Anatomical heterogeneity of tendon: Fascicular and interfascicular tendon compartments have distinct proteomic composition.
- Journal Article
- Research Support
- Non-U.S. Gov't
Summary
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
Publication
Researcher Affiliations
- Institute of Bioengineering, School of Engineering and Materials Science, Queen Mary University of London, Mile End Road, London, E1 4NS, UK.
- Department of Musculoskeletal Biology, Institute of Ageing and Chronic Disease, University of Liverpool, Leahurst Campus, Neston, CH64 7TE, UK.
- Centre for Proteome Research, Institute of Integrative Biology, University of Liverpool, Crown Street, Liverpool, L69 7ZB, UK.
- Department of Musculoskeletal Biology, Institute of Ageing and Chronic Disease, University of Liverpool, Leahurst Campus, Neston, CH64 7TE, UK.
- Institute of Bioengineering, School of Engineering and Materials Science, Queen Mary University of London, Mile End Road, London, E1 4NS, UK.
- 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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