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Insulin receptor has tyrosine kinase activity toward Shc in rat liver BJMBR
Páez-Espinosa,E.V.; Carvalho,C.R.O.; Velloso,L.A.; Saad,M.J.A..
Insulin induces tyrosine phosphorylation of Shc in cell cultures and in insulin-sensitive tissues of the intact rat. However, the ability of insulin receptor (IR) tyrosine kinase to phosphorylate Shc has not been previously demonstrated. In the present study, we investigated insulin-induced IR tyrosine kinase activity towards Shc. Insulin receptor was immunoprecipitated from liver extracts, before and after a very low dose of insulin into the portal vein, and incubated with immunopurified Shc from liver of untreated rats. The kinase assay was performed in vitro in the presence of exogenous ATP and the phosphorylation level was quantified by immunoblotting with antiphosphotyrosine antibody. The results demonstrate that Shc interacted with insulin receptor...
Tipo: Info:eu-repo/semantics/other Palavras-chave: Tyrosine kinase activity; Insulin receptor; Shc; Insulin action.
Ano: 1998 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X1998001100008
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