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Cyclic AMP Stimulates K+ Channel Activity in Mesophyll Cells of Vicia faba L
Author(s) -
Wanyu Li,
Sheng Luan,
S.L. Schreiber,
Sarah M. Assmann
Publication year - 1994
Publication title -
plant physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.554
H-Index - 312
eISSN - 1532-2548
pISSN - 0032-0889
DOI - 10.1104/pp.106.3.957
Subject(s) - protein kinase a , vicia faba , intracellular , patch clamp , cyclic nucleotide phosphodiesterase , adenosine , cyclic nucleotide , protein subunit , phosphodiesterase , phosphodiesterase inhibitor , xanthine , biophysics , biology , biochemistry , protein kinase inhibitor , microbiology and biotechnology , chemistry , nucleotide , kinase , enzyme , botany , receptor , gene
Whole-cell patch-clamp recordings from Vicia faba mesophyll protoplasts reveal that outward K+ current is increased in a dose-dependent fashion by intracellular application of cAMP. The enhancement of the outward current by cAMP is specific and it cannot be mimicked by a series of nucleotides that includes AMP, cGMP, and GMP. The enhancement is evoked by micromolar concentrations of cAMP in the presence of the phosphodiesterase inhibitor 3-isobutyl-1-methyl-xanthine. PKI or Walsh inhibitor, a specific peptide inhibitor of cAMP-dependent protein kinase (PKA), 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 mesophyll cells and suggest that this modulation occurs through a cAMP-regulated protein kinase.

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