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Carbonic anhydrase inhibition and calcium transients in soleus fibers
Author(s) -
Wetzel P.,
Liebner T.,
Gros G.
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)80289-u
Subject(s) - isometric exercise , carbonic anhydrase , biophysics , chemistry , soleus muscle , calcium , endoplasmic reticulum , cytoplasm , skeletal muscle fibers , biochemistry , skeletal muscle , anatomy , enzyme , medicine , biology , organic chemistry
We simultaneously measured cytoplasmic Ca 2+ 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 Ca 2+ 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 Ca 2+ across the sarcoplasmic reticulum membrane.