Insights into the effects of N-glycosylation on the characteristics of the VC1 domain of the human receptor for advanced glycation end products (RAGE) secreted by Pichia pastoris.
LC/mass spectrometry
Pichia pastoris
Protein glycoforms
Protein-protein interactions
Receptor for advanced glycation end products (RAGE)
Released glycan profiling
Thermal stability
Journal
Glycoconjugate journal
ISSN: 1573-4986
Titre abrégé: Glycoconj J
Pays: United States
ID NLM: 8603310
Informations de publication
Date de publication:
02 2019
02 2019
Historique:
received:
10
08
2018
accepted:
18
12
2018
revised:
23
11
2018
pubmed:
7
1
2019
medline:
30
5
2019
entrez:
7
1
2019
Statut:
ppublish
Résumé
Advanced glycation end products (AGEs) and advanced lipoxidation end products (ALEs), resulting from non-enzymatic modifications of proteins, are potentially harmful to human health. They directly act on proteins, affecting structure and function, or through receptor-mediated mechanisms. RAGE, a type I transmembrane glycoprotein, was identified as a receptor for AGEs. RAGE is involved in chronic inflammation, oxidative stress-based diseases and ageing. The majority of RAGE ligands bind to the VC1 domain. This domain was successfully expressed and secreted by Pichia pastoris. Out of two N-glycosylation sites, one (Asn25) was fully occupied while the other (Asn81) was under-glycosylated, generating two VC1 variants, named p36 and p34. Analysis of N-glycans and of their influence on VC1 properties were here investigated. The highly sensitive procainamide labeling method coupled to ES-MS was used for N-glycan profiling. N-glycans released from VC1 ranged from Man
Identifiants
pubmed: 30612271
doi: 10.1007/s10719-018-09855-x
pii: 10.1007/s10719-018-09855-x
doi:
Substances chimiques
Polysaccharides
0
Receptor for Advanced Glycation End Products
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
27-38Références
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