Structural and quantitative characterization of mucin-type O-glycans and the identification of Oglycosylation sites in bovine submaxillary mucin
- Authors
- Kim J.; Ryu C.; Ha J.; Lee J.; Kim D.; Ji M.; Park C.S.; Lee J.; Kim D.K.; Kim H.H.
- Issue Date
- Apr-2020
- Publisher
- MDPI AG
- Keywords
- Bovine submaxillary mucin; Mucin-type O-glycan; O-glycosylation site
- Citation
- Biomolecules, v.10, no.4
- Journal Title
- Biomolecules
- Volume
- 10
- Number
- 4
- URI
- https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/42748
- DOI
- 10.3390/biom10040636
- ISSN
- 2218-273X
2218-273X
- Abstract
- Bovine submaxillary mucin (BSM) is a gel-forming glycoprotein polymer, and Ser/Thr-linked glycans (O-glycans) are important in regulating BSM's viscoelasticity and polymerization. However, details of O-glycosylation have not been reported. This study investigates the structural and quantitative characteristics of O-glycans and identifies O-glycosylation sites in BSM using liquid chromatography-tandem mass spectrometry. The O-glycans (consisting of di- to octa-saccharides) and their quantities (%) relative to total O-glycans (100%; 1.1 pmol per 1μg of BSM) were identified with 14 major (>1.0%), 12 minor (0.1%-1.0%), and eight trace (<0.1%) O-glycans, which were characterized based on their constituents (sialylation (14 O-glycans; 81.9%, sum of relative quantities of each glycan), non-sialylation (20; 18.1%), fucosylation (20; 17.5%), and terminal-galactosylation (6; 3.6%)) and six core structure types [Gal-GalNAc, Gal-(GlcNAc)GalNAc, GlcNAc-GalNAc, GlcNAc-(GlcNAc)GalNAc, and GalNAc-GalNAc]. O-glycosylation sites were identified using O-glycopeptides (bold underlined;56SGETRTSVI,259SHSSSGRSRTI,272GSPSSVSSAEQI,307RPSYGAL,625QTLGPL,728TMTTRTSVVV, and1080RPEDNTAVA) obtained from proteolytic BSM; these sites are in the four domains of BSM. The gel-forming mucins share common domain structures and glycosylation patterns; these results could provide useful information on mucin-type O-glycans. This is the first study to characterize O-glycans and identify O-glycosylation sites in BSM. © 2020 by the authors. Licensee MDPI, Basel, Switzerland.
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