ArticleBioMed research international2013
Dantrolene-induced inhibition of skeletal L-type Ca2+ current requires RyR1 expression.
Article in BioMed research international, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 22 citations in OpenAlex.
- Calsequestrin: a well-known but curious protein in skeletal muscle.Experimental & molecular medicine · 2020Review
- 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
- Ryanodine Receptor 1-Related Myopathies: Diagnostic and Therapeutic Approaches.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2018Review
- Calcium Dynamics Mediated by the Endoplasmic/Sarcoplasmic Reticulum and Related Diseases.International journal of molecular sciences · 2017Review
- In vivo CaPhysiological reports · 2017Article
- PharmGKB summary: very important pharmacogene information for RYR1.Pharmacogenetics and genomics · 2016Review
- Malignant hyperthermia: a review.Orphanet journal of rare diseases · 2015Review
- Calcium homeostasis in myogenic differentiation factor 1 (MyoD)-transformed, virally-transduced, skin-derived equine myotubes.PloS one · 2014Article
- Malignant Hyperthermia.Missouri medicineReview
- Dantrolene, a treatment for Alzheimer disease?Alzheimer disease and associated disordersReview
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Authors and funding
1 author at 1 institution in 1 country.
Funding
Abstract
Malignant hyperthermia (MH) is a pharmacogenetic disorder most often linked to mutations in the type 1 ryanodine receptor (RyR1) or the skeletal L-type Ca(2+) channel (Ca(V)1.1). The only effective treatment for an MH crisis is administration of the hydantoin derivative Dantrolene. In addition to reducing voltage induced Ca(2+) release from the sarcoplasmic reticulum, Dantrolene was recently found to inhibit L-type currents in developing myotubes by shifting the voltage-dependence of Ca(V)1.1 channel activation to more depolarizing potentials. Thus, the purpose of this study was to obtain information regarding the mechanism of Dantrolene-induced inhibition of Ca(V)1.1. A mechanism involving a general depression of plasma membrane excitability was excluded because the biophysical properties of skeletal muscle Na(+) current in normal mouse myotubes were largely unaffected by exposure to Dantrolene. However, a role for RyR1 was evident as Dantrolene failed to alter the amplitude, voltage dependence and inactivation kinetics of L-type currents recorded from dyspedic (RyR1 null) myotubes. Taken together, these results suggest that the mechanism of Dantrolene-induced inhibition of the skeletal muscle L-type Ca(2+) current is related to altered communication between Ca(V)1.1 and RyR1.
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