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J. Biol. Chem., Vol. 265, Issue 31, 18769-18775, 11, 1990
JJ Egan, AS Greenberg, MK Chang and C Londos
In isolated, 32Pi-loaded, rat adipocytes, we have examined phosphorylation
of the major cAMP-dependent protein kinase (A-kinase) substrate, a protein
that appears to be associated with the lipid storage droplet and migrates
in sodium dodecyl sulfate-polyacrylamide gel electrophoresis as a 65-67-kDa
doublet. In control cells, a strong phosphorylation signal is detected as
the (+/- cAMP) A-kinase activity ratio ranges from approximately 0.1 to
approximately 0.3-0.4 with increasing isoproterenol concentrations. By
contrast, insulin-treated cells exhibiting A-kinase activity ratios over
the range of 0.1-0.25 contain less 32P in the 65-67-kDa protein than
control cells exhibiting identical A-kinase activity ratios. At higher
activity ratios (greater than 0.3), this reduction in phosphorylation of
the 65-67-kDa protein by insulin disappears. It is concluded that insulin
stimulates a phosphatase activity that acts on the 65-67-kDa protein.
Insulin actions aside, these studies reveal two interesting phenomena. 1)
Whereas elevated, steady-state A-kinase activities are established rapidly
(1-2 min) upon isoproterenol stimulation, phosphorylation of the 65-67-kDa
substrate proceeds through a burst, followed by a decline to a steady-state
level by 10-12 min. An "adaptation" mechanism, providing for a constant
response to a constant stimulus, may underlie this lack of parallelism
between the time course of phosphorylation and A-kinase activity. 2)
Removal of [32Pi] orthophosphate immediately before isoproterenol
stimulation leads to a rapid (t approximately 10 min) loss in labeling of
the 65-67-kDa protein, whereas the phosphorylation state of other
phosphoproteins are not changed. These data suggest that elevation of
A-kinase activity leads to a rapid exchange of external Pi with an ATP pool
that is used by A-kinase.
Control of endogenous phosphorylation of the major cAMP-dependent protein kinase substrate in adipocytes by insulin and beta-adrenergic stimulation
Membrane Regulation Section, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892.
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