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The Japanese Journal of Physiology
Vol. 55 (2005) No. 6 P 379-383



Short Communications

It is controversial whether the ClC-3 protein, which is one of the voltage-dependent chloride channel ClC family members, is a candidate for the volume-sensitive outwardly rectifying (VSOR) Cl channel per se or its regulator. Here, for the first time, we examined the single-channel properties of the VSOR Cl channel in ventricular myocytes isolated from ClC-3–deficient mice. The single-channel current induced by cell swelling exhibited Cl selectivity, mild outward rectification, and an intermediate unitary conductance (around 38 pS). A Cl channel blocker, 4,4'-diisothiocyanatostilbene-2,2'-disulfonic acid (DIDS), reversibly inhibited the outward current. These single-channel properties were identical with those in ClC-3 expressing wild-type ventricular myocytes. These results indicate that the single-channel activity of the VSOR Cl channel is independent of the expression of ClC-3 proteins in mouse ventricular myocytes.

Copyright © 2005 by The Physiological Society of Japan

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