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Histone Acetylation Modifiers in the Pathogenesis of Alzheimer’s Disease

It is becoming more evident that histone acetylation, as one of the epigenetic modifications or markers, plays a key role in the etiology of Alzheimer’s disease (AD). Histone acetylases and histone deacetylases (HDACs) are the well-known covalent enzymes that modify the reversible acetylation of lys...

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Autores principales: Lu, Xi, Wang, Li, Yu, Caijia, Yu, Daohai, Yu, Gang
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4468862/
https://www.ncbi.nlm.nih.gov/pubmed/26136662
http://dx.doi.org/10.3389/fncel.2015.00226
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author Lu, Xi
Wang, Li
Yu, Caijia
Yu, Daohai
Yu, Gang
author_facet Lu, Xi
Wang, Li
Yu, Caijia
Yu, Daohai
Yu, Gang
author_sort Lu, Xi
collection PubMed
description It is becoming more evident that histone acetylation, as one of the epigenetic modifications or markers, plays a key role in the etiology of Alzheimer’s disease (AD). Histone acetylases and histone deacetylases (HDACs) are the well-known covalent enzymes that modify the reversible acetylation of lysine residues in histone amino-terminal domains. In AD, however, the roles of these enzymes are controversial. Some recent studies indicate that HDAC inhibitors are neuroprotective by regulating memory and synaptic dysfunctions in cellular and animal models of AD; while on the other hand, increase of histone acetylation have been implicated in AD pathology. In this review, we focus on the recent advances on the roles of histone acetylation covalent enzymes in AD and discuss how targeting these enzymes can ultimately lead to therapeutic approaches for treating AD.
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spelling pubmed-44688622015-07-01 Histone Acetylation Modifiers in the Pathogenesis of Alzheimer’s Disease Lu, Xi Wang, Li Yu, Caijia Yu, Daohai Yu, Gang Front Cell Neurosci Neuroscience It is becoming more evident that histone acetylation, as one of the epigenetic modifications or markers, plays a key role in the etiology of Alzheimer’s disease (AD). Histone acetylases and histone deacetylases (HDACs) are the well-known covalent enzymes that modify the reversible acetylation of lysine residues in histone amino-terminal domains. In AD, however, the roles of these enzymes are controversial. Some recent studies indicate that HDAC inhibitors are neuroprotective by regulating memory and synaptic dysfunctions in cellular and animal models of AD; while on the other hand, increase of histone acetylation have been implicated in AD pathology. In this review, we focus on the recent advances on the roles of histone acetylation covalent enzymes in AD and discuss how targeting these enzymes can ultimately lead to therapeutic approaches for treating AD. Frontiers Media S.A. 2015-06-16 /pmc/articles/PMC4468862/ /pubmed/26136662 http://dx.doi.org/10.3389/fncel.2015.00226 Text en Copyright © 2015 Lu, Wang, Yu, Yu and Yu. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Neuroscience
Lu, Xi
Wang, Li
Yu, Caijia
Yu, Daohai
Yu, Gang
Histone Acetylation Modifiers in the Pathogenesis of Alzheimer’s Disease
title Histone Acetylation Modifiers in the Pathogenesis of Alzheimer’s Disease
title_full Histone Acetylation Modifiers in the Pathogenesis of Alzheimer’s Disease
title_fullStr Histone Acetylation Modifiers in the Pathogenesis of Alzheimer’s Disease
title_full_unstemmed Histone Acetylation Modifiers in the Pathogenesis of Alzheimer’s Disease
title_short Histone Acetylation Modifiers in the Pathogenesis of Alzheimer’s Disease
title_sort histone acetylation modifiers in the pathogenesis of alzheimer’s disease
topic Neuroscience
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4468862/
https://www.ncbi.nlm.nih.gov/pubmed/26136662
http://dx.doi.org/10.3389/fncel.2015.00226
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