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Comprehensive Protein Profiling of Synovial Fluid in Osteoarthritis
Author(s) -
Peffers M.,
Riggs C.,
McDermott B.,
Clegg P.
Publication year - 2014
Publication title -
equine veterinary journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.82
H-Index - 87
eISSN - 2042-3306
pISSN - 0425-1644
DOI - 10.1111/evj.12323_42
Subject(s) - osteoarthritis , synovial fluid , synovitis , proteome , pathogenesis , proteases , chemistry , articular cartilage , cartilage , pathology , bioinformatics , medicine , immunology , biology , arthritis , biochemistry , anatomy , enzyme , alternative medicine
Reasons for performing study Synovial fluid ( SF ) is located in joint cavities, tendon sheaths and bursae. In joints it comprises a serum filtrate with additional contributions from articular cartilage, synovium and bone. It represents a potential source of disease specific proteins that could aid in the understanding of the pathogenesis of joint disease and be used in the early diagnosis of disease. Objectives To comprehensively profile the protein complement of SF in health and osteoarthritis ( OA ) using liquid chromatography mass spectrometry ( LC‐MS / MS ) and identify potential OA biomarkers. Study design SF was used from the metacarpophalangeal joints of 9 normal and 9 OA Thoroughbred horses following macroscopic, microscopic and synovitis scoring. Methods Samples were analysed with LC‐MS / MS using a NanoAcquity LC coupled to a LTQ Orbitrap Velos. Progenesis TM LC‐MS software was used for label‐free quantification with data searched using Mascot in the Ensembl database for horse. Adjusted ANOVA values of P<0.05 and regulation of >2‐fold were regarded as significant. Results 754 proteins were identified in SF . Thus Proteominer TM beads concentrated the lower abundance proteins enabling the most comprehensive SF proteome to date. Proteins identified included those relating to matrix proteins, inflammatory factors, complement activation proteins and proteases. A subset of 10 proteins was identified which were differentially expressed in OA SF . Conclusions 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 that may act as potential biomarkers to distinguish between normal and OA joints. S 100‐ A 10, a calcium binding protein has upregulated in OA . This may have a role in the synthesis and activation of matrix degrading proteases. CD 109 is a TGF ‐β co‐receptor, released from the chondrocyte cell surface that inhibits TGF ‐β signalling. Its contribution to the disregulation of TGF ‐β is unknown. Ethical animal research: Ethical committee oversight not currently required by this congress: the study was performed on material collected during post mortem examination. Explicit owner informed consent for participation in this study was not stated. Sources of funding: Horserace Betting Levy Board, Wellcome Trust. Competing interests: None.