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FEBS Lett. 2015 Sep 14;589(19 Pt B):2776-83. doi: 10.1016/j.febslet.2015.08.009. Epub 2015 Aug 20.

Loss of histone deacetylase Hdac1 disrupts metabolic processes in intestinal epithelial cells.

Author information

1
Département d'anatomie et biologie cellulaire, Faculté de médecine et des sciences de la santé, Pavillon de recherche appliquée sur le cancer, Université de Sherbrooke, Sherbrooke, Québec J1E 4K8, Canada.
2
Département d'anatomie et biologie cellulaire, Faculté de médecine et des sciences de la santé, Pavillon de recherche appliquée sur le cancer, Université de Sherbrooke, Sherbrooke, Québec J1E 4K8, Canada. Electronic address: Claude.Asselin@USherbrooke.ca.

Abstract

By using acetyl-CoA as a substrate, acetyltransferases and histone deacetylases regulate protein acetylation by adding or removing an acetyl group on lysines. Nuclear-located Hdac1 is a regulator of intestinal homeostasis. We have previously shown that Hdac1 define specific intestinal epithelial cell basal and inflammatory-dependent gene expression patterns and control cell proliferation. We show here that Hdac1 depletion in cellulo leads to increased histone acetylation after metabolic stresses, and to metabolic disturbances resulting in impaired responses to oxidative stresses, AMPK kinase activation and mitochondrial biogenesis. Thus, nuclear Hdac1 may control intestinal epithelial cell metabolism by regulating the supply of acetyl groups.

KEYWORDS:

AMPK; Acetylation; Hdac1; Intestinal epithelial cell; Mitochondria; Reactive oxygen species

PMID:
26297832
DOI:
10.1016/j.febslet.2015.08.009
[Indexed for MEDLINE]
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