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	Provedor de dados BJMBR (4) Autor Kettelhut,I.C. (4) Baviera,A.M. (1) Brunetti,I.L. (1) Folgado,V.B.B. (1) Foss,M.C. (1) Gouveia,L.M.F.B. (1) Manfredi,L.H. (1) Navegantes,L.C.C. (1) Paula-Gomes,S. (1) Pepato,M.T. (1) Zanon,N.M. (1) Mais... Palavra-chave Skeletal muscle (2) Antidiabetic plant (1) Calpain (1) Calpastatin (1) Cardiomyocytes (1) Diabetic rats (1) Epinephrine (1) Eugenia jambolana (1) Gluconeogenesis (1) Hyperglycemia (1) Insulin resistance (1) Myostatin (1) Norepinephrine (1) Peripheral glucose utilization (1) Protein degradation (1) Protein synthesis (1) Spontaneously hypertensive rats (1) Mais... Tipo do documento Info:eu-repo/semantics/article (4) Ano 2017 (1) 2009 (1) 2001 (1) 2000 (1) País Brazil (4) Idioma Inglês (4)		Ordenar por:  Relevância Autor Título Ano Registros recuperados: 4 Primeira ... 1 ... Última Abnormalities of glucose metabolism in spontaneously hypertensive rats BJMBR Gouveia,L.M.F.B.; Kettelhut,I.C.; Foss,M.C.. Abnormalities in glucose metabolism and insulin action are frequently detected in patients with essential hypertension. Spontaneously hypertensive rats (SHR) have been used as an experimental model to understand this pathological condition. The objective of the present study was to assess glucose metabolism and insulin action in SHR and Wistar rats under fed and fasting conditions. Peripheral glucose utilization was estimated by kinetic studies with [6-³H]-glucose and gluconeogenetic activity was measured during continuous [14C]-bicarbonate infusion. Plasma glucose levels were higher in the SHR group. Plasma insulin levels in the fed state were higher in the SHR group (99.8 ± 6.5 µM) than in the control group (70.4 ± 3.6 µM). Muscle glycogen content was... Tipo: Info:eu-repo/semantics/article Palavras-chave: Peripheral glucose utilization; Gluconeogenesis; Insulin resistance; Spontaneously hypertensive rats. Ano: 2000 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2000001100015 Lack of antidiabetic effect of a Eugenia jambolana leaf decoction on rat streptozotocin diabetes BJMBR Pepato,M.T.; Folgado,V.B.B.; Kettelhut,I.C.; Brunetti,I.L.. Streptozotocin-diabetic rats were treated for 17 days with a decoction of Eugenia jambolana (Myrtaceae) leaves (15%, w/v) as a substitute for water. Body weight, food and fluid intake, urine volume, glycemia, urinary glucose and urea were evaluated every 5 days. The animals were sacrificed by decapitation and blood samples collected for the determination of glycemia, serum cholesterol, HDL-cholesterol, triglycerides and angiotensin-converting enzyme. The weight of adipose and muscle tissues was also determined. There were no statistically significant differences between treated and untreated rats for any of the biochemical or physiological parameters. We conclude that, at least in this experimental model, Eugenia jambolana leaf decoction has no... Tipo: Info:eu-repo/semantics/article Palavras-chave: Antidiabetic plant; Hyperglycemia; Diabetic rats; Eugenia jambolana. Ano: 2001 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2001000300014 Myostatin promotes distinct responses on protein metabolism of skeletal and cardiac muscle fibers of rodents BJMBR Manfredi,L.H.; Paula-Gomes,S.; Zanon,N.M.; Kettelhut,I.C.. Myostatin is a novel negative regulator of skeletal muscle mass. Myostatin expression is also found in heart in a much less extent, but it can be upregulated in pathological conditions, such as heart failure. Myostatin may be involved in inhibiting protein synthesis and/or increasing protein degradation in skeletal and cardiac muscles. Herein, we used cell cultures and isolated muscles from rats to determine protein degradation and synthesis. Muscles incubated with myostatin exhibited an increase in proteolysis with an increase of Atrogin-1, MuRF1 and LC3 genes. Extensor digitorum longus muscles and C2C12 myotubes exhibited a reduction in protein turnover. Cardiomyocytes showed an increase in proteolysis by activating autophagy and the ubiquitin proteasome... Tipo: Info:eu-repo/semantics/article Palavras-chave: Myostatin; Skeletal muscle; Cardiomyocytes; Protein degradation; Protein synthesis. Ano: 2017 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2017001200604 The inhibitory role of sympathetic nervous system in the Ca2+-dependent proteolysis of skeletal muscle BJMBR Navegantes,L.C.C.; Baviera,A.M.; Kettelhut,I.C.. Mammalian cells contain several proteolytic systems to carry out the degradative processes and complex regulatory mechanisms to prevent excessive protein breakdown. Among these systems, the Ca2+-activated proteolytic system involves the cysteine proteases denoted calpains, and their inhibitor, calpastatin. Despite the rapid progress in molecular research on calpains and calpastatin, the physiological role and regulatory mechanisms of these proteins remain obscure. Interest in the adrenergic effect on Ca2+-dependent proteolysis has been stimulated by the finding that the administration of β2-agonists induces muscle hypertrophy and prevents the loss of muscle mass in a variety of pathologic conditions in which calpains are activated. This review summarizes... Tipo: Info:eu-repo/semantics/article Palavras-chave: Epinephrine; Norepinephrine; Calpastatin; Calpain; Skeletal muscle. Ano: 2009 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2009000100005 Registros recuperados: 4 Primeira ... 1 ... Última

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