Abstract
The effects of cyclic AMP-dependent protein kinase on ATP-sensitive K + channels in cultured smooth muscle cells of the porcine coronary artery were investigated using the patch-clamp technique. Extracellular application of isoproterenol (1mM), a beta agonist, or forskolin (2×10 −5M), an activator of adenylate cyclase, activated these channels in cell-attached patch configurations, which were not blocked by phorbol 12-myristate 13-acetate (10 −6M), an activator of protein kinase C. Cyclic AMP-dependent protein kinase activated these channels in inside-out patch configurations. These results suggest that cyclic AMP-dependent phosphorylatlon modulates ATPsensitive K + channels, in addition to its well known effects on Ca 2+-activated K + channels. The activation of ATP-sensltive K + channels by cyclic AMP-dependent phosphorylation contributes to hyperpolarizatlon of the membrane and to the relaxation of vascular smooth muscle cells.
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