Early Activation Of The Multicomponent Signaling Complex Associated With Focal Adhesion Kinase Induced By Pressure Overload In The Rat Heart.

dc.creatorFranchini, K G
dc.creatorTorsoni, A S
dc.creatorSoares, P H
dc.creatorSaad, M J
dc.date2000-Sep
dc.date2015-11-27T12:22:41Z
dc.date2015-11-27T12:22:41Z
dc.date.accessioned2018-03-29T00:54:23Z
dc.date.available2018-03-29T00:54:23Z
dc.identifierCirculation Research. v. 87, n. 7, p. 558-65, 2000-Sep.
dc.identifier1524-4571
dc.identifier
dc.identifierhttp://www.ncbi.nlm.nih.gov/pubmed/11009560
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/194592
dc.identifier11009560
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1294825
dc.descriptionMechanical 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 effectors 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.
dc.description87
dc.description558-65
dc.languageeng
dc.relationCirculation Research
dc.relationCirc. Res.
dc.rightsfechado
dc.rights
dc.sourcePubMed
dc.subjectAdaptor Proteins, Signal Transducing
dc.subjectAnimals
dc.subjectAorta
dc.subjectBlood Pressure
dc.subjectEnzyme Activation
dc.subjectFocal Adhesion Kinase 1
dc.subjectFocal Adhesion Protein-tyrosine Kinases
dc.subjectGrb2 Adaptor Protein
dc.subjectMale
dc.subjectMitogen-activated Protein Kinase 1
dc.subjectMitogen-activated Protein Kinase 3
dc.subjectMitogen-activated Protein Kinases
dc.subjectMyocardium
dc.subjectPhosphatidylinositol 3-kinases
dc.subjectPhosphorylation
dc.subjectPressure
dc.subjectProtein-serine-threonine Kinases
dc.subjectProtein-tyrosine Kinases
dc.subjectProteins
dc.subjectProto-oncogene Proteins
dc.subjectProto-oncogene Proteins C-akt
dc.subjectProto-oncogene Proteins Pp60(c-src)
dc.subjectRats
dc.subjectRats, Wistar
dc.subjectSignal Transduction
dc.subjectTissue Distribution
dc.subjectTyrosine
dc.titleEarly Activation Of The Multicomponent Signaling Complex Associated With Focal Adhesion Kinase Induced By Pressure Overload In The Rat Heart.
dc.typeArtículos de revistas


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