Evidence map›Paper›PMID 26842662›Full record

ArticleScientific reports2016

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

Chavaunne T Thorpe, Mandy J Peffers, Deborah Simpson, Elizabeth Halliwell, Hazel R C Screen, Peter D Clegg

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed, 2 pooled it
8.0field-weighted citation impact, top 2% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

63 citing papers in PubMed, 2 syntheses or guidelines pooled it, 104 citations in OpenAlex.

  1. Pooled it
  2. Epigenetic mechanisms in Tendon Ageing.British medical bulletin · 2020
    Pooled it
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  12. LeveragingFrontiers in bioengineering and biotechnology · 2024
    Review
  13. Earlier proteoglycan turnover promotes higher efficiency matrix remodeling in MRL/MpJ tendons.Journal of orthopaedic research : official publication of the Orthopaedic Research Society · 2023
    Article
  14. Review
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3 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 1 country.

Chavaunne T ThorpeInstitute of Bioengineering, School of Engineering and Materials Science, Queen Mary University of London, Mile End Road, London, E1 4NS, UK.
Mandy J PeffersDepartment of Musculoskeletal Biology, Institute of Ageing and Chronic Disease, University of Liverpool, Leahurst Campus, Neston, CH64 7TE, UK.
Deborah SimpsonCentre for Proteome Research, Institute of Integrative Biology, University of Liverpool, Crown Street, Liverpool, L69 7ZB, UK.
Elizabeth HalliwellDepartment of Musculoskeletal Biology, Institute of Ageing and Chronic Disease, University of Liverpool, Leahurst Campus, Neston, CH64 7TE, UK.
Hazel R C ScreenInstitute of Bioengineering, School of Engineering and Materials Science, Queen Mary University of London, Mile End Road, London, E1 4NS, UK.
Peter D CleggDepartment of Musculoskeletal Biology, Institute of Ageing and Chronic Disease, University of Liverpool, Leahurst Campus, Neston, CH64 7TE, UK.
University of Liverpool · GBQueen Mary University of London · GB

Funding

Biotechnology and Biological Sciences Research Council BB/K008412/1Medical Research Council MR/K006312/1
6 · The paper itself

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.

Indexed as

AgingAnimalsCarrier ProteinsGene OntologyGlycoproteinsHorsesLaser Capture MicrodissectionMass SpectrometryProteomicsSeminal Plasma ProteinsTendonsCarrier ProteinsGlycoproteinsHSP-2 protein, Equus caballusSeminal Plasma Proteins

Identifiers

PMID26842662
PMCPMC4740843
OpenAlexW2426918341

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.