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Whole-cell and single channel monovalent cation currents through the novel rabbit epithelial Ca²⁺ channel ECaC

Bernd Nilius*†, Rudi Vennekens*, Jean Prenen*, Joost G. J Hoenderop†, René J. M. Bindels† and Guy Droogmans*

1. This study describes properties of monovalent cation currents through ECaC, a recently cloned epithelial Ca²⁺-permeable channel from rabbit.

2. The kinetics of currents through ECaC was strongly modulated by divalent cations. Currents were inhibited in the presence of extracellular Ca²⁺. They showed an initial voltage-dependent decay in the presence of 1 mM Mg²⁺ at hyperpolarizing steps in Ca²⁺-free solutions, which represents a voltage-dependent Mg²⁺ block through binding of Mg²⁺ to a site localized in the electrical field of the membrane ( = 0·31) and a voltage-dependent binding constant (at 0 mV 3·1 mM Ca²⁺, obtained from a Woodhull type analysis).

3. Currents were only stable in the absence of divalent cations and showed under these conditions a small time- and voltage-dependent component of activation.

4. Single channel currents in cell-attached and inside-out patches had a conductance of 77·5 ± 4·9 pS (n = 11) and reversed at +14·8 ± 1·6 11imV81i (n = 9) in the absence of divalent cations.

5. The permeation sequence for monovalent cations through ECaC was Na⁺ > Li⁺ > K⁺ > Cs⁺ > NMDG⁺ which is identical to the Eisenmann sequence X for a strong field-strength binding site.

6. It is concluded that the permeation profile of ECaC for monovalent cations suggests a strong field-strength binding site that may be involved in Ca²⁺ permeation and Mg²⁺ block.

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