Angiotensin Ii Induces Tyrosine Phosphorylation Of Insulin Receptor Substrate 1 And Its Association With Phosphatidylinositol 3-kinase In Rat Heart

dc.creatorSaad M.J.A.
dc.creatorVelloso L.A.
dc.creatorCarvalho C.R.O.
dc.date1995
dc.date2015-06-26T17:14:11Z
dc.date2015-11-26T14:20:11Z
dc.date2015-06-26T17:14:11Z
dc.date2015-11-26T14:20:11Z
dc.date.accessioned2018-03-28T21:21:48Z
dc.date.available2018-03-28T21:21:48Z
dc.identifier
dc.identifierBiochemical Journal. , v. 310, n. 3, p. 741 - 744, 1995.
dc.identifier2646021
dc.identifier
dc.identifierhttp://www.scopus.com/inward/record.url?eid=2-s2.0-0029147360&partnerID=40&md5=a921e09854e6012138f63a5e3b83d1f4
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/95855
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/95855
dc.identifier2-s2.0-0029147360
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1244169
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 ocurred 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
dc.description3
dc.description741
dc.description744
dc.languageen
dc.publisher
dc.relationBiochemical Journal
dc.rightsfechado
dc.sourceScopus
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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