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Biophysical Journal 84:2306-2318 (2003)
© 2003 The Biophysical Society

Anion Permeation in Human ClC-4 Channels

Simon Hebeisen*, Hannelore Heidtmann*, Diego Cosmelli{dagger}, Carlos Gonzalez{dagger}, Barbara Poser*, Ramon Latorre{dagger},{ddagger}, Osvaldo Alvarez{dagger},{ddagger} and Christoph Fahlke*,{dagger}

* RWTH Aachen, Institute of Physiology, Aachen, Germany; {dagger} Centro de Estudios Cientificos, Valdivia, Chile; and {ddagger} Departamento de Biologia, Facultad de Ciencias, Universidad de Chile, Santiago, Chile

Correspondence: Address reprint requests to Christoph Fahlke, Institut für Physiologie, RWTH Aachen, Pauwelsstr. 30, D-52074 Aachen, Germany. Tel.: 49-241-80-88810; Fax: 49-241-80-82434; E-mail: chfahlke{at}physiology.rwth-aachen.de.

ClC-4 and ClC-5 are mammalian ClC isoforms with unique ion conduction and gating properties. Macroscopic current recordings in heterologous expression systems revealed very small currents at negative potentials, whereas a substantially larger instantaneous current amplitude and a subsequent activation were observed upon depolarization. Neither the functional basis nor the physiological impact of these channel features are currently understood. Here, we used whole-cell recordings to study pore properties of human ClC-4 channels heterologously expressed in tsA201 or HEK293 cells. Variance analysis demonstrated that the prominent rectification of the instantaneous macroscopic current amplitude is due to a voltage-dependent unitary current conductance. The single channel amplitudes are very small, i.e., 0.10 ± 0.02 pA at +140 mV for external Cl- and internal I-. Conductivity and permeability sequences were determined for various external and internal anions, and both values increase for anions with lower dehydration energies. ClC-4 exhibits pore properties that are distinct from other ClC isoforms. These differences can be explained by assuming differences in the size of the pore narrowing and the electrostatic potentials within the ion conduction pathways.




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