Acute phase inflammation is characterized by rapid changes in plasma/peritoneal fluid N-glycosylation in mice.
Cast your vote
You can rate an item by clicking the amount of stars they wish to award to this item.
When enough users have cast their vote on this item, the average rating will also be shown.
Your vote was cast
Thank you for your feedback
Thank you for your feedback
Jónasdóttir, Hulda S
Hipgrave Ederveen, Agnes L
Reiding, Karli R
Jansen, Bas C
MetadataShow full item record
CitationAcute phase inflammation is characterized by rapid changes in plasma/peritoneal fluid N-glycosylation in mice. 2016, 33 (3):457-70 Glycoconj. J.
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.
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.
- Advanced mass spectrometry and chemical analyses reveal the presence of terminal disialyl motif on mouse B-cell glycoproteins.
- Authors: Wang SH, Tsai CM, Lin KI, Khoo KH
- Issue date: 2013 Jun
- Murine Plasma N-Glycosylation Traits Associated with Sex and Strain.
- Authors: Reiding KR, Hipgrave Ederveen AL, Rombouts Y, Wuhrer M
- Issue date: 2016 Oct 7
- Effluent and serum protein N-glycosylation is associated with inflammation and peritoneal membrane transport characteristics in peritoneal dialysis patients.
- Authors: Ferrantelli E, Farhat K, Ederveen ALH, Reiding KR, Beelen RHJ, van Ittersum FJ, Wuhrer M, Dotz V
- Issue date: 2018 Jan 17
- Plasma protein N-glycan signatures of type 2 diabetes.
- Authors: Dotz V, Lemmers RFH, Reiding KR, Hipgrave Ederveen AL, Lieverse AG, Mulder MT, Sijbrands EJG, Wuhrer M, van Hoek M
- Issue date: 2018 Dec
- Methods in enzymology: O-glycosylation of proteins.
- Authors: Peter-Katalinić J
- Issue date: 2005