ArticleBiophysical journal1994
Gating of the native and purified cardiac SR Ca(2+)-release channel with monovalent cations as permeant species.
Article in Biophysical journal, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.
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Who cites it
57 citing papers in PubMed.
- Flecainide Specifically Targets the Monovalent Countercurrent Through the Cardiac Ryanodine Receptor, While a Dominant Opposing CaInternational journal of molecular sciences · 2024Article
- The biophysical properties of TRIC-A and TRIC-B and their interactions with RyR2.The Journal of general physiology · 2023Article
- The V2475F CPVT1 mutation yields distinct RyR2 channel populations that differ in their responses to cytosolic CaThe Journal of physiology · 2021Article
- Molecular basis for allosteric regulation of the type 2 ryanodine receptor channel gating by key modulators.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Ryanodine Receptor Open Times Are Determined in the Closed State.Biophysical journal · 2018Article
- Regulation of the RyR channel gating by CaBiophysical reviews · 2018Review
- Unambiguous observation of blocked states reveals altered, blocker-induced, cardiac ryanodine receptor gating.Scientific reports · 2016Article
- Effect of flecainide derivatives on sarcoplasmic reticulum calcium release suggests a lack of direct action on the cardiac ryanodine receptor.British journal of pharmacology · 2016Article
- The calcium-frequency response in the rat ventricular myocyte: an experimental and modelling study.The Journal of physiology · 2016Article
- Mechanisms of SR calcium release in healthy and failing human hearts.Biophysical reviews · 2015Article
- Article
- Termination of calcium puffs and coupled closings of inositol trisphosphate receptor channels.Cell calcium · 2014Article
- Differences in the regulation of RyR2 from human, sheep, and rat by Ca²⁺ and Mg²⁺ in the cytoplasm and in the lumen of the sarcoplasmic reticulum.The Journal of general physiology · 2014Article
- Type 2 ryanodine receptors are highly sensitive to alcohol.FEBS letters · 2014Article
- Eudistomin D and penaresin derivatives as modulators of ryanodine receptor channels and sarcoplasmic reticulum Ca2+ ATPase in striated muscle.Molecular pharmacology · 2014Article
- Quercetin as a fluorescent probe for the ryanodine receptor activity in Jurkat cells.Pflugers Archiv : European journal of physiology · 2013Article
- Investigations of the contribution of a putative glycine hinge to ryanodine receptor channel gating.The Journal of biological chemistry · 2013Article
- The contribution of hydrophobic residues in the pore-forming region of the ryanodine receptor channel to block by large tetraalkylammonium cations and Shaker B inactivation peptides.The Journal of general physiology · 2012Article
- FKBP12 activates the cardiac ryanodine receptor Ca2+-release channel and is antagonised by FKBP12.6.PloS one · 2012Article
- Mitsugumin 23 forms a massive bowl-shaped assembly and cation-conducting channel.Biochemistry · 2011Article
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2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The primary aim of this study was to characterize the steady-state gating of the native and the purified cardiac sarcoplasmic reticulum Ca(2+)-release channel using monovalent cations (K+ in the purified, Cs+ in the native) rather than Ca2+ as the permeant ions. The improved resolution of the single-channel events under these conditions has provided a more detailed and accurate description of channel gating than was previously possible. Micromolar cytosolic Ca2+ activates the channel but in the absence of other activating ligands cannot fully open the channel. The relationship between the open probability (Po) and cytosolic free [Ca2+] in both native and purified channels indicates the binding of at least three Ca2+ ions for maximal activation. Lifetime analysis indicates a minimum of three open and five closed states for channels activated solely by Ca2+ and demonstrates that the primary mechanism for the increase in Po is an increase in the frequency of channel opening. Burst analysis also indicates that Ca2+ activates the channel by binding to closed states of the channel to increase the frequency of channel opening. Correlations between successive lifetimes suggest the existence of at least two pathways between the open and closed states. At a given activating [Ca2+], the Po is lower at negative than at positive holding potentials; however, we find no change in the mechanisms of Ca2+ activation at different voltages. Po measurements and lifetime analysis indicate that the gating of the purified channel when activated by Ca2+ is indistinguishable from that of the native channel and indicate that the channels are not modified by the purification procedure.
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