Evidence map›Paper›PMID 25819577›Full record

ArticleOsteoarthritis and cartilage2015

Comprehensive protein profiling of synovial fluid in osteoarthritis following protein equalization.

M J Peffers, B McDermott, P D Clegg, C M Riggs

Open access · hybridAbstract read
In one paragraph

Article in Osteoarthritis and cartilage, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
6.8field-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

26 citing papers in PubMed, 60 citations in OpenAlex.

  1. Trial
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  10. Structural, compositional, and functional effects of blunt and sharp cartilage damage on the joint: A 9-month equine groove model study.Journal of orthopaedic research : official publication of the Orthopaedic Research Society · 2021
    Article
  11. Article
  12. Review
  13. Journal of proteome research · 2020
    Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Journal of proteome research · 2018
    Article
  19. Osteoarthritis and the Complement Cascade.Clinical medicine insights. Arthritis and musculoskeletal disorders · 2018
    Review
  20. Article
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

4 authors at 2 institutions in 2 countries.

M J PeffersComparative Musculoskeletal Biology, Institute of Ageing and Chronic Disease, University of Liverpool, Leahurst, Chester High Road, Neston, Wirral, CH64 7TE, UK. Electronic address: peffs@liv.ac.uk.
B McDermottComparative Musculoskeletal Biology, Institute of Ageing and Chronic Disease, University of Liverpool, Leahurst, Chester High Road, Neston, Wirral, CH64 7TE, UK. Electronic address: benmcd@liverpool.ac.uk.
P D CleggComparative Musculoskeletal Biology, Institute of Ageing and Chronic Disease, University of Liverpool, Leahurst, Chester High Road, Neston, Wirral, CH64 7TE, UK. Electronic address: pclegg@liverpool.ac.uk.
C M RiggsHong Kong Jockey Club, Equine Hospital, Sha Tin Racecourse, New Territories, Hong Kong. Electronic address: christopher.m.riggs@hjkc.org.hk.
University of Liverpool · GBHong Kong Jockey Club · CN

Funding

Medical Research Council MR/K006312/1Wellcome Trust
6 · The paper itself

Abstract

objectiveThe aim of the study was to characterise the protein complement of synovial fluid (SF) in health and osteoarthritis (OA) using liquid chromatography mass spectrometry (LC-MS/MS) following peptide-based depletion of high abundance proteins.

designSF was used from nine normal and nine OA Thoroughbred horses. Samples were analysed with LC-MS/MS using a NanoAcquity™ LC coupled to an LTQ Orbitrap Velos. In order to enrich the lower-abundance protein fractions protein equalisation was first undertaken using ProteoMiner™. Progenesis-QI™ LC-MS software was used for label-free quantification. In addition immunohistochemistry, western blotting and mRNA expression analysis was undertaken on selected joint tissues.

resultsThe number of protein identifications was increased by 33% in the ProteoMiner™ treated SF compared to undepleted SF. A total of 764 proteins (462 with≥2 significant peptides) were identified in SF. A subset of 10 proteins were identified which were differentially expressed in OA SF. S100-A10, a calcium binding protein was upregulated in OA and validated with western blotting and immunohistochemistry. Several new OA specific peptide fragments (neopeptides) were identified.

conclusionThe protein equalisation method compressed the dynamic range of the synovial proteins identifying the most comprehensive SF proteome to date. A number of proteins were identified for the first time in SF which may be involved in the pathogenesis of OA. We identified a distinct set of proteins and neopeptides that may act as potential biomarkers to distinguish between normal and OA joints.

Indexed as

AnimalsAnnexin A2Cartilage, ArticularChromatography, LiquidHorse DiseasesHorsesMaleMass SpectrometryOsteoarthritisPeptide FragmentsProtein Array AnalysisProteomeRNA, MessengerS100 Calcium Binding Protein A10S100 ProteinsSynovial FluidAnnexin A2Peptide FragmentsProteomeRNA, MessengerS100 Calcium Binding Protein A10S100 ProteinsEqualizationNeopeptideOsteoarthritisS100-A10Synovial fluid

Identifiers

PMID25819577
PMCPMC4528073
OpenAlexW2017854718

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Registered trials

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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.