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(Received for publication, July 21, 1994; and in revised form, November 1, 1994) This study was undertaken to define intracellular signaling
pathways upstream to glycogen synthase activation. First, we examined
the role of the two pathways of insulin signaling, Ras-dependent and
wortmannin/LY294002-sensitive, in glycogen synthase activation.
Although negative dominant Ras (Ras17N) induction in PC12 cells
markedly decreased activities of mitogen-activated protein kinase (MAP)
and pp90 S6 kinase in response to insulin or insulin-like growth factor
I (IGF-I), activation of glycogen synthase by these agents was
unaffected by negative dominant Ras induction. In contrast, wortmannin
and 2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one (LY294002),
inhibitors of phosphatidylinositol 3-kinase, antagonized glycogen
synthase activation in response to insulin or IGF-I. Next, we examined
the contribution of pp70 S6 kinase, one of the
wortmannin/LY294002-sensitive signaling molecules on glycogen synthase
activation. Immunosuppressant rapamycin completely blocked activation
of pp70 S6 kinase by insulin or IGF-I, but rapamycin alone or in
combination with induction of negative dominant Ras failed to
antagonize glycogen synthase activation by these hormones. These data
suggest that 1) activation of Ras-MAP kinase is not necessary for
stimulation of glycogen synthase and 2) activation of
wortmannin/LY294002sensitive pathway, independent of pp70 S6 kinase,
plays a key role in glycogen synthase regulation in PC12 cells.
Volume 270,
Number 6,
Issue of February 10, 1995 pp. 2729-2734
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
GLYCOGEN SYNTHASE ACTIVATION IS ANTAGONIZED BY WORTMANNIN OR
LY294002 BUT NOT BY RAPAMYCIN OR BY INHIBITING p21
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