Properties of ATP-dependent K(+) channels in adrenocortical cells.

Bovine adrenocortical zona fasciculata (AZF) cells express a novel ATP-dependent K(+)-permeable channel (I(AC)). Whole cell and single-channel recordings were used to characterize I(AC) channels with respect to ionic selectivity, conductance, and modulation by nucleotides, inorganic phosphates, and angiotensin II (ANG II). In outside-out patch recordings, the activity of unitary I(AC) channels is enhanced by ATP in the patch pipette. These channels were K(+) selective with no measurable Na(+) or Ca(2+) conductance. In symmetrical K(+) solutions with physiological concentrations of divalent cations (M(2+)), I(AC) channels were outwardly rectifying with outward and inward chord conductances of 94.5 and 27.0 pS, respectively. In the absence of M(2+), conductance was nearly ohmic. Hydrolysis-resistant nucleotides including AMP-PNP and NaUTP were more potent than MgATP as activators of whole cell I(AC) currents. Inorganic polytriphosphate (PPP(i)) dramatically enhanced I(AC) activity. In current-clamp recordings, nucleotides and PPP(i) produced resting potentials in AZF cells that correlated with their effectiveness in activating I(AC). ANG II (10 nM) inhibited whole cell I(AC) currents when patch pipettes contained 5 mM MgATP but was ineffective in the presence of 5 mM NaUTP and 1 mM MgATP. Inhibition by ANG II was not reduced by selective kinase antagonists. These results demonstrate that I(AC) is a distinctive K(+)-selective channel whose activity is increased by nucleotide triphosphates and PPP(i). Furthermore, they suggest a model for I(AC) gating that is controlled through a cycle of ATP binding and hydrolysis.