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	Provedor de dados BJMBR (3) BABT (1) Autor Saad,M.J.A. (3) Carvalho,C.R.O. (2) Bezerra,R.M.N. (1) Brenelli,S.L. (1) Carvalho,C.R. (1) Chen,E. (1) Gontijo,J.A.R. (1) López,Jorge A. (1) Páez-Espinosa,E.V. (1) Sasse,A.D. (1) Silva,M.S. (1) Souza,Alzira Martins Ferreira de (1) Tavares,D.Q. (1) Ueno,M. (1) Velloso,L.A. (1) Mais... Palavra-chave Insulin receptor (4) Insulin action (2) Fructose (1) Insulin (1) Insulin receptor substrate (1) Insulin-like (1) Invertebrate (1) Pp185 phosphorylation (1) Shc (1) Tyrosine kinase activity (1) Unicellular (1) Unilateral nephrectomy (1) Mais... Tipo do documento Info:eu-repo/semantics/article (2) Info:eu-repo/semantics/other (2) Ano 2004 (1) 2000 (1) 1998 (1) 1997 (1) País Brazil (4) Idioma Inglês (4)		Ordenar por:  Relevância Autor Título Ano Registros recuperados: 4 Primeira ... 1 ... Última Insulin or insulin-like studies on unicellular organisms: a review BABT Souza,Alzira Martins Ferreira de; López,Jorge A.. This paper presents a review of studies about insulin and insulin-like substances in prokaryotes, eukaryotes and fungi have been published over the last two decades, constituting an updating of our previous review (1988) which included references to invertebrate insulin or insulin-like substances both in uni- and pluricellular Monera, Protoctista, Fungii and Animal species. This present article reviews experiments and evidence obtained using modern techniques in the understanding of molecule evolution and behaviour, which confirm its very ancient molecular structure origin. The involvement of insulin-like and related material in signalling biological pathway and modulator effects is also reported. Tipo: Info:eu-repo/semantics/article Palavras-chave: Unicellular; Invertebrate; Insulin; Insulin-like; Insulin receptor. Ano: 2004 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132004000600017 Tissue-specific regulation of IRS-1 in unilaterally nephrectomized rats BJMBR Sasse,A.D.; Chen,E.; Carvalho,C.R.O.; Gontijo,J.A.R.; Brenelli,S.L.; Saad,M.J.A.. Insulin stimulates the tyrosine kinase activity of its receptor, resulting in the phosphorylation of its cytosolic substrate, insulin receptor substrate 1 (IRS-1). IRS-1 is also a substrate for different peptides and growth factors, and a transgenic mouse "knockout" for this protein does not have normal growth. However, the role of IRS-1 in kidney hypertrophy and/or hyperplasia was not investigated. In the present study we investigated IRS-1 protein and tyrosine phosphorylation levels in the remnant kidney after unilateral nephrectomy (UNX) in 6-week-old male Wistar rats. After insulin stimulation the levels of insulin receptor and IRS-1 tyrosine phosphorylation were reduced to 79 ± 5% (P<0.005) and 58 ± 6% (P<0.0001), respectively, of the... Tipo: Info:eu-repo/semantics/article Palavras-chave: Insulin receptor; Insulin receptor substrate; Unilateral nephrectomy; Insulin action. Ano: 1997 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X1997001000004 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 A high-fructose diet induces changes in pp185 phosphorylation in muscle and liver of rats BJMBR Ueno,M.; Bezerra,R.M.N.; Silva,M.S.; Tavares,D.Q.; Carvalho,C.R.; Saad,M.J.A.. Insulin stimulates the tyrosine kinase activity of its receptor resulting in the tyrosine phosphorylation of pp185, which contains insulin receptor substrates IRS-1 and IRS-2. These early steps in insulin action are essential for the metabolic effects of insulin. Feeding animals a high-fructose diet results in insulin resistance. However, the exact molecular mechanism underlying this effect is unknown. In the present study, we determined the levels and phosphorylation status of the insulin receptor and pp185 (IRS-1/2) in liver and muscle of rats submitted to a high-fructose diet evaluated by immunoblotting with specific antibodies. Feeding fructose (28 days) induced a discrete insulin resistance, as demonstrated by the insulin tolerance test. Plasma... Tipo: Info:eu-repo/semantics/other Palavras-chave: Fructose; Insulin receptor; Pp185 phosphorylation. Ano: 2000 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2000001200004 Registros recuperados: 4 Primeira ... 1 ... Última

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