Morphological and histochemical analysis of a case of superficial digital flexor tendon injury in the horse.
- Comparative Study
- Journal Article
- Research Support
- Non-U.S. Gov't
Summary
This study investigates the changes in the structure and specific biochemical components of a horse’s superficial digital flexor tendon following injury. The research revealed significantly altered collagen structure and concentrations of glycosaminoglycans (GAGs) in the injured tendon compared to a normal one, suggesting the body’s attempt to heal the damage.
Morphological and Histochemical Analysis
The study dissected the superficial digital flexor tendon (SDFT) of an injured 6-year-old male Thoroughbred horse. The researchers observed:
- An abundance of new granulation tissue, angiogenesis (formation of new blood vessels), minor infiltration by white blood cells, and evidence of bleeding.
- Increased activity in tenocytes, the cells responsible for collagen production in tendons.
- A looser and more disorderly arrangement of collagen fibers in the injured tendon compared to a normal one, suggesting a change in the tendon’s structural organization due to injury.
- A narrower range in the diameter of collagen fibrils in the injured tendon, possibly indicating a disruption in collagen production or assembly.
Glycosaminoglycan Content
Glycosaminoglycans (GAGs) such as hyaluronic acid (HA), dermatan sulphate (DS), and chondroitin sulphate (CS) are critical components of the extracellular matrix in tendons, contributing to their strength and flexibility. The researchers found:
- Similar main composition of GAGs in both the injured and normal tendon, including HA, DS, and CS.
- A notable increase in DS levels in the injured tendon, suggesting this component may be involved in the tendon’s attempt to recover.
- Changes in HA and CS content, with a decrease noted in the injured tendon. The researchers hypothesize this could have stimulated the production of new collagen fibers, a process known as fibrillogenesis.
Conclusions
The study concludes that injury to the SDFT changes its collagen structure and GAG content, reflecting the body’s efforts to repair the damage. The observed disruption in the tendon’s structure and biochemical composition indicate abnormal fibrillogenesis in response to the injury. The researchers suggest that modulating the inflammatory response to tendon injury could potentially help it regain its normal structure over time. They highlight the need for further research to validate this hypothesis and develop therapeutic interventions.
Cite This Article
Publication
Researcher Affiliations
- Department of Veterinary Anatomy, School of Veterinary Medicine, Rakuno Gakuen University, 582 Bunkyodai-Midorimachi, Ebetsu, Hokkaido, 069-0851, Japan.
MeSH Terms
- Animals
- Collagen / chemistry
- Collagen / ultrastructure
- Glycosaminoglycans / analysis
- Horses
- Male
- Microscopy, Electron
- Microscopy, Electron, Scanning
- Tendon Injuries / pathology
- Tendon Injuries / veterinary
- Tendons / pathology
- Tendons / ultrastructure
Citations
This article has been cited 3 times.- Peffers MJ, Thorpe CT, Collins JA, Eong R, Wei TK, Screen HR, Clegg PD. Proteomic analysis reveals age-related changes in tendon matrix composition, with age- and injury-specific matrix fragmentation. J Biol Chem 2014 Sep 12;289(37):25867-78.
- Williams RM, Zipfel WR, Webb WW. Interpreting second-harmonic generation images of collagen I fibrils. Biophys J 2005 Feb;88(2):1377-86.
- Hosoyamada Y, Kurihara H, Sakai T. Ultrastructural localisation and size distribution of collagen fibrils in Glisson's sheath of rat liver: implications for mechanical environment and possible producing cells. J Anat 2000 Apr;196 ( Pt 3)(Pt 3):327-40.
