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J Biol Chem, Vol. 274, Issue 2, 776-780, January 8, 1999
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From the The regulation of glycogen synthesis and
associated enzymes was studied in human myoblasts and myotubes
maintained in culture. Both epidermal growth factor (EGF) and insulin
stimulated glycogen synthesis approximately 2-fold, this stimulation
being accompanied by a rapid and stable activation of the controlling
enzyme glycogen synthase (GS). EGF also caused inhibition of glycogen
synthase kinase 3 (GSK-3) and activation of the School of Biochemistry and Genetics, The
Medical School, University of Newcastle upon Tyne, NE2 4HH, United
Kingdom, the ** Adfeling Biochemie, Faculteit Geneeskunde, Katholieke
Universiteit Leuven, B-3000 Leuven, Belgium, Novo Nordisk,
DK-2880, Bagsvaerd, Denmark, and the
§§ Friedrich Miescher-Institut, Maulbeerstrasse
66, CH-4056 Basel, Switzerland
isoform of protein
kinase B (PKB) with the time-course and magnitude of its effects being similar to those induced by insulin. An inhibitor of the
mitogen-activated protein (MAP) kinase pathway did not prevent
stimulation of GS by EGF, suggesting that this pathway is not essential
for the effect. A partial decrease in the fold activation of GS was,
however, observed when p70S6k activation
was blocked with rapamycin, suggesting a contribution of this pathway
to the control of GS by either hormone. Wortmannin, a selective
inhibitor of phosphatidylinositol 3'-kinase (PI-3 kinase) completely
blocked the effects of both EGF and insulin in these cells. These
results demonstrate that EGF, like insulin, activates glycogen
synthesis in muscle, acting principally via the PKB/GSK-3 pathway but
with a contribution from a rapamycin-sensitive component that lies
downstream of PI-3 kinase.
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