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negatively regulates skeletal myotube
hypertrophy
Departments of Veterinary Biomedical Sciences and Physiology, and the Dalton Cardiovascular Institute, University of Missouri, Columbia, Missouri 65211
To
determine whether changes in glycogen synthase kinase-3
(GSK-3)
phosphorylation contribute to muscle hypertrophy, we delineated the
effects of GSK-3 activity on C2C12 myotube
size. We also examined possible insulin-like growth factor I (IGF-I) signaling of NFAT (nuclear factors of activated T cells)-inducible gene
activity and possible modulation of NFAT activation by GSK-3. Application of IGF-I (250 ng/ml) or LiCl (10 mM) alone (i.e., both
inhibit GSK-3 activity) increased the area of
C2C12 myotubes by 80 and 85%, respectively.
The application of IGF-I (250 ng/ml) elevated GSK-3 phosphorylation
and reduced GSK-3 kinase activity by ~800% and ~25%,
respectively. LY-294002 (100 µM) and wortmannin (150 µM), specific
inhibitors of phosphatidylinositol 3'-kinase, attenuated IGF-I-induced
GSK-3 phosphorylation by 67 and 92%, respectively. IGF-I suppressed
the kinase activity of GSK-3. IGF-I (250 ng/ml), but not LiCl (10 mM), induced an increase in NFAT-activated luciferase reporter
activity. Cotransfection of a constitutively active GSK-3
(cGSK-3) inhibited the induction by IGF-I of NFAT-inducible reporter
activity. LiCl, which inhibits GSK-3, removed the block by cGSK-3
on IGF-I-inducible NFAT-responsive reporter gene activity. These data
suggest that the IGF-I-induced increase in skeletal myotube size is
signaled, in part, through the inhibition of GSK-3.
skeletal muscle; signaling; glycogen synthase kinase-3; insulin-like growth factor I; nuclear factors of activated T
cells
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