Whole-cell patch-clamp recordings from Vicia faba mesophyll protoplast
s reveal that outward K+ current is increased in a dose-dependent fash
ion by intracellular application of cAMP. The enhancement of the outwa
rd current by cAMP is specific and it cannot be mimicked by a series o
f nucleotides that includes AMP, cGMP, and GMP. The enhancement is evo
ked by micromolar concentrations of cAMP in the presence of the phosph
odiesterase inhibitor 3-isobutyl-1-methyl-xanthine. PKI or Walsh inhib
itor, a specific peptide inhibitor of cAMP-dependent protein kinase (P
KA), inhibits the outward K+ current. Adenosine 3',5'-phosphothioate,
a competitive inhibitor of PKA, has a similar effect. Conversely, the
catalytic subunit of PKA (cAMP independent) from bovine brain enhances
the magnitude of the outward K+ current in the absence of added cAMP.
Our results indicate that cAMP modulates K+ channel activity in mesop
hyll cells and suggest that this modulation occurs through a cAMP-regu
lated protein kinase.