Characterization of IgG glycosylation in rheumatoid arthritis patients by MALDI-TOF-MS and capillary electrophoresis.

An analytical method based on the combination of multistage mass spectrometry (MS) and capillary electrophoresis (CE) was developed for the analysis of immunoglobulin G (IgG) glycosylation in rheumatoid arthritis (RA) patients. It has been recently suggested that IgG glycosylation defect may be involved in RA immunopathogenesis. Complete characterization of glycans, including both qualitative and quantitative analysis, requires a combination of different techniques, and accurate, robust, sensitive, and high-throughput methodologies are important for analysis of clinical samples. In the present study, N-glycosylation of IgG in RA patients and in healthy people was characterized through identification of the released glycans using multistage matrix-assisted laser desorption/ionization time of flight mass spectrometry (MALDI-TOF-MS), and quantitation by CE. Assignment of the IgG N-glycan structures was made through branching pattern analysis by MS with high-throughput. Further accurate quantitation indicated that galactosylation and sialylation of IgG N-glycans in RA cases were significantly lower than in healthy subjects. The results indicate that CE coupled with MS can identify abnormal glycosylation of IgG in RA patients compared with healthy people, and that the present work is useful for RA mechanism studies and RA diagnosis. Graphical Abstract Qualitative and quantitative analysis of IgG glycosylation in rheumatoid arthritis patients by MALDI-TOF-MS and capillary electrophoresis.