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J. Biol. Chem., Vol. 276, Issue 42, 39264-39270, October 19, 2001
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From the Oregon Health and Science University, Molecular Medicine
Division, Department of Medicine, Portland, Oregon 97201-3098
The differentiation and maturation of skeletal
muscle require interactions between signaling pathways activated by
hormones and growth factors and an intrinsic regulatory network
controlled by myogenic transcription factors. Insulin-like growth
factors (IGFs) play key roles in muscle development in the embryo and in regeneration in the adult. To study mechanisms of IGF action in
muscle, we developed a myogenic cell line that overexpresses IGF-binding protein-5. C2BP5 cells remain quiescent in low serum differentiation medium until the addition of IGF-I. Here we use this
cell line to identify signaling pathways controlling IGF-mediated differentiation. Induction of myogenin by IGF-I and myotube formation were prevented by the phosphatidylinositol (PI) 3-kinase inhibitor, LY294002, even when included 2 days after growth factor addition, whereas expression of active PI 3-kinase could promote differentiation in the absence of IGF-I. Differentiation also was induced by myogenin but was blocked by LY294002. The differentiation-promoting effects of
IGF-I were mimicked by a modified membrane-targeted inducible Akt-1
(iAkt), and iAkt was able to stimulate differentiation of C2 myoblasts
and primary mouse myoblasts incubated with otherwise inhibitory
concentrations of LY294002. These results show that an IGF-regulated PI
3-kinase-Akt pathway controls muscle differentiation by mechanisms
acting both upstream and downstream of myogenin.
Insulin-like Growth Factor-mediated Muscle Differentiation
COLLABORATION BETWEEN PHOSPHATIDYLINOSITOL
3-KINASE-Akt-SIGNALING PATHWAYS AND MYOGENIN*
*
This study was supported by National Institutes of Health
Research Grant 5RO1-DK42748 (to P. R.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed. Tel.: 503-494-0536;
Fax: 503-494-7368; E-mail: rotweinp@ohsu.edu.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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