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Registros recuperados: 13 | |
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Human skinned muscle fibers were used to investigate the effects of bovine serum albumin (BSA) on the tension/pCa relationship and on the functional properties of the Ca2+-release channel of the sarcoplasmic reticulum (SR). In both fast- and slow-type fibers, identified by their tension response to pSr 5.0, BSA (0.7-15 µM) had no effect on the Ca2+ affinity of the contractile proteins and elicited no tension per se in Ca2+-loaded fibers. In contrast, BSA (>1.0 µM) potentiated the caffeine-induced tension in Ca2+-loaded fibers, this effect being more intense in slow-type fibers. Thus, BSA reduced the threshold caffeine concentration required for eliciting detectable tension, and increased the amplitude, the rate of rise and the area under the curve... |
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Palavras-chave: Calcium-release channel; Sarcoplasmic reticulum; Human muscle fiber; Bovine serum albumin; Caffeine. |
Ano: 1997 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X1997000500017 |
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Carneiro-Júnior,M.A.; Quintão-Júnior,J.F.; Drummond,L.R.; Lavorato,V.N.; Drummond,F.R.; Amadeu,M.A.; Oliveira,E.M.; Felix,L.B.; Cruz,J.S.; Mill,J.G.; Natali,A.J.; Prímola-Gomes,T.N.. |
In cardiomyocytes, calcium (Ca2+) release units comprise clusters of intracellular Ca2+ release channels located on the sarcoplasmic reticulum, and hypertension is well established as a cause of defects in calcium release unit function. Our objective was to determine whether endurance exercise training could attenuate the deleterious effects of hypertension on calcium release unit components and Ca2+ sparks in left ventricular myocytes of spontaneously hypertensive rats. Male Wistar and spontaneously hypertensive rats (4 months of age) were divided into 4 groups: normotensive (NC) and hypertensive control (HC), and normotensive (NT) and hypertensive trained (HT) animals (7 rats per group). NC and HC rats were submitted to a low-intensity treadmill running... |
Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Physical activity; Hypertension; Cardiomyocyte; Calcium handling; Sarcoplasmic reticulum. |
Ano: 2014 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2014001100960 |
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HIDALGO,CECILIA; ARACENA,PAULA; SANCHEZ,GINA; DONOSO,PAULINA. |
In skeletal and cardiac muscle cells, specific isoforms of the Ryanodine receptor channels mediate Ca2+ release from the sarcoplasmic reticulum. These channels are highly susceptible to redox modifications, which regulate channel activity. In this work, we studied the effects of Ca2+ (endogenous agonist) and Mg2+ (endogenous inhibitor) on the kinetics of Ca2+ release from sarcoplasmic reticulum vesicles isolated from skeletal or cardiac mammalian muscle. Native skeletal vesicles exhibited maximal stimulation of release kinetics by 10-20 µM [Ca2+], whereas in native cardiac vesicles, maximal stimulation of release required only 1 µM [Ca2+]. In 10 µM [Ca2+], free [Mg2+] < 0.1 mM produced marked inhibition of release from skeletal vesicles but free [Mg2+]... |
Tipo: Journal article |
Palavras-chave: Redox state; Ryanodine receptors; Sarcoplasmic reticulum; Calcium release kinetics; Mg2+ inhibition; S-nitrosoglutathione. |
Ano: 2002 |
URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0716-97602002000200009 |
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FARRELL,EMILY F; ANTARAMIAN,ANAID; BENKUSKY,NANCY; ZHU,XINSHENG; RUEDA,ANGÉLICA; GÓMEZ,ANA M; VALDIVIA,HÉCTOR H. |
Activation of Ca2+ release channels/ryanodine receptors (RyR) by the inward Ca2+ current (I Ca) gives rise to Ca2+-induced Ca2+ release (CICR), the amplifying Ca2+ signaling mechanism that triggers contraction of the heart. CICR, in theory, is a high-gain, self-regenerating process, but an unidentified mechanism stabilizes it in vivo. Sorcin, a 21.6 kDa Ca2+-binding protein, binds to cardiac RyRs with high affinity and completely inhibits channel activity. Sorcin significantly inhibits both the spontaneous activity of RyRs in quiescent cells (visualized as Ca2+ sparks) and the I Ca-triggered activity of RyRs that gives rise to [Ca2+]i transients. Since sorcin decreases the amplitude of the [Ca2+]i transient without affecting the amplitude of I Ca, the... |
Tipo: Journal article |
Palavras-chave: Sorcin; Ryanodine receptors; CICR; Dihydropyridine receptor; Sarcoplasmic reticulum. |
Ano: 2004 |
URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0716-97602004000400015 |
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HIDALGO,CECILIA; BULL,RICARDO; MARENGO,JUAN J; PÉREZ,CLAUDIO F; DONOSO,PAULINA. |
The effects of redox reagents on the activity of the intracellular calcium release channels (ryanodine receptors) of skeletal and cardiac muscle, or brain cortex neurons, was examined. In lipid bilayer experiments, oxidizing agents (2,2'-dithiodipyridine or thimerosal) modified the calcium dependence of all single channels studied. After controlled oxidation channels became active at sub µM calcium concentrations and were not inhibited by increasing the calcium concentration to 0.5 mM. Subsequent reduction reversed these effects. Channels purified from amphibian skeletal muscle exhibited the same behavior, indicating that the SH groups responsible for modifying the calcium dependence belong to the channel protein. Parallel experiments that... |
Tipo: Journal article |
Palavras-chave: Calcium dependence; Neurons; Redox state; Ryanodine receptors; Sarcoplasmic reticulum; Skeletal and cardiac muscle. |
Ano: 2000 |
URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0716-97602000000200011 |
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WILLIAMS,ALAN J; TANNA,BHAVNA. |
Ryanodine binds with high affinity and specificity to a class of Ca2+-release channels known as ryanodine receptors (RyR). The interaction with RyR results in a dramatic alteration in function with open probability (Po) increasing markedly and rates of ion translocation modified. We have investigated the features of ryanodine that govern the interaction of the ligand with RyR and the mechanisms underlying the subsequent alterations in function by monitoring the effects of congeners and derivatives of ryanodine (ryanoids) on individual RyR2 channels. While the interaction of all tested ryanoids results in an increased Po, the amplitude of the modified conductance state depends upon the structure of the ryanoid. We propose that different rates of cation... |
Tipo: Journal article |
Palavras-chave: Calcium; Ca2+-release channel; Sarcoplasmic reticulum; Ryanodine; Single channel. |
Ano: 2004 |
URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0716-97602004000400006 |
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Registros recuperados: 13 | |
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