Cardiac ryanodine receptor activation by high Ca2+ store load is reversed in a reducing cytoplasmic redox environment
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منابع مشابه
Correction: Cardiac ryanodine receptor activation by a high Ca2+ store load is reversed in a reducing cytoplasmic redox environment
There was an error published in J. Cell Sci. 127, 4531-4541. Incorrect concentrations of the components used to establish the oxidising redox potential were given in the ‘Redox buffering’ section of the Materials and Methods. The correct sentence should read: An oxidising redox potential of −180 mV was established with 0.95 mM GSH and 0.1 mM GSSG. The authors apologise to the readers for any co...
متن کاملCardiac ryanodine receptor activation by a high Ca2+ store load is reversed in a reducing cytoplasmic redox environment
Here, we report the impact of redox potential on isolated cardiac ryanodine receptor (RyR2) channel activity and its response to physiological changes in luminal [Ca(2+)]. Basal leak from the sarcoplasmic reticulum is required for normal Ca(2+) handling, but excess diastolic Ca(2+) leak attributed to oxidative stress is thought to lower the threshold of RyR2 for spontaneous sarcoplasmic reticul...
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Caffeine has long been used as a pharmacological probe for studying RyR (ryanodine receptor)-mediated Ca(2+) release and cardiac arrhythmias. However, the precise mechanism by which caffeine activates RyRs is elusive. In the present study, we investigated the effects of caffeine on spontaneous Ca(2+) release and on the response of single RyR2 (cardiac RyR) channels to luminal or cytosolic Ca(2+...
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Introduction Cardiac myocyte contraction is driven by the coordinated release of Ca from the sarcoplasmic reticulum (SR). This release of Ca occurs through the cardiac RyR2. Physiologically, Ca release occurs in response to an influx of Ca through L-type Ca channels, via a mechanism termed CICR. This transient increase in cytosolic Ca activates the RyR2 channel as a result of Ca binding to the ...
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Activation of the cardiac ryanodine receptor (RyR2) by Ca(2)+ is an essential step in excitation-contraction coupling in heart muscle. However, little is known about the molecular basis of activation of RyR2 by Ca(2)+. In this study, we investigated the role in Ca(2)+ sensing of the conserved glutamate 3987 located in the predicted transmembrane segment M2 of the mouse RyR2. Single point mutati...
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ژورنال
عنوان ژورنال: Journal of Cell Science
سال: 2014
ISSN: 1477-9137,0021-9533
DOI: 10.1242/jcs.156760