Characterization of collagen fibrils after equine suspensory ligament injury: an ultrastructural and biochemical approach.
Abstract: Suspensory ligament (SL) injuries are an important cause of lameness in horses. The mechanical properties of connective tissue in normal and pathological ligaments are mainly related to fibril morphology, as well as collagen content and types. The purpose of this study was to evaluate, using biochemical and ultrastructural approaches, the alterations in collagen fibrils after injury. Eight Warmblood horses with visible signs of injury in only one forelimb SL were selected and specimens were examined by transmission electron microscope (TEM). Collagen types I, III and V were purified by differential salt precipitation after collagen extraction with acetic acid containing pepsin. TEM revealed abnormal organization as well as alterations in the diameter and shape of fibrils after SL injury. The bands corresponding to types I, III and V collagen were assessed by densitometry after sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). Densitometric analysis indicated that the proportions of type III and type V collagen were higher (P < 0.001) in damaged tissues compared with normal tissues with a mean increase of 20.9% and 17.3%, respectively. Concurrently, a decrease (P < 0.001) in type I collagen within damaged tissues was recorded with a mean decrease of 15.2%. These alterations could be the hallmark of a decrease in the tissue quality and mechanical properties of the ligament. The findings provide new insight for subsequent research on tissue regeneration that may lead to the development of future treatment strategies for SL injury.
Copyright © 2015 Elsevier Ltd. All rights reserved.
Publication Date: 2015-02-12 PubMed ID: 25795168DOI: 10.1016/j.tvjl.2015.02.011Google Scholar: Lookup
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Summary
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The research article focuses on studying changes in collagen fibrils in horses’ suspensory ligaments after injury using biochemical and ultrastructural methods. It has been found that injuries lead to alterations in the fibril’s organization and composition, potentially impacting the tissue’s quality and mechanical properties.
Research Objectives and Methodologies
The study aimed to understand the changes in horses’ suspensory ligament (SL) collagen fibrils after injury. The reasons for this investigation are:
- SL injuries are a major cause of lameness in horses.
- The quality and mechanical properties of ligament tissues are largely dependent on collagen fibril’s morphology and types.
To carry out this research, the team selected eight Warmblood horses that showed visible signs of injury in one forelimb SL. The steps to investigate included:
- Examining specimens of these injured SLs under a transmission electron microscope (TEM) for abnormalities in fibril organization, diameter, and shape.
- Using a biochemical method to purify collagen types I, III, and V from these samples.
- Analyzing the levels of these collagen types in damaged tissues via densitometric analysis after sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE).
Findings of The Study
TEM revealed changes in the fibrils’ organization, diameter, and shape in the injured ligaments, indicating abnormal collagen behavior due to injury.
The densitometric analysis after SDS-PAGE revealed noteworthy changes in collagen content:
- The percentage of type III and type V collagen was significantly higher in the damaged tissues compared to normal ones, with an average increase of 20.9% and 17.3%, respectively.
- Conversely, the level of type I collagen was significantly lower in the damaged tissues with a mean decrease of 15.2%.
Conclusion and Implication
These changes in collagen fibril organization and types are seen as indicators of a decrease in the quality and mechanical properties of affected ligament tissues. The findings hold significance for future research focusing on tissue regeneration, potentially leading to the development of more effective treatment strategies for SL injuries in horses.
Cite This Article
APA
Shikh Alsook MK, Gabriel A, Salouci M, Piret J, Alzamel N, Moula N, Denoix JM, Antoine N, Baise E.
(2015).
Characterization of collagen fibrils after equine suspensory ligament injury: an ultrastructural and biochemical approach.
Vet J, 204(1), 117-122.
https://doi.org/10.1016/j.tvjl.2015.02.011 Publication
Researcher Affiliations
- Anatomy Unit, FARAH Research Centre and Faculty of Veterinary Medicine, University of Liège, Liège, Belgium. Electronic address: mvet79@hotmail.com.
- Anatomy Unit, FARAH Research Centre and Faculty of Veterinary Medicine, University of Liège, Liège, Belgium.
- Anatomy Unit, FARAH Research Centre and Faculty of Veterinary Medicine, University of Liège, Liège, Belgium.
- Histology Unit, FARAH Research Centre and Faculty of Veterinary Medicine, University of Liège, Liège, Belgium.
- Pathology Unit, FARAH Research Centre and Faculty of Veterinary Medicine, University of Liège, Liège, Belgium.
- Sustainable Animal Production Unit, FARAH Research Centre and Faculty of Veterinary Medicine, University of Liège, Liège, Belgium.
- CIRALE -14430 Goustranville, Université Paris-Est, Ecole Nationale Vétérinaire d'Alfort, Paris, France.
- Histology Unit, FARAH Research Centre and Faculty of Veterinary Medicine, University of Liège, Liège, Belgium.
- FARAH Research Centre and Faculty of Veterinary Medicine, University of Liège, Liège, Belgium.
MeSH Terms
- Animals
- Collagen / chemistry
- Collagen / ultrastructure
- Electrophoresis, Polyacrylamide Gel
- Horse Diseases / pathology
- Horses
- Ligaments / injuries
Citations
This article has been cited 3 times.- Momen M, Brounts SH, Binversie EE, Sample SJ, Rosa GJM, Davis BW, Muir P. Selection signature analyses and genome-wide association reveal genomic hotspot regions that reflect differences between breeds of horse with contrasting risk of degenerative suspensory ligament desmitis.. G3 (Bethesda) 2022 Sep 30;12(10).
- Mienaltowski MJ, Gonzales NL, Beall JM, Pechanec MY. Basic Structure, Physiology, and Biochemistry of Connective Tissues and Extracellular Matrix Collagens.. Adv Exp Med Biol 2021;1348:5-43.
- Lindberg D, Kristoffersen KA, Wubshet SG, Hunnes LMG, Dalsnes M, Dankel KR, Høst V, Afseth NK. Exploring Effects of Protease Choice and Protease Combinations in Enzymatic Protein Hydrolysis of Poultry By-Products.. Molecules 2021 Aug 31;26(17).
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