Impact of ATP-citrate lyase catalytic activity and serine 455 phosphorylation on histone acetylation and inflammatory responses in human monocytic THP-1 cells.
ATP-citrate lyase
histone acetylation
inflammation
macrophages
metabolism
Journal
Frontiers in immunology
ISSN: 1664-3224
Titre abrégé: Front Immunol
Pays: Switzerland
ID NLM: 101560960
Informations de publication
Date de publication:
2022
2022
Historique:
received:
28
03
2022
accepted:
26
10
2022
entrez:
28
11
2022
pubmed:
29
11
2022
medline:
30
11
2022
Statut:
epublish
Résumé
ATP-citrate lyase (ACLY) is a key enzyme provoking metabolic and epigenetic gene regulation. Molecularly, these functions are exerted by the provision of acetyl-coenzyme A, which is then used as a substrate for
Identifiants
pubmed: 36439127
doi: 10.3389/fimmu.2022.906127
pmc: PMC9686385
doi:
Substances chimiques
Histones
0
Serine
452VLY9402
Proto-Oncogene Proteins c-akt
EC 2.7.11.1
Lipopolysaccharides
0
citrate (pro-3S)-lyase
EC 4.1.3.6
ATP Citrate (pro-S)-Lyase
EC 2.3.3.8
Adenosine Triphosphate
8L70Q75FXE
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
906127Informations de copyright
Copyright © 2022 Dominguez, Truemper, Mota, Brüne and Namgaladze.
Déclaration de conflit d'intérêts
The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest.
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