Site-Specific N- and O-Glycosylation Analysis of Human Plasma Fibronectin
dc.contributor.author | Liu, Ding | |
dc.contributor.author | Wang, Shuaishuai | |
dc.contributor.author | Zhang, Junping | |
dc.contributor.author | Xiao, Weidong | |
dc.contributor.author | Miao, Carol H. | |
dc.contributor.author | Konkle, Barbara A. | |
dc.contributor.author | Wan, Xiu-Feng | |
dc.contributor.author | Li, Lei | |
dc.contributor.department | Pediatrics, School of Medicine | |
dc.date.accessioned | 2024-04-01T13:48:22Z | |
dc.date.available | 2024-04-01T13:48:22Z | |
dc.date.issued | 2021-06-15 | |
dc.description.abstract | Human plasma fibronectin is an adhesive protein that plays a crucial role in wound healing. Many studies had indicated that glycans might mediate the expression and functions of fibronectin, yet a comprehensive understanding of its glycosylation is still missing. Here, we performed a comprehensive N- and O-glycosylation mapping of human plasma fibronectin and quantified the occurrence of each glycoform in a site-specific manner. Intact N-glycopeptides were enriched by zwitterionic hydrophilic interaction chromatography, and N-glycosite sites were localized by the 18O-labeling method. O-glycopeptide enrichment and O-glycosite identification were achieved by an enzyme-assisted site-specific extraction method. An RP–LC–MS/MS system functionalized with collision-induced dissociation and stepped normalized collision energy (sNCE)-HCD tandem mass was applied to analyze the glycoforms of fibronectin. A total of 6 N-glycosites and 53 O-glycosites were identified, which were occupied by 38 N-glycoforms and 16 O-glycoforms, respectively. Furthermore, 77.31% of N-glycans were sialylated, and O-glycosylation was dominated by the sialyl-T antigen. These site-specific glycosylation patterns on human fibronectin can facilitate functional analyses of fibronectin and therapeutics development. | |
dc.eprint.version | Final published version | |
dc.identifier.citation | Liu D, Wang S, Zhang J, et al. Site-Specific N- and O-Glycosylation Analysis of Human Plasma Fibronectin. Front Chem. 2021;9:691217. Published 2021 Jun 15. doi:10.3389/fchem.2021.691217 | |
dc.identifier.uri | https://hdl.handle.net/1805/39650 | |
dc.language.iso | en_US | |
dc.publisher | Frontiers Media | |
dc.relation.isversionof | 10.3389/fchem.2021.691217 | |
dc.relation.journal | Frontiers in Chemistry | |
dc.rights | Attribution 4.0 International | en |
dc.rights.uri | http://creativecommons.org/licenses/by/4.0/ | |
dc.source | PMC | |
dc.subject | Fibronectin | |
dc.subject | Glycosylation | |
dc.subject | Mass spectrometer | |
dc.subject | Operator | |
dc.subject | Stepped normalized collision energy | |
dc.title | Site-Specific N- and O-Glycosylation Analysis of Human Plasma Fibronectin | |
dc.type | Article |