ArticleBiophysical journal2016
Oxidation of RyR2 Has a Biphasic Effect on the Threshold for Store Overload-Induced Calcium Release.
Article in Biophysical journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed.
- Trial
- Local calcium dynamics and signalling in cardiomyocytes.Nature reviews. Cardiology · 2026Review
- Time-dependent effect of FKBP12 loss in the development of dilated cardiomyopathy.The Journal of general physiology · 2025Article
- S-nitrosylation of cardiac myocyte proteins may underlie sex differences in cardiac disease.Frontiers in physiology · 2025Review
- Clustering properties of the cardiac ryanodine receptor in health and heart failure.Journal of molecular and cellular cardiology · 2023Review
- Direct regulation of the cardiac ryanodine receptor (RyR2) by O-GlcNAcylation.Cardiovascular diabetology · 2023Article
- NADPH Oxidases and Oxidative Stress in the Pathogenesis of Atrial Fibrillation.Antioxidants (Basel, Switzerland) · 2023Review
- The function and regulation of calsequestrin-2: implications in calcium-mediated arrhythmias.Biophysical reviews · 2022Review
- Regulation of cardiac ryanodine receptor function by the cyclic-GMP dependent protein kinase G.Current research in physiology · 2022Article
- Human Atrial Fibrillation Is Not Associated With Remodeling of Ryanodine Receptor Clusters.Frontiers in cell and developmental biology · 2021Article
- Ryanodine Receptor Type 2: A Molecular Target for Dichlorodiphenyltrichloroethane- and Dichlorodiphenyldichloroethylene-Mediated Cardiotoxicity.Toxicological sciences : an official journal of the Society of Toxicology · 2020Article
- Understanding How Phosphorylation and Redox Modifications Regulate Cardiac Ryanodine Receptor Type 2 Activity to Produce an Arrhythmogenic Phenotype in Advanced Heart Failure.ACS pharmacology & translational science · 2020Review
- Sarcoplasmic reticulum calcium mishandling: central tenet in heart failure?Biophysical reviews · 2020Review
- Fibroblast growth factor 9 (FGF9) inhibits myogenic differentiation of C2C12 and human muscle cells.Cell cycle (Georgetown, Tex.) · 2019Article
- Activation of RyR2 by class I kinase inhibitors.British journal of pharmacology · 2019Article
- Dyadic Plasticity in Cardiomyocytes.Frontiers in physiology · 2018Review
- Control of cardiac ryanodine receptor by sarcoplasmic reticulum luminal CaThe Journal of general physiology · 2017Review
- FK506-binding proteins 12 and 12.6 (FKBPs) as regulators of cardiac Ryanodine Receptors: Insights from new functional and structural knowledge.Channels (Austin, Tex.) · 2017Review
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
At the single-channel level, oxidation of the cardiac ryanodine receptor (RyR2) is known to activate and inhibit the channel depending on the level of oxidation. However, the mechanisms through which these changes alter the activity of RyR2 in a cellular setting are poorly understood. In this study, we determined the effect of oxidation on a common form of RyR2 regulation; store overload-induced Ca(2+) release (SOICR). We found that oxidation resulted in concentration and time-dependent changes in the activation threshold for SOICR. Low concentrations of the oxidant H2O2 resulted in a decrease in the threshold for SOICR, which led to an increase in SOICR events. However, higher concentrations of H2O2, or prolonged exposure, reversed these changes and led to an increase in the threshold for SOICR. This increase in the threshold for SOICR in most cells was to such an extent that it led to the complete inhibition of SOICR. Acute exposure to high concentrations of H2O2 led to an initial decrease and then increase in the threshold for SOICR. In the majority of cells the increased threshold could not be reversed by the application of the reducing agent dithiothreitol. Therefore, our data suggest that low levels of RyR2 oxidation increase the channel activity by decreasing the threshold for SOICR, whereas high levels of RyR2 oxidation irreversibly increase the threshold for SOICR leading to an inhibition of RyR2. Combined, this indicates that oxidation regulates RyR2 by the same mechanism as phosphorylation, methylxanthines, and mutations, via changes in the threshold for SOICR.
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