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Histone deacetylases and their roles in mineralized tissue regeneration

Histone acetylation is an important epigenetic mechanism that controls expression of certain genes. It includes non-sequence-based changes of chromosomal regional structure that can alter the expression of genes. Acetylation of histones is controlled by the activity of two groups of enzymes: the his...

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Autores principales: Huynh, Nam Cong-Nhat, Everts, Vincent, Ampornaramveth, Ruchanee Salingcarnboriboon
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5565747/
https://www.ncbi.nlm.nih.gov/pubmed/28856178
http://dx.doi.org/10.1016/j.bonr.2017.08.001
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author Huynh, Nam Cong-Nhat
Everts, Vincent
Ampornaramveth, Ruchanee Salingcarnboriboon
author_facet Huynh, Nam Cong-Nhat
Everts, Vincent
Ampornaramveth, Ruchanee Salingcarnboriboon
author_sort Huynh, Nam Cong-Nhat
collection PubMed
description Histone acetylation is an important epigenetic mechanism that controls expression of certain genes. It includes non-sequence-based changes of chromosomal regional structure that can alter the expression of genes. Acetylation of histones is controlled by the activity of two groups of enzymes: the histone acetyltransferases (HATs) and histone deacetylases (HDACs). HDACs remove acetyl groups from the histone tail, which alters its charge and thus promotes compaction of DNA in the nucleosome. HDACs render the chromatin structure into a more compact form of heterochromatin, which makes the genes inaccessible for transcription. By altering the transcriptional activity of bone-associated genes, HDACs control both osteogenesis and osteoclastogenesis. This review presents an overview of the function of HDACs in the modulation of bone formation. Special attention is paid to the use of HDAC inhibitors in mineralized tissue regeneration from cells of dental origin.
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spelling pubmed-55657472017-08-30 Histone deacetylases and their roles in mineralized tissue regeneration Huynh, Nam Cong-Nhat Everts, Vincent Ampornaramveth, Ruchanee Salingcarnboriboon Bone Rep Article Histone acetylation is an important epigenetic mechanism that controls expression of certain genes. It includes non-sequence-based changes of chromosomal regional structure that can alter the expression of genes. Acetylation of histones is controlled by the activity of two groups of enzymes: the histone acetyltransferases (HATs) and histone deacetylases (HDACs). HDACs remove acetyl groups from the histone tail, which alters its charge and thus promotes compaction of DNA in the nucleosome. HDACs render the chromatin structure into a more compact form of heterochromatin, which makes the genes inaccessible for transcription. By altering the transcriptional activity of bone-associated genes, HDACs control both osteogenesis and osteoclastogenesis. This review presents an overview of the function of HDACs in the modulation of bone formation. Special attention is paid to the use of HDAC inhibitors in mineralized tissue regeneration from cells of dental origin. Elsevier 2017-08-16 /pmc/articles/PMC5565747/ /pubmed/28856178 http://dx.doi.org/10.1016/j.bonr.2017.08.001 Text en © 2017 The Authors http://creativecommons.org/licenses/by-nc-nd/4.0/ This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
spellingShingle Article
Huynh, Nam Cong-Nhat
Everts, Vincent
Ampornaramveth, Ruchanee Salingcarnboriboon
Histone deacetylases and their roles in mineralized tissue regeneration
title Histone deacetylases and their roles in mineralized tissue regeneration
title_full Histone deacetylases and their roles in mineralized tissue regeneration
title_fullStr Histone deacetylases and their roles in mineralized tissue regeneration
title_full_unstemmed Histone deacetylases and their roles in mineralized tissue regeneration
title_short Histone deacetylases and their roles in mineralized tissue regeneration
title_sort histone deacetylases and their roles in mineralized tissue regeneration
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5565747/
https://www.ncbi.nlm.nih.gov/pubmed/28856178
http://dx.doi.org/10.1016/j.bonr.2017.08.001
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