Matrix metabolism rate differs in functionally distinct tendons.
Abstract: Tendon matrix integrity is vital to ensure adequate mechanical properties for efficient function. Although historically tendon was considered to be relatively inert, recent studies have shown that tendon matrix turnover is active. During normal physiological activities some tendons are subjected to stress and strains much closer to their failure properties than others. Tendons with low safety margins are those which function as energy stores such as the equine superficial digital flexor tendon (SDFT) and human Achilles tendon (AT). We postulate therefore that energy storing tendons suffer a higher degree of micro-damage and thus have a higher rate of matrix turnover than positional tendons. The hypothesis was tested using tissue from the equine SDFT and common digital extensor tendon (CDET). Matrix turnover was assessed indirectly by a combination of measurements for matrix age, markers of degradation, potential for degradation and protein expression. Results show that despite higher cellularity, the SDFT has lower relative levels of mRNA for collagen types I and III. Non-collagenous proteins, although expressed at different levels per cell, do not appear to differ between tendon types. Relative levels of mRNA for MMP1, MMP13 and both pro-MMP3 and MMP13 protein activity were significantly higher in the CDET. Correspondingly levels of cross-linked carboxyterminal telopeptide of type I collagen (ICTP) were higher in the CDET and tissue fluorescence lower suggesting more rapid turnover of the collagenous component. Reduced or inhibited collagen turnover in the SDFT may account for the high level of degeneration and subsequent injury compared to the CDET.
Publication Date: 2007-10-26 PubMed ID: 18032005DOI: 10.1016/j.matbio.2007.10.004Google Scholar: Lookup
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- Journal Article
- Research Support
- Non-U.S. Gov't
Summary
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This research investigates the matrix turnover rates in different types of tendons, particularly energy-storing and positional tendons, using equine tendon tissue samples. Results suggest energy-storing tendons could incur more micro-damage, potentially explaining their higher rates of degeneration and subsequent injury.
Context and Hypothesis
- The research stems from recent findings that contrary to previous beliefs, the tendon matrix is an active turnover, i.e., is consistently being broken down and regenerated.
- Different tendons are subjected to varying levels of stress and strain depending on their function. Energy-storing tendons, like the equine superficial digital flexor tendon (SDFT) and the human Achilles tendon (AT), often experience stress closer to their breaking points than other tendons. This exposure leads the authors to predict that these energy-storing tendons sustain more micro-damage and therefore have a higher matrix turnover rate than positional tendons.
Methodology
- The hypothesis was tested using tissue from the equine SDFT and the common digital extensor tendon (CDET), which serve as models for energy-storing and positional tendons, respectively.
- Matrix turnover was indirectly assessed using measures for matrix age, signs of degradation, potential for decay, and protein expression.
Findings
- The researchers found that the SDFT, despite having more cells, had lower relative levels of mRNA for collagen types I and III, proteins essential for tendon structure and function.
- There was no discernible difference in the expression of non-collagenous proteins between the two tendon types.
- MMP1, MMP13, pro-MMP3 and MMP13 protein activity—involved in collagen degradation—were significantly higher in the CDET.
- The CDET also had higher levels of cross-linked carboxyterminal telopeptide of type I collagen (ICTP)—a marker of collagen degradation—and lower tissue fluorescence, indicating a more rapid turnover of the collagenous component in the CDET.
Conclusion and Implication
- The different levels of matrix turnover in the SDFT and CDET may explain why energy-storing tendons suffer higher rates of degeneration and subsequent injury.
- The findings of reduced or inhibited collagen turnover in the SDFT could provide valuable insights into the high levels of degeneration in energy-storing tendons, which may in turn lead to advancements in injury prevention and treatment in both veterinary and human medicine.
Cite This Article
APA
Birch HL, Worboys S, Eissa S, Jackson B, Strassburg S, Clegg PD.
(2007).
Matrix metabolism rate differs in functionally distinct tendons.
Matrix Biol, 27(3), 182-189.
https://doi.org/10.1016/j.matbio.2007.10.004 Publication
Researcher Affiliations
- Institute of Orthopaedics and Musculoskeletal Science, University College London, Stanmore Campus, Royal National Orthopaedic Hospital, Brockley Hill, Stanmore, HA7 4LP, UK. h.birch@ucl.ac.uk
MeSH Terms
- Achilles Tendon / pathology
- Animals
- Collagen / chemistry
- Collagen Type I / chemistry
- Cross-Linking Reagents / pharmacology
- DNA / metabolism
- Extracellular Matrix / metabolism
- Gene Expression Regulation, Enzymologic
- Horses
- Humans
- Matrix Metalloproteinases / metabolism
- Models, Biological
- RNA, Messenger / metabolism
- Tendons / pathology
Citations
This article has been cited 20 times.- Gsell KY, Veres SP, Kreplak L. Single collagen fibrils isolated from high stress and low stress tendons show differing susceptibility to enzymatic degradation by the interstitial collagenase matrix metalloproteinase-1 (MMP-1). Matrix Biol Plus 2023 Jun;18:100129.
- Abdelhakiem MAH, Hussein A, Seleim SM, Abdelbaset AE, Abd-Elkareem M. Silver nanoparticles and platelet-rich fibrin accelerate tendon healing in donkey. Sci Rep 2023 Feb 28;13(1):3421.
- Zamboulis DE, Thorpe CT, Ashraf Kharaz Y, Birch HL, Screen HR, Clegg PD. Postnatal mechanical loading drives adaptation of tissues primarily through modulation of the non-collagenous matrix. Elife 2020 Oct 16;9.
- Lin AH, Allan AN, Zitnay JL, Kessler JL, Yu SM, Weiss JA. Collagen denaturation is initiated upon tissue yield in both positional and energy-storing tendons. Acta Biomater 2020 Dec;118:153-160.
- Körting C, Schlippe M, Petersson S, Pennati GV, Tarassova O, Arndt A, Finni T, Zhao K, Wang R. In vivo muscle morphology comparison in post-stroke survivors using ultrasonography and diffusion tensor imaging. Sci Rep 2019 Aug 14;9(1):11836.
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- Rowson D, Knight MM, Screen HR. Zonal variation in primary cilia elongation correlates with localized biomechanical degradation in stress deprived tendon. J Orthop Res 2016 Dec;34(12):2146-2153.
- Thorpe CT, Godinho MSC, Riley GP, Birch HL, Clegg PD, Screen HRC. The interfascicular matrix enables fascicle sliding and recovery in tendon, and behaves more elastically in energy storing tendons. J Mech Behav Biomed Mater 2015 Dec;52:85-94.
- Peffers MJ, Thorpe CT, Collins JA, Eong R, Wei TK, Screen HR, Clegg PD. Proteomic analysis reveals age-related changes in tendon matrix composition, with age- and injury-specific matrix fragmentation. J Biol Chem 2014 Sep 12;289(37):25867-78.
- Thorpe CT, Riley GP, Birch HL, Clegg PD, Screen HR. Fascicles from energy-storing tendons show an age-specific response to cyclic fatigue loading. J R Soc Interface 2014 Mar 6;11(92):20131058.
- Rich T, Henderson LB, Becker DL, Cornell H, Patterson-Kane JC. Indicators of replicative damage in equine tendon fibroblast monolayers. BMC Vet Res 2013 Sep 11;9:180.
- Birch HL, Thorpe CT, Rumian AP. Specialisation of extracellular matrix for function in tendons and ligaments. Muscles Ligaments Tendons J 2013 Jan;3(1):12-22.
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- Gsell KY, Kreplak L, Veres SP. In tendons, differing physiological requirements lead to distinct patterns of MMP-1 degradation. Sci Rep 2025 Dec 23;16(1):2420.
- Djalali-Cuevas A, Rettel M, Stein F, Savitski M, Kearns S, Kelly J, Biggs M, Skoufos I, Tzora A, Prassinos N, Diakakis N, Zeugolis DI. Macromolecular crowding in human tenocyte and skin fibroblast cultures: A comparative analysis. Mater Today Bio 2024 Apr;25:100977.
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