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1 Department of Animal Biology, School of Veterinary Medicine, University of Pennsylvania, Philadelphia, Pennsylvania 19104-6046; and 2 Department of Anesthesiology and Comparative Medicine, University of Alabama at Birmingham, Birmingham, Alabama 35249
We coexpressed the human large-conductance, calcium-activated K
(KCa) channel (
- and 
-subunits) and rat atrial
natriuretic peptide (ANP) receptor genes in Xenopus oocytes
to examine the mechanism of guanylyl cyclase stimulatory coupling to
the channel. Exposure of oocytes to ANP stimulated whole cell
KCa currents by 21 ± 3% (at 60 mV), without altering
current kinetics. Similarly, spermine NONOate, a nitric oxide donor,
increased KCa currents (20 ± 4% at 60 mV) in oocytes
expressing the channel subunits alone. Stimulation of KCa
currents by ANP was inhibited in a concentration-dependent manner by a
peptide inhibitor of cGMP-dependent protein kinase (PKG).
Receptor/channel stimulatory coupling was not completely abolished by
mutating the cAMP-dependent protein kinase phosphorylation site on the
-subunit (S869; Nars M, Dhulipals PD, Wang YX, and Kotlikoff MI.
J Biol Chem 273: 14920-14924, 1998) or by mutating a neighboring consensus PKG site (S855), but mutation of both residues
virtually abolished coupling. Spermine NONOate also failed to stimulate
channels expressed from the double mutant cRNAs. These data indicate
that nitric oxide donors stimulate KCa channels through
cGMP-dependent phosphorylation and that two serine residues (855 and
869) underlie this stimulatory coupling.
ion channel; calcium-activated potassium channels; mutagenesis; smooth muscle; cGMP-dependent protein kinase
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