Abstract
Publisher Summary This chapter describes the isolation of the Ca 2+ release channel from heart and skeletal muscle sarcoplasmic reticulum (SR). Significant progress has been made in the past several years with regard to characterizing the Ca 2+ release machinery of SR from both skeletal muscle and heart. (1) Junctional terminal cisternae of sarcoplasmic reticulum have been isolated and characterized. (2) Ca 2+ permeability in terminal cisternae was found to be modulated by ryanodine in pharmacologically significant concentrations. (3) Ryanodine binding in the same concentration range has been localized to the terminal cisternae of SR. (4) The ryanodine receptor has been isolated and found to be equivalent to the feet structures of the junctional terminal cisternae. (5) SR vesicles have been fused into black lipid films and found to contain Ca 2+ channels. These channels have characteristics of the Ca 2+ release observed in vesicles. (6) Ryanodine has been found to modulate the channel in the bilayer—thereby, reinforcing its role in the Ca 2+ release process. (7) The ryanodine receptor incorporated into a bilayer has the Ca 2+ channel characteristics, consistent with calcium release observed in isolated terminal cisternae. The purification procedure of the ryanodine receptor from JTC of skeletal muscle SR is summarized in the chapter. Ryanodine binding is localized to the JTC of SR both in heart and skeletal muscle.
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