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	Provedor de dados Biol. Res. (1) BJMBR (1) Autor Cunha,V.M.N. (1) Einicker-Lamas,M. (1) MEISEL,LEE A (1) Muzi-Filho,H. (1) Noel,F. (1) Quintas,L.E.M. (1) Rodriguez,J.B.R. (1) SILVA,HERMAN (1) URBINA,DANIELA C (1) Valverde,R.H.F. (1) Mais... Palavra-chave Thapsigargin (2) Arabidopsis thaliana (1) Ca2+-ATPases (1) Ca2+/calmodulin-dependent kinase II (1) Calcium (1) Calcium homeostasis (1) Calmodulin (1) Gravitropism (1) Rat vas deferens (1) Root (1) SERCA2 (1) Mais... Tipo do documento Info:eu-repo/semantics/article (1) Journal article (1) Ano 2013 (1) 2006 (1) País Brazil (1) Chile (1) 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 The Ca2+ pump inhibitor, thapsigargin, inhibits root gravitropism in Arabidopsis thaliana Biol. Res. URBINA,DANIELA C; SILVA,HERMAN; MEISEL,LEE A. Thapsigargin, a specific inhibitor of most animal intracellular SERCA-type Ca2+ pumps present in the sarcoplasmic/endoplasmic reticulum, was originally isolated from the roots of the Mediterranean plant Thapsia gargancia L. Here, we demonstrate that this root-derived compound is capable of altering root gravitropism in Arabidopsis thaliana. Thapsigargin concentrations as low as 0.1 µM alter root gravitropism whereas under similar conditions cyclopiazonic acid does not. Furthermore, a fluorescently conjugated thapsigargin (BODIPY FL thapsigargin) suggests that target sites for thapsigargin are located in intracellular organelles in the root distal elongation zone and the root cap, regions known to regulate root gravitropism Tipo: Journal article Palavras-chave: Arabidopsis thaliana; Ca2+-ATPases; Calcium; Gravitropism; Thapsigargin; Root. Ano: 2006 URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0716-97602006000200011 Registros recuperados: 2 Primeira ... 1 ... Última

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