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Scientific reports2016; 6; 20455; doi: 10.1038/srep20455

Anatomical heterogeneity of tendon: Fascicular and interfascicular tendon compartments have distinct proteomic composition.

Abstract: Tendon is a simple aligned fibre composite, consisting of collagen-rich fascicles surrounded by a softer interfascicular matrix (IFM). The composition and interactions between these material phases are fundamental in ensuring tissue mechanics meet functional requirements. However the IFM is poorly defined, therefore tendon structure-function relationships are incompletely understood. We hypothesised that the IFM has a more complex proteome, with faster turnover than the fascicular matrix (FM). Using laser-capture microdissection and mass spectrometry, we demonstrate that the IFM contains more proteins, and that many proteins show differential abundance between matrix phases. The IFM contained more protein fragments (neopeptides), indicating greater matrix degradation in this compartment, which may act to maintain healthy tendon structure. Protein abundance did not alter with ageing, but neopeptide numbers decreased in the aged IFM, indicating decreased turnover which may contribute to age-related tendon injury. These data provide important insights into how differences in tendon composition and turnover contribute to tendon structure-function relationships and the effects of ageing.
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Publication Date: 2016-02-04 PubMed ID: 26842662PubMed Central: PMC4740843DOI: 10.1038/srep20455Google Scholar: Lookup
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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.

This research explores the differences in protein composition in different compartments of a tendon, specifically the fascicular and interfascicular areas and how these variances affect tendon functionality and ageing.

Understanding Tendon Composition

The body of the research focused on understanding the intricate composition of the tendon, specifically between fascicular and interfascicular areas. The tendon is primarily composed of collagen-rich fascicles, which are surrounded by a less dense interfascicular matrix (IFM). Understanding the interaction between these components and their composition is crucial to understanding the functional requirements of the tendon due to its unique structure and function relationship.

  • The researchers hypothesized that the interfascicular matrix has a more intricate proteome and has a faster turnover rate than the fascicular matrix.

Methodology and Findings

The methodology of this research involved laser-capture microdissection and mass spectrometry, both of which are cutting-edge techniques for analyzing proteomic composition and distribution.

  • Through this methodology, the researchers found that the IFM contained a greater number of proteins compared to the fascicular matrix.
  • Additionally, there were notable differences in the abundance of proteins within these matrix phases, giving credibility to their hypothesis that the IFM has a more detailed proteome.
  • The IFM also contained more protein fragments, known as neopeptides, indicating a higher rate of matrix degradation in this area, potentially to maintain tendon health and structure.

Ageing and Protein Abundance

The impact of ageing on the abundance of proteins within the tendon was also examined in the study.

  • The abundance of proteins did not show any change with ageing.
  • However, the number of neopeptides or protein fragments reduced in the older IFM, indicating a decreased turnover rate, which may be a contributing factor to age-related tendon injury.

Significance of the Study

The findings from this study provide vital insights into the unique composition of the tendon and how variances in protein turnover rates at different locations contribute towards tendon function and the impact of ageing.

  • This can be influential in further understanding age-related tendon injuries and devising solutions to alleviate such conditions.
  • Additionally, understanding the intricate structure and function relationship of tendon could have wider implications in the fields of biomechanics and physiology.

Cite This Article

APA
Thorpe CT, Peffers MJ, Simpson D, Halliwell E, Screen HR, Clegg PD. (2016). Anatomical heterogeneity of tendon: Fascicular and interfascicular tendon compartments have distinct proteomic composition. Sci Rep, 6, 20455. https://doi.org/10.1038/srep20455

Publication

Scientific reports
ISSN: 2045-2322
NlmUniqueID: 101563288
Country: England
Language: English
Volume: 6
Pages: 20455
PII: 20455

Researcher Affiliations

Thorpe, Chavaunne T
  • Institute of Bioengineering, School of Engineering and Materials Science, Queen Mary University of London, Mile End Road, London, E1 4NS, UK.
Peffers, Mandy J
  • Department of Musculoskeletal Biology, Institute of Ageing and Chronic Disease, University of Liverpool, Leahurst Campus, Neston, CH64 7TE, UK.
Simpson, Deborah
  • Centre for Proteome Research, Institute of Integrative Biology, University of Liverpool, Crown Street, Liverpool, L69 7ZB, UK.
Halliwell, Elizabeth
  • Department of Musculoskeletal Biology, Institute of Ageing and Chronic Disease, University of Liverpool, Leahurst Campus, Neston, CH64 7TE, UK.
Screen, Hazel R C
  • Institute of Bioengineering, School of Engineering and Materials Science, Queen Mary University of London, Mile End Road, London, E1 4NS, UK.
Clegg, Peter D
  • Department of Musculoskeletal Biology, Institute of Ageing and Chronic Disease, University of Liverpool, Leahurst Campus, Neston, CH64 7TE, UK.

MeSH Terms

  • Aging / metabolism
  • Animals
  • Carrier Proteins
  • Gene Ontology
  • Glycoproteins
  • Horses
  • Laser Capture Microdissection
  • Mass Spectrometry
  • Proteomics / methods
  • Seminal Plasma Proteins
  • Tendons / anatomy & histology
  • Tendons / metabolism

Grant Funding

  • MR/K006312/1 / Medical Research Council
  • BB/K008412/1 / Biotechnology and Biological Sciences Research Council

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Citations

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