The Cross-talk Between Angiotensin And Insulin Differentially Affects Phosphatidylinositol 3-kinase- And Mitogen-activated Protein Kinase-mediated Signaling In Rat Heart: Implications For Insulin Resistance.

dc.creatorCarvalheira, José B C
dc.creatorCalegari, Vivian C
dc.creatorZecchin, Henrique G
dc.creatorNadruz, Wilson
dc.creatorGuimarães, Regina B
dc.creatorRibeiro, Eliane B
dc.creatorFranchini, Kleber G
dc.creatorVelloso, Lício A
dc.creatorSaad, Mario J A
dc.date2003-Dec
dc.date2015-11-27T12:52:24Z
dc.date2015-11-27T12:52:24Z
dc.date.accessioned2018-03-29T00:57:55Z
dc.date.available2018-03-29T00:57:55Z
dc.identifierEndocrinology. v. 144, n. 12, p. 5604-14, 2003-Dec.
dc.identifier0013-7227
dc.identifier10.1210/en.2003-0788
dc.identifierhttp://www.ncbi.nlm.nih.gov/pubmed/12960006
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/195509
dc.identifier12960006
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1295742
dc.descriptionInsulin and angiotensin II (AngII) may act through overlapping intracellular pathways to promote cardiac myocyte growth. In this report insulin and AngII signaling, through the phosphatidylinositol 3-kinase (PI 3-kinase) and MAPK pathways, were compared in cardiac tissues of control and obese Zucker rats. AngII induced Janus kinase 2 tyrosine phosphorylation and coimmunoprecipitation with insulin receptor substrate 1 (IRS-1) and IRS-2 as well as an increase in tyrosine phosphorylation of IRS and its association with growth factor receptor-binding protein 2. Simultaneous treatment with both hormones led to marked increases in the associations of IRS-1 and -2 with growth factor receptor-binding protein 2 and in the dual phosphorylation of ERK1/2 compared with the administration of AngII or insulin alone. In contrast, an acute inhibition of both basal and insulin-stimulated PI 3-kinase activity was induced by both hormones. Insulin stimulated the phosphorylation of MAPK equally in lean and obese rats. Conversely, insulin-induced phosphorylation of Akt in heart was decreased in obese rats. Pretreatment with losartan did not change insulin-induced activation of ERK1/2 and attenuated the reduction of Akt phosphorylation in the heart of obese rats. Thus, the imbalance between PI 3-kinase-Akt and MAPK signaling pathways in the heart may play a role in the development of cardiovascular abnormalities observed in insulin-resistant states, such as in obese Zucker rats.
dc.description144
dc.description5604-14
dc.languageeng
dc.relationEndocrinology
dc.relationEndocrinology
dc.rightsfechado
dc.rights
dc.sourcePubMed
dc.subjectAdaptor Proteins, Signal Transducing
dc.subjectAngiotensin Ii
dc.subjectAnimals
dc.subjectGrb2 Adaptor Protein
dc.subjectHypoglycemic Agents
dc.subjectInsulin
dc.subjectInsulin Resistance
dc.subjectJanus Kinase 2
dc.subjectMap Kinase Signaling System
dc.subjectMale
dc.subjectMitogen-activated Protein Kinase 1
dc.subjectMitogen-activated Protein Kinase 3
dc.subjectMitogen-activated Protein Kinases
dc.subjectMyocardium
dc.subjectObesity
dc.subjectPhosphatidylinositol 3-kinases
dc.subjectPhosphorylation
dc.subjectProtein-serine-threonine Kinases
dc.subjectProtein-tyrosine Kinases
dc.subjectProteins
dc.subjectProto-oncogene Proteins
dc.subjectProto-oncogene Proteins C-akt
dc.subjectRats
dc.subjectRats, Wistar
dc.subjectRats, Zucker
dc.subjectReceptor Cross-talk
dc.subjectVasoconstrictor Agents
dc.titleThe Cross-talk Between Angiotensin And Insulin Differentially Affects Phosphatidylinositol 3-kinase- And Mitogen-activated Protein Kinase-mediated Signaling In Rat Heart: Implications For Insulin Resistance.
dc.typeArtículos de revistas


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