Aldolase potentiates DIDS activation of the ryanodine receptor in rabbit skeletal sarcoplasmic reticulum

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Aldolase potentiates DIDS activation of the ryanodine receptor in rabbit skeletal sarcoplasmic reticulum.

DIDS (4,4'-di-isothiocyanostilbene-2,2'-disulfonate), an anion channel blocker, triggers Ca2+ release from skeletal muscle SR (sarcoplasmic reticulum). The present study characterized the effects of DIDS on rabbit skeletal single Ca2+-release channel/RyR1 (ryanodine receptor type 1) incorporated into a planar lipid bilayer. When junctional SR vesicles were used for channel incorporation (native...

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The ryanodine receptor of rabbit skeletal muscle sarcoplasmic reticulum was purified as a single 450,000-dalton polypeptide from CHAPS-solubilized triads using immunoaffinity chromatography. The purified receptor had a [3H]ryanodine-binding capacity (Bmax) of 490 pmol/mg and a binding affinity (Kd) of 7.0 nM. Using planar bilayer recording techniques, we show that the purified receptor forms ca...

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Abnormal sarcoplasmic reticulum ryanodine receptor in malignant hyperthermia.

Previous studies have demonstrated that skeletal muscle from individuals susceptible to malignant hyperthermia (MH) has a defect associated with the mechanism of calcium release from its intracellular storage sites in the sarcoplasmic reticulum (SR). In this report we demonstrate that the [3H]ryanodine receptor of isolated MH-susceptible (MHS) porcine heavy SR exhibits an altered Ca2+ dependenc...

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Introduction Cardiac myocyte contraction is driven by the coordinated release of Ca from the sarcoplasmic reticulum (SR). This release of Ca occurs through the cardiac RyR2. Physiologically, Ca release occurs in response to an influx of Ca through L-type Ca channels, via a mechanism termed CICR. This transient increase in cytosolic Ca activates the RyR2 channel as a result of Ca binding to the ...

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ژورنال

عنوان ژورنال: Biochemical Journal

سال: 2006

ISSN: 0264-6021,1470-8728

DOI: 10.1042/bj20060701