A large conductance Cl- channel revealed by patch-recordings in human fibroblasts.
A Cl- channel with large single-unit conductance and characteristic voltage-dependent inactivation was studied on cultured human fibroblasts. The channel was activated only after excision and lasting depolarization of the membrane patch. In inside-out configuration and in symmetrical 135 mM NaCl, the conductance was 300 pS. The channel was usually open at the membrane potentials between -20 to +20 mV, while more negative or positive voltages closed the channel. The time course of this apparent inactivation process was dependent on increasing potential. Recovery from inactivation was made possible by returning the membrane potential to 0 mV. The channel was selective to Cl- over Na+ with a PCl/PNa of 6. The order of permeability among anions was: I greater than Br = Cl greater than isethionate greater than F greater than glutamate. The channel was blocked by internal application of a derivative of the diphenylamine-2-carboxilate (Blocker 144) but not by 4,4'-diisothiocyanostilbene-2,2'-disulfonic acid.
Nobile
M
M
Istituto di Cibernetica e Biofisica del Cnr, Genova, Italy.
Galietta
L J
LJ
D002712:Chlorides / Q000378:metabolism*; D004553:Electric Conductivity; D004594:Electrophysiology; D005347:Fibroblasts / Q000502:physiology*; D006801:Humans; D007473:Ion Channels / Q000187:drug effects / Q000502:physiology*; D008564:Membrane Potentials / Q000187:drug effects; D010539:Permeability; D012964:Sodium / Q000378:metabolism
D002712:Chlorides; D007473:Ion Channels; D012964:Sodium