scholarly journals Calcium-dependent energetics of calmodulin domain interactions with regulatory regions of the Ryanodine Receptor Type 1 (RyR1)

2014 ◽  
Vol 193-194 ◽  
pp. 35-49 ◽  
Author(s):  
Rhonda A. Newman ◽  
Brenda R. Sorensen ◽  
Adina M. Kilpatrick ◽  
Madeline A. Shea
Keyword(s):  
Ryanodine Receptor ◽  
Receptor Type ◽  
Regulatory Regions ◽  
Calcium Dependent ◽  
Domain Interactions

scholarly journals Early Findings in Neonatal Cases of RYR1–Related Congenital Myopathies

2021 ◽  
Vol 12 ◽  
Author(s):  
Eleonora Mauri ◽  
Daniela Piga ◽  
Alessandra Govoni ◽  
Roberta Brusa ◽  
Serena Pagliarani ◽  
...  
Keyword(s):  
Ryanodine Receptor ◽  
Brain Mri ◽  
Fetal Brain ◽  
Congenital Myopathy ◽  
Receptor Type ◽  
Congenital Myopathies ◽  
Muscle Mri ◽  
Next Generation Sequencing Ngs ◽  
Generation Sequencing

Ryanodine receptor type 1-related congenital myopathies are the most represented subgroup among congenital myopathies (CMs), typically presenting a central core or multiminicore muscle histopathology and high clinical heterogeneity. We evaluated a cohort of patients affected with Ryanodine receptor type 1-related congenital myopathy (RYR1-RCM), focusing on four patients who showed a severe congenital phenotype and underwent a comprehensive characterization at few months of life. To date there are few reports on precocious instrumental assessment. In two out of the four patients, a muscle biopsy was performed in the first days of life (day 5 and 37, respectively) and electron microscopy was carried out in two patients detecting typical features of congenital myopathy. Two patients underwent brain MRI in the first months of life (15 days and 2 months, respectively), one also a fetal brain MRI. In three children electromyography was performed in the first week of life and neurogenic signs were excluded. Muscle MRI obtained within the first years of life showed a typical pattern of RYR1-CM. The diagnosis was confirmed through genetic analysis in three out of four cases using Next Generation Sequencing (NGS) panels. The development of a correct and rapid diagnosis is a priority and may lead to prompt medical management and helps optimize inclusion in future clinical trials.

scholarly journals Amino Acid Residues Gln4020and Lys4021of the Ryanodine Receptor Type 1 Are Required for Activation by 4-Chloro-m-cresol

2006 ◽  
Vol 281 (30) ◽  
pp. 21022-21031 ◽  
Author(s):  
James D. Fessenden ◽  
Wei Feng ◽  
Isaac N. Pessah ◽  
Paul D. Allen
Keyword(s):  
Amino Acid ◽  
Ryanodine Receptor ◽  
Receptor Type ◽  
Amino Acid Residues

scholarly journals Interactions of Dichlorodiphenyltrichloroethane (DDT) and Dichlorodiphenyldichloroethylene (DDE) With Skeletal Muscle Ryanodine Receptor Type 1

2019 ◽  
Vol 170 (2) ◽  
pp. 509-524
Author(s):  
Kim M Truong ◽  
Gennady Cherednichenko ◽  
Isaac N Pessah
Keyword(s):  
Skeletal Muscle ◽  
Ryanodine Receptor ◽  
Membrane Vesicles ◽  
Receptor Type ◽  
Dependent Manner ◽  
Concentration Dependent Manner ◽  
Voltage Gated Sodium Channels ◽  
Muscle Health ◽  
Living Organisms

Abstract Dichlorodiphenyltrichloroethane (DDT) and its metabolite dichlorodiphenyldichloroethylene (DDE) are ubiquitous in the environment and detected in tissues of living organisms. Although DDT owes its insecticidal activity to impeding closure of voltage-gated sodium channels, it mediates toxicity in mammals by acting as an endocrine disruptor (ED). Numerous studies demonstrate DDT/DDE to be EDs, but studies examining muscle-specific effects mediated by nonhormonal receptors in mammals are lacking. Therefore, we investigated whether o,p′-DDT, p,p′-DDT, o,p′-DDE, and p,p′-DDE (DDx, collectively) alter the function of ryanodine receptor type 1 (RyR1), a protein critical for skeletal muscle excitation-contraction coupling and muscle health. DDx (0.01–10 µM) elicited concentration-dependent increases in [3H]ryanodine ([3H]Ry) binding to RyR1 with o,p′-DDE showing highest potency and efficacy. DDx also showed sex differences in [3H]Ry-binding efficacy toward RyR1, where [3H]Ry-binding in female muscle preparations was greater than male counterparts. Measurements of Ca2+ transport across sarcoplasmic reticulum (SR) membrane vesicles further confirmed DDx can selectively engage with RyR1 to cause Ca2+ efflux from SR stores. DDx also disrupts RyR1-signaling in HEK293T cells stably expressing RyR1 (HEK-RyR1). Pretreatment with DDx (0.1–10 µM) for 100 s, 12 h, or 24 h significantly sensitized Ca2+-efflux triggered by RyR agonist caffeine in a concentration-dependent manner. o,p′-DDE (24 h; 1 µM) significantly increased Ca2+-transient amplitude from electrically stimulated mouse myotubes compared with control and displayed abnormal fatigability. In conclusion, our study demonstrates DDx can directly interact and modulate RyR1 conformation, thereby altering SR Ca2+-dynamics and sensitize RyR1-expressing cells to RyR1 activators, which may ultimately contribute to long-term impairments in muscle health.

scholarly journals Homer Regulates Gain of Ryanodine Receptor Type 1 Channel Complex

2002 ◽  
Vol 277 (47) ◽  
pp. 44722-44730 ◽  
Author(s):  
Wei Feng ◽  
Jiancheng Tu ◽  
Tianzhong Yang ◽  
Patty Shih Vernon ◽  
Paul D. Allen ◽  
...  
Keyword(s):  
Ryanodine Receptor ◽  
Receptor Type

scholarly journals Ca2+ Current and Charge Movements in Skeletal Myotubes Promoted by the β-Subunit of the Dihydropyridine Receptor in the Absence of Ryanodine Receptor Type 1

2003 ◽  
Vol 84 (2) ◽  
pp. 942-959 ◽  
Author(s):  
Chris A. Ahern ◽  
David. C. Sheridan ◽  
Weijun Cheng ◽  
Lindsay Mortenson ◽  
Priya Nataraj ◽  
...  
Keyword(s):  
Ryanodine Receptor ◽  
Dihydropyridine Receptor ◽  
Receptor Type ◽  
Β Subunit ◽  
Skeletal Myotubes ◽  
Charge Movements

An α‐helical C‐terminal tail segment of the skeletal L‐type Ca 2+ channel β 1a subunit activates ryanodine receptor type 1 via a hydrophobic surface

2012 ◽  
Vol 26 (12) ◽  
pp. 5049-5059 ◽  
Author(s):  
Yamuna Karunasekara ◽  
Robyn T. Rebbeck ◽  
Llara M. Weaver ◽  
Philip G. Board ◽  
Angela F. Dulhunty ◽  
...  
Keyword(s):  
Ryanodine Receptor ◽  
Hydrophobic Surface ◽  
Receptor Type

Several Ryanodine Receptor Type 1 Gene Mutations of p.Arg2508 Are Potential Sources of Malignant Hyperthermia

2015 ◽  
Vol 121 (4) ◽  
pp. 994-1000 ◽  
Author(s):  
Hirotsugu Miyoshi ◽  
Toshimichi Yasuda ◽  
Sachiko Otsuki ◽  
Takashi Kondo ◽  
Toshiaki Haraki ◽  
...  
Keyword(s):  
Malignant Hyperthermia ◽  
Ryanodine Receptor ◽  
Gene Mutations ◽  
Receptor Type ◽  
Potential Sources
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