Isoform-specific Inhibition of N-methyl-D-aspartate Receptors by Bile Salts.
Allosteric Regulation
Animals
Bile Acids and Salts
/ metabolism
Chenodeoxycholic Acid
/ metabolism
Cloning, Molecular
Computer Simulation
Hydrogen Bonding
Models, Molecular
Mutagenesis, Site-Directed
Mutation
/ genetics
Protein Binding
Protein Conformation
Protein Isoforms
/ genetics
Receptors, N-Methyl-D-Aspartate
/ chemistry
Signal Transduction
Structure-Activity Relationship
Xenopus laevis
Journal
Scientific reports
ISSN: 2045-2322
Titre abrégé: Sci Rep
Pays: England
ID NLM: 101563288
Informations de publication
Date de publication:
11 07 2019
11 07 2019
Historique:
received:
28
01
2019
accepted:
18
06
2019
entrez:
13
7
2019
pubmed:
13
7
2019
medline:
11
11
2020
Statut:
epublish
Résumé
The N-methyl-D-aspartate subfamily of ionotropic glutamate receptors (NMDARs) is well known for its important roles in the central nervous system (CNS), e.g. learning and memory formation. Besides the CNS, NMDARs are also expressed in numerous peripheral tissues including the pancreas, kidney, stomach, and blood cells, where an understanding of their physiological and pathophysiological roles is only evolving. Whereas subunit composition increases functional diversity of NMDARs, a great number of endogenous cues tune receptor signaling. Here, we characterized the effects of the steroid bile salts cholate and chenodeoxycholate (CDC) on recombinantly expressed NMDARs of defined molecular composition. CDC inhibited NMDARs in an isoform-dependent manner, preferring GluN2D and GluN3B over GluN2A and GluN2B receptors. Determined IC
Identifiants
pubmed: 31296930
doi: 10.1038/s41598-019-46496-y
pii: 10.1038/s41598-019-46496-y
pmc: PMC6624251
doi:
Substances chimiques
Bile Acids and Salts
0
NR2B NMDA receptor
0
Protein Isoforms
0
Receptors, N-Methyl-D-Aspartate
0
Chenodeoxycholic Acid
0GEI24LG0J
N-methyl D-aspartate receptor subtype 2A
VH92ICR8HX
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
10068Références
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