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Am J Physiol Cell Physiol 285: C215-C221, 2003. First published March 19, 2003; doi:10.1152/ajpcell.00034.2002
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RECEPTORS AND SIGNAL TRANSDUCTION

Skeletal muscle sarcoplasmic reticulum contains a NADH-dependent oxidase that generates superoxide

Ruohong Xia,1,2 Jason A. Webb,1 Lisa L. M. Gnall,3 Kerry Cutler,1 and Jonathan J. Abramson1

Departments of 1Physics and 3Biology, Portland State University, Portland, Oregon 97207; and 2Department of Physics, Eastern China Normal University, Shanghai 200062, China

Submitted 22 January 2002 ; accepted in final form 11 March 2003

Skeletal muscle sarcoplasmic reticulum (SR) is shown to contain an NADH-dependent oxidase (NOX) that reduces molecular oxygen to generate superoxide. Its activity is coupled to an activation of the Ca2+ release mechanism, as evident by stimulation in the rate of high-affinity ryanodine binding. NOX activity, coupled to the production of superoxide, is not derived from the mitochondria but is SR in origin. The SR preparation also contains a significant NADH oxidase activity, which is not coupled to the production of superoxide and appears to be mitochondrial in origin. This mitochondrial component is preferentially associated with the terminal cisternae region of the SR. Its activity is inhibited by diphenylene iodonium (10 µM), antimycin A (200 nM), and rotenone (40 nM) but is not coupled to the generation of superoxide or the stimulation of the ryanodine receptor. The rate of superoxide production per milligram of protein is larger in SR than in mitochondria. This NOX may be a major source of oxidative stress in muscle.

NADH-dependent superoxide production; ryanodine receptor; oxidative stress; sarcoplasmic reticulum


Address for reprint requests and other correspondence: J. Abramson, Physics Dept., Portland State Univ., P.O. Box 751, Portland, OR 97207 (E-mail: abramsonj{at}pdx.edu).




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