Key result
Recombinant human myostatin blocked human myoblast proliferation and differentiation by upregulating p21 and Notch signaling, and inhibiting MyoD via Smad signaling.
Myostatin negatively regulates human skeletal muscle growth by blocking myoblast proliferation via p21 and inhibiting differentiation through Smad and Notch signaling pathways.
Supports myostatin pathway targeting in muscle wasting; leaves open translation to human cardiovascular therapeutics.
Myostatin, a member of the transforming growth factor-β superfamily, has been implicated in the potent negative regulation of myogenesis in murine models. However, little is known about the mechanism(s) through which human myostatin negatively regulates human skeletal muscle growth. Using human primary myoblasts and recombinant human myostatin protein, we show here that myostatin blocks human myoblast proliferation by regulating cell cycle progression through targeted upregulation of p21. We further show that myostatin regulates myogenic differentiation through the inhibition of key myogenic regulatory factors including MyoD, via canonical Smad signaling. In addition, we have for the first time demonstrated the capability of myostatin to regulate the Notch signaling pathway during inhibition of human myoblast differentiation. Treatment with myostatin results in the upregulation of Hes1, Hes5, and Hey1 expression during differentiation; moreover, when we interfere with Notch signaling, through treatment with the γ-secretase inhibitor L-685,458, we find enhanced myotube formation despite the presence of excess myostatin. Therefore, blockade of the Notch pathway relieves myostatin repression of differentiation, and myostatin upregulates Notch downstream target genes. Immunoprecipitation studies demonstrate that myostatin treatment of myoblasts results in enhanced association of Notch1-intracellular domain with Smad3, providing an additional mechanism through which myostatin targets and represses the activity of the myogenic regulatory factor MyoD. On the basis of these results, we suggest that myostatin function and mechanism of action are very well conserved between species, and that myostatin regulation of postnatal myogenesis involves interactions with numerous downstream signaling mediators, including the Notch pathway.
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McFarlane et al. (2011) studied Skeletal muscle growth and differentiation. Recombinant human myostatin protein was evaluated. Recombinant human myostatin blocked human myoblast proliferation and differentiation by upregulating p21 and Notch signaling, and inhibiting MyoD via Smad signaling.
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