Sabiia Seb
PortuguêsEspañolEnglish
Embrapa
        Busca avançada

Botão Atualizar


Botão Atualizar

Ordenar por: 

RelevânciaAutorTítuloAnoImprime registros no formato resumido
Registros recuperados: 4
Primeira ... 1 ... Última
Imagem não selecionada

Imprime registro no formato completo
A high-fructose diet induces insulin resistance but not blood pressure changes in normotensive rats BJMBR
Bezerra,R.M.N.; Ueno,M.; Silva,M.S.; Tavares,D.Q.; Carvalho,C.R.O.; Saad,M.J.A.; Gontijo,J.A.R..
Rats fed a high-fructose diet represent an animal model for insulin resistance and hypertension. We recently showed that a high-fructose diet containing vegetable oil but a normal sodium/potassium ratio induced mild insulin resistance with decreased insulin receptor substrate-1 tyrosine phosphorylation in the liver and muscle of normal rats. In the present study, we examined the mean blood pressure, serum lipid levels and insulin sensitivity by estimating in vivo insulin activity using the 15-min intravenous insulin tolerance test (ITT, 0.5 ml of 6 µg insulin, iv) followed by calculation of the rate constant for plasma glucose disappearance (Kitt) in male Wistar-Hannover rats (110-130 g) randomly divided into four diet groups: control, 1:3 sodium/potassium...
Tipo: Info:eu-repo/semantics/article Palavras-chave: High-fructose diet; Insulin resistance; Blood pressure; Hypertriglyceridemia; Plasma cholesterol.
Ano: 2001 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2001000900008
Imagem não selecionada

Imprime registro no formato completo
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
Imagem não selecionada

Imprime registro no formato completo
The insulin receptor substrate 1 associates with phosphotyrosine phosphatase SHPTP2 in liver and muscle of rats BJMBR
Lima,M.H.M.; Zambelli,J.E.; Carvalho,C.R.O.; 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) which, in turn, associates with proteins containing SH2 domains. It has been shown that IRS-1 associates with the tyrosine phosphatase SHPTP2 in cell cultures. While the effect of the IRS-1/SHPTP2 association on insulin signal transduction is not completely known, this association may dephosphorylate IRS-1 and may play a critical role in the mitogenic actions of insulin. However, there is no physiological demonstration of this pathway of insulin action in animal tissues. In the present study we investigated the ability of insulin to induce association between IRS-1 and SHPTP2 in liver and muscle...
Tipo: Info:eu-repo/semantics/other Palavras-chave: Insulin action; Insulin receptor substrate; Phosphotyrosine phosphatase; SHPTP2.
Ano: 1998 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X1998001100007
Imagem não selecionada

Imprime registro no formato completo
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
Registros recuperados: 4
Primeira ... 1 ... Última
 

Empresa Brasileira de Pesquisa Agropecuária - Embrapa
Todos os direitos reservados, conforme Lei n° 9.610
Política de Privacidade
Área restrita

Embrapa
Parque Estação Biológica - PqEB s/n°
Brasília, DF - Brasil - CEP 70770-901
Fone: (61) 3448-4433 - Fax: (61) 3448-4890 / 3448-4891 SAC: https://www.embrapa.br/fale-conosco

Valid HTML 4.01 Transitional