겨울 심포지움
2018겨울초록
발표자 및 발표 내용
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공동저자
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Mouse has been used as an animal model for scientific research owing to its physiological similarity to human. However, their N- and O-glycosylation of glycoproteins showed many differences between mouse and human. Usually glycosylation is directly involved in various biological process and plays crucial role in human diseases due to their unusual biological sensitivity. Therefore, the site-specific characterization of glycosylation in model mouse is necessary in order to investigate progression of disease.
This study provided comparison of the site-specific N- and O-glycosylation between human and mouse plasma using LC-MS/MS with I-GPA (Integrated GlycoProteome Analyzer) search system1. The site-specific glycosylation between human and mouse has three differences in plasma. First, the sialic acid of N- and O-glycopeptides was almost entirely Neu5Gc in mouse plasma, while in human plasma was Neu5Ac. Second, O-acetylated NeuGc of N-glycopeptides was identified in mouse plasma only. Third, antennal HexNAc-NeuGc of N-glycopeptides was specifically identified from several glycoproteins in mouse plasma only. In conclusion, our study has provided a comprehensive overview of the site-specific N- and O-glycosylation of human and mouse in plasma.
Reference
1. Gun Wook Park and Jin Young Kim et al., Scientific Reports, 6:21175 (2016)
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