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Journal articles on the topic 'RyR3'

Author: Grafiati

Published: 9 March 2023

Last updated: 31 July 2025

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1

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 (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 a

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2

Zheng, Yun-Min, Qing-Song Wang, Rakesh Rathore, et al. "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 (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-cre

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3

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 (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 loade

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4

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 (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 a

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5

Tian, Chengju, Caronda J. Moore, Puttappa Dodmane, et al. "Dust from hog confinement facilities impairs Ca2+ mobilization from sarco(endo)plasmic reticulum by inhibiting ryanodine receptors." Journal of Applied Physiology 114, no. 5 (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 chan

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6

OTTINI, Laura, Giovanna MARZIALI, Antonio CONTI, Alexandra CHARLESWORTH та Vincenzo SORRENTINO. "α and β isoforms of ryanodine receptor from chicken skeletal muscle are the homologues of mammalian RyR1 and RyR3". Biochemical Journal 315, № 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 15

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7

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 (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 expressi

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8

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 (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 advancin

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9

Rossi, Daniela, Ilenia Simeoni, Marcella Micheli, et al. "RyR1 and RyR3 isoforms provide distinct intracellular Ca2+signals in HEK 293 cells." Journal of Cell Science 115, no. 12 (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

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10

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 (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 skele

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11

Flucher, Bernhard E., Antonio Conti, Hiroshi Takeshima, and Vincenzo Sorrentino. "Type 3 and Type 1 Ryanodine Receptors Are Localized in Triads of the Same Mammalian Skeletal Muscle Fibers." Journal of Cell Biology 146, no. 3 (1999): 621–30. http://dx.doi.org/10.1083/jcb.146.3.621.

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The type 3 ryanodine receptor (RyR3) is a ubiquitous calcium release channel that has recently been found in mammalian skeletal muscles. However, in contrast to the skeletal muscle isoform (RyR1), neither the subcellular distribution nor the physiological role of RyR3 are known. Here, we used isoform-specific antibodies to localize RyR3 in muscles of normal and RyR knockout mice. In normal hind limb and diaphragm muscles of young mice, RyR3 was expressed in all fibers where it was codistributed with RyR1 and with the skeletal muscle dihydropyridine receptor. This distribution pattern indicates

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12

Vaithianathan, Thirumalini, Damodaran Narayanan, Maria T. Asuncion-Chin, et al. "Subtype identification and functional characterization of ryanodine receptors in rat cerebral artery myocytes." American Journal of Physiology-Cell Physiology 299, no. 2 (2010): C264—C278. http://dx.doi.org/10.1152/ajpcell.00318.2009.

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Ryanodine receptors (RyRs) regulate contractility in resistance-size cerebral artery smooth muscle, yet their molecular identity, subcellular location, and phenotype in this tissue remain unknown. Following rat resistance-size cerebral artery myocyte sarcoplasmic reticulum (SR) purification and incorporation into POPE-POPS-POPC (5:3:2; wt/wt) bilayers, unitary conductances of 110 ± 8, 334 ± 15, and 441 ± 27 pS in symmetric 300 mM Cs+ were usually detected. The most frequent (34/40 bilayers) conductance (334 pS) decreased to ≤100 pS when Cs+ was replaced with Ca2+. The predominant conductance d

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13

Morrissette, Jeffery, Le Xu, Alexandra Nelson, Gerhard Meissner, and Barbara A. Block. "Characterization of RyR1-slow, a ryanodine receptor specific to slow-twitch skeletal muscle." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 279, no. 5 (2000): R1889—R1898. http://dx.doi.org/10.1152/ajpregu.2000.279.5.r1889.

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Two distinct skeletal muscle ryanodine receptors (RyR1s) are expressed in a fiber type–specific manner in fish skeletal muscle (11). In this study, we compare [3H]ryanodine binding and single channel activity of RyR1-slow from fish slow-twitch skeletal muscle with RyR1-fast and RyR3 isolated from fast-twitch skeletal muscle. Scatchard plots indicate that RyR1-slow has a lower affinity for [3H]ryanodine when compared with RyR1-fast. In single channel recordings, RyR1-slow and RyR1-fast had similar slope conductances. However, the maximum open probability (Po) of RyR1-slow was threefold less tha

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14

Yang, Xiao-Ru, Mo-Jun Lin, Kay-Pong Yip, et al. "Multiple ryanodine receptor subtypes and heterogeneous ryanodine receptor-gated Ca2+ stores in pulmonary arterial smooth muscle cells." American Journal of Physiology-Lung Cellular and Molecular Physiology 289, no. 2 (2005): L338—L348. http://dx.doi.org/10.1152/ajplung.00328.2004.

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Ryanodine receptors (RyRs) of pulmonary arterial smooth muscle cells (PASMCs) play important roles in major physiological processes such as hypoxic pulmonary vasoconstriction and perinatal pulmonary vasodilatation. Recent studies show that three subtypes of RyRs are coexpressed and RyR-gated Ca2+ stores are distributed heterogeneously in systemic vascular myocytes. However, the molecular identity and subcellular distribution of RyRs have not been examined in PASMCs. In this study we detected mRNA and proteins of all three subtypes in rat intralobar PASMCs using RT-PCR and Western blot. Quantit

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15

Meissner, Gerhard. "The structural basis of ryanodine receptor ion channel function." Journal of General Physiology 149, no. 12 (2017): 1065–89. http://dx.doi.org/10.1085/jgp.201711878.

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Large-conductance Ca2+ release channels known as ryanodine receptors (RyRs) mediate the release of Ca2+ from an intracellular membrane compartment, the endo/sarcoplasmic reticulum. There are three mammalian RyR isoforms: RyR1 is present in skeletal muscle; RyR2 is in heart muscle; and RyR3 is expressed at low levels in many tissues including brain, smooth muscle, and slow-twitch skeletal muscle. RyRs form large protein complexes comprising four 560-kD RyR subunits, four ∼12-kD FK506-binding proteins, and various accessory proteins including calmodulin, protein kinases, and protein phosphatases

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16

Bultynck, Geert, Daniela Rossi, Geert Callewaert, et al. "The Conserved Sites for the FK506-binding Proteins in Ryanodine Receptors and Inositol 1,4,5-Trisphosphate Receptors Are Structurally and Functionally Different." Journal of Biological Chemistry 276, no. 50 (2001): 47715–24. http://dx.doi.org/10.1074/jbc.m106573200.

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We compared the interaction of the FK506-binding protein (FKBP) with the type 3 ryanodine receptor (RyR3) and with the type 1 and type 3 inositol 1,4,5-trisphosphate receptor (IP3R1 and IP3R3), using a quantitative GST-FKBP12 and GST-FKBP12.6 affinity assay. We first characterized and mapped the interaction of the FKBPs with the RyR3. GST-FKBP12 as well as GST-FKBP12.6 were able to bind ∼30% of the solubilized RyR3. The interaction was completely abolished by FK506, strengthened by the addition of Mg2+, and weakened in the absence of Ca2+but was not affected by the addition of cyclic ADP-ribos

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17

Rousseau, Eric, and Sonia Proteau. "Functional properties of the native type 3 ryanodine receptor Ca2+-release channel from canine diaphragm." Canadian Journal of Physiology and Pharmacology 79, no. 4 (2001): 310–19. http://dx.doi.org/10.1139/y00-127.

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mRNA and protein analyses have previously shown that the diaphragm expresses two ryanodine receptor isoforms: RyR1 and RyR3.RyR1 is the main Ca2+-releasing pathway in this muscle type. We now report the conducting, gating, and immunological properties of the native and purified forms of the less abundant RyR3 channel. The conductance of this native Ca2+-release channel was 330 pS in 50 mM/250 mM trans/cis CsCH3SO3. It was activated by Ca2+ concentrations of 1-1000 µM, and did not inactivate at mM concentrations of Ca2+. Both isoforms were purified by either a sucrose density gradient or immuno

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18

Ji, Guangju, Morris E. Feldman, Kai Su Greene, Vincenzo Sorrentino, Hong-Bo Xin, and Michael I. Kotlikoff. "RYR2 Proteins Contribute to the Formation of Ca2+ Sparks in Smooth Muscle." Journal of General Physiology 123, no. 4 (2004): 377–86. http://dx.doi.org/10.1085/jgp.200308999.

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Calcium release through ryanodine receptors (RYR) activates calcium-dependent membrane conductances and plays an important role in excitation-contraction coupling in smooth muscle. The specific RYR isoforms associated with this release in smooth muscle, and the role of RYR-associated proteins such as FK506 binding proteins (FKBPs), has not been clearly established, however. FKBP12.6 proteins interact with RYR2 Ca2+ release channels and the absence of these proteins predictably alters the amplitude and kinetics of RYR2 unitary Ca2+ release events (Ca2+ sparks). To evaluate the role of specific

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19

Murayama, Takashi, and Yasuo Ogawa. "RyR1 exhibits lower gain of CICR activity than RyR3 in the SR: evidence for selective stabilization of RyR1 channel." American Journal of Physiology-Cell Physiology 287, no. 1 (2004): C36—C45. http://dx.doi.org/10.1152/ajpcell.00395.2003.

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We showed that frog α-ryanodine receptor (α-RyR) had a lower gain of Ca2+-induced Ca2+ release (CICR) activity than β-RyR in sarcoplasmic reticulum (SR) vesicles, indicating selective “stabilization” of the former isoform (Murayama T and Ogawa Y. J Biol Chem 276: 2953–2960, 2001). To know whether this is also the case with mammalian RyR1, we determined [3H]ryanodine binding of RyR1 and RyR3 in bovine diaphragm SR vesicles. The value of [3H]ryanodine binding (B) was normalized by the number of maximal binding sites (Bmax), whereby the specific activity of each isoform was expressed. This B/Bmax

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20

Van Petegem, Filip. "The Ryanodine Receptor: Arrhythmias and Muscle Disorders at High Resolution." Acta Crystallographica Section A Foundations and Advances 70, a1 (2014): C798. http://dx.doi.org/10.1107/s2053273314092018.

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Calcium ions play crucial roles in our bodies, acting as second messengers in multiple signaling pathways. The resting calcium levels in the cytosol are very low, but can increase rapidly and transiently by influx from the extracellular space, or by release from intracellular stores. The Endoplasmic and Sarcoplasmic Reticulum (ER/SR) form major intracellular calcium stores. The `Ryanodine Receptor' (RyR) is a protein that dictates calcium release from the ER/SR. It forms a huge ion channel with a molecular weight exceeding 2 MegaDalton. RyRs are expressed in multiple cell types, but are partic

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21

BULTYNCK, Geert, Patrick DE SMET, Daniela ROSSI, et al. "Characterization and mapping of the 12kDa FK506-binding protein (FKBP12)-binding site on different isoforms of the ryanodine receptor and of the inositol 1,4,5-trisphosphate receptor." Biochemical Journal 354, no. 2 (2001): 413–22. http://dx.doi.org/10.1042/bj3540413.

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We investigated the interaction of the 12kDa FK506-binding protein (FKBP12) with two ryanodine-receptor isoforms (RyR1 and RyR3) and with two myo-inositol 1,4,5-trisphosphate (IP3) receptor isoforms (IP3R1 and IP3R3). Using glutathione S-transferase (GST)-FKBP12 affinity chromatography, we could efficiently extract RyR1 (42±7% of the solubilized RyR1) from terminal cisternae of skeletal muscle as well as RyR3 (32±4% of the solubilized RyR3) from RyR3-overexpressing HEK-293 cells. These interactions were completely abolished by FK506 (20µM) but were largely unaffected by RyR-channel modulators.

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Jo, Michiko, Andrea N. Trujillo, Ying Yang, and Jerome W. Breslin. "Evidence of functional ryanodine receptors in rat mesenteric collecting lymphatic vessels." American Journal of Physiology-Heart and Circulatory Physiology 317, no. 3 (2019): H561—H574. http://dx.doi.org/10.1152/ajpheart.00564.2018.

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In the current study, the potential contributions of ryanodine receptors (RyRs) to intrinsic pumping and responsiveness to substance P (SP) were investigated in isolated rat mesenteric collecting lymphatic vessels. Responses to SP were characterized in lymphatic vessels in the absence or presence of pretreatment with nifedipine to block L-type Ca2+ channels, caffeine to block normal release and uptake of Ca2+ from the sarcoplasmic reticulum, ryanodine to block all RyR isoforms, or dantrolene to more selectively block RyR1 and RyR3. RyR expression and localization in lymphatics was also assesse

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23

Matsuki, Katsuhito, Daiki Kato, Masashi Takemoto, et al. "Negative regulation of cellular Ca2+ mobilization by ryanodine receptor type 3 in mouse mesenteric artery smooth muscle." American Journal of Physiology-Cell Physiology 315, no. 1 (2018): C1—C9. http://dx.doi.org/10.1152/ajpcell.00006.2018.

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Physiological functions of type 3 ryanodine receptors (RyR3) in smooth muscle (SM) tissues are not well understood, in spite of their wide expression. However, the short isoform of RyR3 is known to be a dominant-negative variant (DN-RyR3), which may negatively regulate functions of both RyR2 and full-length (FL) RyR3 by forming hetero-tetramers. Here, functional roles of RyR3 in the regulation of Ca2+ signaling in mesenteric artery SM cells (MASMCs) were examined using RyR3 homozygous knockout mice (RyR3−/−). Quantitative PCR analyses suggested that the predominant RyR3 subtype in MASMs from w

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24

Marks, A. R. "Intracellular calcium-release channels: regulators of cell life and death." American Journal of Physiology-Heart and Circulatory Physiology 272, no. 2 (1997): H597—H605. http://dx.doi.org/10.1152/ajpheart.1997.272.2.h597.

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Intracellular Ca2+-release channels on the sarcoplasmic reticulum of striated muscle [ryanodine receptors (RyRs)] and on the endoplasmic reticulum of almost all types of cells [inositol 1,4,5-trisphosphate receptors (IP3Rs)] comprise a unique family of molecules that are structurally and functionally distinct from all other known ion channels. These channels play crucial roles in Ca2+-mediated signaling that triggers excitation-contraction coupling, T-lymphocyte activation, fertilization, and many other cellular functions. Three forms of RyR have been identified: RyR1, expressed predominantly

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AWAD, Suad S., Heather K. LAMB, Joanna M. MORGAN, William DUNLOP, and James I. GILLESPIE. "Differential expression of ryanodine receptor RyR2 mRNA in the non-pregnant and pregnant human myometrium." Biochemical Journal 322, no. 3 (1997): 777–83. http://dx.doi.org/10.1042/bj3220777.

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We describe here the expression of the ryanodine receptor isoforms RyR2 and RyR3 in human non-pregnant and pregnant (non-labouring) myometrium, and in isolated cultured myometrial cells. The mRNA encoding the RyR3 isoform was found in both non-pregnant and pregnant myometrial tissue samples; however, the mRNA for RyR2 was found only in pregnant samples. It can be speculated that the appearance of this additional isoform in the pregnant myometrium may increase the ability of this tissue to contract at term. Control of expression of the RyR2 gene may therefore be another example of an up-regulat

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Clancy, J. S., H. Takeshima, S. L. Hamilton, and M. B. Reid. "Contractile function is unaltered in diaphragm from mice lacking calcium release channel isoform 3." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 277, no. 4 (1999): R1205—R1209. http://dx.doi.org/10.1152/ajpregu.1999.277.4.r1205.

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Skeletal muscle expresses at least two isoforms of the calcium release channel in the sarcoplasmic reticulum (RyR1 and RyR3). Whereas the function of RyR1 is well defined, the physiological significance of RyR3 is unclear. Some authors have suggested that RyR3 participates in excitation-contraction coupling and that RyR3 may specifically confer resistance to fatigue. To test this hypothesis, we measured contractile function of diaphragm strips from adult RyR3-deficient mice (exon 2-targeted mutation) and their heterozygous and wild-type littermates. In unfatigued diaphragm, there were no diffe

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Gaburjakova, Jana, and Marta Gaburjakova. "Molecular Aspects Implicated in Dantrolene Selectivity with Respect to Ryanodine Receptor Isoforms." International Journal of Molecular Sciences 24, no. 6 (2023): 5409. http://dx.doi.org/10.3390/ijms24065409.

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Dantrolene is an intra-cellularly acting skeletal muscle relaxant used for the treatment of the rare genetic disorder, malignant hyperthermia (MH). In most cases, MH susceptibility is caused by dysfunction of the skeletal ryanodine receptor (RyR1) harboring one of nearly 230 single-point MH mutations. The therapeutic effect of dantrolene is the result of a direct inhibitory action on the RyR1 channel, thus suppressing aberrant Ca2+ release from the sarcoplasmic reticulum. Despite the almost identical dantrolene-binding sequence exits in all three mammalian RyR isoforms, dantrolene appears to b

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Martin, Cécile, Jean-Marc Hyvelin, Karen E. Chapman, Roger Marthan, Richard H. Ashley, and Jean-Pierre Savineau. "Pregnant rat myometrial cells show heterogeneous ryanodine- and caffeine-sensitive calcium stores." American Journal of Physiology-Cell Physiology 277, no. 2 (1999): C243—C252. http://dx.doi.org/10.1152/ajpcell.1999.277.2.c243.

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Intracellular Ca2+ release channels such as ryanodine receptors play crucial roles in the Ca2+-mediated signaling that triggers excitation-contraction coupling in muscles. Although the existence and the role of these channels are well characterized in skeletal and cardiac muscles, their existence in smooth muscles, and more particularly in the myometrium, is very controversial. We have now clearly demonstrated the expression of ryanodine receptor Ca2+ release channels in rat myometrial smooth muscle, and for the first time, intracellular Ca2+ concentration experiments with indo 1 on single myo

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Perni, Stefano, Kurt C. Marsden, Matias Escobar, Stephen Hollingworth, Stephen M. Baylor, and Clara Franzini-Armstrong. "Structural and functional properties of ryanodine receptor type 3 in zebrafish tail muscle." Journal of General Physiology 145, no. 3 (2015): 173–84. http://dx.doi.org/10.1085/jgp.201411303.

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The ryanodine receptor (RyR)1 isoform of the sarcoplasmic reticulum (SR) Ca2+ release channel is an essential component of all skeletal muscle fibers. RyR1s are detectable as “junctional feet” (JF) in the gap between the SR and the plasmalemma or T-tubules, and they are required for excitation–contraction (EC) coupling and differentiation. A second isoform, RyR3, does not sustain EC coupling and differentiation in the absence of RyR1 and is expressed at highly variable levels. Anatomically, RyR3 expression correlates with the presence of parajunctional feet (PJF), which are located on the side

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Rossi, R., R. Bottinelli, V. Sorrentino, and C. Reggiani. "Response to caffeine and ryanodine receptor isoforms in mouse skeletal muscles." American Journal of Physiology-Cell Physiology 281, no. 2 (2001): C585—C594. http://dx.doi.org/10.1152/ajpcell.2001.281.2.c585.

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The response to caffeine was studied in mouse muscles [diaphragm, soleus, and extensor digitorum longus (EDL)] with different ryanodine receptor isoform (RyR1, RyR3) composition and in single permeabilized muscle fibers dissected from diaphragm of wild-type (WT) and RyR3-deficient (RyR3−/−) mice at 1, 15, 30, and 60 postnatal days (PND). The caffeine response decreased during development, and, in adult mice, was greater in diaphragm, lower in EDL, and intermediate in soleus. This suggests a direct relation between response to caffeine and RyR3 expression. The lack of RyR3 reduced caffeine resp

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Murayama, Takashi, Toshiharu Oba, Shigeki Kobayashi, Noriaki Ikemoto, and Yasuo Ogawa. "Postulated role of interdomain interactions within the type 1 ryanodine receptor in the low gain of Ca2+-induced Ca2+ release activity of mammalian skeletal muscle sarcoplasmic reticulum." American Journal of Physiology-Cell Physiology 288, no. 6 (2005): C1222—C1230. http://dx.doi.org/10.1152/ajpcell.00415.2004.

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Ryanodine receptor (RyR) type 1 (RyR1) exhibits a markedly lower gain of Ca2+-induced Ca2+ release (CICR) activity than RyR type 3 (RyR3) in the sarcoplasmic reticulum (SR) of mammalian skeletal muscle (selective stabilization of the RyR1 channel), and this reduction in the gain is largely eliminated using 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonic acid (CHAPS). We have investigated whether the hypothesized interdomain interactions within RyR1 are involved in the selective stabilization of the channel using [3H]ryanodine binding, single-channel recordings, and Ca2+ release from t

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KISELYOV, Kirill, Dong Min SHIN, Nikolay SHCHEYNIKOV, Tomohiro KUROSAKI, and Shmuel MUALLEM. "Regulation of Ca2+-release-activated Ca2+ current (Icrac) by ryanodine receptors in inositol 1,4,5-trisphosphate-receptor-deficient DT40 cells." Biochemical Journal 360, no. 1 (2001): 17–22. http://dx.doi.org/10.1042/bj3600017.

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Persistence of capacitative Ca2+ influx in inositol 1,4,5-trisphosphate (IP3) receptor (IP3R)-deficient DT40 cells (DT40IP3R-/−) raises the question of whether gating of Ca2+-release activated Ca2+ current (Icrac) by conformational coupling to Ca2+-release channels is a general mechanism of gating of these channels. In the present work we examined the properties and mechanism of activation of Icrac Ca2+ current in wild-type and DT40IP3R-/− cells. In both cell types passive depletion of internal Ca2+ stores by infusion of EGTA activated a Ca2+ current with similar characteristics and time cours

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Eckhardt, Jan, Christoph Bachmann, Marijana Sekulic-Jablanovic, et al. "Extraocular muscle function is impaired in ryr3−/− mice." Journal of General Physiology 151, no. 7 (2019): 929–43. http://dx.doi.org/10.1085/jgp.201912333.

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Calcium is an ubiquitous second messenger mediating numerous physiological processes, including muscle contraction and neuronal excitability. Ca2+ is stored in the ER/SR and is released into the cytoplasm via the opening of intracellular inositol trisphosphate receptor and ryanodine receptor calcium channels. Whereas in skeletal muscle, isoform 1 of the RYR is the main channel mediating calcium release from the SR leading to muscle contraction, the function of ubiquitously expressed ryanodine receptor 3 (RYR3) is far from clear; it is not known whether RYR3 plays a role in excitation–contracti

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Lifshitz, Lawrence M., Jeffrey D. Carmichael, F. Anthony Lai, et al. "Spatial organization of RYRs and BK channels underlying the activation of STOCs by Ca2+ sparks in airway myocytes." Journal of General Physiology 138, no. 2 (2011): 195–209. http://dx.doi.org/10.1085/jgp.201110626.

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Short-lived, localized Ca2+ events mediate Ca2+ signaling with high efficiency and great fidelity largely as a result of the close proximity between Ca2+-permeable ion channels and their molecular targets. However, in most cases, direct evidence of the spatial relationship between these two types of molecules is lacking, and, thus, mechanistic understanding of local Ca2+ signaling is incomplete. In this study, we use an integrated approach to tackling this issue on a prototypical local Ca2+ signaling system composed of Ca2+ sparks resulting from the opening of ryanodine receptors (RYRs) and sp

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Tsai, Shu-Huei, Emily Yun-Chia Chang, Yi-Cheng Chang, et al. "Knockdown of RyR3 Enhances Adiponectin Expression Through an atf3-Dependent Pathway." Endocrinology 154, no. 3 (2013): 1117–29. http://dx.doi.org/10.1210/en.2012-1515.

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Abstract Adiponectin is an important adipose-specific protein, which possesses insulin (INS)-sensitizing, antiinflammatory, and antiatherosclerotic functions. However, its regulation remains largely unknown. In this study, we identified that ryanodine receptor (RyR)3 plays an important role in the regulation of adiponectin expression. RyR3 was expressed in 3T3-L1 preadipocytes, and its level was decreased upon adipogenesis. Silencing of RyR3 expression in 3T3-L1 preadipocytes resulted in up-regulated adiponectin promoter activity, enhanced adiponectin mRNA expression, and more adiponectin prot

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Chun, Lois G., Christopher W. Ward, and Martin F. Schneider. "Ca2+ sparks are initiated by Ca2+ entry in embryonic mouse skeletal muscle and decrease in frequency postnatally." American Journal of Physiology-Cell Physiology 285, no. 3 (2003): C686—C697. http://dx.doi.org/10.1152/ajpcell.00072.2003.

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“Spontaneous” Ca2+ sparks and ryanodine receptor type 3 (RyR3) expression are readily detected in embryonic mammalian skeletal muscle but not in adult mammalian muscle, which rarely exhibits Ca2+ sparks and expresses predominantly RyR1. We have used confocal fluorescence imaging and systematic sampling of enzymatically dissociated single striated muscle fibers containing the Ca2+ indicator dye fluo 4 to show that the frequency of spontaneous Ca2+ sparks decreases dramatically from embryonic day 18 (E18) to postnatal day 14 (P14) in mouse diaphragm and from P1 to P14 in mouse extensor digitorum

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Mattei, M. G., G. Giannini, F. Moscatelli, and V. Sorrentino. "Chromosomal Localization of Murine Ryanodine Receptor Genes RYR1, RYR2, and RYR3 by in Situ Hybridization." Genomics 22, no. 1 (1994): 202–4. http://dx.doi.org/10.1006/geno.1994.1362.

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Hori, Atsushi, Haruka Inaba, Takashi Hato, et al. "Carvedilol suppresses ryanodine receptor-dependent Ca2+ bursts in human neurons bearing PSEN1 variants found in early onset Alzheimer’s disease." PLOS ONE 19, no. 8 (2024): e0291887. http://dx.doi.org/10.1371/journal.pone.0291887.

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Seizures are increasingly being recognized as the hallmark of Alzheimer’s disease (AD). Neuronal hyperactivity can be a consequence of neuronal damage caused by abnormal amyloid β (Aß) depositions. However, it can also be a cell-autonomous phenomenon causing AD by Aß-independent mechanisms. Various studies using animal models have shown that Ca2+ is released from the endoplasmic reticulum (ER) via type 1 inositol triphosphate receptors (InsP3R1s) and ryanodine receptors (RyRs). To investigate which is the main pathophysiological mechanism in human neurons, we measured Ca2+ signaling in neural

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Huddleston, A. Tara, Wei Tang, Hiroshi Takeshima, Susan L. Hamilton, and Eric Klann. "Superoxide-Induced Potentiation in the Hippocampus Requires Activation of Ryanodine Receptor Type 3 and ERK." Journal of Neurophysiology 99, no. 3 (2008): 1565–71. http://dx.doi.org/10.1152/jn.00659.2007.

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Reactive oxygen species (ROS) are required for the induction of long-term potentiation (LTP) and behave as signaling molecules via redox modifications of target proteins. In particular, superoxide is necessary for induction of LTP, and application of superoxide to hippocampal slices is sufficient to induce LTP in area CA1. Although a rise in postsynaptic intracellular calcium is necessary for LTP induction, superoxide-induced potentiation does not require calcium flux through N-methyl-d-aspartate (NMDA) receptors. Ryanodine receptors (RyRs) mediate calcium-induced calcium release from intracel

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Iacomino, Nicola, Letizia Scandiffio, Fabio Conforti, et al. "Muscle and Muscle-like Autoantigen Expression in Myasthenia Gravis Thymus: Possible Molecular Hint for Autosensitization." Biomedicines 11, no. 3 (2023): 732. http://dx.doi.org/10.3390/biomedicines11030732.

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The thymus is widely recognized as an immunological niche where autoimmunity against the acetylcholine receptor (AChR) develops in myasthenia gravis (MG) patients, who mostly present thymic hyperplasia and thymoma. Thymoma-associated MG is frequently characterized by autoantibodies to the muscular ryanodine receptor 1 (RYR1) and titin (TTN), along with anti-AChR antibodies. By real-time PCR, we analyzed muscle—CHRNA1, RYR1, and TTN—and muscle-like—NEFM, RYR3 and HSP60—autoantigen gene expression in MG thymuses with hyperplasia and thymoma, normal thymuses and non-MG thymomas, to check for mole

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Thorne, George D., and Richard J. Paul. "Effects of organ culture on arterial gene expression and hypoxic relaxation: role of the ryanodine receptor." American Journal of Physiology-Cell Physiology 284, no. 4 (2003): C999—C1005. http://dx.doi.org/10.1152/ajpcell.00158.2002.

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Organ culture specifically inhibits vasorelaxation to acute hypoxia and preferentially decreases specific voltage-dependent K+channel expression over other K+ and Ca2+channel subtypes. To isolate further potential oxygen-sensing mechanisms correlated with altered gene expression, we performed differential display analysis on RNA isolated from control and cultured coronary arterial rings. We hypothesize that organ culture results in altered gene expression important for vascular smooth muscle contractility important to the mechanism of hypoxia-induced relaxation. Our results indicate a milieu o

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Dahan, Diana, Thomas Ducret, Jean-François Quignard, Roger Marthan, Jean-Pierre Savineau, and Eric Estève. "Implication of the ryanodine receptor in TRPV4-induced calcium response in pulmonary arterial smooth muscle cells from normoxic and chronically hypoxic rats." American Journal of Physiology-Lung Cellular and Molecular Physiology 303, no. 9 (2012): L824—L833. http://dx.doi.org/10.1152/ajplung.00244.2011.

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There is a growing body of evidence indicating that transient receptor potential (TRP) channels are implicated in calcium signaling and various cellular functions in the pulmonary vasculature. The aim of this study was to investigate the expression, functional role, and coupling to reticulum calcium channels of the type 4 vanilloid TRP subfamily (TRPV4) in the pulmonary artery from both normoxic (Nx) and chronically hypoxic (CH) rats. Activation of TRPV4 with the specific agonist 4α-phorbol-12,13-didecanoate (4α-PDD, 5 μM) increased the intracellular calcium concentration ([Ca2+]i). This effec

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Zahradníková, Alexandra, Jana Pavelková, Miroslav Sabo, Sefer Baday, and Ivan Zahradník. "Structure-based mechanism of RyR channel operation by calcium and magnesium ions." PLOS Computational Biology 21, no. 4 (2025): e1012950. https://doi.org/10.1371/journal.pcbi.1012950.

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Ryanodine receptors (RyRs) serve for excitation-contraction coupling in skeletal and cardiac muscle cells in a noticeably different way, not fully understood at the molecular level. We addressed the structure of skeletal (RyR1) and cardiac (RyR2) isoforms relevant to gating by Ca2+ and Mg2+ ions (M2+). Bioinformatics analysis of RyR structures ascertained the EF-hand loops as the M2+ binding inhibition site and revealed its allosteric coupling to the channel gate. The intra-monomeric inactivation pathway interacts with the Ca2+-activation pathway in both RyR isoforms, and the inter-monomeric p

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Frank, Daniel F., Galen W. Miller, Richard E. Connon, Juergen Geist, and Pamela J. Lein. "Transcriptomic profiling of mTOR and ryanodine receptor signaling molecules in developing zebrafish in the absence and presence of PCB 95." PeerJ 5 (November 29, 2017): e4106. http://dx.doi.org/10.7717/peerj.4106.

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The mechanistic target of rapamycin (mTOR) and ryanodine receptor (RyR) signaling pathways regulate fundamental processes of neurodevelopment, and genetic mutations within these pathways have been linked to neurodevelopmental disorders. While previous studies have established that these signaling molecules are expressed in developing zebrafish, a detailed characterization of the ontogenetic profile of these signaling molecules is lacking. Thus, we evaluated the spatiotemporal expression of key transcripts in mTOR and RyR signaling pathways in wildtype zebrafish at 24, 72 and 120 hours post fer

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Hoyer, Joachim, Meike Kuehn, Christiane Degenhardt, et al. "Expression of Ryanodine Receptor 3 and Trp Channels in Endothelium of Human Mesenteric Artery: A Single-Cell Rt-Pcr and Patch-Clamp Analysis in Situ ." Hypertension 36, suppl_1 (2000): 719. http://dx.doi.org/10.1161/hyp.36.suppl_1.719-d.

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P146 Ca 2+ mobilization plays an important role in endothelial function by stimulating Ca 2+ -dependent synthesis of vasodilating factors. In addition to InsP 3 - mediated Ca 2+ store depletion, Ca 2+ release from ryanodine-sensitive pools and Ca 2+ -influx through cation channels of the TRP-gene family have been suggested to be involved in endothelial Ca 2+ signaling. In cultured endothelial cells (EC) the function and expression of ryanodine-receptors (RyR) and TRP channels might differ substantially from those in native endothelium of human blood vessels. We, therefore, characterized expres

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Savoia, Carlo P., Qing-Hua Liu, Yun-Min Zheng, et al. "Calcineurin upregulates local Ca2+ signaling through ryanodine receptor-1 in airway smooth muscle cells." American Journal of Physiology-Lung Cellular and Molecular Physiology 307, no. 10 (2014): L781—L790. http://dx.doi.org/10.1152/ajplung.00149.2014.

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Local Ca2+ signals (Ca2+ sparks) play an important role in multiple cellular functions in airway smooth muscle cells (ASMCs). Protein kinase Cϵ is known to downregulate ASMC Ca2+ sparks and contraction; however, no complementary phosphatase has been shown to produce opposite effects. Here, we for the first time report that treatment with a specific calcineurin (CaN) autoinhibitory peptide (CAIP) to block CaN activity decreases, whereas application of nickel to activate CaN increases, Ca2+ sparks in both the presence and absence of extracellular Ca2+. Treatment with xestospogin-C to eliminate f

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Ooashi, Noriko, Akira Futatsugi, Fumie Yoshihara, Katsuhiko Mikoshiba, and Hiroyuki Kamiguchi. "Cell adhesion molecules regulate Ca2+-mediated steering of growth cones via cyclic AMP and ryanodine receptor type 3." Journal of Cell Biology 170, no. 7 (2005): 1159–67. http://dx.doi.org/10.1083/jcb.200503157.

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Axonal growth cones migrate along the correct paths during development, not only directed by guidance cues but also contacted by local environment via cell adhesion molecules (CAMs). Asymmetric Ca2+ elevations in the growth cone cytosol induce both attractive and repulsive turning in response to the guidance cues (Zheng, J.Q. 2000. Nature. 403:89–93; Henley, J.R., K.H. Huang, D. Wang, and M.M. Poo. 2004. Neuron. 44:909–916). Here, we show that CAMs regulate the activity of ryanodine receptor type 3 (RyR3) via cAMP and protein kinase A in dorsal root ganglion neurons. The activated RyR3 mediate

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Torres, Rodrigo F., and Bredford Kerr. "Spatial Learning Is Associated with Antagonist Outcomes for DNA Methylation and DNA Hydroxymethylation in the Transcriptional Regulation of the Ryanodine Receptor 3." Neural Plasticity 2021 (August 11, 2021): 1–8. http://dx.doi.org/10.1155/2021/9930962.

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Increasing attention has been drawn to the role that intracellular calcium stores play in neuronal function. Ryr3 is an intracellular calcium channel that contributes to hippocampal long-term potentiation, dendritic spine function, and higher cognitive processes. Interestingly, stimuli that increase neuronal activity upregulate the transcriptional activity of Ryr3 and augment DNA methylation in its proximal promoter. However, if these observations are valid for complex behavioral tasks such as learning and memory remains being evaluated. Relative expression analysis revealed that spatial learn

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MOUTON, Jérôme, Isabelle MARTY, Michel VILLAZ, Anne FELTZ, and Yves MAULET. "Molecular interaction of dihydropyridine receptors with type-1 ryanodine receptors in rat brain." Biochemical Journal 354, no. 3 (2001): 597–603. http://dx.doi.org/10.1042/bj3540597.

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In striated muscles, Ca2+ release from internal stores through ryanodine receptor (RyR) channels is triggered by functional coupling to voltage-activated Ca2+ channels known as dihydropyridine receptors (DHPRs) located in the plasma membrane. In skeletal muscle, this occurs by a direct conformational link between the tissue-specific DHPR (Cav1.1) and RyR1, whereas in the heart the signal is carried from the cardiac-type DHPR (Cav1.2) to RyR2 by calcium ions acting as an activator. Subtypes of both channels are expressed in the central nervous system, but their functions and mechanisms of coupl

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Yang, Dongmei, Zui Pan, Hiroshi Takeshima, et al. "RyR3 Amplifies RyR1-mediated Ca2+-induced Ca2+Release in Neonatal Mammalian Skeletal Muscle." Journal of Biological Chemistry 276, no. 43 (2001): 40210–14. http://dx.doi.org/10.1074/jbc.m106944200.

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