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J. Biol. Chem., Vol. 266, Issue 26, 17454-17458, Sep, 1991
DD Ginty, D Glowacka, DS Bader, H Hidaka and JA Wagner
Agents that activate cAMP-dependent protein kinase (PKA) as well as agents
that increase intracellular calcium induce the expression of certain
immediate early genes (IEGs). Recently, it has been demonstrated that the
same cis-acting element in the 5' region of the c- fos gene has the ability
to mediate both cAMP- and calcium-induced c- fos expression in PC12 cells
(Sheng, M., McFadden, G., and Greenberg, M. (1990) Neuron 4, 571-582). Here
we demonstrate that both cAMP- and calcium-mediated induction of c-fos and
egr1 are dependent on PKA activity. Addition of either depolarizing
concentrations of KCl or the calcium ionophore, ionomycin, to PC12 cells
increased the expression of both c-fos and egr1, but these inductions were
dramatically reduced in three PKA-deficient cell lines, 123.7, AB.11, and
A126-1B2. Furthermore, pretreatment of PC12 cells with 20 microM H89, a
specific inhibitor of PKA, inhibited forskolin, dibutyryl cAMP, and
KCl-induced c-fos and egr1 induction, while having no effect on NGF
induction. Likewise, in the PKA-deficient cells, NGF or an activator of
protein kinase C induced c-fos and egr1 normally. To determine if PKA
deficiency modifies the ability of Ca2+ to activate calcium-dependent
kinases, autophosphorylation of multifunctional Ca2+/calmodulin- dependent
protein kinase (CaM kinase) in response to Ca2+ influx was determined. In
parental PC12 cells, PC12 cells pretreated with H89, and PKA-deficient cell
lines, CaM kinase was activated equivalently in response to KCl
depolarization. These results suggest that PKA is not required for
Ca(2+)-induced increase in CaM kinase activity and that the induction of
IEGs in response to Ca2+ influx is PKA-dependent. Thus, the requirement for
PKA resides at a point distal to the activation of calmodulin-dependent
processes.
Induction of immediate early genes by Ca2+ influx requires cAMP- dependent protein kinase in PC12 cells
Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts.
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