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Whole-cell and single channel monovalent cation currents through the novel rabbit epithelial Ca2+ channel ECaC Nilius B; Vennekens R; Prenen J; Hoenderop JG; Bindels RJ; Droogmans GJ Physiol 2000[Sep]; 527 Pt 2 (Pt 2): 239-48This study describes properties of monovalent cation currents through ECaC, a recently cloned epithelial Ca2+-permeable channel from rabbit. 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 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 (delta = 0.31) and a voltage-dependent binding constant (at 0 mV 3.1 mM Ca2+, obtained from a Woodhull type analysis). Currents were only stable in the absence of divalent cations and showed under these conditions a small time- and voltage-dependent component of activation. 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. 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. 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.|Algorithms[MESH]|Animals[MESH]|Calcium Channels/*metabolism[MESH]|Cations/*metabolism[MESH]|Cell Line[MESH]|Electrophysiology[MESH]|Epithelium/metabolism[MESH]|Extracellular Space/metabolism[MESH]|Humans[MESH]|Ion Channels/*metabolism[MESH]|Kinetics[MESH]|Magnesium/metabolism[MESH]|Patch-Clamp Techniques[MESH]|Rabbits[MESH]|TRPV Cation Channels[MESH]|Transfection[MESH] |
