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Registros recuperados: 4
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Control of dual isoforms of Ca2+ release channels in muscle Biol. Res.
RÍOS,EDUARDO; ZHOU,JINGSONG.
Here we compare excitation-contraction coupling in single muscle cells of frogs and rats. Because amphibians have isoform 3 (or b) of the ryanodine receptor/Ca2+ release channel, in addition to 1 (a), which is also present in the mammal, any extra feature present in the frog may in principle be attributed to isoform 3. Ca2+ release under voltage clamp depolarization has a peak and a steady phase in both taxonomic classes, but the peak is more marked in the frog, where the ratio of amplitudes of the two phases is voltage-dependent. This dependence is a hallmark of CICR. Confocal imaging identified Ca2+ sparks in the frog, but not in the voltage-clamped rat cells. Because Ca2+ sparks involve CICR both observations indicate that the contribution of CICR is...
Tipo: Journal article Palavras-chave: Excitation-contraction coupling; Sarcoplasmic reticulum; Ca2+ sparks; Ryanodine receptor; Calcium-induced calcium release.
Ano: 2004 URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0716-97602004000400012
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Modulation of sarcoplasmic reticulum calcium release by calsequestrin in cardiac myocytes Biol. Res.
GYÖRKE,SANDOR; GYÖRKE,INNA; TERENTYEV,DMITRY; VIATCHENKO-KARPINSKI,SERGE; WILLIAMS,SIMON C.
Calsequestrin (CASQ2) is a high capacity Ca-binding protein expressed inside the sarcoplasmic reticulum (SR). Mutations in the cardiac calsequestrin gene (CASQ2) have been linked to arrhythmias and sudden death induced by exercise and emotional stress. We have studied the function of CASQ2 and the consequences of arrhythmogenic CASQ2 mutations on intracellular Ca signalling using a combination of approaches of reverse genetics and cellular physiology in adult cardiac myocytes. We have found that CASQ2 is an essential determinant of the ability of the SR to store and release Ca2+ in cardiac muscle. CASQ2 serves as a reservoir for Ca2+ that is readily accessible for Ca2+-induced Ca2+ release (CICR) and also as an active Ca2+ buffer that modulates the local...
Tipo: Journal article Palavras-chave: Excitation-contraction coupling; Calcium-induced calcium release; Ryanodine receptor; Calsequestrin; Arrhythmia.
Ano: 2004 URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0716-97602004000400014
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Multigenerational Brazilian family with malignant hyperthermia and a novel mutation in the RYR1 gene BJMBR
Matos,A.R.; Sambuughin,N.; Rumjanek,F.D.; Amoedo,N.D.; Cunha,L.B.P.; Zapata-Sudo,G.; Sudo,R.T..
Malignant hyperthermia (MH) is a pharmacogenetic disease triggered in susceptible individuals by the administration of volatile halogenated anesthetics and/or succinylcholine, leading to the development of a hypermetabolic crisis, which is caused by abnormal release of Ca2+ from the sarcoplasmic reticulum, through the Ca2+ release channel ryanodine receptor 1 (RyR1). Mutations in the RYR1 gene are associated with MH in the majority of susceptible families. Genetic screening of a 5-generation Brazilian family with a history of MH-related deaths and a previous MH diagnosis by the caffeine halothane contracture test (CHCT) in some individuals was performed using restriction and sequencing analysis. A novel missense mutation, Gly4935Ser, was found in an...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Malignant hyperthermia; Mutation; Ryanodine receptor; Calcium channel.
Ano: 2009 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2009001200016
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Phosphorylation of Ryanodine Receptors Biol. Res.
DANILA,CRISTINA I; HAMILTON,SUSAN L.
Both cardiac and skeletal muscle ryanodine receptors (RyRs) are parts of large complexes that include a number of kinases and phosphatases. These RyRs have several potential phosphorylation sites in their cytoplasmic domains, but the functional consequences of phosphorylation and the identity of the enzymes responsible have been subjects of considerable controversy. Hyperphosphorylation of Ser-2809 in RyR2 (cardiac isoform) and Ser-2843 in RyR1 (skeletal isoform) has been suggested to cause the dissociation of the FK506-binding protein (FKBP) from RyRs, producing "leaky channels," but some laboratories find no relationship between phosphorylation and FKBP binding. Also debated is the identity of the kinases that phosphorylate these serines: cAMP-dependent...
Tipo: Journal article Palavras-chave: Ryanodine receptor; Phosphorylation site; Protein kinase; Ser-2809/Ser-2843; FK506-binding protein.
Ano: 2004 URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0716-97602004000400005
Registros recuperados: 4
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