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Articles in PresS, published online ahead of print April 3, 2002
Am J Physiol Cell Physiol, 10.1152/ajpcell.00049.2002
Submitted on January 30, 2002
Accepted on March 28, 2002
1 Veterinary Biomedical Sciences, University of Missouri, Columbia, MO, USA
* To whom correspondence should be addressed. E-mail: boothf{at}missouri.edu.
In order to determine if changes in GSK-3ß phosphorylation contribute to muscle hypertrophy, we delineated the effects of GSK-3ß activity on C2C12 myotube size. In addition, we also examined possible IGF-I signaling of NFAT-inducible gene activity and possible modulation of NFAT activation by GSK-3ß. Application of IGF-I (250ng/mL) or LiCl (10 mM) alone (i.e. both inhibit GSK-3ß activity) increased the area of C2C12 myotubes by 80 and 85%, respectively. The application of IGF-I (250 ng/mL) elevated GSK-3ß phosphorylation and reduced GSK-3ß kinase activity by ~800% and ~25%, respectively. LY294002 (100µM) and wortmannin (150µM), specific inhibitors of PI3'-K, attenuated IGF-I-induced GSK-3ß phosphorylation by 67% and 92%, respectively. IGF-I suppressed the kinase activity of GSK-3ß. IGF-I (250ng/mL), but not LiCl, (10 mM) induced an increase in NFAT-activated luciferase reporter activity. Co-transfection of a constitutively active GSK-3ß (cGSK-3ß) inhibited IGF-I's induction of NFAT-inducible reporter activity. LiCl, which inhibits GSK-3ß, removed cGSK-3ß's block 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-3ß.
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