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AJP - Regulatory, Integrative and Comparative Physiology, Vol 260, Issue 3 615-R621, Copyright © 1991 by American Physiological Society
ARTICLES |
P. Fremont, H. Riverin, J. Frenette, P. A. Rogers and C. Cote
Muscle Biology Research Group, Laval University, Ste-Foy, Quebec, Canada.
Carbonic anhydrase III (CA III; EC 4.2.1.1) is the most abundant cytosolic enzyme in type I skeletal muscle fibers. Methazolamide, a specific CA inhibitor, was used to characterize the effects of inhibiting CA III on the resistance to fatigue and recovery of the rat soleus muscle using a 60-min fatigue protocol performed in vitro at 25 degrees C. Incubation with 10(-3) M methazolamide resulted in a smaller decrease in tension production during the fatigue protocol, thereby increasing the total tension-time integral for the fatigue test. However, the rate and extent of recovery after the test were lower in the experimental group compared with the control group. A similar effect was observed at physiological temperature (35 degrees C). The results indicate that inhibition of CA III significantly influences tension production as early as 30 s into the stimulation protocol. Inhibition of CA III only during the recovery period did not influence the recovery profile, thereby indicating that the impaired recovery was related to the presence of methazolamide during the stimulation period.
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