Interdependence of ryanodine binding, oligomeric receptor interactions, and Ca2+ release regulation in junctional sarcoplasmic reticulum☆
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Structural Basis for Gating and Activation of RyR1
2016, CellCitation Excerpt :Increased ryanoid concentrations (∼100 μM) lock the channel in a non-conducting state (Zimányi et al., 1992). RyRs possess one high-affinity ryanodine-binding site per tetramer, and up to three lower-affinity sites (Carroll et al., 1991). Several lines of evidence suggest that the high-affinity ryanodine-binding site is located within the transmembrane pore of the channel.
Inhibitory ryanodine prevents ryanodine receptor-mediated Ca<sup>2+</sup> release without affecting endoplasmic reticulum Ca<sup>2+</sup> content in primary hippocampal neurons
2015, Biochemical and Biophysical Research CommunicationsCitation Excerpt :Mounting evidence also points to a significant role of RyR-mediated Ca2+ release on normal [7,8] and pathological neuronal function [5,9]. Ryanodine is a cell permeant plant alkaloid [10] that binds selectively and with high affinity to the RyR channel protein but dissociates very slowly once bound [11]. These binding properties allowed the initial identification of the RyR protein (reviewed in Ref. [12]).
RyR1 S-Nitrosylation Underlies Environmental Heat Stroke and Sudden Death in Y522S RyR1 Knockin Mice
2008, CellCitation Excerpt :The previously described binding assays were performed at room temperature. RyR1 is, however, not stable for extended periods of time at higher temperatures (Carroll et al., 1991), making equilibrium binding studies at physiologic temperatures difficult. To circumvent this problem, we assessed the rate of association of [3H] ryanodine to skeletal muscle membranes from RyR1Y522S/wt and RyR1wt/wt mice at different temperatures and in the presence or absence of either DTT or AA.
Effects of quercetin on single Ca<sup>2+</sup> release channel behavior of skeletal muscle
2002, Biophysical JournalCitation Excerpt :An analysis of Po and the gating mode of single CRC showed that the mean open-time and closed-time constants (τo and τc) and their proportions were significantly different for the caffeine- and quercetin-activated CRCs, even though Po values were similar (Table 2). Ryanodine binding to its high-affinity site(s) stabilizes the open state of CRC, however, open channel conductance is subnormal (Rousseau et al., 1987; Carroll et al., 1991; Pessah and Zimanyi, 1991; Buck et al., 1992). The I-V relations in Fig. 3 D show that the conductances and levels of subconductance state formed by 10 μM ryanodine were similar in all cases (Fig. 3), suggesting that quercetin does not modify the ion selectivity of the CRC.
The structure, function, and cellular regulation of ryanodine-sensitive Ca<sup>2+</sup> release channels
1998, International Review of Cytology
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This work was supported by grants from the National Institutes of Health (HL-27867) and the Muscular Dystrophy Association.