Literature DB >> 2776080

Inhibition of carbonic anhydrases in type I muscle fibers influences contractility.

C Côté1, D Tremblay, H Riverin, P Frémont, P A Rogers.   

Abstract

We tested the effects of inhibiting the carbonic anhydrase activity of rat soleus and extensor digitorum longus muscles on the isometric contractile properties and the resistance to fatigue. SOL and EDL muscles from female rats were incubated in vitro in the presence of methazolamide, a specific inhibitor of carbonic anhydrase, before determining their contractile properties. Methazolamide had no effects on the contractile properties of the soleus muscle (10(-5) or 10(-3) M) and extensor digitorum longus (10(-3) M), except for the half-relaxation time of the soleus muscle which increased significantly. Values for half-relaxation time were significantly increased with both concentrations of the inhibitor. Muscles were then submitted to a fatigue protocol lasting 30 min. During the fatigue test, no significant difference was observed between control and 10(-5) M methazolamide soleus muscles. In presence of 10(-3) M methazolamide however, the soleus muscle showed a significantly increased resistance to fatigue compared with control preparations. No significant effect was observed with the extensor digitorum longus muscle exposed to 10(-3) M methazolamide. Results are discussed in terms of the presence of two different isoforms of carbonic anhydrase that may be associated with calcium uptake and energy metabolic processes, respectively.

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Year:  1989        PMID: 2776080     DOI: 10.1139/y89-103

Source DB:  PubMed          Journal:  Can J Physiol Pharmacol        ISSN: 0008-4212            Impact factor:   2.273


  1 in total

1.  Acetazolamide-insensitive carbonic anhydrase activities in liver and tonic skeletal muscle of adult male rats with streptozotocin-induced diabetes mellitus.

Authors:  J B Moynihan; S Ennis
Journal:  Biochem J       Date:  1990-12-01       Impact factor: 3.857

  1 in total

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