ArticleBiophysical journal1994
Chicken skeletal muscle ryanodine receptor isoforms: ion channel properties.
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 39 papers.
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Who cites it
39 citing papers in PubMed, 103 citations in OpenAlex.
- The biophysical properties of TRIC-A and TRIC-B and their interactions with RyR2.The Journal of general physiology · 2023Article
- Inositol-1,4,5-Trisphosphate Receptor-1 and -3 and Ryanodine Receptor-3 May Increase Ooplasmic CaThe journal of poultry science · 2022Article
- The Ryanodine Receptor as a Sensor for Intracellular Environments in Muscles.International journal of molecular sciences · 2021Review
- Finite element analysis predicts CaScientific reports · 2021Article
- Skeletal Muscle Transcriptome Analysis of Hanzhong Ma Duck at Different Growth Stages Using RNA-Seq.Biomolecules · 2021Article
- Extraocular muscle function is impaired inThe Journal of general physiology · 2019Article
- The structural basis of ryanodine receptor ion channel function.The Journal of general physiology · 2017Review
- Smooth Muscle Ion Channels and Regulation of Vascular Tone in Resistance Arteries and Arterioles.Comprehensive Physiology · 2017Review
- The couplonopathies: A comparative approach to a class of diseases of skeletal and cardiac muscle.The Journal of general physiology · 2015Review
- Structural and functional properties of ryanodine receptor type 3 in zebrafish tail muscle.The Journal of general physiology · 2015Article
- Action of perchlorate on the voltage dependent inactivation of excitation-contraction coupling in frog skeletal muscle fibres.Journal of muscle research and cell motility · 2007Article
- Differential sensitivity to perchlorate and caffeine of tetracaine-resistant Ca2+ release in frog skeletal muscle.Journal of muscle research and cell motility · 2006Article
- The inhibition of the sarcoplasmic/endoplasmic reticulum Ca2+-ATPase by macrocyclic lactones and cyclosporin A.The Biochemical journal · 2002Article
- DIDS modifies the conductance, gating, and inactivation mechanisms of the cardiac ryanodine receptor.Biophysical journal · 2002Article
- Calcium-induced transitions between the spontaneous miniature outward and the transient outward currents in retinal amacrine cells.The Journal of general physiology · 2002Article
- Type 3 ryanodine receptors of skeletal muscle are segregated in a parajunctional position.Proceedings of the National Academy of Sciences of the United States of America · 2002Article
- Markovian models of low and high activity levels of cardiac ryanodine receptors.Biophysical journal · 2001Article
- Comparison of Ca(2+) sparks produced independently by two ryanodine receptor isoforms (type 1 or type 3).Biophysical journal · 2000Article
- Spatially segregated control of Ca2+ release in developing skeletal muscle of mice.The Journal of physiology · 1999Article
- Contribution of ryanodine receptor type 3 to Ca(2+) sparks in embryonic mouse skeletal muscle.Biophysical journal · 1999Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
To define the roles of the alpha- and beta-ryanodine receptor (RyR) (sarcoplasmic reticulum Ca2+ release channel) isoforms expressed in chicken skeletal muscles, we investigated the ion channel properties of these proteins in lipid bilayers. alpha- and beta RyRs embody Ca2+ channels with similar conductances (792, 453, and 118 pS for K+, Cs+ and Ca2+) and selectivities (PCa2+/PK+ = 7.4), but the two channels have different gating properties. alpha RyR channels switch between two gating modes, which differ in the extent they are activated by Ca2+ and ATP, and inactivated by Ca2+. Either mode can be assumed in a spontaneous and stable manner. In a low activity mode, alpha RyR channels exhibit brief openings (tau o = 0.14 ms) and are minimally activated by Ca2+ in the absence of ATP. In a high activity mode, openings are longer (tau o1-3 = 0.17, 0.51, and 1.27 ms), and the channels are activated by Ca2+ in the absence of ATP and are in general less sensitive to the inactivating effects of Ca2+. beta RyR channel openings are longer (tau 01-3 = 0.34, 1.56, and 3.31 ms) than those of alpha RyR channels in either mode. beta RyR channels are activated to a greater relative extent by Ca2+ than ATP and are inactivated by millimolar Ca2+ in the absence, but not the presence, of ATP. Both alpha- and beta RyR channels are activated by caffeine, inhibited by Mg2+ and ruthenium red, inactivated by voltage (cytoplasmic side positive), and modified to a long-lived substate by ryanodine, but only alpha RyR channels are activated by perchlorate anions. The differences in gating and responses to channel modifiers may give the alpha- and beta RyRs distinct roles in muscle activation.
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