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Title: Myostatin inhibits IGF-I-induced myotube hypertrophy through Akt
Authors: Morissette M.R.
Cook S.A. 
Buranasombati C.
Rosenberg M.A.
Rosenzweig A.
Keywords: C2C12
Growth differentiation factor-8
Muscle growth
Issue Date: 2009
Publisher: APS
Citation: Morissette M.R., Cook S.A., Buranasombati C., Rosenberg M.A., Rosenzweig A. (2009). Myostatin inhibits IGF-I-induced myotube hypertrophy through Akt. American Journal of Physiology - Cell Physiology 297 (5) : C1124-C1132. ScholarBank@NUS Repository.
Abstract: Myo-statin is a highly conserved negative regulator of skeletal muscle growth. Loss of functional myostatin in cattle, mice, sheep, dogs, and humans results in increased muscle mass. The molecular mechanisms responsible for this increase in muscle growth are not fully understood. Previously, we have reported that phenylephrine-induced cardiac muscle growth and Akt activation are enhanced in myostatin knockout mice compared with controls. Here we report that skeletal muscle from myostatin knockout mice show increased Akt protein expression and overall activity at baseline secondary to an increase in Akt mRNA. We examined the functional role of myostatin modulation of Akt in C2C12 myotubes, a well-established in vitro model of skeletal muscle hypertrophy. Adenoviral overexpression of myostatin attenuated the insulin-like growth factor-I (IGF-I)-mediated increase in myotube diameter, as well as IGF-I-stimulated Akt phosphorylation. Inhibition of myostatin by overexpression of the NH2-terminal portion of myostatin was sufficient to increase myotube diameter and Akt phosphorylation. Coexpression of myostatin and constitutively active Akt (myr-Akt) restored the increase in myotube diameter. Conversely, expression of dominant negative Akt (dn-Akt) with the inhibitory myostatin propeptide blocked the increase in myotube diameter. Of note, ribosomal protein S6 phosphorylation and atrogin-1/muscle atrophy F box mRNA were increased in skeletal muscle from myostain knockout mice. Together, these data suggest myostatin regulates muscle growth at least in part through regulation of Akt. Copyright � 2009 the American Physiological Society.
Source Title: American Journal of Physiology - Cell Physiology
ISSN: 3636143
DOI: 10.1152/ajpcell.00043.2009
Appears in Collections:Staff Publications

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