Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/2403
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dc.contributor.CRUESPUNIVERSIDADE ESTADUAL DE CAMPINASpt_BR
dc.typeArtigo de periódicopt_BR
dc.titlePotential Contribution of Translational Factors to Triiodo-L-Thyronine-Induced Insulin Synthesis by Pancreatic Beta Cellspt_BR
dc.contributor.authorGoulart-Silva, Francemilsonpt_BR
dc.contributor.authorTeixeira, Silvania da Silvapt_BR
dc.contributor.authorLuchessi, Augusto Ducatipt_BR
dc.contributor.authorBichara dos Santos, Laila Romagueirapt_BR
dc.contributor.authorRebelato, Eduardopt_BR
dc.contributor.authorCarpinelli, Angelo Rafaelpt_BR
dc.contributor.authorNunes, Maria Terezapt_BR
unicamp.authorLuchessi, Augusto Ducatipt_BR
unicamp.author.externalGoulart-Silva, Francemilsonpt
unicamp.author.externalTeixeira, Silvania da Silvapt
unicamp.author.externalBichara dos Santos, Laila Romagueirapt
unicamp.author.externalRebelato, Eduardopt
unicamp.author.externalCarpinelli, Angelo Rafaelpt
unicamp.author.externalNunes, Maria Terezapt
dc.subject.wosPROTEIN-SYNTHESISpt_BR
dc.subject.wosELONGATIONpt_BR
dc.subject.wosEXPRESSIONpt_BR
dc.subject.wosINITIATIONpt_BR
dc.subject.wosINHIBITIONpt_BR
dc.subject.wosMETABOLISMpt_BR
dc.subject.wosSECRETIONpt_BR
dc.subject.wosRIBOSOMEpt_BR
dc.subject.wosBINDINGpt_BR
dc.subject.wosEIF2pt_BR
dc.description.abstractBackground: Thyroid hormones (THs) are known to regulate protein synthesis by acting at the transcriptional level and inducing the expression of many genes. However, little is known about their role in protein expression at the post-transcriptional level, even though studies have shown enhancement of protein synthesis associated with mTOR/p70S6K activation after triiodo-l-thyronine (T3) administration. On the other hand, the effects of TH on translation initiation and polypeptidic chain elongation factors, being essential for activating protein synthesis, have been poorly explored. Therefore, considering that preliminary studies from our laboratory have demonstrated an increase in insulin content in INS-1E cells in response to T3 treatment, the aim of the present study was to investigate if proteins of translational nature might be involved in this effect. Methods: INS-1E cells were maintained in the presence or absence of T3 (10(-6) or 10(-8) M) for 12 hours. Thereafter, insulin concentration in the culture medium was determined by radioimmunoassay, and the cells were processed for Western blot detection of insulin, eukaryotic initiation factor 2 (eIF2), p-eIF2, eIF5A, EF1A, eIF4E binding protein (4E-BP), p-4E-BP, p70S6K, and p-p70S6K. Results: It was found that, in parallel with increased insulin generation, T3 induced p70S6K phosphorylation and the expression of the translational factors eIF2, eIF5A, and eukaryotic elongation factor 1 alpha (eEF1A). In contrast, total and phosphorylated 4E-BP, as well as total p70S6K and p-eIF2 content, remained unchanged after T3 treatment. Conclusions: Considering that (i) p70S6K induces S6 phosphorylation of the 40S ribosomal subunit, an essential condition for protein synthesis; (ii) eIF2 is essential for the initiation of messenger RNA translation process; and (iii) eIF5A and eEF1A play a central role in the elongation of the polypeptidic chain during the transcripts decoding, the data presented here lead us to suppose that a part of T3-induced insulin expression in INS-1E cells depends on the protein synthesis activation at the post-transcriptional level, as these proteins of the translational machinery were shown to be regulated by T3.pt
dc.relation.ispartofThyroidpt_BR
dc.publisher.cityNew Rochellept_BR
dc.publisherMary Ann Liebert Incpt_BR
dc.date.issued2012pt_BR
dc.identifier.citationThyroid. Mary Ann Liebert Inc, v.22, n.6, p.637-642, 2012pt_BR
dc.language.isoengpt_BR
dc.description.volume22pt_BR
dc.description.issuenumber6pt_BR
dc.description.firstpage637pt_BR
dc.description.lastpage642pt_BR
dc.rightsfechadopt_BR
dc.sourceWOSpt_BR
dc.identifier.issn1050-7256pt_BR
dc.identifier.wosidWOS:000305001200013pt_BR
dc.identifier.doi10.1089/thy.2011.0252pt_BR
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)pt_BR
dc.description.sponsorship1Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)pt_BR
dc.date.available2013-09-19T18:06:47Z-
dc.date.accessioned2013-09-19T18:06:47Z-
dc.description.provenanceMade available in DSpace on 2013-09-19T18:06:47Z (GMT). No. of bitstreams: 0 Previous issue date: 2012en
dc.identifier.urihttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/2403-
dc.contributor.unidadeFCApt
Appears in Collections:FCA - Artigos e Outros Documentos

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