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J. Biol. Chem., Vol. 264, Issue 13, 7345-7348, May, 1989
D Carroll and DR Marshak
We have tested the effects of serum-stimulated growth of quiescent WI38
human lung fibroblasts on cellular casein kinase II (CK-II) activity. Using
the casein kinase II synthetic substrate RRREEETEEE we find a transient
6-fold elevation in CK-II activity in cell homogenates within 30 min
following serum stimulation. Additional cycles of CK-II activation and
inactivation are seen at 12 and 24 h after stimulation. The oscillations in
CK-II activity are largely independent of de novo protein synthesis, and,
thus, are likely to reflect cycles of post- translational activation and
inhibition of the cellular kinase pool. In contrast to the activity profile
of CK-II, we find that cyclic AMP- dependent protein kinase is rapidly
inhibited upon serum-stimulation of WI38 cells. These results demonstrate
that CK-II activity is subject to unique cellular regulation during
proliferation and are consistent with the postulate that CK-II plays an
important role in cell growth.
Serum-stimulated cell growth causes oscillations in casein kinase II activity
Cold Spring Harbor Laboratory, Cold Spring Harbor, New York 11724.
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