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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
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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
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