The Role of Histones Proteins in Hematological Neoplasias
Autor(a) principal: | |
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Data de Publicação: | 2007 |
Outros Autores: | |
Tipo de documento: | Artigo |
Idioma: | por |
Título da fonte: | Revista Brasileira de Cancerologia (Online) |
Texto Completo: | https://rbc.inca.gov.br/index.php/revista/article/view/1787 |
Resumo: | The basic unit of chromatin is the nucleosome, consisting of approximately 146 DNA base pairs wrapped around a core octamer of proteins known as histones. These basic proteins were initially regarded as merely structural components but are now recognized for their important role in maintaining the dynamic equilibrium of chromatin. The amino terminal tails of histones are susceptible to a variety of post-translational modifications, like methylation, acetylation, phosphorylation, and others, which regulate their functions. Some modifications are generally associated with active genes, whereas others are associated with repressed genes. Currently one of the most widely studied modifications is acetylation, which depends on two families of enzymes, histone acetyltransferases (HAT) and histone deacetylases (HDAC). The chromosomal mutations or translocations involving HAT and HDAC genes result in hematological malignancies such as acute promyelocytic leukemia, lymphoma, and others. Histone deacetylase inhibitors (HDACI) have appeared as a new class of anticancer agents. HDACI have shown activity against various types of cancer and notable effects on tumor cell proliferation, programmed cell death, differentiation, and angiogenesis in vitro and in vivo. |
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The Role of Histones Proteins in Hematological NeoplasiasO Papel das Proteínas Histonas nas Neoplasias HematológicasModificações pós-traducionais nas histonasHistonas acetiltransferases (HAT)Histonas desacetilases (HDAC)CâncerInibidores das histonas desacetilases (IHDAC)Post-translational modifications of histoneHistone acetyltransferases (HAT)Histone deacetylases (HDAC)CancerHistone deacetylase inhibitors (HDACI)The basic unit of chromatin is the nucleosome, consisting of approximately 146 DNA base pairs wrapped around a core octamer of proteins known as histones. These basic proteins were initially regarded as merely structural components but are now recognized for their important role in maintaining the dynamic equilibrium of chromatin. The amino terminal tails of histones are susceptible to a variety of post-translational modifications, like methylation, acetylation, phosphorylation, and others, which regulate their functions. Some modifications are generally associated with active genes, whereas others are associated with repressed genes. Currently one of the most widely studied modifications is acetylation, which depends on two families of enzymes, histone acetyltransferases (HAT) and histone deacetylases (HDAC). The chromosomal mutations or translocations involving HAT and HDAC genes result in hematological malignancies such as acute promyelocytic leukemia, lymphoma, and others. Histone deacetylase inhibitors (HDACI) have appeared as a new class of anticancer agents. HDACI have shown activity against various types of cancer and notable effects on tumor cell proliferation, programmed cell death, differentiation, and angiogenesis in vitro and in vivo.A unidade básica da cromatina é o nucleossomo que consiste em, aproximadamente, 146 pares de bases do DNA enroladas ao redor de um octâmero central de proteínas conhecidas como histonas. Essas proteínas básicas, inicialmente, foram consideradas como componentes meramente estruturais, mas agora são reconhecidas pelo importante papel que desempenham na manutenção do equilíbrio dinâmico da cromatina. As caudas aminoterminais das histonas estão sujeitas a uma variedade de modificações pós-traducionais, como metilação, acetilação, fosforilação, entre outras, que regulam suas funções. Algumas modificações estão associadas a genes ativos, enquanto outras a genes silenciosos. Uma das modificações mais estudadas atualmente é a acetilação, que depende da atividade de duas famílias de enzimas, histonas acetiltransferases (HAT) e histonas desacetilases (HDAC). As mutações ou translocações cromossomais, envolvendo genes HAT e HDAC, resultam no desenvolvimento de malignidades hematológicas, como leucemia promielocítica aguda, linfoma e outras. Inibidores das histonas desacetilases (iHDAC) têm emergido como uma nova classe de agentes anticâncer. Estes iHDAC têm demonstrado atividades contra diversos tipos de câncer e notáveis efeitos na proliferação da célula tumoral, na morte celular programada, na diferenciação e angiogênese in vitro e in vivo.INCA2007-12-31info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionRevisão de literaturaapplication/pdfhttps://rbc.inca.gov.br/index.php/revista/article/view/178710.32635/2176-9745.RBC.2007v53n4.1787Revista Brasileira de Cancerologia; Vol. 53 No. 4 (2007): Oct./Nov./Dec.; 453-460Revista Brasileira de Cancerologia; Vol. 53 Núm. 4 (2007): oct./nov./dic.; 453-460Revista Brasileira de Cancerologia; v. 53 n. 4 (2007): out./nov./dez.; 453-4602176-9745reponame:Revista Brasileira de Cancerologia (Online)instname:Instituto Nacional de Câncer José Alencar Gomes da Silva (INCA)instacron:INCAporhttps://rbc.inca.gov.br/index.php/revista/article/view/1787/1070Menditi, Karla Baptista da Cunha Kang, Hye Chung info:eu-repo/semantics/openAccess2021-11-29T20:24:41Zoai:rbc.inca.gov.br:article/1787Revistahttps://rbc.inca.gov.br/index.php/revistaPUBhttps://rbc.inca.gov.br/index.php/revista/oairbc@inca.gov.br0034-71162176-9745opendoar:2021-11-29T20:24:41Revista Brasileira de Cancerologia (Online) - Instituto Nacional de Câncer José Alencar Gomes da Silva (INCA)false |
dc.title.none.fl_str_mv |
The Role of Histones Proteins in Hematological Neoplasias O Papel das Proteínas Histonas nas Neoplasias Hematológicas |
title |
The Role of Histones Proteins in Hematological Neoplasias |
spellingShingle |
The Role of Histones Proteins in Hematological Neoplasias Menditi, Karla Baptista da Cunha Modificações pós-traducionais nas histonas Histonas acetiltransferases (HAT) Histonas desacetilases (HDAC) Câncer Inibidores das histonas desacetilases (IHDAC) Post-translational modifications of histone Histone acetyltransferases (HAT) Histone deacetylases (HDAC) Cancer Histone deacetylase inhibitors (HDACI) |
title_short |
The Role of Histones Proteins in Hematological Neoplasias |
title_full |
The Role of Histones Proteins in Hematological Neoplasias |
title_fullStr |
The Role of Histones Proteins in Hematological Neoplasias |
title_full_unstemmed |
The Role of Histones Proteins in Hematological Neoplasias |
title_sort |
The Role of Histones Proteins in Hematological Neoplasias |
author |
Menditi, Karla Baptista da Cunha |
author_facet |
Menditi, Karla Baptista da Cunha Kang, Hye Chung |
author_role |
author |
author2 |
Kang, Hye Chung |
author2_role |
author |
dc.contributor.author.fl_str_mv |
Menditi, Karla Baptista da Cunha Kang, Hye Chung |
dc.subject.por.fl_str_mv |
Modificações pós-traducionais nas histonas Histonas acetiltransferases (HAT) Histonas desacetilases (HDAC) Câncer Inibidores das histonas desacetilases (IHDAC) Post-translational modifications of histone Histone acetyltransferases (HAT) Histone deacetylases (HDAC) Cancer Histone deacetylase inhibitors (HDACI) |
topic |
Modificações pós-traducionais nas histonas Histonas acetiltransferases (HAT) Histonas desacetilases (HDAC) Câncer Inibidores das histonas desacetilases (IHDAC) Post-translational modifications of histone Histone acetyltransferases (HAT) Histone deacetylases (HDAC) Cancer Histone deacetylase inhibitors (HDACI) |
description |
The basic unit of chromatin is the nucleosome, consisting of approximately 146 DNA base pairs wrapped around a core octamer of proteins known as histones. These basic proteins were initially regarded as merely structural components but are now recognized for their important role in maintaining the dynamic equilibrium of chromatin. The amino terminal tails of histones are susceptible to a variety of post-translational modifications, like methylation, acetylation, phosphorylation, and others, which regulate their functions. Some modifications are generally associated with active genes, whereas others are associated with repressed genes. Currently one of the most widely studied modifications is acetylation, which depends on two families of enzymes, histone acetyltransferases (HAT) and histone deacetylases (HDAC). The chromosomal mutations or translocations involving HAT and HDAC genes result in hematological malignancies such as acute promyelocytic leukemia, lymphoma, and others. Histone deacetylase inhibitors (HDACI) have appeared as a new class of anticancer agents. HDACI have shown activity against various types of cancer and notable effects on tumor cell proliferation, programmed cell death, differentiation, and angiogenesis in vitro and in vivo. |
publishDate |
2007 |
dc.date.none.fl_str_mv |
2007-12-31 |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion Revisão de literatura |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
https://rbc.inca.gov.br/index.php/revista/article/view/1787 10.32635/2176-9745.RBC.2007v53n4.1787 |
url |
https://rbc.inca.gov.br/index.php/revista/article/view/1787 |
identifier_str_mv |
10.32635/2176-9745.RBC.2007v53n4.1787 |
dc.language.iso.fl_str_mv |
por |
language |
por |
dc.relation.none.fl_str_mv |
https://rbc.inca.gov.br/index.php/revista/article/view/1787/1070 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
application/pdf |
dc.publisher.none.fl_str_mv |
INCA |
publisher.none.fl_str_mv |
INCA |
dc.source.none.fl_str_mv |
Revista Brasileira de Cancerologia; Vol. 53 No. 4 (2007): Oct./Nov./Dec.; 453-460 Revista Brasileira de Cancerologia; Vol. 53 Núm. 4 (2007): oct./nov./dic.; 453-460 Revista Brasileira de Cancerologia; v. 53 n. 4 (2007): out./nov./dez.; 453-460 2176-9745 reponame:Revista Brasileira de Cancerologia (Online) instname:Instituto Nacional de Câncer José Alencar Gomes da Silva (INCA) instacron:INCA |
instname_str |
Instituto Nacional de Câncer José Alencar Gomes da Silva (INCA) |
instacron_str |
INCA |
institution |
INCA |
reponame_str |
Revista Brasileira de Cancerologia (Online) |
collection |
Revista Brasileira de Cancerologia (Online) |
repository.name.fl_str_mv |
Revista Brasileira de Cancerologia (Online) - Instituto Nacional de Câncer José Alencar Gomes da Silva (INCA) |
repository.mail.fl_str_mv |
rbc@inca.gov.br |
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1797042248091697152 |