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SummaryTo determine the abnormal glycosylation patterns of IgG in patients with rheumatoid arthritis (RA), we analyzed these oligosaccharide profiles using a recently established high-performance liquid chromatography (HPLC) method. Oligosaccharides of IgG proteins purified from sera of RA patients were labeled with a fluorescent reagent, 2-aminopyridine. The oligosaccharide derivatives were separated into 12 peaks by HPLC, and compared with those of age-matched controls. Serum IgG from patients with RA (RA-IgG) contained a higher content of oligosaccharides with bisecting GlcNAc than normal IgG, which was accompanied by an increase in the glycosylation of the bisected oligosaccharides. The ratio of the glycosylation of bisected to nonbisected oligosaccharides correlated with RA disease activity as well as with its clinical markers. This ratio reflecting the balance of glycosylation between bisected and nonbisected oligosaccharides may be a useful clinical parameter to monitor RA activity.

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