CHARACTERIZATION OF A CATION CHANNEL ON THE APICAL SURFACE OF THE FROG LENS EPITHELIUM

Publisher Website
Google Scholar
Abstract
The properties of a single conductance pathway of the apical (fiber-facing) surface of the frog lens epithelium are reported. Using the patch-clamp technique, the most common single-channel currents had an amplitude of 1.9 pA, the mean open time 2.1 ms and a conductance of 25 pS. One open-state time constant (to = 3.3 ms) and 2 closed-state time constants (.tau.1c = 0.9 ms, .tau.2c = 23.1 ms) were resolved. The channel current and the mean open time were both increased when Ca2+ was removed from the external solution and the open time distribution was no longer fitted by a single exponential. Multiple-channel events in cell-attached patches containing 2 or more identical channels were distributed in a binomial fashion and the probability that an individual channel was open, obtained by fitting the binomial distribution, was 0.039. The channel had a Na+:K+ selectivity ratio of 3:1. When Ca2+ was removed from the pipette solution the probability that an individual channel was open increased to 0.137 and the Na+:K+ selectivity ratio increased to 4:1. Channel activity was observed in the presence of tetrodotoxin (10-6 M) in the bathing medium and the pipette solution but was abolished by internal perfusion of the patch pipette with 0.5 .times. 10-4 M amiloride. This apical conductance pathway is identified as an amiloride-sensitive cation channel. These channels are clustered in groups on the apical membrane, spontaneously active at the resting potential and with the possibility of altering their Na+:K+ selectivity. They represent a distinct type of channel, that differ from nerve and muscle NA+ channels in their manner of activation, but do share some common features with both Na+ and Ca2+ channels in excitable cells.