Proteomic Analysis Reveals Age-related Changes in Tendon Matrix Composition, with Age- and Injury-specific Matrix Fragmentation

Peffers, Mandy ORCID: 0000-0001-6979-0440, Thorpe, Chavaunne, Collins, John, Eong, R, Wei, T, Screen, H and Clegg, Peter ORCID: 0000-0003-0632-0032 (2014) Proteomic Analysis Reveals Age-related Changes in Tendon Matrix Composition, with Age- and Injury-specific Matrix Fragmentation. The Journal of Biological Chemistry, 289 (37). pp. 25867-25878.

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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 cel- lular 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 differ- entially 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 regu- lation of cell tension. Furthermore, we identified several new peptide fragments (neopeptides) present in aged tendons, sug- gesting 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 knowl- edge 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.

Item Type:	Article
Additional Information:	This research was originally published in the Journal of Biological Chemistry. Mandy J. Peffers, Chavaunne T. Thorpe, John A. Collins, Robin Eong, Timothy K. J. Wei, Hazel R. C. Screen and Peter D. Clegg. J. Biol. Chem. 2014; 289:25867-25878 © the American Society for Biochemistry and Molecular Biology.
Uncontrolled Keywords:	aging, collagen, mass spectrometry (MS), protein degradation, proteoglycan, disease, equine, fibromodulin, neopeptide
Depositing User:	Symplectic Admin
Date Deposited:	16 Apr 2015 15:22
Last Modified:	15 Dec 2022 23:50
DOI:	10.1074/jbc.M114.566554
Related URLs:	Author Publisher
URI:	https://livrepository.liverpool.ac.uk/id/eprint/2010086