Carbonic anhydrase inhibition and calcium transients in soleus fibers

We simultaneously measured cytoplasmic Ca2+ transients using Fura-2 and isometric force in rat soleus fiber bundles. In the presence of the carbonic anhydrase inhibitor, chlorzolamide, we observed a decreased amplitude and retarded decay of the Ca2+ signal. This corresponded with a decreased isometric force and a retarded muscle relaxation. We conclude that muscle carbonic anhydrase participates in excitation-contraction coupling, possibly by rapidly providing protons that are exchanged for Ca2+ across the sarcoplasmic reticulum membrane.