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dc.contributor.authorStavenhagen, Kathrin
dc.contributor.authorKayili, H. Mehmet
dc.contributor.authorHolst, Stephanie
dc.contributor.authorKoeleman, Carolien A. M.
dc.contributor.authorEngel, Ruchira
dc.contributor.authorWouters, Diana
dc.contributor.authorZeerleder, Sacha
dc.contributor.authorSalih, Bekir
dc.contributor.authorWuhrer, Manfred
dc.date.accessioned2019-12-16T09:19:13Z
dc.date.available2019-12-16T09:19:13Z
dc.date.issued2018
dc.identifier.issn1535-9476
dc.identifier.urihttps://doi.org/10.1074/mcp.RA117.000240
dc.identifier.urihttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5986245/
dc.identifier.urihttp://hdl.handle.net/11655/19637
dc.description.abstractHuman C1-inhibitor (C1-Inh) is a serine protease inhibitor and the major regulator of the contact activation pathway as well as the classical and lectin complement pathways. It is known to be a highly glycosylated plasma glycoprotein. However, both the structural features and biological role of C1-Inh glycosylation are largely unknown. Here, we performed for the first time an in-depth site-specific N- and O-glycosylation analysis of C1-Inh combining various mass spectrometric approaches, including C18-porous graphitized carbon (PGC)-LC-ESI-QTOF-MS/MS applying stepping-energy collision-induced dissociation (CID) and electron-transfer dissociation (ETD). Various proteases were applied, partly in combination with PNGase F and exoglycosidase treatment, in order to analyze the (glyco)peptides. The analysis revealed an extensively O-glycosylated N-terminal region. Five novel and five known O-glycosylation sites were identified, carrying mainly core1-type O-glycans. In addition, we detected a heavily O-glycosylated portion spanning from Thr82-Ser121 with up to 16 O-glycans attached. Likewise, all known six N-glycosylation sites were covered and confirmed by this site-specific glycosylation analysis. The glycoforms were in accordance with results on released N-glycans by MALDI-TOF/TOF-MS/MS. The comprehensive characterization of C1-Inh glycosylation described in this study will form the basis for further functional studies on the role of these glycan modifications.
dc.relation.isversionof10.1074/mcp.RA117.000240
dc.rightsinfo:eu-repo/semantics/openAccess
dc.titleN- And O-Glycosylation Analysis Of Human C1-Inhibitor Reveals Extensive Mucin-Type O-Glycosylation
dc.typeinfo:eu-repo/semantics/article
dc.relation.journalMolecular & Cellular Proteomics : MCP
dc.contributor.departmentKimya
dc.identifier.volume17
dc.identifier.issue6
dc.identifier.startpage1225
dc.identifier.endpage1238
dc.description.indexPubMed
dc.description.indexWoS
dc.description.indexScopus


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