Proteasomal degradation of the histone acetyl transferase p300 contributes to beta-cell injury in a diabetes environment

Détails

ID Serval
serval:BIB_91A24FC7CF15
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Proteasomal degradation of the histone acetyl transferase p300 contributes to beta-cell injury in a diabetes environment
Périodique
Cell Death & Disease
Auteur⸱e⸱s
Ruiz L., Gurlo T., Ravier M. A., Wojtusciszyn A., Mathieu J., Brown M. R., Broca C., Bertrand G., Butler P. C., Matveyenko A. V., Dalle S., Costes S.
ISSN
2041-4889
Statut éditorial
Publié
Date de publication
2018
Volume
9
Langue
anglais
Notes
Gh0la
Times Cited:4
Cited References Count:61
Résumé
In type 2 diabetes, amyloid oligomers, chronic hyperglycemia, lipotoxicity, and pro-inflammatory cytokines are detrimental to beta-cells, causing apoptosis and impaired insulin secretion. The histone acetyl transferase p300, involved in remodeling of chromatin structure by epigenetic mechanisms, is a key ubiquitous activator of the transcriptional machinery. In this study, we report that loss of p300 acetyl transferase activity and expression leads to beta-cell apoptosis, and most importantly, that stress situations known to be associated with diabetes alter p300 levels and functional integrity. We found that proteasomal degradation is the mechanism subserving p300 loss in beta-cells exposed to hyperglycemia or pro-inflammatory cytokines. We also report that melatonin, a hormone produced in the pineal gland and known to play key roles in beta-cell health, preserves p300 levels altered by these toxic conditions. Collectively, these data imply an important role for p300 in the pathophysiology of diabetes.
Mots-clé
endoplasmic-reticulum stress, rubinstein-taybi-syndrome, islet-amyloid-polypeptide, activated protein-kinase, oxidative stress, binding protein, gene-expression, p38 mapk, melatonin, apoptosis
Web of science
Création de la notice
14/06/2021 9:59
Dernière modification de la notice
18/09/2021 6:38
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