Lentil Lectin-Bound Glycoproteins of Cultured Rheumatoid Synovial Cells

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Abstract
Synovial cell lines were cultured from 5 rheumatoid arthritis (RA) patients, from 4 patients with other synovial inflammation and from 4 non-inflammatory controls. Protein synthesis was studied by [35S]methionine labelling. Glycoproteins containing D-glucose or D-mannose were separated by affinity chromatography with immobilized lentil lectin and analysed by SDS-electrophoresis in polyacrylamide gradient gels (SDS-gradient PAGE). About 12% of labelled protein was bound to the lectin column (range 7.9-20.0%). Proteins of RA cells showed no differences in binding compared with proteins of the reference cells. At least 40 glycoproteins were separated by SDS-gradient PAGE. No new or missing bands were observed in RA cells, but several quantitative changes and microheterogeneity of some polypeptide molecular weights were noted.