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dc.contributor.CRUESPUniversidade Estadual de Campinaspt_BR
dc.typeArtigo de periódicopt_BR
dc.titleEarly activation of the multicomponent signaling complex associated with focal adhesion kinase induced by pressure overload in the rat heartpt_BR
dc.contributor.authorFranchini, KGpt_BR
dc.contributor.authorTorsoni, ASpt_BR
dc.contributor.authorSoares, PHApt_BR
dc.contributor.authorSaad, MJApt_BR
unicamp.authorUniv Estadual Campinas, Sch Med, Dept Internal Med, BR-13081970 Campinas, SP, Brazilpt_BR
dc.subjectmyocardiumpt_BR
dc.subjectsignalingpt_BR
dc.subjectratspt_BR
dc.subjectkinasept_BR
dc.subject.wosProtein-kinasept_BR
dc.subject.wosCardiac Myocytespt_BR
dc.subject.wosPhosphatidylinositol 3-kinasept_BR
dc.subject.wosTyrosine Phosphorylationpt_BR
dc.subject.wosHypertrophic Responsept_BR
dc.subject.wosVentricular Myocytespt_BR
dc.subject.wosCell-adhesionpt_BR
dc.subject.wosIn-vitropt_BR
dc.subject.wosC-srcpt_BR
dc.subject.wosTransductionpt_BR
dc.description.abstractMechanical overload elicits functional and structural adaptive mechanisms in cardiac muscle. Signaling pathways Linked to integrin/cytoskeleton complexes may have a function in mediation of the effects of mechanical stimulus in myocardial cells. We investigated the tyrosine phosphorylation and the assembly of the multicomponent signaling complex associated with focal adhesion kinase (Fak) and the actin cytoskeleton in the overloaded myocardium of rats. Pressure overload induced a 3-fold increase in Fak tyrosine phosphorylation within 3 minutes after a 60-mm Hg rise in aortic pressure. A pressure stimulus that lasted for 60 minutes was accompanied by a 5-fold increase in the amount of tyrosine-phosphorylated Fak, and a stimulus as low as 10 mm Hg doubled the amount of tyrosine-phosphorylated Fak in the myocardium within 10 minutes. Pressure overload also induced a time-dependent association of actin with Fak and an increase in the amount of Fak detected in the cytoskeletal fraction of the myocardium. These events were paralleled by c-Src activation and binding to Fak and by an association of Grb2 and p85 subunit of phosphatidylinositol 3-kinase with Fak. Erk1/2 and Akt, two possible downstream effecters of Fak via Grb2 and phosphatidylinositol 3-kinase, were also shown to be activated in parallel with Fak. These findings show that pressure overload induced a rapid activation of the Fak multiple signaling complex in the myocardium of rats, which Suggests that this mechanism may have a role in mechanotransduction in the myocardium.pt
dc.description.noteO TEXTO COMPLETO DESTE ARTIGO, ESTARÁ DISPONÍVEL À PARTIR DE FEVEREIRO DE 2015.pt
dc.relation.ispartofCirculation Researchpt_BR
dc.relation.ispartofabbreviationCirc.Res.pt_BR
dc.publisher.cityPhiladelphiapt_BR
dc.publisher.countryEUApt_BR
dc.publisherLippincott Williams & Wilkinspt_BR
dc.date.issued2000pt_BR
dc.date.monthofcirculationSEP 29pt_BR
dc.identifier.citationCirculation Research. Lippincott Williams & Wilkins, v. 87, n. 7, n. 558, n. 565, 2000.pt_BR
dc.language.isoenpt_BR
dc.description.volume87pt_BR
dc.description.issuenumber7pt_BR
dc.description.firstpage558pt_BR
dc.description.lastpage565pt_BR
dc.rightsembargopt_BR
dc.sourceWeb of Sciencept_BR
dc.identifier.issn0009-7330pt_BR
dc.identifier.wosidWOS:000089755500010pt_BR
dc.date.available2014-12-02T16:30:49Z
dc.date.available2015-11-26T17:40:41Z-
dc.date.accessioned2014-12-02T16:30:49Z
dc.date.accessioned2015-11-26T17:40:41Z-
dc.description.provenanceMade available in DSpace on 2014-12-02T16:30:49Z (GMT). No. of bitstreams: 1 WOS000089755500010.pdf: 1363842 bytes, checksum: 8dbed2e8d41f0e7454223f2ce5e7a465 (MD5) Previous issue date: 2000en
dc.description.provenanceMade available in DSpace on 2015-11-26T17:40:41Z (GMT). No. of bitstreams: 2 WOS000089755500010.pdf: 1363842 bytes, checksum: 8dbed2e8d41f0e7454223f2ce5e7a465 (MD5) WOS000089755500010.pdf.txt: 36216 bytes, checksum: 5bf5c35bb7e79e7b8d7f62303fe2d774 (MD5) Previous issue date: 2000en
dc.identifier.urihttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/79717pt_BR
dc.identifier.urihttp://www.repositorio.unicamp.br/handle/REPOSIP/79717
dc.identifier.urihttp://repositorio.unicamp.br/jspui/handle/REPOSIP/79717-
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