Abstract
Abstract Type V adenylyl cyclase (AC) was stably over-expressed in HEK293 cells (293AC-V). Forskolin-stimulated cAMP accumulation in 293AC-V was 5 times as great as that in control cells. PMA, a protein kinase C (PKC) activator, enhanced cAMP accumulation in 293AC-V cells dose-and time-dependently and this enhancement was abolished by staurosporine. Insulin also enhanced cAMP accumulation in 293AC-V cells. Co-transfection of PKC-zeta, but not PKC-alpha, potentiated the effects of insulin. These data suggest that type V AC activity is regulated in cells by PKC isoenzymes through different extracellular stimuli.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Adenylyl Cyclases / genetics
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Adenylyl Cyclases / metabolism*
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Alkaloids / pharmacology
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Cells, Cultured
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Cyclic AMP / biosynthesis
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Cyclic AMP / metabolism
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Dose-Response Relationship, Drug
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Enzyme Activation / drug effects
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Enzyme Inhibitors / pharmacology
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Humans
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Insulin / pharmacology
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Isoenzymes / metabolism*
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Kidney / cytology*
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Kidney / embryology
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Molecular Sequence Data
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Protein Kinase C / antagonists & inhibitors
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Protein Kinase C / metabolism*
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Staurosporine
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Tetradecanoylphorbol Acetate / pharmacology*
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Time Factors
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Transfection
Substances
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Alkaloids
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Enzyme Inhibitors
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Insulin
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Isoenzymes
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Cyclic AMP
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Protein Kinase C
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Adenylyl Cyclases
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Staurosporine
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Tetradecanoylphorbol Acetate