Poteomic analysis of human osteoarthritis synovial fluid
Publication Type:Journal Article
Source:Clinical Proteomics, BioMed Central Ltd., Volume 11, Number 1 (2014)
Keywords:ADAMDEC1 gene, affinity chromatography, aged, ANPEP gene, article, ASPN gene, attractin, bioassay, CD84 gene, cell communication, clinical article, COLEC10 gene, dickkopf 1 protein, DKK3 gene, female, fibrillin 1, fibulin, fibulin 1, gene, Gene ontology, glycoprotein, human, human cell, lectin, male, mass spectrometry, microsomal aminopeptidase, MMRN2 gene, multiple reaction monitoring, OGN gene, osteoarthritis, osteopontin, priority journal, protein ADAMDEC1, protein AFM, protein CD84, protein determination, protein expression, protein glycosylation, protein MXRA5, protein OCG, protein SPON2, protein SPP2, protein VSN, proteomics, signal transduction, SPARCL1 gene, synovial fluid, THY1 gene, tissue inhibitor of metalloproteinase 1, Transferrin, unclassified drug, VSIG4 gene
Background: Osteoarthritis is a chronic musculoskeletal disorder characterized mainly by progressive degradation of the hyaline cartilage. Patients with osteoarthritis often postpone seeking medical help, which results in the diagnosis being made at an advanced stage of cartilage destruction. Sustained efforts are needed to identify specific markers that might help in early diagnosis, monitoring disease progression and in improving therapeutic outcomes. We employed a multipronged proteomic approach, which included multiple fractionation strategies followed by high resolution mass spectrometry analysis to explore the proteome of synovial fluid obtained from osteoarthritis patients. In addition to the total proteome, we also enriched glycoproteins from synovial fluid using lectin affinity chromatography. Results: We identified 677 proteins from synovial fluid of patients with osteoarthritis of which 545 proteins have not been previously reported. These novel proteins included ADAM-like decysin 1 (ADAMDEC1), alanyl (membrane) aminopeptidase (ANPEP), CD84, fibulin 1 (FBLN1), matrix remodelling associated 5 (MXRA5), secreted phosphoprotein 2 (SPP2) and spondin 2 (SPON2). We identified 300 proteins using lectin affinity chromatography, including the glycoproteins afamin (AFM), attractin (ATRN), fibrillin 1 (FBN1), transferrin (TF), tissue inhibitor of metalloproteinase 1 (TIMP1) and vasorin (VSN). Gene ontology analysis confirmed that a majority of the identified proteins were extracellular and are mostly involved in cell communication and signaling. We also confirmed the expression of ANPEP, dickkopf WNT signaling pathway inhibitor 3 (DKK3) and osteoglycin (OGN) by multiple reaction monitoring (MRM) analysis of osteoarthritis synovial fluid samples. Conclusions: We present an in-depth analysis of the synovial fluid proteome from patients with osteoarthritis. We believe that the catalog of proteins generated in this study will further enhance our knowledge regarding the pathophysiology of osteoarthritis and should assist in identifying better biomarkers for early diagnosis. © 2014 Balakrishnan et al.; licensee BioMed Central Ltd.
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