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A G protein-activated K+ current in bovine adrenal chromaffin cells: possible regulatory role in exocytosis.

Guanine nucleotide binding proteins (G proteins) act as signal transducers between membrane receptors and ion channels. In the present study, the whole-cell arrangement of the patch clamp technique was used to examine the effect of G proteins on K+ channels in cultured bovine adrenal chromaffin cells. Internal dialysis of chromaffin cells with guanosine 5'-O-(3-thiotriphosphate) (GTP gamma S) or external application of AIF-4, to stimulate G proteins, resulted in a voltage-dependent increase in the amplitude of the outward K+ currents. The half-maximal voltage required for activation of the currents was shifted by -16 mV in the presence of GTP gamma S. The augmentation in the K+ currents was accompanied by the appearance of a fast component of current activation measured at potentials positive to 0 mV. The GTP gamma S-sensitive current could not be detected when internal K+ was replaced with Cs+ and was reversibly inhibited by tetraethylammonium (IC50, 2 mM). In contrast, the scorpion venom charybdotoxin (50 nM) and the bee venom apamin (250 nM) only slightly reduced the K+ currents during stimulation by GTP gamma S and did not alter the activation kinetics. In addition, the GTP gamma S-sensitive K+ current could be activated in the absence of internal Ca2+ and when the inward Ca2+ current was inhibited with CdCl2. Treatment of the chromaffin cells with fluoride decreased nicotine-evoked secretion of catecholamines in a concentration-dependent manner. Thus, bovine chromaffin cells contain a G protein-stimulated K+ channel that may play a regulatory role in secretagogue-mediated exocytosis.