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The synovial proteome: analysis of fibroblast-like synoviocytes

Kumar Dasuri1, Mihaela Antonovici2, Keding Chen1, Ken Wong1, Kenneth Standing23, Werner Ens23, Hani El-Gabalawy1 and John A Wilkins123*

Author Affiliations

1 Rheumatic Diseases Research Laboratory, University of Manitoba, Winnipeg, Canada

2 Manitoba Centre for Proteomics, Department of Medicine, University of Manitoba, Winnipeg, Canada

3 Time of Flight Laboratory, Department of Physics and Astronomy, University of Manitoba, Winnipeg, Canada

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Arthritis Res Ther 2004, 6:R161-R168  doi:10.1186/ar1153

Published: 16 February 2004


The present studies were initiated to determine the protein expression patterns of fibroblast-like synovial (FLS) cells derived from the synovia of rheumatoid arthritis patients. The cellular proteins were separated by two-dimensional polyacrylamide gel electrophoresis and the in-gel digested proteins were analyzed by matrix-assisted laser desorption ionization mass spectrometry. A total of 368 spots were examined and 254 identifications were made. The studies identified a number of proteins that have been implicated in the normal or pathological FLS function (e.g. uridine diphosphoglucose dehydrogenase, galectin 1 and galectin 3) or that have been characterized as potential autoantigens in rheumatoid arthritis (e.g. BiP, colligin, HC gp-39). A novel uncharacterized protein product of chromosome 19 open reading frame 10 was also detected as an apparently major component of FLS cells. These results demonstrate the utility of high-content proteomic approaches in the analysis of FLS composition.

autoantigens; fibroblast-like synovial cells; galectins; matrix-assisted laser desorption ionization mass spectrometry; proteomics