Age-related changes of physiological and biochemical properties were examined in the diaphragm muscle, which has particularly high activation compared to that of other skeletal muscles. The diaphragm from 10-week-, 50-week- and 100-week-old male Wistar rats were used to measure in vitro isometric contractile properties, sarcoplasmic reticulum (SR) Ca2+-ATPase activity, and myosin heavy chain (MHC) isoform composition. Although there were no significant differences in specific twitch tension of the diaphragm among the groups, there was significant reduction in specific tetanic tension in the 50-week to 100-week groups. The contraction time and 1/2 relaxation time of twitch contraction extended with aging, and significant differences were found between 10-week-old and 100-week-old diaphragms. Regarding the activity of SR Ca2+-ATPase, the pattern of age-related change was similar to that in the 1/2 relaxation time and there was a significant difference between 10-week-old and 100-week-old diaphragms. There was a significant increase in the relative composition of the MHC I isoform in 100-week-diaphragms compared to that in 10-week-old diaphragms and a concomitant decrease in the relative composition of fast myosin was noted. These findings demonstrated that older diaphragms have slower contraction and relaxation speeds, and these alterations were attributed to changes in SR Ca2+-ATPase activity and MHC isoform composition.
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