c-Jun is regulated by combination of enhanced expression and phosphorylation in acute-overloaded rat heart

dc.creatorNadruz, W
dc.creatorKobarg, CB
dc.creatorKobarg, J
dc.creatorFranchini, KG
dc.date2004
dc.dateFEB 1
dc.date2014-11-15T16:30:16Z
dc.date2015-11-26T16:12:00Z
dc.date2014-11-15T16:30:16Z
dc.date2015-11-26T16:12:00Z
dc.date.accessioned2018-03-28T23:00:30Z
dc.date.available2018-03-28T23:00:30Z
dc.identifierAmerican Journal Of Physiology-heart And Circulatory Physiology. Amer Physiological Soc, v. 286, n. 2, n. H760, n. H767, 2004.
dc.identifier0363-6135
dc.identifierWOS:000187911900034
dc.identifier10.1152/ajpheart.00430.2003
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/55948
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/55948
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/55948
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1267227
dc.descriptionThe transient increase in the expression of transcription factors encoded by immediate- early genes has been considered to play a critical role in the coordination of early gene expression during the hypertrophic growth of cardiac myocytes. Here, we investigated the regulation of c- Jun and its upstream activators JNKs in the myocardium of rats subjected to acute pressure overload induced by transverse aortic constriction. Western blotting and immunohistochemistry analysis demonstrated that both JNK1 and JNK2 were transiently activated by pressure overload, but only JNK1 was activated at the nuclei of cardiac myocytes. JNK1 activation was paralleled by phosphorylation of c- Jun at serine- 63 in the myocardial nuclear fraction and by an increase in c- Jun expression in cardiac myocytes. A consistent increase in DNA binding of activator protein-1 ( AP- 1) complex was observed after 10 and 30 min of pressure overload and Supershift assays confirmed that c- Jun was a major component of activated AP- 1 complex. Moreover, experiments performed with the specific JNK inhibitor SP- 600125 abolished c- Jun phosphorylation and markedly attenuated its expression as well as the expression of the fetal gene beta- myosin heavy chain. Overall, these findings demonstrate a molecular basis for load- induced activation of c- Jun in cardiac myocytes and its connection with the regulation of fetal gene, characteristic of the acute response to pressure overload.
dc.descriptiono TEXTO COMPLETO DESTE ARTIGO, ESTARÁ DISPONÍVEL À PARTIR DE AGOSTO DE 2015.
dc.description286
dc.description2
dc.descriptionH760
dc.descriptionH767
dc.languageen
dc.publisherAmer Physiological Soc
dc.publisherBethesda
dc.publisherEUA
dc.relationAmerican Journal Of Physiology-heart And Circulatory Physiology
dc.relationAm. J. Physiol.-Heart Circul. Physiol.
dc.rightsembargo
dc.sourceWeb of Science
dc.subjectpressure overload
dc.subjectprotein
dc.subjectmyocardium
dc.subjectactivator protein-1
dc.subjectCardiac Gene-expression
dc.subjectPressure-overload
dc.subjectMechanical-stress
dc.subjectProtooncogene Induction
dc.subjectNuclear Translocation
dc.subjectNh2-terminal Kinases
dc.subjectPositive Regulation
dc.subjectIn-vivo
dc.subjectHypertrophy
dc.subjectProtein
dc.titlec-Jun is regulated by combination of enhanced expression and phosphorylation in acute-overloaded rat heart
dc.typeArtículos de revistas


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