A predominant inward rectifier and a small outward potassium current were obtained in whole-cell patch-clamp recordings from cultured bovine pulmonary arterial endothelial cells. Application of endothelin-l (ET-1; 10-100 nmol/l) inhibited the inward rectifier. Washout with bath solution did not recover the current decreased by ET-1. In cell-attached studies, ET-1 (1 nmol/l) inhibited single-channel activity of the inward rectifier and in some patches enhanced activity of the outward potassium current without change of conductance. A non-specific cation current which is permeable to calcium was identified in cell-attached patches in cultured human umbilical vein endothelial cells. ET-1 (1 nmol/l) increased activity of the nonspecific cation channel. ET-1 may increase calcium influx into endothelial cells and promote synthase and release of endothelium-derived factors.

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