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Equine veterinary journal1994; 26(4); 291-296; doi: 10.1111/j.2042-3306.1994.tb04389.x

Differential scanning calorimetric studies of superficial digital flexor tendon degeneration in the horse.

Abstract: Differential scanning calorimetry (DSC) of equine superficial digital flexor tendons revealed the presence of a small exothermic peak at 23 degrees C of unknown origin, and a large endothermic peak at 70 degrees C due to denaturation of cross-linked collagen fibres. In the central degenerated core of damaged tendons the denaturation temperature remained at 70 degrees C but the enthalpy decreased in relation to the extent of degeneration of the tendon. We suggest that this reduction in enthalpy is due to depolymerisation and denaturation of the collagen fibres. This contention is supported by the observed increased activity of the degradative enzyme cathepsin B secreted by the fibroblasts. DSC analysis of cultured porcine tendon fibroblasts revealed a multicomponent endotherm, denaturation beginning at 46 degrees C, a temperature capable of being achieved within the tendon during intensive exercise. DSC clearly has considerable potential in complementing morphological and biochemical studies to determine the aetiology and progress of equine tendon degeneration.
Publication Date: 1994-07-01 PubMed ID: 8575396DOI: 10.1111/j.2042-3306.1994.tb04389.xGoogle Scholar: Lookup
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  • Journal Article

Summary

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The research attempts to study degeneration in a horse’s superficial digital flexor tendon using differential scanning calorimetry (DSC) and examines how the changes observed align with the degeneration process in the structure and function of the tendon, particularly collagen fibers.

Research Methods

  • The researchers employed Differential scanning calorimetry (DSC) as a tool to study the breakdown in the superficial digital flexor tendons in horses. DSC measures the heat flow associated with physical and chemical transitions in material, in this case, the tendon tissue.
  • The degenerated core of damaged tendons was specifically observed under DSC to grasp the extent of damage and understand the denaturation process.

Findings

  • They discovered a small exothermic peak at 23 degrees Celsius of unknown origin and a large endothermic peak at 70 degrees Celsius indicating denaturation of cross-linked collagen fibers.
  • The denaturation temperature remained constant at 70 degrees Celsius even in the damaged core of the tendons, yet the enthalpy (a measure of heat energy) decreased, corresponding to the degree of tendon degradation.
  • The research suggests that the enthalpy reduction is attributable to depolymerisation and denaturation (breaking down) of collagen fibers, the principal structural protein in the tendon.
  • The evidence supporting this claim is the increased activity of the enzyme cathepsin B, a degradative enzyme secreted by fibroblasts, cells that produce collagen and other fibers. This enzyme helps break down proteins and is active when tissue or cells are undergoing stress or death.
  • DSC analyses of cultured porcine (pig) tendon fibroblasts exhibited a multicomponent endotherm (absorption of heat), with denaturation beginning at 46 degrees Celsius, a temperature which the tendons could reach during heavy exercise.

Conclusion

  • This research concludes that DSC can be a significant tool along with morphological and biochemical studies to understand the causes and progress of equine tendon degeneration.

Cite This Article

APA
Miles CA, Wardale RJ, Birch HL, Bailey AJ. (1994). Differential scanning calorimetric studies of superficial digital flexor tendon degeneration in the horse. Equine Vet J, 26(4), 291-296. https://doi.org/10.1111/j.2042-3306.1994.tb04389.x

Publication

ISSN: 0425-1644
NlmUniqueID: 0173320
Country: United States
Language: English
Volume: 26
Issue: 4
Pages: 291-296

Researcher Affiliations

Miles, C A
  • Department of Veterinary Medicine, School of Veterinary Science, University of Bristol, Langford, UK.
Wardale, R J
    Birch, H L
      Bailey, A J

        MeSH Terms

        • Animals
        • Calorimetry, Differential Scanning / methods
        • Calorimetry, Differential Scanning / veterinary
        • Cathepsin B / analysis
        • Cathepsin B / metabolism
        • Cell Line
        • Collagen / analysis
        • Collagen / metabolism
        • Fibroblasts / metabolism
        • Fibroblasts / pathology
        • Fibroblasts / physiology
        • Horse Diseases / metabolism
        • Horse Diseases / pathology
        • Horses / injuries
        • Horses / metabolism
        • Temperature
        • Tendon Injuries / metabolism
        • Tendon Injuries / pathology
        • Tendon Injuries / veterinary
        • Tendons / chemistry
        • Tendons / metabolism
        • Tendons / pathology
        • Water / analysis

        Citations

        This article has been cited 3 times.
        1. Ignatieva NY, Zakharkina OL, Masayshvili CV, Maximov SV, Bagratashvili VN, Lunin VV. The role of laser power and pullback velocity in the endovenous laser ablation efficacy: an experimental study. Lasers Med Sci 2017 Jul;32(5):1105-1110.
          doi: 10.1007/s10103-017-2214-xpubmed: 28466194google scholar: lookup
        2. Giannini S, Buda R, Di Caprio F, Agati P, Bigi A, De Pasquale V, Ruggeri A. Effects of freezing on the biomechanical and structural properties of human posterior tibial tendons. Int Orthop 2008 Apr;32(2):145-51.
          doi: 10.1007/s00264-006-0297-2pubmed: 17216243google scholar: lookup
        3. Knott L, Whitehead CC, Fleming RH, Bailey AJ. Biochemical changes in the collagenous matrix of osteoporotic avian bone. Biochem J 1995 Sep 15;310 ( Pt 3)(Pt 3):1045-51.
          doi: 10.1042/bj3101045pubmed: 7575401google scholar: lookup