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Journal of anatomy2016; 229(3); 450-458; doi: 10.1111/joa.12485

Distribution of proteins within different compartments of tendon varies according to tendon type.

Abstract: Although the predominant function of all tendons is to transfer force from muscle to bone and position the limbs, some tendons additionally function as energy stores, reducing the energetic cost of locomotion. To maximise energy storage and return, energy-storing tendons need to be more extensible and elastic than tendons with a purely positional function. These properties are conferred in part by a specialisation of a specific compartment of the tendon, the interfascicular matrix, which enables sliding and recoil between adjacent fascicles. However, the composition of the interfascicular matrix is poorly characterised and we therefore tested the hypothesis that the distribution of elastin and proteoglycans differs between energy-storing and positional tendons, and that protein distribution varies between the fascicular matrix and the interfascicular matrix, with localisation of elastin and lubricin to the interfascicular matrix. Protein distribution in the energy-storing equine superficial digital flexor tendon and positional common digital extensor tendon was assessed using histology and immunohistochemistry. The results support the hypothesis, demonstrating enrichment of lubricin in the interfascicular matrix in both tendon types, where it is likely to facilitate interfascicular sliding. Elastin was also localised to the interfascicular matrix, specifically in the energy-storing superficial digital flexor tendon, which may account for the greater elasticity of the interfascicular matrix in this tendon. A differential distribution of proteoglycans was identified between tendon types and regions, which may indicate a distinct role for each of these proteins in tendon. These data provide important advances into fully characterising structure-function relationships within tendon.
Publication Date: 2016-04-25 PubMed ID: 27113131PubMed Central: PMC4974547DOI: 10.1111/joa.12485Google Scholar: Lookup
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  • Journal Article
  • Research Support
  • Non-U.S. Gov't

Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

The research article focuses on the difference in protein distributions within different parts of positional and energy-storing tendons, which contributes to their respective functionalities in body movement and energy storage.

Objective of the Research

  • The aim of this research was to closely examine the composition of a specific tendon compartment, known as the interfascicular matrix, which is responsible for providing elasticity to the tendons. The researchers hypothesised that the distribution of elastin and proteoglycans, two types of protein, differ between energy-storing tendons and positional tendons. They further theorised that the distribution of such proteins varies even in the different regions of a tendon, in the fascicular matrix and the interfascicular matrix.

Methodology of the Research

  • The research was conducted by examining the protein distribution in two types of tendons in horses – the energy-storing superficial digital flexor tendon and the positional common digital extensor tendon. The researchers used histology and immunohistochemistry to assess the protein distribution.

Findings of the Research

  • The study demonstrated that both the energy-storing superficial digital flexor tendon and the positional common digital extensor tendon had an enrichment of lubricin, a type of protein, within the interfascicular matrix. This protein likely facilitates the sliding action between fascicles.
  • The energy-storing tendons were found to contain elastin proteins uniquely in the interfascicular matrix, which could be the reason for the increased elasticity in these tendons.
  • Proteoglycans were distributed differently between the two types of tendons and even within their respective regions. This could suggest a distinct role for each of these proteins in tendon functionality.

Significance of the Research

  • The findings provide a significant contribution to our understanding of structure-function relationships in tendons. By establishing the links between protein distribution, and tendon type and functionality, the research can influence future studies or treatments related to tendons.

Cite This Article

APA
Thorpe CT, Karunaseelan KJ, Ng Chieng Hin J, Riley GP, Birch HL, Clegg PD, Screen HR. (2016). Distribution of proteins within different compartments of tendon varies according to tendon type. J Anat, 229(3), 450-458. https://doi.org/10.1111/joa.12485

Publication

ISSN: 1469-7580
NlmUniqueID: 0137162
Country: England
Language: English
Volume: 229
Issue: 3
Pages: 450-458

Researcher Affiliations

Thorpe, Chavaunne T
  • Institute of Bioengineering, School of Engineering and Materials Science, Queen Mary University of London, London, UK.
Karunaseelan, Kabelan J
  • Institute of Bioengineering, School of Engineering and Materials Science, Queen Mary University of London, London, UK.
Ng Chieng Hin, Jade
  • Institute of Bioengineering, School of Engineering and Materials Science, Queen Mary University of London, London, UK.
Riley, Graham P
  • School of Biological Sciences, University of East Anglia, Norwich Research Park, Norwich, UK.
Birch, Helen L
  • Institute of Orthopaedics and Musculoskeletal Science, University College London, Royal National Orthopaedic Hospital, Stanmore, UK.
Clegg, Peter D
  • Department of Musculoskeletal Biology, Institute of Ageing and Chronic Disease, University of Liverpool, Neston, UK.
Screen, Hazel R C
  • Institute of Bioengineering, School of Engineering and Materials Science, Queen Mary University of London, London, UK.

MeSH Terms

  • Animals
  • Elastin
  • Glycoproteins
  • Horses
  • Image Processing, Computer-Assisted
  • Immunohistochemistry
  • Tendons / metabolism

Grant Funding

  • MR/K006312/1 / Medical Research Council

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Citations

This article has been cited 25 times.
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