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The Journal of biological chemistry2014; 289(37); 25867-25878; doi: 10.1074/jbc.M114.566554

Proteomic analysis reveals age-related changes in tendon matrix composition, with age- and injury-specific matrix fragmentation.

Abstract: Energy storing tendons, such as the human Achilles and equine superficial digital flexor tendon (SDFT), are highly prone to injury, the incidence of which increases with aging. The cellular and molecular mechanisms that result in increased injury in aged tendons are not well established but are thought to result in altered matrix turnover. However, little attempt has been made to fully characterize the tendon proteome nor determine how the abundance of specific tendon proteins changes with aging and/or injury. The aim of this study was, therefore, to assess the protein profile of normal SDFTs from young and old horses using label-free relative quantification to identify differentially abundant proteins and peptide fragments between age groups. The protein profile of injured SDFTs from young and old horses was also assessed. The results demonstrate distinct proteomic profiles in young and old tendon, with alterations in the levels of proteins involved in matrix organization and regulation of cell tension. Furthermore, we identified several new peptide fragments (neopeptides) present in aged tendons, suggesting that there are age-specific cleavage patterns within the SDFT. Proteomic profile also differed between young and old injured tendon, with a greater number of neopeptides identified in young injured tendon. This study has increased the knowledge of molecular events associated with tendon aging and injury, suggesting that maintenance and repair of tendon tissue may be reduced in aged individuals and may help to explain why the risk of injury increases with aging.
Publication Date: 2014-07-30 PubMed ID: 25077967PubMed Central: PMC4162187DOI: 10.1074/jbc.M114.566554Google Scholar: Lookup
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  • Journal Article
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  • 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 focuses on studying the changes in the composition of tendon proteins caused by aging and injuries using the superficial digital flexor tendon (SDFT) in horses. It indicates that older tendons differ in their protein profile compared with young ones, suggesting decreased maintenance and repair in aged tissues which might increase the risk of injury.

Study Objective and Methodology

  • The primary objective of this research was to analyze and compare the protein profile of normal SDFTs in young and old horses. The study seeks to identify proteins and peptide fragments that vary in their abundance between different age groups.
  • The research was conducted using label-free relative quantification, an analytical biochemistry technique which allows for comparative measurement of different protein samples without a need for an isotope or fluorescent tags.
  • The researchers also assessed the protein profile of injured SDFTs in both old and young horses, providing a comparative analysis between healthy and injured tendon tissues across different age groups.

Research Findings

  • The results revealed noticeable differences in the proteomic profiles of young and old tendons, specifically alterations in proteins associated with matrix organization and cell tension regulation.
  • The study also discovered several new peptide fragments (neopeptides) present in the aged tendons, suggesting age-specific cleavage patterns within the SDFT. These neopeptides are newly formed peptides that result from the breakdown of their parent proteins, and their presence may indicate changes/negligence in the normal repair process of the tissue.
  • The research established that there is a difference in the proteomic profile between young and old injured tendons. More neopeptides were identified in the young injured tendons compared to the older injured tendons.

Implications of the Findings

  • This research contributes to the broader understanding of the molecular events related to tendon aging and injury, enhancing the knowledge about the biochemical changes that occur with aging.
  • Moreover, the differences in protein profiles and the presence of neopeptides in aged tendons suggest that the maintenance and repair mechanisms in tendon tissues might be compromised with aging. This could provide an explanation for the increasing risk of injury with age.
  • The findings of this study may have implications for the development of future therapeutic strategies aimed at enhancing tendon repair, especially in the context of aging.

Cite This Article

APA
Peffers MJ, Thorpe CT, Collins JA, Eong R, Wei TK, Screen HR, Clegg PD. (2014). Proteomic analysis reveals age-related changes in tendon matrix composition, with age- and injury-specific matrix fragmentation. J Biol Chem, 289(37), 25867-25878. https://doi.org/10.1074/jbc.M114.566554

Publication

ISSN: 1083-351X
NlmUniqueID: 2985121R
Country: United States
Language: English
Volume: 289
Issue: 37
Pages: 25867-25878

Researcher Affiliations

Peffers, Mandy J
  • From the Department of Musculoskeletal Biology, Institute of Ageing and Chronic Disease, University of Liverpool, Leahurst Campus, Neston CH64 7TE.
Thorpe, Chavaunne T
  • From the Department of Musculoskeletal Biology, Institute of Ageing and Chronic Disease, University of Liverpool, Leahurst Campus, Neston CH64 7TE, Institute of Bioengineering, Queen Mary University of London, Mile End Road, London E1 4NS, and c.thorpe@qmul.ac.uk.
Collins, John A
  • From the Department of Musculoskeletal Biology, Institute of Ageing and Chronic Disease, University of Liverpool, Leahurst Campus, Neston CH64 7TE.
Eong, Robin
  • From the Department of Musculoskeletal Biology, Institute of Ageing and Chronic Disease, University of Liverpool, Leahurst Campus, Neston CH64 7TE, School of Life Sciences, Ngee Ann Polytechnic, Singapore 599489.
Wei, Timothy K J
  • From the Department of Musculoskeletal Biology, Institute of Ageing and Chronic Disease, University of Liverpool, Leahurst Campus, Neston CH64 7TE, School of Life Sciences, Ngee Ann Polytechnic, Singapore 599489.
Screen, Hazel R C
  • Institute of Bioengineering, Queen Mary University of London, Mile End Road, London E1 4NS, and.
Clegg, Peter D
  • From the Department of Musculoskeletal Biology, Institute of Ageing and Chronic Disease, University of Liverpool, Leahurst Campus, Neston CH64 7TE.

MeSH Terms

  • Age Factors
  • Aging / genetics
  • Aging / pathology
  • Animals
  • Electrophoresis, Polyacrylamide Gel
  • Extracellular Matrix / metabolism
  • Horses / genetics
  • Horses / physiology
  • Humans
  • Proteomics
  • Tendon Injuries / genetics
  • Tendon Injuries / pathology
  • Tendons / metabolism
  • Tendons / pathology

Grant Funding

  • MR/K006312/1 / Medical Research Council
  • WT088557MA / Wellcome Trust
  • BB/K008412/1 / Biotechnology and Biological Sciences Research Council

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