article

Summary

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The research article discusses how the structure and composition of collagen fibrils, which are parts of the superficial digital flexor tendons in young thoroughbred horses, mature by the age of two.

Objective and Importance of the Study

  • The study aims to understand the age-based changes in normal morphology of collagen fibrils, the tensile units in the superficial digital flexor tendon of racing Thoroughbred, which is a frequently injured tendon.
  • Understanding the age at which these fibrils mature in both structure and composition is crucial, hence the research gauges the association of age with the collagen fibril crosslink composition, diameter distribution, and crimp morphology in superficial and deep digital flexor tendons of Thoroughbreds up to the age of three.

Methodology and Findings

  • The study investigates the tendons at different ages, observing the replacement of immature crosslinks, evaluation of the collagen fibril mass-average diameter, and changes in the collagen fibril index.
  • The research also tracks progress in stabilization of collagen crimp morphology changes.
  • The findings support the initial hypothesis that the structure of both digital flexor tendons in Thoroughbreds becomes mature by the age of two.

Implications of the Research

  • The outcomes of the study offer significant insights that can be crucial for preventing injuries and for the treatment of tendon-related health issues in Thoroughbred horses, especially those involved in racing.
  • Knowing that the tendon matures by two years of age, precautions or treatments can be specifically tailored for horses of this age to avert likely injuries.
  • Moreover, the study contributes to the broader understanding of animal physiology, specifically equine tendon maturation.

Cite This Article

APA
Patterson-Kane JC, Parry DA, Birch HL, Goodship AE, Firth EC. (1997). An age-related study of morphology and cross-link composition of collagen fibrils in the digital flexor tendons of young thoroughbred horses. Connect Tissue Res, 36(3), 253-260. https://doi.org/10.3109/03008209709160225

Publication

ISSN: 0300-8207
NlmUniqueID: 0365263
Country: England
Language: English
Volume: 36
Issue: 3
Pages: 253-260

Researcher Affiliations

Patterson-Kane, J C
  • Department of Veterinary Clinical Sciences, Massey University Palmerston North, New Zealand.
Parry, D A
    Birch, H L
      Goodship, A E
        Firth, E C

          MeSH Terms

          • Aging / metabolism
          • Animals
          • Collagen / chemistry
          • Collagen / metabolism
          • Collagen / ultrastructure
          • Cross-Linking Reagents
          • Horses
          • Image Enhancement
          • Microscopy, Electron
          • Microscopy, Polarization / methods
          • Tendons / chemistry
          • Tendons / metabolism
          • Tendons / ultrastructure

          Citations

          This article has been cited 18 times.
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