Detection of immunoglobulin G glycosylation changes in patients with rheumatoid arthritis by means of isoelectric focusing and lectin-affinoblotting.
Patients with rheumatoid arthritis have a reduced prevalence of immunoglobulin G (IgG) oligosaccharide chains terminating in galactose, thus exposing N-acetylglucosamine. We analyzed IgG glycosylation in patients with rheumatoid arthritis, patients with early synovitis, and in controls by means of isoelectric focusing and lectin-affinoblotting. The ratio of N-terminal N-acetylglucosamine and galactose was determined using specific biotin-labeled lectins. The IgG glycosylation state may well be of clinical value in the differential diagnosis of patients presenting with early synovitis.
Hänsler
M
M
Department of Rheumatology, Leipzig University, Germany.
Kötz
K
K
Häntzschel
H
H
D001172:Arthritis, Rheumatoid / Q000276:immunology*; D004591:Electrophoresis, Polyacrylamide Gel / Q000379:methods; D006031:Glycosylation; D006801:Humans; D015151:Immunoblotting / Q000379:methods*; D007074:Immunoglobulin G / Q000378:metabolism*; D007525:Isoelectric Focusing / Q000379:methods*; D037102:Lectins; D037121:Plant Lectins; D012276:Ricin; D013585:Synovitis / Q000276:immunology
C045475:Griffonia simplicifolia lectins; D007074:Immunoglobulin G; D037102:Lectins; D037121:Plant Lectins; D012276:Ricin