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Osteoarthritis and cartilage2015; 23(7); 1204-1213; doi: 10.1016/j.joca.2015.03.019

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

Abstract: The 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. Methods: SF 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. Results: The 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. Conclusions: The 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.
Copyright © 2015 The Authors. Published by Elsevier Ltd.. All rights reserved.
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Publication Date: 2015-03-26 PubMed ID: 25819577PubMed Central: PMC4528073DOI: 10.1016/j.joca.2015.03.019Google Scholar: Lookup
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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 article discusses a study that aimed to identify the protein structure of Synovial Fluid (SF) in healthy and unhealthy (osteoarthritis or OA) conditions using Liquid Chromatography Mass Spectrometry (LC-MS/MS). They identified several proteins and new molecules, some of which may serve as potential indicators of normal and OA conditions.

Methods Used in the Study

  • The study utilized SF from nine normal and nine OA thoroughbred horses.
  • The samples were analyzed using LC-MS/MS technology, with a NanoAcquity™ LC connected to an LTQ Orbitrap Velos. This technology allows for the precise and accurate identification and quantification of proteins.
  • To enrich the less-abundant proteins, protein equalization was undertaken using ProteoMiner™, a technology designed to equalize the abundance of proteins in biology samples.
  • Progenesis-QI™ LC-MS software was used for label-free quantification, which is a method for determining the amount of proteins without the need for a label or tag.
  • Immunohistochemistry, western blotting, and mRNA expression analysis were performed on selected joint tissues to analyze the protein expression and localization in the tissue samples.

Results of the Study

  • Following the protein equalization process, the number of protein identifications in the SF increased by 33% compared to the undepleted SF.
  • A total of 764 proteins (462 with at least two significant peptides) were identified in the SF.
  • They found 10 proteins that were differently expressed in OA SF, which implies that these proteins might be involved in the disease.
  • They found an upregulation of S100-A10, a calcium binding protein, in the OA samples. This was confirmed through western blotting and immunohistochemistry.
  • Several new OA-specific peptide fragments (neopeptides) were identified for the first time.

Conclusion of the Study

  • The protein equalization method allowed the researchers to develop the most comprehensive SF proteome — the entire set of proteins expressed by SF — to date.
  • They identified several proteins and neopeptides for the first time in SF. These molecules might play a significant role in the development and progression of OA.
  • They also identified a specific set of proteins and neopeptides that might differentiate between normal and OA joints, highlighting their potential as biomarkers for the disease.

Cite This Article

APA
Peffers MJ, McDermott B, Clegg PD, Riggs CM. (2015). Comprehensive protein profiling of synovial fluid in osteoarthritis following protein equalization. Osteoarthritis Cartilage, 23(7), 1204-1213. https://doi.org/10.1016/j.joca.2015.03.019

Publication

Osteoarthritis and cartilage
ISSN: 1522-9653
NlmUniqueID: 9305697
Country: England
Language: English
Volume: 23
Issue: 7
Pages: 1204-1213
PII: S1063-4584(15)00861-4

Researcher Affiliations

Peffers, M J
  • Comparative 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.
McDermott, B
  • Comparative 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.
Clegg, P D
  • Comparative 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.
Riggs, C M
  • Hong Kong Jockey Club, Equine Hospital, Sha Tin Racecourse, New Territories, Hong Kong. Electronic address: christopher.m.riggs@hjkc.org.hk.

MeSH Terms

  • Animals
  • Annexin A2 / biosynthesis
  • Cartilage, Articular / metabolism
  • Chromatography, Liquid / methods
  • Horse Diseases / metabolism
  • Horse Diseases / pathology
  • Horses
  • Male
  • Mass Spectrometry / methods
  • Osteoarthritis / metabolism
  • Osteoarthritis / pathology
  • Osteoarthritis / veterinary
  • Peptide Fragments / metabolism
  • Protein Array Analysis / methods
  • Proteome / metabolism
  • RNA, Messenger / genetics
  • S100 Proteins / biosynthesis
  • Synovial Fluid / metabolism
  • Synovial Membrane / metabolism

Grant Funding

  • Wellcome Trust
  • MR/K006312/1 / Medical Research Council

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