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1 Department of Internal Medicine, Pulmonary and Critical Care Medicine, 2 Biophysics Program, and 3 Departments of Anesthesiology, 4 Medical Biochemistry, and 5 Chemistry, Ohio State University, Columbus, Ohio 43210
Skeletal
muscles are exposed to increased temperatures during intense exercise,
particularly in high environmental temperatures. We hypothesized that
heat may directly stimulate the reactive oxygen species (ROS) formation
in diaphragm (one kind of skeletal muscle) and thus potentially play a
role in contractile and metabolic activity. Laser scan confocal
microscopy was used to study the conversion of hydroethidine (a probe
for intracellular ROS) to ethidium (ET) in mouse diaphragm. During a
30-min period, heat (42°C) increased ET fluorescence by 24 ± 4%, whereas in control (37°C), fluorescence decreased by 8 ± 1% compared with baseline (P < 0.001). The superoxide
scavenger Tiron (10 mM) abolished the rise in intracellular
fluorescence, whereas extracellular superoxide dismutase (SOD; 5,000 U/ml) had no significant effect. Reduction of oxidized cytochrome
c was used to detect extracellular ROS in rat diaphragm.
After 45 min, 53 ± 7 nmol cytochrome c · g dry
wt
1 · ml1 were reduced in heat
compared with 22 ± 13 nmol · g1 · ml1 in controls
(P < 0.001). SOD decreased cytochrome c
reduction in heat to control levels. The results suggest that heat
stress stimulates intracellular and extracellular superoxide
production, which may contribute to the physiological responses to
severe exercise or the pathology of heat shock.
cytochrome c; ethidium; laser scan confocal fluorescence imaging; exercise
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