Abstract
The novel K + channel blocker 6,10-diaza-3(1,3)8,(1,4)-dibenzena-1,5(1,4)-diquinolinacyclodecaphane (UCL 1684) has been tested for its ability to inhibit Ca 2+-activated K + currents in cultured rat chromaffin cells. Low nanomolar concentrations of UCL 1684 produced a rapid and reversible inhibition of the slow, apamin-sensitive, tail current activated by a depolarizing voltage command. This compound also inhibited the muscarine activated outward current with an IC 50 of 6 nM. These results confirm UCL 1684 to be the most potent non-peptidic blocker of the apamin-sensitive Ca 2+-activated K + channel so far described.
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