Regulation of type V adenylyl cyclase by PMA-sensitive and -insensitive protein kinase C isoenzymes in intact cells

• Published in: FEBS letters 1996-04, Vol.384 (3), p.273-276
• Main Authors: Kawabe, Jun-ichi, Ebina, Toshiaki, Toya, Yoshiyuki, Oka, Naoki, Schwencke, Carsten, Duzic, Emir, Ishikawa, Yoshihiro
• Format: Article
• Language: English
• Subjects: 3-isobutyl-1-methylxanthine; 4α-phorbol 12,13-didecanoate; Adenylyl Cyclases - genetics; Adenylyl Cyclases - metabolism; Adenylylcyclase; Alkaloids - pharmacology; Cells, Cultured; cyclic AMP; Cyclic AMP - biosynthesis; Cyclic AMP - metabolism; Dose-Response Relationship, Drug; Enzyme Activation - drug effects; Enzyme Inhibitors - pharmacology; Humans; IBMX; Insulin; Insulin - pharmacology; Isoenzymes - metabolism; Kidney - cytology; Kidney - embryology; Molecular Sequence Data; phorbol 12-myristate 13-acetate; Phorbol ester; PKC; PMA; Protein kinase C; Protein Kinase C - antagonists & inhibitors; Protein Kinase C - metabolism; Staurosporine; Tetradecanoylphorbol Acetate - pharmacology; Time Factors; Transfection; αPDD
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/0014-5793(96)00331-6

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-ζ, but not PKC-α, potentiated the effects of insulin. These data suggest that type V AC activity is regulated in cells by PKC isoenzymes through different extracellular stimuli.