Histone Deacetylase 1 Is Essential for Rod Photoreceptor Differentiation by Regulating Acetylation at Histone H3 Lysine 9 and Histone H4 Lysine 12 in the Mouse Retina
Autor(a) principal: | |
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Data de Publicação: | 2017 |
Outros Autores: | , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNIFESP |
Texto Completo: | https://repositorio.unifesp.br/handle/11600/55106 http://dx.doi.org/10.1074/jbc.M116.756643 |
Resumo: | Histone acetylation has a regulatory role in gene expression and is necessary for proper tissue development. To investigate the specific roles of histone deacetylases (HDACs) in rod differentiation in neonatal mouse retinas, we used a pharmacological approach that showed that inhibition of class I but not class IIa HDACs caused the same phenotypic changes seen with broad spectrum HDAC inhibitors, most notably a block in the differentiation of rod photoreceptors. Inhibition of HDAC1 resulted in increase of acetylation of lysine 9 of histone 3 (H3K9) and lysine 12 of histone 4 (H4K12) but not lysine 27 of histone 3 (H3K27) and led to maintained expression of progenitor-specific genes such as Vsx2 and Hes1 with concomitant block of expression of rod-specific genes. ChiP experiments confirmed these changes in the promoters of a group of progenitor genes. Based on our results, we suggest that HDAC1-specific inhibition prevents progenitor cells of the retina from exiting the cell cycle and differentiating. HDAC1 may be an essential epigenetic regulator of the transition from progenitor cells to terminally differentiated photoreceptors. |
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Ferreira, Renata C. [UNIFESP]Popova, Evgenya Y.James, JessicaBriones, Marcelo R. S. [UNIFESP]Zhang, Samuel S.Barnstable, Colin J.2020-07-17T14:02:58Z2020-07-17T14:02:58Z2017Journal Of Biological Chemistry. Bethesda, v. 292, n. 6, p. 2422-2440, 2017.0021-9258https://repositorio.unifesp.br/handle/11600/55106http://dx.doi.org/10.1074/jbc.M116.75664310.1074/jbc.M116.756643WOS:000395530300031Histone acetylation has a regulatory role in gene expression and is necessary for proper tissue development. To investigate the specific roles of histone deacetylases (HDACs) in rod differentiation in neonatal mouse retinas, we used a pharmacological approach that showed that inhibition of class I but not class IIa HDACs caused the same phenotypic changes seen with broad spectrum HDAC inhibitors, most notably a block in the differentiation of rod photoreceptors. Inhibition of HDAC1 resulted in increase of acetylation of lysine 9 of histone 3 (H3K9) and lysine 12 of histone 4 (H4K12) but not lysine 27 of histone 3 (H3K27) and led to maintained expression of progenitor-specific genes such as Vsx2 and Hes1 with concomitant block of expression of rod-specific genes. ChiP experiments confirmed these changes in the promoters of a group of progenitor genes. Based on our results, we suggest that HDAC1-specific inhibition prevents progenitor cells of the retina from exiting the cell cycle and differentiating. HDAC1 may be an essential epigenetic regulator of the transition from progenitor cells to terminally differentiated photoreceptors.National Council for Scientific and Technological Development of BrazilSao Paulo Research Foundation (FAPESP)Macula Vision Research FoundationPenn State Univ, Coll Med, Dept Neural & Behav Sci, 500 Univ Dr, Hershey, PA 17033 USAPenn State Hershey Eye Ctr, Hershey, PA 17033 USAUniv Fed Sao Paulo, Escola Paulista Med, Lab Evolutionary Genom & Biocomplex, BR-04039032 Sao Paulo, BrazilUniv Fed Sao Paulo, Escola Paulista Med, Lab Evolutionary Genom & Biocomplex, BR-04039032 Sao Paulo, BrazilCNPq: 206445/2014-8FAPESP: 2013/078380FAPESP: 2014/256026Web of Science2422-2440engAmer Soc Biochemistry Molecular Biology IncJournal Of Biological ChemistryHistone Deacetylase 1 Is Essential for Rod Photoreceptor Differentiation by Regulating Acetylation at Histone H3 Lysine 9 and Histone H4 Lysine 12 in the Mouse Retinainfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleBethesda2926info:eu-repo/semantics/openAccessreponame:Repositório Institucional da UNIFESPinstname:Universidade Federal de São Paulo (UNIFESP)instacron:UNIFESP11600/551062021-10-04 21:26:15.293metadata only accessoai:repositorio.unifesp.br:11600/55106Repositório InstitucionalPUBhttp://www.repositorio.unifesp.br/oai/requestopendoar:34652023-05-25T12:16:38.470915Repositório Institucional da UNIFESP - Universidade Federal de São Paulo (UNIFESP)false |
dc.title.en.fl_str_mv |
Histone Deacetylase 1 Is Essential for Rod Photoreceptor Differentiation by Regulating Acetylation at Histone H3 Lysine 9 and Histone H4 Lysine 12 in the Mouse Retina |
title |
Histone Deacetylase 1 Is Essential for Rod Photoreceptor Differentiation by Regulating Acetylation at Histone H3 Lysine 9 and Histone H4 Lysine 12 in the Mouse Retina |
spellingShingle |
Histone Deacetylase 1 Is Essential for Rod Photoreceptor Differentiation by Regulating Acetylation at Histone H3 Lysine 9 and Histone H4 Lysine 12 in the Mouse Retina Ferreira, Renata C. [UNIFESP] |
title_short |
Histone Deacetylase 1 Is Essential for Rod Photoreceptor Differentiation by Regulating Acetylation at Histone H3 Lysine 9 and Histone H4 Lysine 12 in the Mouse Retina |
title_full |
Histone Deacetylase 1 Is Essential for Rod Photoreceptor Differentiation by Regulating Acetylation at Histone H3 Lysine 9 and Histone H4 Lysine 12 in the Mouse Retina |
title_fullStr |
Histone Deacetylase 1 Is Essential for Rod Photoreceptor Differentiation by Regulating Acetylation at Histone H3 Lysine 9 and Histone H4 Lysine 12 in the Mouse Retina |
title_full_unstemmed |
Histone Deacetylase 1 Is Essential for Rod Photoreceptor Differentiation by Regulating Acetylation at Histone H3 Lysine 9 and Histone H4 Lysine 12 in the Mouse Retina |
title_sort |
Histone Deacetylase 1 Is Essential for Rod Photoreceptor Differentiation by Regulating Acetylation at Histone H3 Lysine 9 and Histone H4 Lysine 12 in the Mouse Retina |
author |
Ferreira, Renata C. [UNIFESP] |
author_facet |
Ferreira, Renata C. [UNIFESP] Popova, Evgenya Y. James, Jessica Briones, Marcelo R. S. [UNIFESP] Zhang, Samuel S. Barnstable, Colin J. |
author_role |
author |
author2 |
Popova, Evgenya Y. James, Jessica Briones, Marcelo R. S. [UNIFESP] Zhang, Samuel S. Barnstable, Colin J. |
author2_role |
author author author author author |
dc.contributor.author.fl_str_mv |
Ferreira, Renata C. [UNIFESP] Popova, Evgenya Y. James, Jessica Briones, Marcelo R. S. [UNIFESP] Zhang, Samuel S. Barnstable, Colin J. |
description |
Histone acetylation has a regulatory role in gene expression and is necessary for proper tissue development. To investigate the specific roles of histone deacetylases (HDACs) in rod differentiation in neonatal mouse retinas, we used a pharmacological approach that showed that inhibition of class I but not class IIa HDACs caused the same phenotypic changes seen with broad spectrum HDAC inhibitors, most notably a block in the differentiation of rod photoreceptors. Inhibition of HDAC1 resulted in increase of acetylation of lysine 9 of histone 3 (H3K9) and lysine 12 of histone 4 (H4K12) but not lysine 27 of histone 3 (H3K27) and led to maintained expression of progenitor-specific genes such as Vsx2 and Hes1 with concomitant block of expression of rod-specific genes. ChiP experiments confirmed these changes in the promoters of a group of progenitor genes. Based on our results, we suggest that HDAC1-specific inhibition prevents progenitor cells of the retina from exiting the cell cycle and differentiating. HDAC1 may be an essential epigenetic regulator of the transition from progenitor cells to terminally differentiated photoreceptors. |
publishDate |
2017 |
dc.date.issued.fl_str_mv |
2017 |
dc.date.accessioned.fl_str_mv |
2020-07-17T14:02:58Z |
dc.date.available.fl_str_mv |
2020-07-17T14:02:58Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.citation.fl_str_mv |
Journal Of Biological Chemistry. Bethesda, v. 292, n. 6, p. 2422-2440, 2017. |
dc.identifier.uri.fl_str_mv |
https://repositorio.unifesp.br/handle/11600/55106 http://dx.doi.org/10.1074/jbc.M116.756643 |
dc.identifier.issn.none.fl_str_mv |
0021-9258 |
dc.identifier.doi.none.fl_str_mv |
10.1074/jbc.M116.756643 |
dc.identifier.wos.none.fl_str_mv |
WOS:000395530300031 |
identifier_str_mv |
Journal Of Biological Chemistry. Bethesda, v. 292, n. 6, p. 2422-2440, 2017. 0021-9258 10.1074/jbc.M116.756643 WOS:000395530300031 |
url |
https://repositorio.unifesp.br/handle/11600/55106 http://dx.doi.org/10.1074/jbc.M116.756643 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.ispartof.none.fl_str_mv |
Journal Of Biological Chemistry |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
2422-2440 |
dc.coverage.none.fl_str_mv |
Bethesda |
dc.publisher.none.fl_str_mv |
Amer Soc Biochemistry Molecular Biology Inc |
publisher.none.fl_str_mv |
Amer Soc Biochemistry Molecular Biology Inc |
dc.source.none.fl_str_mv |
reponame:Repositório Institucional da UNIFESP instname:Universidade Federal de São Paulo (UNIFESP) instacron:UNIFESP |
instname_str |
Universidade Federal de São Paulo (UNIFESP) |
instacron_str |
UNIFESP |
institution |
UNIFESP |
reponame_str |
Repositório Institucional da UNIFESP |
collection |
Repositório Institucional da UNIFESP |
repository.name.fl_str_mv |
Repositório Institucional da UNIFESP - Universidade Federal de São Paulo (UNIFESP) |
repository.mail.fl_str_mv |
|
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1783460270907064320 |