dc.creatorSaad, M J
dc.creatorVelloso, L A
dc.creatorCarvalho, C R
dc.date1995-Sep
dc.date2015-11-27T12:18:33Z
dc.date2015-11-27T12:18:33Z
dc.date.accessioned2018-03-29T00:51:23Z
dc.date.available2018-03-29T00:51:23Z
dc.identifierThe Biochemical Journal. v. 310 ( Pt 3), p. 741-4, 1995-Sep.
dc.identifier0264-6021
dc.identifier
dc.identifierhttp://www.ncbi.nlm.nih.gov/pubmed/7575404
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/193813
dc.identifier7575404
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1294046
dc.descriptionWe have investigated whether angiotensin II (AII) is able to induce insulin receptor substrate 1 (IRS-1) phosphorylation and its association with phosphatidylinositol 3-kinase (PI 3-kinase) in the rat heart in vivo. The phosphorylation state of IRS-1 following infusion of insulin or AII via the vena cava was assessed after immunoprecipitation with an anti-peptide antibody to IRS-1 followed by immunoblotting with an anti-phosphotyrosine antibody and an anti-PI 3-kinase antibody. Densitometry indicated a 5.6 +/- 1.3-fold increase in IRS-1 phosphorylation after stimulation with AII and a 12.8 +/- 3.1-fold increase after insulin. The effect was maximal at an AII concentration of 10(-8) M and occurred 1 min after infusion. There was also a 6.1 +/- 1.2-fold increase in IRS-1-associated PI 3-kinase in response to AII. In the isolated perfused heart the result was similar, showing a direct effect of AII on this pathway. When the animals were pretreated for 1 h with DuP 753, a non-peptide AII-receptor 1 (AT1 receptor) antagonist, there was a marked reduction in the AII-induced tyrosine phosphorylation of IRS-1, suggesting that phosphorylation is initially mediated by the AT1 receptor. We conclude that AII stimulates tyrosine phosphorylation of IRS-1 and its association with PI 3-kinase. This pathway thus represents an additional signalling mechanism stimulated by AII in the rat heart in vivo.
dc.description310 ( Pt 3)
dc.description741-4
dc.languageeng
dc.relationThe Biochemical Journal
dc.relationBiochem. J.
dc.rightsfechado
dc.rights
dc.sourcePubMed
dc.subjectAngiotensin Ii
dc.subjectAnimals
dc.subjectElectrophoresis, Polyacrylamide Gel
dc.subjectImmunoblotting
dc.subjectIn Vitro Techniques
dc.subjectInsulin
dc.subjectInsulin Receptor Substrate Proteins
dc.subjectMale
dc.subjectMolecular Weight
dc.subjectMyocardium
dc.subjectPhosphatidylinositol 3-kinases
dc.subjectPhosphoproteins
dc.subjectPhosphorylation
dc.subjectPhosphotransferases (alcohol Group Acceptor)
dc.subjectPhosphotyrosine
dc.subjectRats
dc.subjectTyrosine
dc.titleAngiotensin Ii Induces Tyrosine Phosphorylation Of Insulin Receptor Substrate 1 And Its Association With Phosphatidylinositol 3-kinase In Rat Heart.
dc.typeArtículos de revistas


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