dc.creator | Saad, M J | |
dc.creator | Velloso, L A | |
dc.creator | Carvalho, C R | |
dc.date | 1995-Sep | |
dc.date | 2015-11-27T12:18:33Z | |
dc.date | 2015-11-27T12:18:33Z | |
dc.date.accessioned | 2018-03-29T00:51:23Z | |
dc.date.available | 2018-03-29T00:51:23Z | |
dc.identifier | The Biochemical Journal. v. 310 ( Pt 3), p. 741-4, 1995-Sep. | |
dc.identifier | 0264-6021 | |
dc.identifier | | |
dc.identifier | http://www.ncbi.nlm.nih.gov/pubmed/7575404 | |
dc.identifier | http://repositorio.unicamp.br/jspui/handle/REPOSIP/193813 | |
dc.identifier | 7575404 | |
dc.identifier.uri | http://repositorioslatinoamericanos.uchile.cl/handle/2250/1294046 | |
dc.description | We 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.description | 310 ( Pt 3) | |
dc.description | 741-4 | |
dc.language | eng | |
dc.relation | The Biochemical Journal | |
dc.relation | Biochem. J. | |
dc.rights | fechado | |
dc.rights | | |
dc.source | PubMed | |
dc.subject | Angiotensin Ii | |
dc.subject | Animals | |
dc.subject | Electrophoresis, Polyacrylamide Gel | |
dc.subject | Immunoblotting | |
dc.subject | In Vitro Techniques | |
dc.subject | Insulin | |
dc.subject | Insulin Receptor Substrate Proteins | |
dc.subject | Male | |
dc.subject | Molecular Weight | |
dc.subject | Myocardium | |
dc.subject | Phosphatidylinositol 3-kinases | |
dc.subject | Phosphoproteins | |
dc.subject | Phosphorylation | |
dc.subject | Phosphotransferases (alcohol Group Acceptor) | |
dc.subject | Phosphotyrosine | |
dc.subject | Rats | |
dc.subject | Tyrosine | |
dc.title | Angiotensin Ii Induces Tyrosine Phosphorylation Of Insulin Receptor Substrate 1 And Its Association With Phosphatidylinositol 3-kinase In Rat Heart. | |
dc.type | Artículos de revistas | |