The synovial proteome: analysis of fibroblast-like synoviocytes |
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Authors: | Kumar?Dasuri Mihaela?Antonovici Keding?Chen Ken?Wong Kenneth?Standing Werner?Ens Hani?El-Gabalawy Email author" target="_blank">John?A?WilkinsEmail author |
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Institution: | (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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Abstract: | 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. |
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