Characterization of IgG glycosylation in rheumatoid arthritis patients by MALDI-TOF-MSn and capillary electrophoresis
0301 basic medicine
Glycosylation
Electrophoresis, Capillary
Galactose
Middle Aged
3. Good health
Arthritis, Rheumatoid
03 medical and health sciences
Isomerism
Polysaccharides
Immunoglobulin G
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Humans
DOI:
10.1007/s00216-017-0302-1
Publication Date:
2017-04-10T10:07:56Z
AUTHORS (5)
ABSTRACT
An analytical method based on the combination of multistage mass spectrometry (MSn) 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-MSn), and quantitation by CE. Assignment of the IgG N-glycan structures was made through branching pattern analysis by MSn 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 MSn 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-MSn and capillary electrophoresis.
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