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Am J Physiol Cell Physiol 279: C1366-C1374, 2000;
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Vol. 279, Issue 5, C1366-C1374, November 2000

H2O2 and ethanol act synergistically to gate ryanodine receptor/calcium-release channel

Toshiharu Oba1, Tatsuya Ishikawa2, Takashi Murayama3, Yasuo Ogawa3, and Mamoru Yamaguchi4

Departments of 1 Physiology and 2 Pediatrics, Nagoya City University Medical School, Nagoya 467-8601; 3 Department of Pharmacology, Juntendo University School of Medicine, Tokyo 113-8421, Japan; and 4 Department of Veterinary Biosciences, College of Veterinary Medicine, The Ohio State University, Columbus, Ohio 43210

We examined the effect of low concentrations of H2O2 on the Ca2+-release channel/ryanodine receptor (RyR) to determine if H2O2 plays a physiological role in skeletal muscle function. Sarcoplasmic reticulum vesicles from frog skeletal muscle and type 1 RyRs (RyR1) purified from rabbit skeletal muscle were incorporated into lipid bilayers. Channel activity of the frog RyR was not affected by application of 4.4 mM (0.02%) ethanol. Open probability (Po) of such ethanol-treated RyR channels was markedly increased on subsequent addition of 10 µM H2O2. Increase of H2O2 to 100 µM caused a further increase in channel activity. Application of 4.4 mM ethanol to 10 µM H2O2-treated RyRs activated channel activity. Exposure to 10 or 100 µM H2O2 alone, however, failed to increase Po. Synergistic action of ethanol and H2O2 was also observed on the purified RyR1 channel, which was free from FK506 binding protein (FKBP12). H2O2 at 100-500 µM had no effect on purified channel activity. Application of FKBP12 to the purified RyR1 drastically decreased channel activity but did not alter the effects of ethanol and H2O2. These results suggest that H2O2 may play a pathophysiological, but probably not a physiological, role by directly acting on skeletal muscle RyRs in the presence of ethanol.

12-kiloDalton FK506-binding protein; skeletal muscle sarcoplasmic reticulum; acetaldehyde; single-channel current


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