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dc.contributor.authorRombouts, Yoann
dc.contributor.authorJónasdóttir, Hulda S
dc.contributor.authorHipgrave Ederveen, Agnes L
dc.contributor.authorReiding, Karli R
dc.contributor.authorJansen, Bas C
dc.contributor.authorFreysdottir, Jona
dc.contributor.authorHardardottir, Ingibjörg
dc.contributor.authorIoan-Facsinay, Andreea
dc.contributor.authorGiera, Martin
dc.contributor.authorWuhrer, Manfred
dc.date.accessioned2016-07-01T15:53:23Z
dc.date.available2016-07-01T15:53:23Z
dc.date.issued2016-06
dc.date.submitted2016
dc.identifier.citationAcute phase inflammation is characterized by rapid changes in plasma/peritoneal fluid N-glycosylation in mice. 2016, 33 (3):457-70 Glycoconj. J.en
dc.identifier.issn1573-4986
dc.identifier.pmid26924641
dc.identifier.doi10.1007/s10719-015-9648-9
dc.identifier.urihttp://hdl.handle.net/2336/615376
dc.descriptionTo access publisher's full text version of this article, please click on the hyperlink in Additional Links field or click on the hyperlink at the top of the page marked Files. This article is open access.en
dc.description.abstractMurine zymosan-induced peritonitis is a widely used model for studying the molecular and cellular events responsible for the initiation, persistence and/or resolution of inflammation. Among these events, it is becoming increasingly evident that changes in glycosylation of proteins, especially in the plasma and at the site of inflammation, play an important role in the inflammatory response. Using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF-MS)-based glycosylation profiling, we investigated the qualitative and quantitative effect of zymosan-induced peritonitis on N-glycosylation in mouse plasma and peritoneal fluid. Our results show that both N-glycomes exhibit highly similar glycosylation patterns, consisting mainly of diantennary and triantennary complex type N-glycans with high levels (>95 %) of galactosylation and sialylation (mostly NeuGc) and a medium degree of core fucosylation (30 %). Moreover, MS/MS structural analysis, assisted by linkage-specific derivatization of sialic acids, revealed the presence of O-acetylated sialic acids as well as disialylated antennae ("branching sialylation") characterized by the presence of α2-6-linked NeuGc on the GlcNAc of the NeuGcα2-3-Galβ1-3-GlcNAc terminal motif. A significant decrease of (core) fucosylation together with an increase of both α2-3-linked NeuGc and "branching sialylation" were observed in N-glycomes of mice challenged with zymosan, but not in control mice injected with PBS. Importantly, substantial changes in glycosylation were already observed 12 h after induction of peritonitis, thereby demonstrating an unexpected velocity of the biological mechanisms involved.
dc.description.sponsorshipDutch Arthritis Association (Reumafonds) LLP-24 Innovative Medicines Initiative Joint Undertaking (IMI JU)/ 115142-2 Netherlands Genomic Initiative/93511033 info:eu-repo/grantAgreement/EC/FP7/278535en
dc.description.sponsorshipinfo:eu-repo/grantAgreement/EC/FP7/278535en
dc.language.isoenen
dc.publisherSpringeren
dc.relationinfo:eu-repo/grantAgreement/EC/FP7/278535en
dc.relation.urlhttp://dx.doi.org/ 10.1007/s10719-015-9648-9en
dc.relation.urlhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC4891370/en
dc.rightsopenAccessen
dc.subjectNAF12
dc.subjectAAI12
dc.subjectRHE12
dc.subject.meshMiceen
dc.subject.meshCongenital Disorders of Glycosylationen
dc.subject.meshAscitic Fluiden
dc.subject.meshPlasmaen
dc.subject.meshPeritonitisen
dc.titleAcute phase inflammation is characterized by rapid changes in plasma/peritoneal fluid N-glycosylation in mice.en
dc.typearticleen
dc.contributor.department[ 1 ] Leiden Univ, Med Ctr, Ctr Prote & Metab, Leiden, Netherlands [ 2 ] Leiden Univ, Dept Rheumatol, Med Ctr, Leiden, Netherlands [ 3 ] Univ Toulouse, CNRS, UPS, Inst Pharmacol & Biol Struct, Toulouse, France [ 4 ] Univ Iceland, Fac Med, Biomed Ctr, Sch Hlth Sci, Reykjavik, Iceland [ 5 ] Landspitali Natl Univ Hosp Iceland, Dept Immunol, Reykjavik, Iceland [ 6 ] Landspitali Natl Univ Hosp Iceland, Ctr Rheumatol Res, Reykjavik, Iceland [ 7 ] Vrije Univ Amsterdam, Div BioAnalyt Chem, Amsterdam, Netherlandsen
dc.identifier.journalGlycoconjugate journalen
dc.rights.accessOpen Access - Opinn aðganguren
refterms.dateFOA2018-09-12T16:06:02Z
html.description.abstractMurine zymosan-induced peritonitis is a widely used model for studying the molecular and cellular events responsible for the initiation, persistence and/or resolution of inflammation. Among these events, it is becoming increasingly evident that changes in glycosylation of proteins, especially in the plasma and at the site of inflammation, play an important role in the inflammatory response. Using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF-MS)-based glycosylation profiling, we investigated the qualitative and quantitative effect of zymosan-induced peritonitis on N-glycosylation in mouse plasma and peritoneal fluid. Our results show that both N-glycomes exhibit highly similar glycosylation patterns, consisting mainly of diantennary and triantennary complex type N-glycans with high levels (>95 %) of galactosylation and sialylation (mostly NeuGc) and a medium degree of core fucosylation (30 %). Moreover, MS/MS structural analysis, assisted by linkage-specific derivatization of sialic acids, revealed the presence of O-acetylated sialic acids as well as disialylated antennae ("branching sialylation") characterized by the presence of α2-6-linked NeuGc on the GlcNAc of the NeuGcα2-3-Galβ1-3-GlcNAc terminal motif. A significant decrease of (core) fucosylation together with an increase of both α2-3-linked NeuGc and "branching sialylation" were observed in N-glycomes of mice challenged with zymosan, but not in control mice injected with PBS. Importantly, substantial changes in glycosylation were already observed 12 h after induction of peritonitis, thereby demonstrating an unexpected velocity of the biological mechanisms involved.


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