ArticleProceedings of the National Academy of Sciences of the United States of America1997
Functional nonequality of the cardiac and skeletal ryanodine receptors.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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Who cites it
38 citing papers in PubMed, 102 citations in OpenAlex.
- Review
- Activation of CaMolecular and cellular biochemistry · 2024Article
- Activation of Ca transport in cardiac microsomes enriches functional sets of ER and SR proteins.Research square · 2023Article
- Loss of dysferlin or myoferlin results in differential defects in excitation-contraction coupling in mouse skeletal muscle.Scientific reports · 2021Article
- Improper Remodeling of Organelles Deputed to CaInternational journal of molecular sciences · 2021Review
- Regulatory mechanisms of ryanodine receptor/CaJournal of muscle research and cell motility · 2021Review
- Physiological and Pathological Relevance of Selective and Nonselective CaAdvances in experimental medicine and biology · 2021Article
- Preclinical model systems of ryanodine receptor 1-related myopathies and malignant hyperthermia: a comprehensive scoping review of works published 1990-2019.Orphanet journal of rare diseases · 2020Article
- Excitation-contraction coupling in skeletal muscle: recent progress and unanswered questions.Biophysical reviews · 2020Review
- Voltage sensing mechanism in skeletal muscle excitation-contraction coupling: coming of age or midlife crisis?Skeletal muscle · 2018Review
- New Insights in Cardiac Calcium Handling and Excitation-Contraction Coupling.Advances in experimental medicine and biology · 2018Review
- Regions of ryanodine receptors that influence activation by the dihydropyridine receptor β1a subunit.Skeletal muscle · 2015Article
- Amino acid residues 489-503 of dihydropyridine receptor (DHPR) β1a subunit are critical for structural communication between the skeletal muscle DHPR complex and type 1 ryanodine receptor.The Journal of biological chemistry · 2014Article
- Ryanodine receptor 2 contributes to hemorrhagic shock-induced bi-phasic vascular reactivity in rats.Acta pharmacologica Sinica · 2014Article
- Direct association of the reticulon protein RTN1A with the ryanodine receptor 2 in neurons.Biochimica et biophysica acta · 2013Article
- Three-dimensional localization of the α and β subunits and of the II-III loop in the skeletal muscle L-type Ca2+ channel.The Journal of biological chemistry · 2012Article
- Alteration of Ryanodine-receptors in Cultured Rat Aortic Smooth Muscle Cells.The Korean journal of physiology & pharmacology : official journal of the Korean Physiological Society and the Korean Society of Pharmacology · 2011Article
- Reciprocal dihydropyridine and ryanodine receptor interactions in skeletal muscle activation.Journal of muscle research and cell motility · 2011Review
- Reduced gain of excitation-contraction coupling in triadin-null myotubes is mediated by the disruption of FKBP12/RyR1 interaction.Cell calcium · 2011Article
- Role of ryanodine receptor subtypes in initiation and formation of calcium sparks in arterial smooth muscle: comparison with striated muscle.Journal of biomedicine & biotechnology · 2009Review
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Dihydropyridine receptors (DHPRs), which are voltage-gated Ca2+ channels, and ryanodine receptors (RyRs), which are intracellular Ca2+ release channels, are expressed in diverse cell types, including skeletal and cardiac muscle. In skeletal muscle, there appears to be reciprocal signaling between the skeletal isoforms of both the DHPR and the RyR (RyR-1), such that Ca2+ release activity of RyR-1 is controlled by the DHPR and Ca2+ channel activity of the DHPR is controlled by RyR-1. Dyspedic skeletal muscle cells, which do not express RyR-1, lack excitation-contraction coupling and have an approximately 30-fold reduction in L-type Ca2+ current density. Here we have examined the ability of the predominant cardiac and brain RyR isoform, RyR-2, to substitute for RyR-1 in interacting with the skeletal DHPR. When RyR-2 is expressed in dyspedic muscle cells, it gives rise to spontaneous intracellular Ca2+ oscillations and supports Ca2+ entry-induced Ca2+ release. However, unlike RyR-1, the expressed RyR-2 does not increase the Ca2+ channel activity of the DHPR, nor is the gating of RyR-2 controlled by the skeletal DHPR. Thus, the ability to participate in skeletal-type reciprocal signaling appears to be a unique feature of RyR-1.
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Registered trials
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