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Journal articles on the topic "RyR3"
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Dabertrand, Fabrice, Nicolas Fritz, Jean Mironneau, Nathalie Macrez, and Jean-Luc Morel. "Role of RYR3 splice variants in calcium signaling in mouse nonpregnant and pregnant myometrium." American Journal of Physiology-Cell Physiology 293, no. 3 (September 2007): C848—C854. http://dx.doi.org/10.1152/ajpcell.00069.2007.
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Alternative splicing of ryanodine receptor subtype 3 (RYR3) may generate a short isoform (RYR3S) without channel function and a functional full-length isoform (RYR3L). The RYR3S isoform has been shown to negatively regulate the native RYR2 subtype in smooth muscle cells as well as the RYR3L isoform when both isoforms were coexpressed in HEK-293 cells. Mouse myometrium expresses only the RYR3 subtype, but the role of RYR3 isoforms obtained by alternative splicing and their activation by cADP-ribose during pregnancy have never been investigated. Here, we show that both RYR3S and RYR3L isoforms are differentially expressed in nonpregnant and pregnant mouse myometrium. The use of antisense oligonucleotides directed against each isoform indicated that only RYR3L was activated by caffeine and cADP-ribose in nonpregnant myometrium. These RYR3L-mediated Ca2+ releases were negatively regulated by RYR3S expression. At the end of pregnancy, the relative expression of RYR3L versus RYR3S and its ability to respond to cADP-ribose were increased. Therefore, our results suggest that physiological regulation of RYR3 alternative splicing may play an essential role at the end of pregnancy.
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Zheng, Yun-Min, Qing-Song Wang, Rakesh Rathore, Wan-Hui Zhang, Joseph E. Mazurkiewicz, Vincenzo Sorrentino, Harold A. Singer, Michael I. Kotlikoff, and Yong-Xiao Wang. "Type-3 Ryanodine Receptors Mediate Hypoxia-, but Not Neurotransmitter-induced Calcium Release and Contraction in Pulmonary Artery Smooth Muscle Cells." Journal of General Physiology 125, no. 4 (March 28, 2005): 427–40. http://dx.doi.org/10.1085/jgp.200409232.
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In this study we examined the expression of RyR subtypes and the role of RyRs in neurotransmitter- and hypoxia-induced Ca2+ release and contraction in pulmonary artery smooth muscle cells (PASMCs). Under perforated patch clamp conditions, maximal activation of RyRs with caffeine or inositol triphosphate receptors (IP3Rs) with noradrenaline induced equivalent increases in [Ca2+]i and Ca2+-activated Cl− currents in freshly isolated rat PASMCs. Following maximal IP3-induced Ca2+ release, neither caffeine nor chloro-m-cresol induced a response, whereas prior application of caffeine or chloro-m-cresol blocked IP3-induced Ca2+ release. In cultured human PASMCs, which lack functional expression of RyRs, caffeine failed to affect ATP-induced increases in [Ca2+]i in the presence and absence of extracellular Ca2+. The RyR antagonists ruthenium red, ryanodine, tetracaine, and dantrolene greatly inhibited submaximal noradrenaline– and hypoxia-induced Ca2+ release and contraction in freshly isolated rat PASMCs, but did not affect ATP-induced Ca2+ release in cultured human PASMCs. Real-time quantitative RT-PCR and immunofluorescence staining indicated similar expression of all three RyR subtypes (RyR1, RyR2, and RyR3) in freshly isolated rat PASMCs. In freshly isolated PASMCs from RyR3 knockout (RyR3−/−) mice, hypoxia-induced, but not submaximal noradrenaline–induced, Ca2+ release and contraction were significantly reduced. Ruthenium red and tetracaine can further inhibit hypoxic increase in [Ca2+]i in RyR3−/− mouse PASMCs. Collectively, our data suggest that (a) RyRs play an important role in submaximal noradrenaline– and hypoxia-induced Ca2+ release and contraction; (b) all three subtype RyRs are expressed; and (c) RyR3 gene knockout significantly inhibits hypoxia-, but not submaximal noradrenaline–induced Ca2+ and contractile responses in PASMCs.
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Protasi, Feliciano, Alexander Shtifman, Fred J. Julian, and Paul D. Allen. "All three ryanodine receptor isoforms generate rapid cooling responses in muscle cells." American Journal of Physiology-Cell Physiology 286, no. 3 (March 2004): C662—C670. http://dx.doi.org/10.1152/ajpcell.00081.2003.
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The rapid cooling (RC) response in muscle is an increase in cytoplasmic Ca2+concentration ([Ca2+]i) that is probably caused by Ca2+release from the sarcoplasmic reticulum (SR). However, the molecular bases of this response have not been completely elucidated. Three different isoforms of the SR Ca2+release channels, or ryanodine receptors (RyRs), have been isolated (RyR1, RyR2, and RyR3). In the current investigation, the RC response was studied in RyR-null muscle cells (1B5) before and after transduction with HSV-1 virions containing the cDNAs encoding for RyR1, RyR2, or RyR3. Cells were loaded with fluo 4-AM to monitor changes in [Ca2+]iand perfused with either cold (∼0°C), room temperature (RT), or RT buffer containing 40 mM caffeine. Control cells showed no significant response to cold or caffeine, whereas robust Ca2+transients were recorded in response to both RC and caffeine in transduced cells expressing any one of the three RyR isoforms. Our data demonstrate directly that RyRs are responsible for the RC response and that all three isoforms respond in a similar manner. Ca2+release from RyRs is likely caused by a RC-induced conformational change of the channel from the closed to the open state.
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Giannini, G., A. Conti, S. Mammarella, M. Scrobogna, and V. Sorrentino. "The ryanodine receptor/calcium channel genes are widely and differentially expressed in murine brain and peripheral tissues." Journal of Cell Biology 128, no. 5 (March 1, 1995): 893–904. http://dx.doi.org/10.1083/jcb.128.5.893.
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Ryanodine receptors (RyRs) are intracellular calcium release channels that participate in controlling cytosolic calcium levels. At variance with the probably ubiquitous inositol 1,4,5-trisphosphate-operated calcium channels (1,4,5-trisphosphate receptors), RyRs have been mainly regarded as the calcium release channels controlling skeletal and cardiac muscle contraction. Increasing evidence has recently suggested that RyRs may be more widely expressed, but this has never been extensively examined. Therefore, we cloned three cDNAs corresponding to murine RyR homologues to carry a comprehensive analysis of their expression in murine tissues. Here, we report that the three genes are expressed in almost all tissues analyzed, where tissue-specific patterns of expression were observed. In the uterus and vas deferens, expression of RyR3 was localized to the smooth muscle component of these organs. In the testis, expression of RyR1 and RyR3 was detected in germ cells. RyR mRNAs were also detected in in vitro-cultured cell lines. RyR1, RyR2, and RyR3 mRNA were detected in the cerebrum and in the cerebellum. In situ analysis revealed a cell type-specific pattern of expression in the different regions of the central nervous system. The differential expression of the three ryanodine receptor genes in the central nervous system was also confirmed using specific antibodies against the respective proteins. This widespread pattern of expression suggests that RyRs may participate in the regulation of intracellular calcium homeostasis in a range of cells wider than previously recognized.
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Tian, Chengju, Caronda J. Moore, Puttappa Dodmane, Chun Hong Shao, Debra J. Romberger, Myron L. Toews, and Keshore R. Bidasee. "Dust from hog confinement facilities impairs Ca2+ mobilization from sarco(endo)plasmic reticulum by inhibiting ryanodine receptors." Journal of Applied Physiology 114, no. 5 (March 1, 2013): 665–74. http://dx.doi.org/10.1152/japplphysiol.00661.2012.
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Individuals working in commercial hog confinement facilities have elevated incidences of headaches, depression, nausea, skeletal muscle weakness, fatigue, gastrointestinal disorders, and cardiovascular diseases, and the molecular mechanisms for these nonrespiratory ailments remain incompletely undefined. A common element underlying these diverse pathophysiologies is perturbation of intracellular Ca2+ homeostasis. This study assessed whether the dust generated inside hog confinement facilities contains compounds that alter Ca2+ mobilization via ryanodine receptors (RyRs), key intracellular channels responsible for mobilizing Ca2+ from internal stores to elicit an array of physiologic functions. Hog barn dust (HBD) was extracted with phosphate-buffered saline, sterile-filtered (0.22 μm), and size-separated using Sephadex G-100 resin. Fractions (F) 1 through 9 (Mw >10,000 Da) had no measurable effects on RyR isoforms. However, F10 through F17, which contained compounds of Mw ≤2,000 Da, modulated the [3H]ryanodine binding to RyR1, RyR2, and RyR3 in a biphasic (Gaussian) manner. The Ki values for F13, the most potent fraction, were 3.8 ± 0.2 μg/ml for RyR1, 0.2 ± 0.01 μg/ml and 19.1 ± 2.8 μg/ml for RyR2 (two binding sites), and 44.9 ± 2.8 μg/ml and 501.6 ± 9.2 μg/ml for RyR3 (two binding sites). In lipid bilayer assays, F13 dose-dependently decreased the open probabilities of RyR1, RyR2, and RyR3. Pretreating differentiated mouse skeletal myotubes (C2C12 cells) with F13 blunted the amplitudes of ryanodine- and K+-induced Ca2+ transients. Because RyRs are present in many cell types, impairment in Ca2+ mobilization from internal stores via these channels is a possible mechanism by which HBD may trigger these seemingly unrelated pathophysiologies.
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OTTINI, Laura, Giovanna MARZIALI, Antonio CONTI, Alexandra CHARLESWORTH, and Vincenzo SORRENTINO. "α and β isoforms of ryanodine receptor from chicken skeletal muscle are the homologues of mammalian RyR1 and RyR3." Biochemical Journal 315, no. 1 (April 1, 1996): 207–16. http://dx.doi.org/10.1042/bj3150207.
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To define the relationship between the two ryanodine receptor (RyR) isoforms present in chicken skeletal muscle, we cloned two groups of cDNAs encoding the chicken homologues of mammalian RyR1 and RyR3. Equivalent amounts of the two chicken isoform mRNAs were detected in thigh and pectoral skeletal muscles. RyR1 and RyR3 mRNAs were co-expressed in testis and cerebellum whereas RyR3 mRNA was expressed also in cerebrum and heart. The full-length sequence of the chicken RyR3 cDNA was established. The RyR3 receptor from chicken had the same general structure as mammalian and amphibian RyRs. The 15089 nt cDNA encoded a 4869-amino-acid-long protein with a molecular mass of 552445. The predicted amino acid sequence of the chicken RyR3 showed 86.9% identity to mammalian RyR3 and 85.6% to frog RyR3. Antibodies specific for chicken RyR1 and RyR3 recognized two different proteins with an apparent molecular mass of about 500 kDa. The two proteins differ slightly in their apparent molecular mass on SDS/PAGE: the protein recognized by antibodies against RyR3 had a higher mobility than the protein recognized by the antiserum against RyR1. Antibodies against RyR1 detected a protein already present in chicken skeletal muscle from 12-day-old embryos and older, while antibodies against RyR3 isoform detected a protein in muscle from only 18-day-old embryos and older. The expression patterns of RyR1 and RyR3 superimpose with those previously reported for the α and the β isoforms respectively. We conclude that α and β isoforms present in chicken skeletal muscle are the homologues of mammalian RyR1 and RyR3.
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Perez, Claudio F., José R. López, and Paul D. Allen. "Expression levels of RyR1 and RyR3 control resting free Ca2+ in skeletal muscle." American Journal of Physiology-Cell Physiology 288, no. 3 (March 2005): C640—C649. http://dx.doi.org/10.1152/ajpcell.00407.2004.
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To better understand the role of the transient expression of ryanodine receptor (RyR) type 3 (RyR3) on Ca2+ homeostasis during the development of skeletal muscle, we have analyzed the effect of expression levels of RyR3 and RyR1 on the overall physiology of cultured myotubes and muscle fibers. Dyspedic myotubes were infected with RyR1 or RyR3 containing virions at 0.2, 0.4, 1.0, and 4.0 moieties of infection (MOI), and analysis of their pattern of expression, caffeine sensitivity, and resting free Ca2+ concentration ([Ca2+]r) was performed. Although increased MOI resulted in increased expression of each receptor isoform, it did not significantly affect the immunopattern of RyRs or the expression levels of calsequestrin, triadin, or FKBP-12. Interestingly, myotubes expressing RyR3 always had significantly higher [Ca2+]r and lower caffeine EC50 than did cells expressing RyR1. Although some of the increased sensitivity of RyR3 to caffeine could be attributed to the higher [Ca2+]r in RyR3-expressing cells, studies of [3H]ryanodine binding demonstrated intrinsic differences in caffeine sensitivity between RyR1 and RyR3. Tibialis anterior (TA) muscle fibers at different stages of postnatal development exhibited a transient increase in [Ca2+]r coordinately with their level of RyR3 expression. Similarly, adult soleus fibers, which also express RyR3, had higher [Ca2+]r than did adult TA fibers, which exclusively express RyR1. These data show that in skeletal muscle, RyR3 increases [Ca2+]r more than RyR1 does at any expression level. These data suggest that the coexpression of RyR1 and RyR3 at different levels may constitute a novel mechanism by which to regulate [Ca2+]r in skeletal muscle.
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Vanterpool, Conwin K., Elaine A. Vanterpool, William J. Pearce, and John N. Buchholz. "Advancing age alters the expression of the ryanodine receptor 3 isoform in adult rat superior cervical ganglia." Journal of Applied Physiology 101, no. 2 (August 2006): 392–400. http://dx.doi.org/10.1152/japplphysiol.00167.2006.
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Sympathetic nerves arising from the superior cervical ganglion (SCG) protect the cerebrovasculature during periods of acute hypertension and may play a role in homeostasis of target organs. The functions of these nerves depend on calcium release triggered by activation of ryanodine receptor (RyR) channels. The function of RyR channels is in part dependent on genetic expression and regulation by numerous protein modulators such as neuronal nitric oxide synthase (nNOS) neurons also found in the SCG. We have shown that release of calcium in SCG cells is altered during late maturation and advancing age. However, the underlying molecular mechanisms that may in part account for these data are elusive. Therefore we used molecular techniques to test the hypothesis that advancing age alters the pattern of genetic expression and/or protein levels of RyRs and their modulation by nNOS in the SCG in F344 rats aged 6, 12, and 24 mo. Surprisingly, ryr1 expression was undetectable in all age groups and ryr2 and ryr3 are the predominantly transcribed isoforms in the adult rat SCG. mRNA and protein levels for RyR2 isoform did not change with advancing age. However, ryr3 mRNA levels increased from 6 to 12 mo and declined from 12 to 24 mo. Similarly, RyR3 receptor protein levels also increased from 6 to 12 mo and declined from 12 to 24 mo. Because nNOS and the phosphorylation of the RyRs have been shown to modulate the function of RyRs, total phosphorylation and nNOS protein levels were analyzed in all age groups. Phosphorylation levels of the RyRs were similar in all age groups. However, nNOS protein levels increased from 6 to 12 mo followed by decline from 12 to 24 mo. These data suggest that advancing age selectively impacts the genetic expression and protein levels of RyR3 as well as modulatory nNOS protein levels. In addition, these data may part provide some insight into the possible changes in the function of RyRs that may occur with the normal aging process.
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Rossi, Daniela, Ilenia Simeoni, Marcella Micheli, Martin Bootman, Peter Lipp, Paul D. Allen, and Vincenzo Sorrentino. "RyR1 and RyR3 isoforms provide distinct intracellular Ca2+signals in HEK 293 cells." Journal of Cell Science 115, no. 12 (June 15, 2002): 2497–504. http://dx.doi.org/10.1242/jcs.115.12.2497.
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Ryanodine receptors (RyRs) are expressed on the endoplasmic reticulum of many cells, where they form intracellular Ca2+-release channels that participate in the generation of intracellular Ca2+ signals. Here we report studies on the intracellular localisation and functional properties of transfected RyR1 or RyR3 channels in HEK 293 cells. Immunofluorescence studies indicated that both RyR1 and RyR3 did not form clusters but were homogeneously distributed throughout the endoplasmic reticulum. Ca2+ release experiments showed that transfected RyR1 and RyR3 channels responded to caffeine, although with different sensitivity,generating a global release of Ca2+ from the entire endoplasmic reticulum. However, video imaging and confocal microscopy analysis revealed that, in RyR3-expressing cells, local spontaneous Ca2+ release events were observed. No such spontaneous activity was observed in RyR1-expressing cells or in control cells. Interestingly, the spontaneous release events observed in RyR3-expressing cells were restricted to one or two regions of the endoplasmic reticulum, suggesting the formation of a further subcellular organisation of RyR3 in Ca2+ release units. These results demonstrate that different RyR isoforms can engage in the generation of distinct intracellular Ca2+ signals in HEK 293 cells.
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CONTI, Antonio, L. GORZA, and Vincenzo SORRENTINO. "Differential distribution of ryanodine receptor type 3 (RyR3) gene product in mammalian skeletal muscles." Biochemical Journal 316, no. 1 (May 15, 1996): 19–23. http://dx.doi.org/10.1042/bj3160019.
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Activation of intracellular Ca2+-release channels/ryanodine receptors (RyRs) is a fundamental step in the regulation of muscle contraction. In mammalian skeletal muscle, Ca2+-release channels containing the type 1 isoform of RyR (RyR1) open to release Ca2+ from the sarcoplasmic reticulum (SR) upon stimulation by the voltage-activated dihydropyridine receptor on the T-tubule/plasma membrane. In addition to RyR1, low levels of the mRNA of the RyR3 isoform have been recently detected in mammalian skeletal muscles. Here we report data on the distribution of the RyR3 gene product in mammalian skeletal muscles. Western-blot analysis of SR of individual muscles indicated that, at variance with the even distribution of the RyR1 isoform, the RyR3 content varies among different muscles, with relatively higher amounts being detected in diaphragm and soleus, and lower levels in abdominal muscles and tibialis anterior. In these muscles RyR3 was localized in the terminal cisternae of the SR. No detectable levels of RyR3 were observed in the extensor digitorum longus. Preferential high content of RyR3 in the diaphragm muscle was observed in several mammalian species. In situ hybridization analysis demonstrated that RyR3 transcripts are not restricted to a specific subset of skeletal-muscle fibres. Differential utilization of the RyR3 isoform in skeletal muscle may be relevant to the modulation of Ca2+ release with respect to specific muscle-contraction properties.
Dissertations / Theses on the topic "RyR3"
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BONCORAGLIO, GIORGIO BATTISTA. "Role of Ryanodine Receptor type 3 (RyR3) in ischemic stroke." Doctoral thesis, Università degli Studi di Milano-Bicocca, 2021. http://hdl.handle.net/10281/317052.
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L'ictus è una delle principali cause di mortalità e disabilità acquisita in tutto il mondo. Il primo studio di associazione genome-wide in pazienti con ictus ischemico italiano ha trovato un'associazione significativa con il polimorfismo missenso a singolo nucleotide (SNP) rs4780144 nel gene del recettore della rianodina di tipo 3 (RyR3), che porta a una potenziale perdita di funzione. Molteplici evidenze hanno suggerito che una ridotta funzione di RyR3 potrebbe migliorare l'esito dell'ictus.
Con questo studio abbiamo mirato a indagare il ruolo di RyR3 nell'ictus ischemico a livello funzionale, genomico e cellulare.
Le cellule staminali mesenchimali di derivazione adiposa (Ad-MSC) esprimono RyR3 ma non gli altri recettori della rianodina (RyR1 e RyR2). Abbiamo valutato l'effetto del genotipo rs4780144 sull'omeostasi del calcio intracellulare nelle linee Ad-MSC. I nostri risultati hanno confermato la riduzione della funzione RyR3 (ridotto rilascio di ioni calcio nel citoplasma) nelle cellule con alleli mutati, che era statisticamente significativa nel donatore omozigote.
Una seconda coorte di 319 pazienti italiani con ictus ischemico con buon esito clinico è stata genotipizzata con Illumina Human-24 720. I genotipi dei casi (sia la prima che la seconda coorte) e i controlli sono stati imputati utilizzando il pannello di riferimento TOPMed degli aplotipi umani. Questo secondo GWAS ha replicato l'associazione con rs4780144 e altri SNP nel gene RyR3.
Infine, il danno ischemico indotto dalla deprivazione di ossigeno-glucosio (OGD) è stato valutato in fette di cervello organotipiche da topi wild-type e RyR3-knockout. Il knockout di RyR3 ha mostrato una ridotta suscettibilità al danno ischemico rispetto alle sezioni wild-type come indicato dalla ridotta incorporazione di ioduro di propidio e dal rilascio di LDH a 48 e 72 ore dopo OGD. RyR3- fette knockout hanno mostrato anche un gonfiore ridotto dopo OGD, indicando una riduzione dell'edema citotossico. Tuttavia, ad oggi non sono state trovate differenze significative nell'analisi dell'espressione genica eseguita su geni correlati allo stress ossidativo e neuronale.
I risultati di questo lavoro confermano che RyR3 può svolgere un ruolo nell'ictus ischemico. In particolare, l'inibizione di RyR3 potrebbe modulare positivamente il danno ischemico, determinando una nuova e promettente strategia neuroprotettiva nei pazienti con ictus ischemico acuto. Tuttavia, sono necessari ulteriori studi per chiarire i meccanismi che potrebbero eventualmente essere alla base della neuroprotezione osservata.Stroke is a leading cause of mortality and acquired disability worldwide. The first genome-wide association study in Italian ischemic stroke patients found a significant association with the missense single nucleotide polymorphism (SNP) rs4780144 in the ryanodine receptor type 3 (RyR3) gene, which leads to a potential loss of function. Multiple evidences suggested that a reduced function of RyR3 could improve stroke outcome. With this study we aimed at investigating the role of RyR3 in ischemic stroke at functional, genomic, and cellular level. Adipose-derived mesenchymal stem cells (Ad-MSCs) express RyR3 but not the other ryanodine receptors (RyR1 and RyR2). We assessed the effect of the rs4780144 genotype on intracellular calcium homeostasis in Ad-MSC lines. Our results confirmed the reduction of the RyR3 function (reduced release of calcium ions into the cytoplasm) in cells with the mutated alleles, which was statistically significant in homozygous donor. A second cohort of 319 Italian ischemic stroke patients with good clinical outcome was genotyped with Illumina Human-24 720. Genotypes of cases (both first and second cohorts) and controls were imputed using the TOPMed reference panel of human haplotypes. This second GWAS replicated the association with rs4780144 and other SNPs in the RyR3 gene. Finally, ischemic injury induced by oxygen-glucose deprivation (OGD) was evaluated in organotypic brain slices from wild-type and RyR3-knockout mice. RyR3- knockout showed a decreased susceptibility to ischemic damage compared to wild-type slices as indicated by the reduced propidium iodide incorporation and LDH release at 48 and 72 h after OGD. RyR3- knockout slices showed also a reduced swelling after OGD, indicating reduction of cytotoxic edema. However, to date no significant differences were found in gene expression analysis performed on neuronal and oxidative stress related genes. The results of this work confirm that RyR3 may play a role in ischemic stroke. In particular, the inhibition of RyR3 could positively modulate ischemic damage, resulting in a new and promising neuroprotective strategy in patients with acute ischemic stroke. However, further studies are needed to clarify the mechanisms that could possibly underlie the observed neuroprotection.
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Dabertrand, Fabrice. "Identification et rôle fonctionnels de variants d'épissage du récepteur de la ryanodine de type 3 (RyR3)." Bordeaux 2, 2006. http://www.theses.fr/2006BOR21351.
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La fonction du sous-type RYR 3 du récepteur de la ryanodine ne peut se comprendre qu'à travers l'étude de ses différents variants d'épissage. Dans les muscles lisses de souris, nous avons mis en évidence l'existence d'un variant court dominant négatif. En effet, dans le duodenum, celui-ci inhibe le sous-type RYR 2 responsable de la libération du calcium stocké dans le reticulum. L'isoforme complète de RYR3 n'interagit pas avec l'isoforme courte et code des oscillations calciques spontanées lors d'une surharge du contenu en calcium du reticulum. Enfin, cet épissage alternatif est modulé dans le myomètre lors de la gestation. A l'approche de la parturition, l'expression de l'isoforme complète domine ce qui permet aux voies de transduction aboutissant à la production d'ADP-ribose cyclique de produire la libération du calcium stocké, phénomène participant à la contraction utérineThe understanding of the function of ryanodine receptor subtype RYR3 needs the study of RYR3 alternative splicing. In mouse smooth muscles, we have shown the expression of short dominant negative variant. In fact, in duodenum, the short isoform inhibits the RYR2 subtype responsible for the release of stored calcium in reticulum. The complete isoform of RYR3 cannot interact with the short isoform but encodes spontaneous calcium oscillations only when the reticulum is calcium overloaded. This alternative splicing is also modulated in myometrium during pregnancy. Near the term, the expression of complete RYR3 isoform is dominant whch allows cyclic ADP-ribose-dependent transduction pathways to release stored calcium that participates to uterine contraction
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Chameau, Pascal. "Le recepteur de la ryanodine de type 3 (ryr3) : localisation et role dans l'excitabilite neuronale et la transmission synaptique." Paris 6, 1999. http://www.theses.fr/1999PA066101.
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Le recepteur de la ryanodine de type 3 (ryr3), exprime dans les neurones, est l'isoforme la moins caracterisee de cette famille de recepteurs-canaux ca 2 + du reticulum endoplasmique. J'ai developpe un anticorps polyclonal dirige contre ryr3 qui m'a permis de determiner la localisation de cette isoforme dans la region proximale des dendrites apicaux des neurones pyramidaux de la region ca1 de l'hippocampe de souris. Cet anticorps s'est avere bloquant du mecanisme de calcium-induced calcium release (cicr) dans lequel ryr3 est implique. Dans les neurones ca1, l'injection de l'anticorps anti-ryr3 reduit le courant k+ active par le ca2+ (courant isahp, pour slow after hyperpolarization, sensible a la ryanodine). Ce resultat montre que l'activation du courant isahp est declenchee en partie par le ca2+ libere du reticulum endoplasmique par ryr3. Ce ryr3 joue donc un role essentiel dans la mise en jeu de la phase de post-hyperpolarisation prolongee de la membrane neuronale, phenomene a l'origine du mecanisme d'adaptation de la frequence de decharge des potentiels d'action. L'etude du courant isahp souligne egalement le role des proteines associees a ryr3, cibles de la rapamycine et du cadp-ribose, comme elements determinants de l'activation de ce ryr. Chez l'aplysie un recepteur de type ryr3 est localise principalement dans les axones des neurones du ganglion buccal. L'injection de l'anticorps anti-ryr3, dans le neurone presynaptique d'un couple synaptique cholinergique parfaitement identifie, induit une diminution de la quantite d'acetylcholine liberee par un potentiel d'action presynaptique comparable a celle de la ryanodine. Ce resultat met en evidence le role d'un recepteur de type ryr3 dans la modulation de la transmission synaptique. La sequence peptidique utilisee comme antigene est situee dans une boucle cytoplasmique de ryr3. Ce peptide lie les ions ca2+ et a la capacite d'affecter les phenomenes physiologiques dependants du ca2+ : il reduit l'amplitude des courants isahp dans les neurones pyramidaux ca1 de l'hippocampe de souris et la liberation evoquee d'acetylcholine dans les neurones presynaptiques d'aplysie. Cette sequence peptidique pourrait donc jouer un role essentiel comme tout ou partie du site de liaison du ca2+ sur ryr3.
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Whiteley, Gareth. "Molecular architecture of Caveolin-3 and the investigation of an interaction with the ryanodine receptor." Thesis, University of Manchester, 2012. https://www.research.manchester.ac.uk/portal/en/theses/molecular-architecture-of-caveolin3-and-the-investigation-of-an-interaction-with-the-ryanodine-receptor(d5d4e1f1-88c5-4619-b208-7742d0cd81f5).html.
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The muscle-specific membrane protein, Caveolin-3, is a building block of caveolae a type of specialised lipid raft. Caveolin-3 is proposed to play a central role in variety of cellular functions both structural and functional, from cell signalling to cholesterol homeostasis. Caveolin-3 has also been implicated in processes involved in targeting membrane proteins to the plasma membrane, as well as mediating a host of cell signalling processes. Initial attempts were made to express full-length Caveolin-3 in E.coli. However, more success was achieved in expressing and purifying domains of Caveolin-3. To produce purified full-length Caveolin-3 the baculovirus expression system was employed and we report here that the expression of Caveolin-3 in insect (Sf9) cells leads to the formation of caveolae comparable in size to those observed in native vesicles. We subsequently purified the recombinant Caveolin-3 and determined, using multi-angle laser light scattering, that the isolated protein forms an oligomer with a molecular mass of ~200-220kDa. Using negative-stain transmission electron microscopy in conjunction with single particle analysis we have determined the first three-dimensional structure for Caveolin-3 with data converging to suggest that it forms a nonamer. The 9-fold symmetric three-dimensional Caveolin-3 volume is toroidal, ~16.5nm in diameter and 5.5nm thick, and is characterised by an outer rim of protein connected to a central 'cone-shaped' domain. Labelling studies revealed that the C-terminal domain of each of the contributing Caveolin-3 monomers associate to form the central cone density. There is also evidence to suggest that Caveolin-3 is associated with a range of proteins involved in excitation-contraction coupling. Having identified multiple potential caveolin-binding motifs within the Ryanodine Receptor, one of the key protein components of excitation-contraction coupling, we have purified the skeletal isoform of the Ryanodine Receptor (Ryanodine Receptor-1) from sheep calf muscle and using several biophysical techniques probed whether there is an interaction between Caveolin-3 and Ryanodine Receptor-1. Co-immunoprecipitation experiments indicated that the two proteins do indeed interact, but functional studies for analysis of binding characteristics were inconclusive. In conclusion, this thesis describes both the successfully purification and structural determination of Caveolin-3, generating the first 3D data for any of the caveolin proteins, as well as work aimed at understanding its functional relationship with Ryanodine Receptor-1.
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King, James Harmsworth. "Arrhythmogenic mechanisms in RYR2-P2328S murine hearts." Thesis, University of Cambridge, 2014. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.648837.
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Klipp, Robert Carl. "Novel Compound, 84F2, Inhibits Calmodulin Deficient RyR2." PDXScholar, 2017. https://pdxscholar.library.pdx.edu/open_access_etds/3484.
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The cardiac ryanodine receptor (RyR2) plays a key role in excitation-contraction coupling (ECC). Mutations in RyR2 are known to be linked to the arrhythmogenic disorder, catecholaminergic polymorphic ventricular tachycardia (CPVT), a deadly disease which is characterized by a leak of calcium from sarcoplasmic reticulum and a decrease in calmodulin (CaM) binding. A novel drug, 84F2, shown to inhibit arrhythmias in RyR2-R176Q heterozygous CPVT mouse hearts (2.5 µg/kg), decrease spark frequency in cells derived from CPVT mice (IC50 = 35 nM), and inhibit RyR2 single channel activity at low nanomolar concentrations (IC50 = 8 nM). When CaM is added back to RyR2, 84F2's ability to inhibit channel activity is suppressed approximately 250 fold. A metabolite of 84F2, 78F3, is shown to also be active in the inhibition of RyR2. We propose that 84F2 decreases arrhythmias by binding to the CaM deficient RyR2, but does not affect normal ECC when CaM is present. This work characterizes for the first time a class of drugs whose inhibitory affects are dependent upon the removal of CaM from RyR2.
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Wang, YueYi. "Ca2+ handling in a mice model of CPVT." Thesis, Université Paris-Saclay (ComUE), 2016. http://www.theses.fr/2016SACLS156/document.
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Le canal calcique de libération du Ca2+, appelé récepteur à la ryanodine (RyR) est localisé dans la membrane du réticulum sarcoplasmique des cardiomyocytes, en incluant ceux du pacemaker, et a un rôle important dans le couplage excitation contraction et la génération du rythme cardiaque. Des mutations dans leur gène sont responsables de la tachycardie catécholergique (CPVT), qui est une maladie létale, manifestée par des syncopes ou mort subite lors de stress émotionnel ou physique. Au repos, ces patients ont un électrocardiogramme normal, mais une tendance plus importante à la bradycardie.Nos collaborateurs ont identifié la mutation RyR2R420Q dans une famille espagnole atteinte de CPVT. Nous avons construit une souris portant cette mutation et étudié l’activité du nœud sinoatrial (NSA, pacemaker principale) afin d’élucider les mécanismes.Nous avons trouvé que les cellules du NSA présentent une activité spontanée plus lente que les souris sauvages (WT). Dans la cellule in situ, on peut étudier l’activité des RyRs par l’analyse des « sparks » Ca2+, qui sont des évenements élémentaires produits par l’activation d’un cluster des RyRs. Nos analyses en microscopie confocale sur des NSA disséquées on montré que la fréquence des sparks Ca2+ était légèrement augmentée. Par contre, la longueur de ces sparks est fortement prolongée dans les cellules KI. Ceci produit une libération plus importante de Ca2+ pendant la diastole dans les cellules KI qui réduit l’automatisme, en réduisant la charge en Ca2+ du réticulum sarcoplasmique et en inactivant le courant calcique type L. Donc les thérapies en étude qi favoriseraient la stabilisation du RyR2 en état fermé pourraient ne pas Être efficaces, et il faudra plutôt essayer des thérapies qui faciliteraient la fermeture du canal, une fois il est ouvertThe cardiac type-2 ryanodine receptor (RyR2) encodes a Ca2+ release channel on sarcoplasmic reticulum (SR) membrane in cardiomyocytes, including sinoatrial node (SAN) myocytes, and releases Ca2+ required for contraction and SAN spontaneous rhythm. Its genetic defects are related to catecholaminergic polymorphic ventricular tachycardia (CPVT), which is a lethal heritable disease characterized by exercise/stress-induced syncope and/or sudden cardiac death. Interestingly, CPVT patients frequently present SAN dysfunction as bradycardia at rest.In a previous study, a novel CPVT-related RyR2 mutation (RyR2R420Q) in a Spanish family, associated with SAN dysfunction was reported. R420 is located at the N-terminal portion of the channel and seems to be an important site for maintaining a stable A/B/C domain of N-terminus in RyR2. As N-terminal mutation resultant RyR2 behaviour and SAN function are never analyzed before, we created the KI mice model bearing mutation R420Q to understand the underlying mechanism.In this thesis, we found increased Ca2+ release during diastole, indicating a gain-of-function effect of RyR2 N-terminal mutation R420Q. Interestingly, this defect may not be only an enhanced activity, as the Ca2+ sparks frequency was only slightly increased in KI, but also the closing mechanism, producing longer Ca2+ sparks. That is, the number of Ca2+ sparks is increased by the RyR2R420Q mutation, and meanwhile the amount of Ca2+ released in each Ca2+ spark is also dramatically enhanced. This increased Ca2+ release retards SR Ca2+ replenishment, disrupting the Ca2+ clock and the coupled clock, resulting in the slower SAN function. Thus favouring RyR stabilization in the closing state might not be an adequate therapy but accelerating its closure
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Yin, Liheng. "Impact of the catecholaminergic polymorphic ventricular tachycardia (CPVT) mutation RyR2R420Q in cell function." Thesis, université Paris-Saclay, 2020. http://www.theses.fr/2020UPASS068.
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La tachycardie ventriculaire polymorphe catécholergique (CPVT) est une arythmie génétique létale qui se manifeste par une syncope ou une mort subite chez les enfants et les jeunes adultes dans des conditions de stress sans anomalie structurelle cardiaque évidente. Plusieurs mécanismes ont été proposés pour expliquer les altérations fonctionnelles sous-jacentes de la libération de Ca2+ dues aux mutations de RyR2 ou de ses protéines accessoires. Une nouvelle mutation CPVT située sur la partie N terminale de RyR2 a été identifiée dans une famille espagnole (RyR2R420Q). Ici, nous avons utilisé un modèle de souris KI exprimant le canal RyR2R420Q et des cardiomyocytes différenciés de cellules souches pluripotentes induites (hiPS-CM) générées à partir de deux patients frères (l'un avec mutation, l'autre sans mutation utilisé comme témoin). L’analyse des cardiomyocytes ventriculaires exprimant le RyR2R420Q humain et de souris étudiées par imagerie Ca2+confocale montre une augmentation des libérations de Ca2+spontanée durant la diastole (visualisé par les Sparks Ca2+), une libération fractionnelle plus élevée et une fréquence de vagues Ca2+ proarythmogènes augmentée après stimulation à l'isoprotérénol. L’analyse électrophysiologique, étudiée en enregistrant les potentiels d'action (AP) en utilisant les techniques de micro-électrodes sur les hiPSC-CM et de patch-clamp sur les cellules ventriculaires de souris KI, a montré des post-dépolarisations retardées dépendants du Ca2+ (DAD). L’amplitude des transitoires [Ca2+]i des cellules stimulées à 1 Hz étaient plus faible chez le groupe muté. La charge en Ca2+ du réticulum sarcoplasmique (SR), estimée par application rapide de caféine (10 mM), était aussi plus réduite dans les hiPS-CM exprimant RyR2R420Q, avant et après l'application ISO (1 μM). Cependant, le RyR2R420Q semble plus enclin à libérer du Ca2+, car le transitoire [Ca2+]i normalisé par la quantité de Ca2+ stockée dans le SR, la libération fractionnaire, était plus élevée dans les cellules mutées. Même si la charge Ca2+ du SR était plus petite dans les cellules RyR2R420Q, elles présentaient souvent un comportement pro-arythmogène tel que les vagues Ca2+ pendant les périodes diastoliques. Ce comportement est encore augmentée lors de la stimulation -adrénergique. Des résultats similaires ont été observés chez les souris KI, montrant ce modèle comme un outil précieux pour étudier la maladie CPVT. Nous avons ensuite étudié l'effet antiarythmique potentiel de la venlafaxine et de la prégabaline dans les cardiomyocytes de souris KI et le hiPS-CM, deux médicaments parmi d'autres prescrits à un membre porteur de la famille et qui a montré une réversion des symptômes du CPVT après le traitement. Nous avons constaté que ces deux médicaments atténuaient les événements arythmogènes de libération du Ca2+ induits par l'ISO dans les cardiomyocytes de souris KI. La venlafaxine a montré un effet antiarythmique dans hiPS-CM à la fois en traitements aigus et chroniques.Ainsi 1) le RyR2R420Q montre une augmentation de la libération diastolique du Ca2+ , encore plus augmentée par la stimulation à l ’isoproterénol, induisant des évènements proarythmogènes. 2) les effets sont retrouvés chez des cardiomyocytes ventriculaires des souris KI et chez des cellules hiPSC-CM, montrant que ces dernières sont un outil valable pour étudier les mécanismes pathologiques ; et 3) que la Venlafaxine peut protéger des arythmies chez les patients CPVT, bien que d’avantage d’expériences sont nécessaires afin de conclure quant à son utilité antiarythmiqueCatecholaminergic polymorphic ventricular tachycardia (CPVT) is a lethal genetic arrhythmia that manifests by syncope or sudden death in children and young adults under stress conditions without obvious cardiac structural abnormality. Several mechanisms have been proposed to explain the underlying Ca2+ release functional alterations due to mutations of RyR2 or of its accessory proteins. A novel CPVT mutation located on RyR2 N terminal portion has been identified in a Spanish family (RyR2R420Q). Here we used a KI mice model expressing the RyR2R420Q channel, and differentiated cardiomyocytes from induced pluripotent stem cells (hiPS-CM) generated from two brother patients (one with mutation, the other without mutation used as control). Confocal Ca2+ imaging analysis showed that human and mouse RyR2R420Q expressing ventricular cardiomyocytes have higher occurrence of Ca2+ sparks, enhanced fractional release, and significantly more proarrhythmogenic Ca2+ waves after isoproterenol stimulation. The action potential (AP) analysis, recorded using the micro-electrode technique in hiPSC-CMs and patch-clamp in KI mouse ventricular cells, showed Ca2+ -dependent delayed after depolarizations (DADs). The [Ca2+]i transient amplitudes of 1-Hz paced CPVT hiPSC-CMs was similar to control hiPSC-CMs. Whereas sarcoplasmic reticulum (SR) Ca2+ load, estimated by rapid caffeine (10 mM) application, was smaller in hiPS-CM from the RyR2R420Q carrier, both before and after 1 microM ISO application. However, the RyR2R420Q seems more prone to release Ca2+, as the [Ca2+]i transient normalized by the amount of Ca2+ stored in the SR, the fractional release, was higher in CPVT hiPSC-CMs. Even if SR Ca2+ load was smaller in CPVT hiPSC-CMs, they often presented proarrythmogenic behavior such as Ca2+ waves during diastolic periods. This behavior was further enhanced during β-adrenergic stimulation. Similar results were observed in KI mice, pointing to this model as a valuable tool to study the CPVT disease. We then studied the potential antiarrhythmic effect of venlafaxine and pregabalin in KI mouse cardiomyocytes and hiPS-CMs, two drugs among other medications that have been prescribed to one family carrier member and devoted of CPVT symptoms. We found that both of those drugs blunted ISO induced arrhythmogenic events in KI mouse cardiomyocytes. Venlafaxine showed antiarrhythmic effect in hiPS-CMs both by acute and chronic treatments.On overall, 1) the RyR2R420Q mutation shows enhanced diastolic Ca2+ release, which is further enhanced by isoproterenol inducing proarrhythmogenic events. 2) The effects were similar in hiPSC-CM and RyR2R420Q KI mice cardiomyocytes, pointing to hiPSC-CM as a valuable model to analyze pathological mechanisms; and 3) Venlafaxine may protect from arrhythmic CPVT patients, although more experiments are needed for in vivo test and to determine the mechanism of this antiarrhythmic effect
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Kathirvel, Paramasivam. "Mapping and manipulation of the murine ryanodine receptor gene (Ryr1)." Thesis, University of Edinburgh, 2000. http://hdl.handle.net/1842/12330.
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In this present study, experiments were carried out a) to characterise the mouse skeletal muscle ryanodine receptor (Ryr1) gene cDNA, b) to construct a contiguous map of the murine Ryr1 gene and c) to evaluate the phenotype of the Ryr1 knockout transgenic mice and to develop a mouse model, which carries a homologue of the C1843T mutation, associated with MH in pigs and some humans. The murine Ryrl cDNA has been characterised by cDNA cloning and sequence analysis. Murine Ryrl exon-specific RT-PCR primers were designed and used to generate Ryrl cDNA fragments from skeletal muscle total RNA of the mouse strain 129. The cloned RT-PCR products are overlapping and yield about 15 kb cDNA sequence. The cDNA sequence has higher sequence similarity with mammalian sequences than other vertebrate and invertebrate ryanodine receptor gene(s). A contiguous map of the Ryr1 gene has been constructed by DNA fingerprint analysis and STS mapping. Large fragment genomic clones containing murine Ryr1 sequences have been isolated from two libraries - a Bacterial Artificial Chromosome (BAC) library and P1-derived artificial chromosome (PAC) library. Of the 33 clones isolated, 4 were from the BAC and 29 were from the PAC library. The BACs form tow contiguous fragments separated by a gap. The relationships among the BACs were confirmed by DNA fingerprinting using human RYR1 cDNA fragments. This experiment also confirms the isolated clones are skeletal muscle ryanodine receptor isoform (Ryr1) specific. Sequence information from these BAC genomic clones and cDNA sequence information from this study has been used to develop STS markers. A contiguous map of the clones and flanking sequences has been established by STS analysis in BAC/PAC clones, which together span about 495 kb. The presence of all tested STS markers in two single PACs indicates that the murine Ryr1 gene is about 150 kb.
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Nicoll, Baines Katie Mhairi. "Muscle energetics and ageing in the context of RYR1 variants." Thesis, University of Leeds, 2017. http://etheses.whiterose.ac.uk/17288/.
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In aged muscle, from humans and mice, the ryanodine receptor (RyR1) is leaky, leading to increased levels of resting Ca2+ in the myoplasm. This is also a feature of skeletal muscle disorders caused by variants in RyR1 such as malignant hyperthermia (MH), central core disease (CCD), exertional heat illness (EHI) and late-onset axial myopathy (LOAM). Elevated Ca2+ is damaging to mitochondria, leading to production of reactive oxygen and nitrogen species associated with MH susceptibility to inhalational anaesthetics. Mice with Ryr1 variants show premature muscle ageing and highlight the cycle of inefficient calcium handling and oxidative damage to mitochondria that impairs skeletal muscle energetics. Caenorhabditis elegans models of MH CCD EHI and LOAM variants, both homozygous and heterozygous forms, showed increased sensitivity to halothane. Altered caffeine sensitivity was evident in MH and CCD models, and at very high concentrations in EHI models. Strains with RyR1 variants exhibit age-related accelerated myosin disorganisation. Whole genome Affymetrix arrays revealed genes and pathways correlated with skeletal muscle ageing and MH. Of additional genes of interest investigated UNC13, CASQ1, ORAI1, MCU and MICU1 showed altered expression with age. Array data from blood has been used to identify a signature for MH susceptibility. There is loss of mitochondrial membrane integrity and alteration in mitochondrial number in MH. New apparatus, capable of quantifying heat produced during muscle contraction, has enabled calculation of skeletal muscle efficiency. Preliminary data indicates that there was loss of skeletal muscle efficiency in aged muscle from wild type mice. This work provides new information on the role of RYR1 variants in skeletal muscle ageing and the importance of calcium handling in muscle energetics.
Books on the topic "RyR3"
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Robertson, Will C. Ryr: Rich Young Ruler. Covenant Books, 2020.
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Dialektord från Örs och Sundals-Ryrs socknar på Dal. 5th ed. Calluna, 2010.
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Schwartz, Peter J., and Lia Crotti. Monogenic and oligogenic cardiovascular diseases: genetics of arrhythmias—catecholaminergic polymorphic ventricular tachycardia. Oxford University Press, 2018. http://dx.doi.org/10.1093/med/9780198784906.003.0152.
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Catecholaminergic polymorphic ventricular tachycardia (CPVT) is a rare inherited disorder associated with syncope and sudden death manifesting in the young during sympathetic activation. The electrocardiogram is normal and the heart is structurally normal. The diagnosis is usually made with an exercise stress test that shows a typical pattern of onset and offset of adrenergically induced ventricular arrhythmias. Molecular screening of RyR2, the major CPVT gene, is recommended whenever the suspicion of CPVT is high. If a disease-causing mutation is identified, cascade screening allows pre-symptomatic diagnosis among family members. All affected subjects should be treated with beta blockers (nadolol or propranolol). Preliminary data support the association of beta blockers with flecainide. After a cardiac arrest, an implantable cardioverter defibrillator (ICD) should be implanted, but it is accompanied by a disquietingly high incidence of adverse effects. After syncope on beta blocker therapy, left cardiac sympathetic denervation is most effective, preserves quality of life, and does not preclude a subsequent ICD implantation.
Book chapters on the topic "RyR3"
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Nederend, Ineke, Christian van der Werf, and Arthur A. M. Wilde. "RyR2 in Cardiac Disorders." In Pathologies of Calcium Channels, 601–14. Berlin, Heidelberg: Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-40282-1_29.
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Aracena, Paula, Cecilia Hidalgo, and Susan L. Hamilton. "RYR1 Modulation by Calmodulin." In Ryanodine Receptors, 163–68. Boston, MA: Springer US, 2005. http://dx.doi.org/10.1007/0-387-23188-9_16.
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Van Petegem, Filip, and Kelvin Lau. "Ryanodine Receptor (RyR)." In Encyclopedia of Signaling Molecules, 4786–92. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-67199-4_99.
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Martemyanov, Kirill A., Pooja Parameswaran, Irene Aligianis, Mark Handley, Marga Gual-Soler, Tomohiko Taguchi, Jennifer L. Stow, et al. "Ryanodine Receptor (RyR)." In Encyclopedia of Signaling Molecules, 1704–9. New York, NY: Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_99.
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Parness, Jerome. "The Dantrolene Binding Site on RYR1." In Ryanodine Receptors, 243–51. Boston, MA: Springer US, 2005. http://dx.doi.org/10.1007/0-387-23188-9_24.
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Besch, Henry R., Chun Hong Shao, and Keshore R. Bidasee. "Ryanoids, Receptor Affinity and RYR Channel Subconductance." In Ryanodine Receptors, 179–89. Boston, MA: Springer US, 2005. http://dx.doi.org/10.1007/0-387-23188-9_18.
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Patel, Seema, and Nadeem Akhtar. "Fungus Monascus-Fermented Red Yeast Rice (RYR): Natural Therapeutic Statin Source or Mycotoxin?" In Fungi and their Role in Sustainable Development: Current Perspectives, 739–52. Singapore: Springer Singapore, 2018. http://dx.doi.org/10.1007/978-981-13-0393-7_38.
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Koivumaki, J. T., J. Takalo, T. Korhonen, M. Weckstrom, and P. Tavi. "Calcium Dependent Release and Its Regulation in Cardiac Myocytes: Mathematical Model of the RyR Channel." In IFMBE Proceedings, 669–72. Berlin, Heidelberg: Springer Berlin Heidelberg, 2009. http://dx.doi.org/10.1007/978-3-642-03882-2_179.
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MacLennan, David H. "Mutations in the Skeletal Muscle Ryanodine Receptor (RYR1) Gene are Linked to Malignant Hyperthermia and Central-Core Disease." In Malignant Hyperthermia, 79–86. Tokyo: Springer Japan, 1996. http://dx.doi.org/10.1007/978-4-431-68346-9_12.
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Sako, Shinji, Ryuichi Yamamoto, and Tadashi Kitamura. "Ryry: A Real-Time Score-Following Automatic Accompaniment Playback System Capable of Real Performances with Errors, Repeats and Jumps." In Active Media Technology, 134–45. Cham: Springer International Publishing, 2014. http://dx.doi.org/10.1007/978-3-319-09912-5_12.
Full textConference papers on the topic "RyR3"
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Wilson, Kirsty, Maslinda Musa, Lynne Bingle, C. Jeremy Craven, and Colin D. Bingle. "Vomeromodulin/RYF3: PLUNC’s Most Distant Cousin." In American Thoracic Society 2011 International Conference, May 13-18, 2011 • Denver Colorado. American Thoracic Society, 2011. http://dx.doi.org/10.1164/ajrccm-conference.2011.183.1_meetingabstracts.a2090.
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Ryvkin, Alexander, and Nikita Markov. "RyRs Coupling Causes a Calcium Leak in Cardiac Cell." In 2018 Computing in Cardiology Conference. Computing in Cardiology, 2018. http://dx.doi.org/10.22489/cinc.2018.323.
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Hermann, Katharina, Katja Kloth, Jessika Johannsen, and Jonas Denecke. "P 1147. Pyridostigmine Leads to Relevant Improvement of Motor Function in an Infant with RYR1-Related Congenital Myopathy." In Abstracts of the 44th Annual Meeting of the Society for Neuropediatrics. Georg Thieme Verlag KG, 2018. http://dx.doi.org/10.1055/s-0038-1676024.
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Lu, Haiquan, and Gregg Semenza. "Abstract 3066: Chemotherapy-induced GSTO1 interacts with ryanodine receptor RYR1 to trigger Ca2+-dependent breast cancer stem cell enrichment." In Proceedings: AACR Annual Meeting 2018; April 14-18, 2018; Chicago, IL. American Association for Cancer Research, 2018. http://dx.doi.org/10.1158/1538-7445.am2018-3066.
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Souvannakitti, Dangjai, Guoxiang Yuan, Jayasri Nanduri, Ganesh K. Kumar, Aaron Fox, and Nanduri R. Prabhakar. "Intermittent Hypoxia Activates Ryanodine Receptors (RyRs) Via S-glutathionylation In Neonatal Rat Adrenal Chromaffin Cells And Contributes To Augmented Catecholamines secretion." In American Thoracic Society 2010 International Conference, May 14-19, 2010 • New Orleans. American Thoracic Society, 2010. http://dx.doi.org/10.1164/ajrccm-conference.2010.181.1_meetingabstracts.a2479.
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Resende, Ana Flávia Morais, Guilherme Rabelo Nasuk, Bruna Calixto de Jesus, Allan Luis Barboza Atum, and José Antônio Silva Júnior. "EXPRESSÃO MIOCÁRDICA RELACIONADA À CINÉTICA DO CÁLCIO EM ANIMAIS COM EXPOSIÇÃO PRÉ-NATAL AO ÁLCOOL." In Congresso Médico Acadêmico da Universidade Nove de Julho. Universidade Nove de Julho, 2022. http://dx.doi.org/10.5585/comamedvg.2022.16.
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Introdução: A exposição alcoólica pré-natal (E.P.A.) é considerada uma das principais responsáveis pelas alterações congênitas humanas. No sistema cardiovascular, a E.P.A. pode levar a alterações na expressão de genes relacionados à homeostase cardiovascular. Estudos têm mostrado que miócitos cardíacos expostos ao etanol durante a embriogênese não amadurecem morfológica ou funcionalmente, bem como apresentam alterações no transporte e captação/ligação de Ca2+ pelo retículo sarcoplasmático (SR). Uma diminuição da concentração citosólica de Ca2+ resultante do um efeito inibitório do álcool nas proteínas reguladoras desse íon pode resultar em diminuição do volume sistólico e alterações na frequência cardíaca. Objetivo: Analisar o impacto da E.P.A. na ativação da via de transdução de sinal da cinética do cálcio pela análise da expressão de RNA mensageiro de componentes desta via. Materiais e Métodos: O estudo foi aprovado pelo Comitê de Ética no Uso de Animais (CEUA = 9355120319 ID 000115). Foram utilizados camundongos isogênicos da linhagem C57Bl/6. As fêmeas progenitoras foram separadas e randomizadas no grupo controle (n=4) e no grupo de exposição ao álcool (n=11). O protocolo do grupo E.P.A. durante a gestação, foi a exposição do álcool na proporção de 10% (v/v) diluídos em água de consumo. Após 45 dias, 10 filhotes de cada grupo (n=20) foram anestesiados com isoflurano (<20 seg.) e decapitados. O ventrículo esquerdo (VE) foi coletado e tratado. A expressão relativa foi obtida por técnica RT-qPCR utilizando placas customizadas TaqMan®, sendo utilizado como controle endógeno o gene rRNA 18S. A estatística foi calculada com a aplicação IBM SPSS Statistics for Windows, Version 25.0. (Armonk, NY: IBM Corp., 2017); A normalidade foi testada através do teste de Shapiro-Wilk e os dados representados por média ± EPM. Comparação entre grupos: Teste T para amostras independentes sendo considerado o valor de significância p ≤0,05. Resultados: No grupo E.P.A, houve redução de 65,51% (p<0,001) e 60,17% (p<0,001) na expressão dos genes Calsequestrina 2 (Casq2) e Família de trocadores de soluto (Na-Ca) 8, membro A1 (Slc8a1), respectivamente, quando comparados ao grupo Controle. Por sua vez, o grupo E.P.A. apresentou aumento de 254,86% (p<0,001), 231,70% (p<0,001) e 183,37% (p<0,001) na expressão dos genes ATPase, transporte de Ca ++, músculo cardíaco, contração lenta 2 (Atp2a2), Receptor 2 de Rianodina, Cardíaco (RyR-2) e Fosfolamban (Pln) nessa ordem, quando comparado ao grupo Controle. Conclusão: Concluímos que a agressão mediada pelo álcool no miocárdio pode modular a via de cinética de cálcio. Estes resultados indicam que o insulto gerado pelo álcool, por meio de EPA e dependendo da concentração e/ou duração do estímulo, pode comprometer a expressão proteica de componentes da cinética do cálcio em favor de uma disfunção cardíaca. Palavras-chave: Álcool; cálcio; genes.
Reports on the topic "RyR3"
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Klipp, Robert. Novel Compound, 84F2, Inhibits Calmodulin Deficient RyR2. Portland State University Library, January 2000. http://dx.doi.org/10.15760/etd.5368.
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Zhao, Fangfang, Chunli Lu, Luying Chen, Yaxin Guo, Lijie Lu, Yuerong Jiang, Jianping Liu, and Keji Chen. Red yeast rice preparations for dyslipidemia: A protocol for an overview of systematic review and meta-analysis. INPLASY - International Platform of Registered Systematic Review and Meta-analysis Protocols, March 2022. http://dx.doi.org/10.37766/inplasy2022.3.0032.
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Review question / Objective: What is the quality of systematic reviews/meta-analysis of red yeast rice (RYR) preparations for dyslipidemia? What is the comparative benefit of red yeast rice preparations on dyslipidemia compared to other lipid-lowering drugs? Based on the current controversies in dyslipidemia guidelines and clinical practice, to explore the relative benefits of red yeast rice compared with other lipid-lowering drugs, we plan to perform an overview of existing SRs/MAs. Condition being studied: Red yeast rice (RYR) has been used as an alternative to statin therapy in treating patients with dyslipidemia, particularly in those considered to be statin intolerant due to statin-associated myalgia (SAM), and clinical studies suggest that RYR is well-tolerated, safe, and effective for cardiovascular disease (CVD) primary prevention. Several studies support the beneficial effect of RYR on blood lipid profiles. Dyslipidemia is a worldwide public health challenge because of its high prevalence, leading to significant economic and social burdens. Many systematic reviews (SRs) /meta-analysis (MAs) have been performed to prove the effects of RYR on dyslipidemia during the past several years. High-quality SRs/MAs can provide clinicians, patients, and other decision-makers with a reliable scientific basis. However, existing SRs/MAs showed varied and heterogeneous results.
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Dornan, Thomas. Antioxidant Anthocyanidins and Calcium Transport Modulation of the Ryanodine Receptor of Skeletal Muscle (RyR1). Portland State University Library, January 2000. http://dx.doi.org/10.15760/etd.319.
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Dornan, Thomas. Calcium Transport Inhibition, Stimulation, and Light Dependent Modulation of the Skeletal Calcium Release Channel (RyR1) by the Prototropic Forms of Pelargonidin. Portland State University Library, January 2000. http://dx.doi.org/10.15760/etd.1930.
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