N-glycans of bovine submaxillary mucin contain core-fucosylated and sulfated glycans but not sialylated glycans
- Authors
- Kim, J.; Lee, J.; Jang, Y.; Ha, J.; Kim, D.; Ji, M.; Lee, Y.K.; Kim, W.; You, S.; Do, J.; Ryu, C.; Kim, H.H.
- Issue Date
- Oct-2019
- Publisher
- Elsevier B.V.
- Keywords
- Bovine submaxillary mucin; Glycosylation site; N-glycan analysis
- Citation
- International Journal of Biological Macromolecules, v.138, pp 1072 - 1078
- Pages
- 7
- Journal Title
- International Journal of Biological Macromolecules
- Volume
- 138
- Start Page
- 1072
- End Page
- 1078
- URI
- https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/36485
- DOI
- 10.1016/j.ijbiomac.2019.07.108
- ISSN
- 0141-8130
1879-0003
- Abstract
- Bovine submaxillary mucin (BSM) is a heavily-glycosylated macromolecular (approximately 4 MDa) protein and is used in various biomaterial applications in light of its high viscosity and biocompatibility, in addition to use as a biochemical substrate or inhibitor as a result of its abundant O-glycans. Although it has been reported that N-glycosylation provides stability of human mucins, most BSM research has been focused on its O-glycans, while N-glycans have not been reported to date. In this study, a common N-glycan core component was detected by monosaccharide analysis of BSM, and the structures of the N-glycans and their relative quantities were determined by liquid chromatography–tandem mass spectrometry. Seventeen N-glycans comprising ten complex-type [Fucose0~2Hexose3~4N-acetylhexosamine1~6Sulfate0~1; 61.1% (the sum of the relative quantities of each N-glycan out of the total N-glycans)], two high-mannose-type (Hexose5~6N-acetylhexosamine2; 12.0%), and five paucimannose type (Fucose0~1Hexose3~4N-acetylhexosamine2~3; 26.9%) were identified, but no hybrid-type or sialylated N-glycans were found. Additionally, these are less-branched structures compared to human mucins. Of these, ten glycans (77.2%), including two sulfated glycans (8.0%), were core fucosylated, which confer unique biological functions to glycoproteins. The N-glycosylation sites were identified from the analysis of glycopeptides from BSM. This study is the first confirmation of N-glycan attachment to BSM. © 2019 Elsevier B.V.
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