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Departments of 1 Physiology and 2 Pediatrics, Nagoya City University Medical School, Mizuho-ku, Nagoya 467, Japan; and 3 Department of Veterinary Bioscience, Ohio State University, Columbus, Ohio 43210
The mechanism underlying H2O2-induced activation of frog skeletal muscle ryanodine receptors was studied using skinned fibers and by measuring single Ca2+-release channel current. Exposure of skinned fibers to 3-10 mM H2O2 elicited spontaneous contractures. H2O2 at 1 mM potentiated caffeine contracture. When the Ca2+-release channels were incorporated into lipid bilayers, open probability (Po) and open time constants were increased on intraluminal addition of H2O2 in the presence of cis catalase, but unitary conductance and reversal potential were not affected. Exposure to cis H2O2 at 1.5 mM failed to activate the channel in the presence of trans catalase. Application of 1.5 mM H2O2 to the trans side of a channel that had been oxidized by cis p-chloromercuriphenylsulfonic acid (pCMPS; 50 µM) still led to an increase in Po, comparable to that elicited by trans 1.5 mM H2O2 without pCMPS. Addition of cis pCMPS to channels that had been treated with or without trans H2O2 rapidly resulted in high Po followed by closure of the channel. These results suggest that oxidation of luminal sulfhydryls in the Ca2+-release channel may contribute to H2O2-induced channel activation and muscle contracture.
frog skeletal muscle; calcium-release channel; sulfhydryl oxidation; p-chloromercuriphenylsulfonic acid
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