Lentil lectin-bound glycoproteins of cultured rheumatoid synovial cells.
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.
D000328:Adult; D000368:Aged; D001172:Arthritis, Rheumatoid / Q000378:metabolism* / Q000473:pathology; D001799:Blood Sedimentation; D002462:Cell Membrane / Q000378:metabolism; D002478:Cells, Cultured; D002846:Chromatography, Affinity; D004586:Electrophoresis; D005260:Female; D006023:Glycoproteins / Q000302:isolation & purification*; D006801:Humans; D037102:Lectins / Q000494:pharmacology*; D008297:Male; D008875:Middle Aged; D008970:Molecular Weight; D037121:Plant Lectins; D011485:Protein Binding; D013583:Synovial Membrane / Q000378:metabolism* / Q000473:pathology; D013585:Synovitis / Q000378:metabolism* / Q000473:pathology
D006023:Glycoproteins; D037102:Lectins; D037121:Plant Lectins; C033619:lentil lectin