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J Appl Physiol 96: 1776-1781, 2004; doi:10.1152/japplphysiol.00795.2002
8750-7587/04 $5.00
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Endurance exercise training inhibits activity of plasma GOT and liver caspase-3 of rats exposed to stress by induction of heat shock protein 70

Toshio Mikami,1 Satoshi Sumida,2 Yoshitomo Ishibashi,3 and Shigeo Ohta3

1Department of Health and Sports Science, Nippon Medical School, Kawasaki, Kanagawa 211-0063; 2Laboratory of Exercise Physiology and Biochemistry, Osaka Gakuin University, Suita, Osaka 564-8511; and 3Department of Biochemistry and Cell Biology, Institute of Gerontology, Nippon Medical School, Kawasaki, Kanagawa 211-8533, Japan

Submitted 30 August 2002 ; accepted in final form 8 October 2003

A single bout of exercise increases production of heat shock protein 70 (HSP70), which protects cells against various stresses. In this study, we investigated whether endurance exercise training enhances liver level of HSP70 and, if so, whether HSP70 contributes to hepatic protection against stress in vivo. Mice of an exercise-training group performed 60 min of treadmill running 5 days/wk for 4 wk. The resting level of liver HSP70 was 4.5 times higher in the trained than in sedentary mice. After 4 wk of exercise training, both groups of mice were exposed to the following stresses: 1) heat stress, 2) cold stress, 3) oxidative stress, 4) ethanol stress, and 5) exercise stress by compelling the mice to run on a treadmill until exhausted. After exposure to the stresses, the liver was immediately isolated. Elevation of liver HSP70 in the trained mice was evident, whereas no elevation was found in the sedentary mice. On exposure to heat, diethyldithiocarbamate and ethanol, activities of glutanic oxalacetic transaminase in plasma, and liver caspase-3, a key enzyme of apoptotic processing, were elevated in the sedentary mice but not in the trained mice. These results suggest that exercise training enhanced the resting level of liver HSP70 and hepatic protection against various stresses, at least partly attributing to the suppression of caspase-3 activity by the increase in HSP70.

glutanic oxalacetic transaminase



Address for reprint requests and other correspondence: T. Mikami, Dept. of Health and Sports Science, Nippon Medical School, 2-297-2 Kosugi-cho, Nakahara-ku, Kawasaki, Kanagawa 211-0063, Japan (E-mail: mikami{at}nms.ac.jp).







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