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*
Pulmonary/Critical Care Medicine Branch and
Hypertension-Endocrine Branch, National Heart, Lung, and Blood Institute, and
Laboratory of Cellular and Molecular Biology, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892; and
§
Section for Molecular Signaling, Department of Cell and Molecular Biology, Lund University, Lund, Sweden
Wild-type (F/B), constitutively active (F/B*), and three
kinase-inactive (F/Ba-, F/Bb-,
F/Bc-) forms of Akt/protein kinase B (PKB) were
permanently overexpressed in FDCP2 cells. In the absence of
insulin-like growth factor-1 (IGF-1), activities of PKB, cyclic
nucleotide phosphodiesterase 3B (PDE3B), and PDE4 were similar in
nontransfected FDCP2 cells, mock-transfected (F/V) cells, and F/B and
F/B- cells. In F/V cells, IGF-1 increased PKB, PDE3B, and
PDE4 activities 
2-fold. In F/B cells, IGF-1, in a
wortmannin-sensitive manner, increased PKB activity 10-fold and
PDE3B phosphorylation and activity (4-fold), but increased PDE4 to
the same extent as in F/V cells. In F/B* cells, in the absence of
IGF-1, PKB activity was markedly increased (10-fold) and PDE3B was
phosphorylated and activated (3- to 4-fold); wortmannin inhibited these
effects. In F/B* cells, IGF-1 had little further effect on PKB and
activation/phosphorylation of PDE3B. In F/B- cells, IGF-1
activated PDE4, not PDE3B, suggesting that kinase-inactive PKB behaved
as a dominant negative with respect to PDE3B activation. Thymidine
incorporation was greater in F/B* cells than in F/V cells and was
inhibited to a greater extent by PDE3 inhibitors than by rolipram, a
PDE4 inhibitor. In F/B cells, IGF-1-induced phosphorylation of the
apoptotic protein BAD was inhibited by the PDE3 inhibitor cilostamide.
Activated PKB phosphorylated and activated rPDE3B in vitro. These
results suggest that PDE3B, not PDE4, is a target of PKB and that
activated PDE3B may regulate cAMP pools that modulate effects of PKB on
thymidine incorporation and BAD phosphorylation in FDCP2
cells.
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