Saturation of calcium channels in single isolated smooth muscle cells of guinea-pig taenia caeci.

1. Calcium channel currents were recorded in Cs+-dialysed voltage-clamped single smooth muscle cells isolated from the guinea-pig taenia caeci to evaluate the current-carrying ability of Ca2+, Ba2+, Sr2+ and Mg2+ ions. 2. Ba2+ and Sr2+ ions, as well as Ca2+ ions, were able to carry an inward current through calcium channels. Calcium channel current was not observed when Mg2+ was the only divalent cation in the external solution. 3. Concentration dependences of calcium (ICa), barium (IBa) and strontium (ISr) currents were studied. It was found that currents through calcium channels saturated with increasing the extracellular concentration of a current carrier. Saturation of each current can be fitted with a Langmuir curve with apparent dissociation constants of 1.2 mM for Ca2+, 1.8 mM for Sr2+ and 9.6 mM for Ba2+ ions. 4. External Mg2+ ions reduced both ICa and IBa.IBa was depressed to a greater extent than ICa by Mg2+ ions. Reduction of ICa by Mg2+ ions seems to agree with competitive antagonism between Ca2+ and Mg2+ ions (Hagiwara & Takahashi, 1967). 5. When the external divalent cation concentration [( C2+]o) was changed, the current-voltage relationship of currents through calcium channels was shifted along the potential axis suggesting that activation gating of calcium channels was affected by [C2+]o. These voltage shifts can be fitted with the Gouy-Chapman theory supposing the density of surface charges near calcium channels to be 0.5 e nm-2 and including more potent binding of Ca2+ ions to surface charges than of Ba2+, Sr2+ and Mg2+ ions. 6. The changes in the Ca2+, Ba2+ and Sr2+ concentrations at the surface of the membrane were calculated. It was found that saturation of IBa can be explained by saturation of Ba2+ surface concentration while saturation of ICa and ISr cannot. 7. It was suggested that barium ions were able to carry the larger current through calcium channels in smooth muscle cells due to their much weaker binding within the calcium channel.