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

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Abstract

Type V adenylyl cyclase (AC) was stably overexpressed 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.

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Kawabe, J. I., Ebina, T., Toya, Y., Oka, N., Schwencke, G., Duzic, E., & Ishikawa, Y. (1996). Regulation of type V adenylyl cyclase by PMA-sensitive and -insensitive protein kinase C isoenzymes in intact cells. FEBS Letters, 384(3), 273–276. https://doi.org/10.1016/0014-5793(96)00331-6

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