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	Provedor de dados BJMBR (2) Autor Cunha,V.M.N. (2) Quintas,L.E.M. (2) Barreto,F. (1) Caricati-Neto,A. (1) Einicker-Lamas,M. (1) Jurkiewicz,A. (1) Muzi-Filho,H. (1) Noel,F. (1) Noël,F. (1) Rezende,D.C. (1) Rodriguez,J.B.R. (1) Scaramello,C.B.V. (1) Silva,C.L.M. (1) Valverde,R.H.F. (1) Mais... Palavra-chave Ca2+-ATPases (1) Ca2+/calmodulin-dependent kinase II (1) Calcium homeostasis (1) Calmodulin (1) Cardiac hypertrophy (1) Mitogen-activated protein kinases (1) Na+/K+-ATPase (1) Rat vas deferens (1) SERCA2 (1) Thapsigargin (1) Α1B-adrenoceptors (1) Mais... Tipo do documento Info:eu-repo/semantics/article (2) Ano 2013 (1) 2010 (1) País Brazil (2) Idioma Inglês (2)		Ordenar por:  Relevância Autor Título Ano Registros recuperados: 2 Primeira ... 1 ... Última Rat vas deferens SERCA2 is modulated by Ca2+/calmodulin protein kinase II-mediated phosphorylation BJMBR Rodriguez,J.B.R.; Muzi-Filho,H.; Valverde,R.H.F.; Quintas,L.E.M.; Noel,F.; Einicker-Lamas,M.; Cunha,V.M.N.. Ca2+ pumps are important players in smooth muscle contraction. Nevertheless, little information is available about these pumps in the vas deferens. We have determined which subtype of sarco(endo)plasmic reticulum Ca2+-ATPase isoform (SERCA) is expressed in rat vas deferens (RVD) and its modulation by calmodulin (CaM)-dependent mechanisms. The thapsigargin-sensitive Ca2+-ATPase from a membrane fraction containing the highest SERCA levels in the RVD homogenate has the same molecular mass (∼115 kDa) as that of SERCA2 from the rat cerebellum. It has a very high affinity for Ca2+ (Ca0.5 = 780 nM) and a low sensitivity to vanadate (IC50 = 41 µM). These facts indicate that SERCA2 is present in the RVD. Immunoblotting for CaM and Ca2+/calmodulin-dependent protein... Tipo: Info:eu-repo/semantics/article Palavras-chave: Ca2+/calmodulin-dependent kinase II; Calcium homeostasis; Calmodulin; Rat vas deferens; SERCA2; Thapsigargin. Ano: 2013 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2013000300227 Lack of evidence for regulation of cardiac P-type ATPases and MAP kinases in transgenic mice with cardiac-specific overexpression of constitutively active α1B-adrenoceptors BJMBR Barreto,F.; Rezende,D.C.; Scaramello,C.B.V.; Silva,C.L.M.; Cunha,V.M.N.; Caricati-Neto,A.; Jurkiewicz,A.; Noël,F.; Quintas,L.E.M.. The regulatory function of α1B-adrenoceptors in mammalian heart homeostasis is controversial. The objective of the present study was to characterize the expression/activity of key proteins implicated in cardiac calcium handling (Na+/K+-ATPase and Ca2+-ATPases) and growth (ERK1/2, JNK1/2 and p38) in mice with cardiac-selective overexpression of constitutively active mutant α1B-adrenoceptor (CAMα1B-AR), which present a mild cardiac hypertrophy phenotype. Immunoblot assays showed that myocardial plasma membrane Ca2+-ATPase (PMCA) expression was increased by 30% in CAMα1B-AR mice (N = 6, P < 0.05), although there was no change in sarco/endoplasmic reticulum Ca2+-ATPase (SERCA2) expression. Moreover, total Ca2+-ATPase activity was not modified, but a... Tipo: Info:eu-repo/semantics/article Palavras-chave: Α1B-adrenoceptors; Ca2+-ATPases; Cardiac hypertrophy; Na+/K+-ATPase; Mitogen-activated protein kinases. Ano: 2010 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2010000500012 Registros recuperados: 2 Primeira ... 1 ... Última

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