Abstract
In skeletal muscle, halothane affects the functions of several Ca 2+-regulatory membrane proteins involved in the excitation–contraction–relaxation cycle. To investigate the mechanism by which this volatile anesthetic interferes with Ca 2+-homeostasis, we studied potential changes in protein–protein interactions by halothane. Using comparative immunoblotting of microsomal muscle proteins separated on native and denaturing gels, we show here that halothane induces oligomerization of the terminal cisternae Ca 2+-binding protein calsequestrin, the junctional ryanodine receptor Ca 2+-release channel and the transverse-tubular α 1-dihydropyridine receptor. This agrees with previous reports on the modulation of Ca 2+-release activity by halothane since interactions between the voltage-sensing α 1-dihydropyridine receptor, the ryanodine receptor and the luminal Ca 2+-reservoir might result in a rapid release of Ca 2+-ions. Furthermore, this study supports the idea that specific protein sites are involved in the action of inhalational anesthetics and that halothane might trigger abnormal Ca 2+-homeostasis in malignant hyperthermia via oligomerization of the mutated ryanodine receptor.
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