期刊
JOURNAL OF PROTEOME RESEARCH
卷 9, 期 3, 页码 1367-1373出版社
AMER CHEMICAL SOC
DOI: 10.1021/pr900913k
关键词
mucin-type O-glycan; glycopeptide; mass spectrometry; quantitation; rheumatoid arthritis; galactose
资金
- Ministry Of Education, Culture, Sports, Science and Technology, Japan [19390093]
- Takeda Science Foundation
- Grants-in-Aid for Scientific Research [19390093] Funding Source: KAKEN
Profiling of oligosaccharide structures is widely utilized for both identification and evaluation of glycobiomarkers, and site-specific profiling of N-linked glycans of glycoproteins is conducted by mass spectrometry of glycopeptides. However, our knowledge of mucin-type O-glycans including site occupancy and profile variance, as well as attachment sites, is quite limited. Saccharide compositions and site-occupancy of O-glycans were calculated from the signal intensity of glycopeptide ions in the mass spectra and tandem mass spectra from electron transfer dissociation. The results for two major plasma glycoproteins, IgA1 and hemopexin, representing clustered and scattered O-glycan attachments, respectively, indicated that the variability in modifications among individuals is so small as to justify rigorous standards enabling reliable detection of disease-related alterations. Indeed, this method revealed a novel abnormality associated with rheumatoid arthritis: a significant decrease in the N-acetylgalactosamine content of IgA1 O-glycans, indicating that the glycosylation abnormality is not limited to hypogalactosylation of IgG N-glycans in chronic inflammatory conditions.
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