Cross-talk Between The Insulin And Angiotensin Signaling Systems.

dc.creatorVelloso, L A
dc.creatorFolli, F
dc.creatorSun, X J
dc.creatorWhite, M F
dc.creatorSaad, M J
dc.creatorKahn, C R
dc.date1996-Oct
dc.date2015-11-27T12:18:47Z
dc.date2015-11-27T12:18:47Z
dc.date.accessioned2018-03-29T00:51:55Z
dc.date.available2018-03-29T00:51:55Z
dc.identifierProceedings Of The National Academy Of Sciences Of The United States Of America. v. 93, n. 22, p. 12490-5, 1996-Oct.
dc.identifier0027-8424
dc.identifier
dc.identifierhttp://www.ncbi.nlm.nih.gov/pubmed/8901609
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/193948
dc.identifier8901609
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1294181
dc.descriptionAngiotensin II (AII), acting via its G-protein linked receptor, is an important regulator of cardiac, vascular, and renal function. Following injection of AII into rats, we find that there is also a rapid tyrosine phosphorylation of the major insulin receptor substrates 1 and 2 (IRS-1 and IRS-2) in the heart. This phenomenon appears to involve JAK2 tyrosine kinase, which associates with the AT1 receptor and IRS-1/IRS-2 after AII stimulation. AII-induced phosphorylation leads to binding of phosphatidylinositol 3-kinase (PI 3-kinase) to IRS-1 and IRS-2; however, in contrast to other ligands, AII injection results in an acute inhibition of both basal and insulin-stimulated PI 3-kinase activity. The latter occurs without any reduction in insulin receptor or IRS phosphorylation or in the interaction of the p85 and p110 subunits of PI 3-kinase with each other or with IRS-1/IRS-2. These effects of AII are inhibited by AT1 receptor antagonists. Thus, there is direct cross-talk between insulin and AII signaling pathways at the level of both tyrosine phosphorylation and PI 3-kinase activation. These interactions may play an important role in the association of insulin resistance, hypertension, and cardiovascular disease.
dc.description93
dc.description12490-5
dc.languageeng
dc.relationProceedings Of The National Academy Of Sciences Of The United States Of America
dc.relationProc. Natl. Acad. Sci. U.S.A.
dc.rightsaberto
dc.rights
dc.sourcePubMed
dc.subjectAngiotensin Ii
dc.subjectAnimals
dc.subjectElectrophoresis, Polyacrylamide Gel
dc.subjectInsulin
dc.subjectInsulin Receptor Substrate Proteins
dc.subjectIntracellular Signaling Peptides And Proteins
dc.subjectJanus Kinase 1
dc.subjectJanus Kinase 2
dc.subjectJanus Kinase 3
dc.subjectMale
dc.subjectPhosphatidylinositol 3-kinases
dc.subjectPhosphoproteins
dc.subjectPhosphorylation
dc.subjectPhosphotransferases (alcohol Group Acceptor)
dc.subjectProtein-tyrosine Kinases
dc.subjectProto-oncogene Proteins
dc.subjectRats
dc.subjectRats, Wistar
dc.subjectSignal Transduction
dc.subjectTyrosine
dc.titleCross-talk Between The Insulin And Angiotensin Signaling Systems.
dc.typeArtículos de revistas


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