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-Adrenergic Agonists in Rat Epididymal Fat Cells
(Received for publication, October 2, 1996, and in revised form, November 21, 1996)
From the ‡ Department of Biochemistry, Previous studies using L6 myotubes have suggested
that glycogen synthase kinase-3 (GSK-3) is phosphorylated and
inactivated in response to insulin by protein kinase B (PKB, also known
as Akt or RAC) (Cross, D. A. E., Alessi, D. R., Cohen, P., Andjelkovic, M., and Hemmings, B. A. (1995) Nature 378, 785-789). In
the present study, marked increases in the activity of PKB have been
shown to occur in insulin-treated rat epididymal fat cells with a time course compatible with the observed decrease in GSK-3 activity. Isoproterenol, acting primarily through
3-adrenoreceptors, was found to decrease GSK-3 activity
to a similar extent (approximately 50%) to insulin. However, unlike
the effect of insulin, the inhibition of GSK by isoproterenol was not
found to be sensitive to inhibition by the phosphatidylinositol
3
-kinase inhibitors, wortmannin or LY 294002. The change in GSK-3
activity brought about by isoproterenol could not be mimicked by the
addition of permeant cyclic AMP analogues or forskolin to the cells,
although at the concentrations used, these agents were able to
stimulate lipolysis. Isoproterenol, but again not the cyclic AMP
analogues, was found to increase the activity of PKB, although to a
lesser extent than insulin. While wortmannin abolished the stimulation
of PKB activity by insulin, it was without effect on the activation
seen in response to isoproterenol. The activation of PKB by
isoproterenol was not accompanied by any detectable change in the
electrophoretic mobility of the protein on SDS-polyacrylamide gel
electrophoresis. It would therefore appear that distinct mechanisms
exist for the stimulation of PKB by insulin and isoproterenol in rat
fat cells.
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