ERO1 alpha deficiency impairs angiogenesis by increasing N-glycosylation of a proangiogenic VEGFA.
Angiogenesis
ERO1 alpha
N-glycosylation
Oxidative folding
VEGFA
Journal
Redox biology
ISSN: 2213-2317
Titre abrégé: Redox Biol
Pays: Netherlands
ID NLM: 101605639
Informations de publication
Date de publication:
10 2022
10 2022
Historique:
received:
18
07
2022
revised:
16
08
2022
accepted:
22
08
2022
pubmed:
6
9
2022
medline:
28
9
2022
entrez:
5
9
2022
Statut:
ppublish
Résumé
N-glycosylation and disulfide bond formation are two essential steps in protein folding that occur in the endoplasmic reticulum (ER) and reciprocally influence each other. Here, to analyze crosstalk between N-glycosylation and oxidation, we investigated how the protein disulfide oxidase ERO1-alpha affects glycosylation of the angiogenic VEGF
Identifiants
pubmed: 36063727
pii: S2213-2317(22)00227-0
doi: 10.1016/j.redox.2022.102455
pmc: PMC9463388
pii:
doi:
Substances chimiques
Disulfides
0
Lectins
0
Membrane Glycoproteins
0
VEGFA protein, human
0
Vascular Endothelial Growth Factor A
0
Thioredoxins
52500-60-4
ERO1A protein, human
EC 1.-
Oxidoreductases
EC 1.-
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
102455Informations de copyright
Copyright © 2022 The Authors. Published by Elsevier B.V. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of competing interest The authors declare no conflicting interests.