Home Itens selecionados Provedores de dados OAI Créditos Sobre Ajuda

			Busca avançada
	Provedor de dados 56 (2) Autor Giachini,F.R. (2) Lima,V.V. (2) Tostes,R.C. (2) Webb,R.C. (2) Carneiro,F.S. (1) Filgueira,F.P. (1) Hannan,J.L. (1) Lobato,N.S. (1) Mais... Palavra-chave Ca2+ influx (1) Ca2+ release-activated Ca2+ channel (1) Intracellular Ca2+ store (1) Myosin light chain (1) O-GlcNAcylation (1) Sarcoplasmic reticulum (1) Vascular reactivity (1) Mais... Tipo do documento Info:eu-repo/semantics/article (2) Ano 2014 (1) 2011 (1) País Brazil (2) Idioma Inglês (2)		Ordenar por:  Relevância Autor Título Ano Registros recuperados: 2 Primeira ... 1 ... Última STIM1/Orai1-mediated store-operated Ca2+ entry: the tip of the iceberg 56 Giachini,F.R.; Lima,V.V.; Hannan,J.L.; Carneiro,F.S.; Webb,R.C.; Tostes,R.C.. Highly efficient mechanisms regulate intracellular calcium (Ca2+) levels. The recent discovery of new components linking intracellular Ca2+ stores to plasma membrane Ca2+ entry channels has brought new insight into the understanding of Ca2+ homeostasis. Stromal interaction molecule 1 (STIM1) was identified as a Ca2+ sensor essential for Ca2+ store depletion-triggered Ca2+ influx. Orai1 was recognized as being an essential component for the Ca2+ release-activated Ca2+ (CRAC) channel. Together, these proteins participate in store-operated Ca2+ channel function. Defective regulation of intracellular Ca2+ is a hallmark of several diseases. In this review, we focus on Ca2+ regulation by the STIM1/Orai1 pathway and review evidence that implicates STIM1/Orai1 in... Tipo: Info:eu-repo/semantics/article Palavras-chave: Ca2+ release-activated Ca2+ channel; Sarcoplasmic reticulum; Intracellular Ca2+ store; Ca2+ influx. Ano: 2011 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2011001100002 Vascular O-GlcNAcylation augments reactivity to constrictor stimuli by prolonging phosphorylated levels of the myosin light chain 56 Lima,V.V.; Lobato,N.S.; Filgueira,F.P.; Webb,R.C.; Tostes,R.C.; Giachini,F.R.. O-GlcNAcylation is a modification that alters the function of numerous proteins. We hypothesized that augmented O-GlcNAcylation levels enhance myosin light chain kinase (MLCK) and reduce myosin light chain phosphatase (MLCP) activity, leading to increased vascular contractile responsiveness. The vascular responses were measured by isometric force displacement. Thoracic aorta and vascular smooth muscle cells (VSMCs) from rats were incubated with vehicle or with PugNAc, which increases O-GlcNAcylation. In addition, we determined whether proteins that play an important role in the regulation of MLCK and MLCP activity are directly affected by O-GlcNAcylation. PugNAc enhanced phenylephrine (PE) responses in rat aortas (maximal effect, 14.2±2 vs 7.9±1 mN for... Tipo: Info:eu-repo/semantics/article Palavras-chave: O-GlcNAcylation; Myosin light chain; Vascular reactivity. Ano: 2014 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2014001000826 Registros recuperados: 2 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