Hypernitrosylated ryanodine receptor calcium release channels are leaky in dystrophic muscle [PDF]
Duchenne muscular dystrophy is characterized by progressive muscle weakness and early death resulting from dystrophin deficiency. Loss of dystrophin results in disruption of a large dystrophin glycoprotein complex, leading to pathological calcium (Ca2+)-dependent signals that damage muscle cells. We have identified a structural and functional defect in
Andrew M. Bellinger +8 more
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Nitric oxide-induced calcium release: activation of type 1 ryanodine receptor, a calcium release channel, through non-enzymatic posttranslational modification by nitric oxide [PDF]
Nitric oxide (NO) is a typical gaseous messenger involved in a wide range of biological processes. In our classical knowledge, effects of NO are largely achieved by activation of soluble guanylyl cyclase to form cyclic guanosine-3’, 5’-monophosphate ...
Sho eKakizawa
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Calsequestrin Is an Inhibitor of Skeletal Muscle Ryanodine Receptor Calcium Release Channels [PDF]
We provide novel evidence that the sarcoplasmic reticulum calcium binding protein, calsequestrin, inhibits native ryanodine receptor calcium release channel activity. Calsequestrin dissociation from junctional face membrane was achieved by increasing luminal (trans) ionic strength from 250 to 500 mM with CsCl or by exposing the luminal side of ...
Nicole A. Beard +3 more
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Calmodulin Binding and Inhibition of Cardiac Muscle Calcium Release Channel (Ryanodine Receptor) [PDF]
Metabolically (35)S-labeled calmodulin (CaM) was used to determine the CaM binding properties of the cardiac ryanodine receptor (RyR2) and to identify potential channel domains for CaM binding. In addition, regulation of RyR2 by CaM was assessed in [(3)H]ryanodine binding and single-channel measurements.
David M. Balshaw +4 more
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SH Oxidation Stimulates Calcium Release Channels (Ryanodine Receptors) From Excitable Cells
The effects of redox reagents on the activity of the intracellular calcium release channels (ryanodine receptors) of skeletal and cardiac muscle, or brain cortex neurons, was examined. In lipid bilayer experiments, oxidizing agents (2,2'-dithiodipyridine or thimerosal) modified the calcium dependence of all single channels studied.
Cecilia Hidalgo +4 more
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Structural and Functional Regulation of RyR2 in Cardiac Calcium Handling and Arrhythmogenesis [PDF]
Cardiac Ca2+ handling is critical for excitation–contraction coupling (ECC), with the ryanodine receptor type 2 (RyR2) serving as the key sarcoplasmic reticulum (SR) Ca2+ release channel in cardiomyocytes.
Kaiyang Gao +11 more
doaj +2 more sources
Caffeine Analogs: Effects on Ryanodine-Sensitive Calcium-Release Channels and GABAA Receptors
1. Caffeine at 0.3-10 mM enhanced the binding of [3H]ryanodine to calcium-release channels of rabbit muscle sarcoplasmic reticulum. A variety of other xanthines were as efficacious as caffeine or nearly so, but none appeared markedly more potent. 2. Caffeine at 1 mM markedly inhibited binding of [3H]diazepam to GABAA receptors in rat cerebral cortical ...
Dan Shi +2 more
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Intracellular Calcium Release Channels Mediate Their Own Countercurrent: The Ryanodine Receptor Case Study [PDF]
Intracellular calcium release channels like ryanodine receptors (RyRs) and inositol trisphosphate receptors (IP(3)Rs) mediate large Ca(2+) release events from Ca(2+) storage organelles lasting >5 ms. To have such long-lasting Ca(2+) efflux, a countercurrent of other ions is necessary to prevent the membrane potential from becoming the Ca(2+) Nernst ...
Dirk Gillespie, Michael Fill
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Primary structure and distribution of a novel ryanodine receptor/calcium release channel from rabbit brain [PDF]
Yoji Hakamata +3 more
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FK506 binding protein associated with the calcium release channel (ryanodine receptor).
The calcium release channel (CRC)/ryanodine receptor (RyRec) has been identified as the foot structure of the sarcoplasmic reticulum (SR) and provides the pathway for calcium efflux required for excitation-contraction coupling in skeletal muscle. The CRC has previously been reported to consist of four identical 565-kDa protomers.
T Jayaraman +6 more
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