Increasing Complexity of the N-Glycome During Caenorhabditis Development.
fucose
galactose
glycomics
mass spectrometry
phosphorylcholine
Journal
Molecular & cellular proteomics : MCP
ISSN: 1535-9484
Titre abrégé: Mol Cell Proteomics
Pays: United States
ID NLM: 101125647
Informations de publication
Date de publication:
03 2023
03 2023
Historique:
received:
05
10
2022
revised:
06
01
2023
accepted:
24
01
2023
medline:
28
3
2023
pubmed:
31
1
2023
entrez:
30
1
2023
Statut:
ppublish
Résumé
Caenorhabditis elegans is a frequently employed genetic model organism and has been the object of a wide range of developmental, genetic, proteomic, and glycomic studies. Here, using an off-line MALDI-TOF-MS approach, we have analyzed the N-glycans of mixed embryos and liquid- or plate-grown L4 larvae. Of the over 200 different annotatable N-glycan structures, variations between the stages as well as the mode of cultivation were observed. While the embryonal N-glycome appears less complicated overall, the liquid- and plate-grown larvae differ especially in terms of methylation of bisecting fucose, α-galactosylation of mannose, and di-β-galactosylation of core α1,6-fucose. Furthermore, we analyzed the O-glycans by LC-electrospray ionization-MS following β-elimination; especially the embryonal O-glycomes included a set of phosphorylcholine-modified structures, previously not shown to exist in nematodes. However, the set of glycan structures cannot be clearly correlated with levels of glycosyltransferase transcripts in developmental RNA-Seq datasets, but there is an indication for coordinated expression of clusters of potential glycosylation-relevant genes. Thus, there are still questions to be answered in terms of how and why a simple nematode synthesizes such a diverse glycome.
Identifiants
pubmed: 36717059
pii: S1535-9476(23)00014-2
doi: 10.1016/j.mcpro.2023.100505
pmc: PMC7614267
mid: EMS170519
pii:
doi:
Substances chimiques
Fucose
28RYY2IV3F
Polysaccharides
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
100505Subventions
Organisme : Austrian Science Fund FWF
ID : P 29466
Pays : Austria
Organisme : Austrian Science Fund FWF
ID : P 30021
Pays : Austria
Organisme : Austrian Science Fund FWF
ID : TRP 127
Pays : Austria
Organisme : Austrian Science Fund FWF
ID : P 23922
Pays : Austria
Organisme : Austrian Science Fund FWF
ID : W 1224
Pays : Austria
Organisme : Austrian Science Fund FWF
ID : P 32572
Pays : Austria
Informations de copyright
Copyright © 2023 The Authors. Published by Elsevier Inc. All rights reserved.
Déclaration de conflit d'intérêts
Conflict of interest The authors declare no competing interests.