Role of amelogenin phosphorylation in regulating dental enamel formation.
Acidification
amelogenesis
amelogenin
biomineralization
enamel
protein phosphorylation
Journal
Matrix biology : journal of the International Society for Matrix Biology
ISSN: 1569-1802
Titre abrégé: Matrix Biol
Pays: Netherlands
ID NLM: 9432592
Informations de publication
Date de publication:
15 May 2024
15 May 2024
Historique:
received:
21
03
2024
revised:
08
05
2024
accepted:
14
05
2024
medline:
18
5
2024
pubmed:
18
5
2024
entrez:
17
5
2024
Statut:
aheadofprint
Résumé
Amelogenin (AMELX), the predominant matrix protein in enamel formation, contains a singular phosphorylation site at Serine 16 (S16) that greatly enhances AMELX's capacity to stabilize amorphous calcium phosphate (ACP) and inhibit its transformation to apatitic enamel crystals. To explore the potential role of AMELX phosphorylation in vivo, we developed a knock-in (KI) mouse model in which AMELX phosphorylation is prevented by substituting S16 with Ala (A). As anticipated, AMELX
Identifiants
pubmed: 38759902
pii: S0945-053X(24)00065-9
doi: 10.1016/j.matbio.2024.05.004
pii:
doi:
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Informations de copyright
Copyright © 2024. Published by Elsevier B.V.