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The calcium-ryanodine receptor complex of skeletal and cardiac muscle
Authors:I N Pessah  A L Waterhouse  J E Casida
Affiliation:1. Neurophysiology Research Center, Urmia University of Medical Sciences, Urmia, Iran;2. Department of Physiology, Faculty of Medicine, Urmia University of Medical Sciences, Urmia, Iran;3. Cellular and Molecular Research Center, Urmia University of Medical Sciences, Urmia, Iran;4. Physiology Research Center, Department of Physiology, School of Medicine, Iran University of Medical Sciences, Tehran, Iran;1. Laboratory of Pharmacology, Department of Physics and Chemistry, School of Pharmaceutical Sciences of Ribeirão Preto, University of São Paulo, Ribeirão Preto, SP, Brazil;2. Department of Pharmacology, School of Medicine of Ribeirão Preto, University of São Paulo, Ribeirão Preto, SP, Brazil;3. Center for Interdisciplinary Research on Applied Neurosciences (NAPNA), University of São Paulo, SP, Brazil
Abstract:[3H]Ryanodine binds with high affinity to saturable and Ca2+-dependent sites in heavy sarcoplasmic reticulum (SR) preparations from rabbit skeletal and cardiac muscle. Ruthenium red, known to interfere with Ca2+-induced Ca2+ release from SR vesicles, inhibits [3H]ryanodine specific binding in both skeletal and cardiac preparations whereas Mg2+, Ba2+, Cd2+ and La3+ selectively inhibit the skeletal preparation. The toxicological relevance of the [3H]ryanodine binding site is established by the correlation of binding inhibition with toxicity for seven ryanoids including two botanical insecticides. These findings provide direct evidence for Ca2+-ryanodine receptor complexes that may play a role in excitation-contraction coupling.
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