Trichostatin A induces Trypanosoma cruzi histone and tubulin acetylation: effects on cell division and microtubule cytoskeleton remodelling

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dc.contributorLCC - Laboratório de Ciclo Celularpt_BR
dc.contributor.authorSantos, Jean de Oliveirapt_BR
dc.contributor.authorZuma, Aline Araujopt_BR
dc.contributor.authorVitorino, Francisca Nathália de Lunapt_BR
dc.contributor.authorda Cunha, Julia Pinheiro Chagaspt_BR
dc.contributor.authorde Souza, Wanderleypt_BR
dc.contributor.authorMotta, Maria Cristina M.pt_BR
dc.identifier.citationSantos JO, Zuma AA, Vitorino FNL, da Cunha JPC, de Souza W, Motta MCM.. Trichostatin A induces Trypanosoma cruzi histone and tubulin acetylation: effects on cell division and microtubule cytoskeleton remodelling. Parasitology. 2019 Apr;146(4):543-552. doi:10.1017/S0031182018001828.pt_BR
dc.description.abstractTrypanosoma cruzi, the causative agent of Chagas disease, is a public health concern in Latin America. Epigenetic events, such as histone acetylation, affect DNA topology, replication and gene expression. Histone deacetylases (HDACs) are involved in chromatin compaction and post-translational modifications of cytoplasmic proteins, such as tubulin. HDAC inhibitors, like trichostatin A (TSA), inhibit tumour cell proliferation and promotes ultrastructural modifications. In the present study, TSA effects on cell proliferation, viability, cell cycle and ultrastructure were evaluated, as well as on histone acetylation and tubulin expression of the T. cruzi epimastigote form. Protozoa proliferation and viability were reduced after treatment with TSA. Quantitative proteomic analyses revealed an increase in histone acetylation after 72 h of TSA treatment. Surprisingly, results obtained by different microscopy methodologies indicate that TSA does not affect chromatin compaction, but alters microtubule cytoskeleton dynamics and impair kDNA segregation, generating polynucleated cells with atypical morphology. Confocal fluorescence microscopy and flow cytometry assays indicated that treated cell microtubules were more intensely acetylated. Increases in tubulin acetylation may be directly related to the higher number of parasites in the G2/M phase after TSA treatment. Taken together, these results suggest that deacetylase inhibitors represent excellent tools for understanding trypanosomatid cell biology.pt_BR
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado do Rio de Janeiro (FAPERJ)pt_BR
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)pt_BR
dc.format.extentp. 543-552pt_BR
dc.titleTrichostatin A induces Trypanosoma cruzi histone and tubulin acetylation: effects on cell division and microtubule cytoskeleton remodellingpt_BR
dc.contributor.externalUniversidade Federal do Rio de Janeiro (UFRJ)¦¦Brasilpt_BR
dc.identifier.citationissuen. 4pt_BR
dc.subject.keywordhistone deacetylases inhibitor (HDACi)pt_BR
dc.subject.keywordmicrotubule cytoskeletonpt_BR
dc.subject.keywordtrichostatin A (TSA)pt_BR
dc.subject.keywordTrypanosoma cruzipt_BR
dc.identifier.citationabntv. 146, n. 4, p. 543-552, abr. 2019pt_BR
dc.identifier.citationvancouver2019 Apr;146(4):543-552pt_BR
dc.contributor.butantanVitorino, Francisca Nathália de Luna|:Aluno|:LCC - Laboratório de Ciclo Celular|:pt_BR
dc.contributor.butantanda Cunha, Julia Pinheiro Chagas|:Pesquisador|:LCC - Laboratório de Ciclo Celular|:pt_BR
dc.sponsorship.butantanConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)¦¦pt_BR
dc.sponsorship.butantanFundação de Amparo à Pesquisa do Estado do Rio de Janeiro (FAPERJ)¦¦pt_BR
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