Myostatin reduces Akt/TORC1/p70S6K signaling, inhibiting myoblast differentiation and myotube size.
By A. Trendelenburg, Angelika Meyer, D. Rohner, Joseph Boyle, S. Hatakeyama, D. Glass. American Journal of Physiology - Cell Physiology, 2009
780 citations recorded by the source corpus.
Subfields: Molecular Biology
View Paper: https://www.semanticscholar.org/paper/9bfa482490777f4b17da7337c1dbc8103a8c7806
How researchers see this paper
The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.
In Molecular Biology
- M. Sandri
- S. Schiaffino
- P. Bonaldo
- C. Mammucari
- A. Goldberg
- P. Delafontaine
- Tadashi Yoshida
- D. Glass
Citations in the corpus
- Regulation of skeletal muscle growth by the IGF1-Akt/PKB pathway: insights from genetic models (2011, background): “Myostatin, together with activin A, another member of the TGFb family, acts via its receptor activin receptor IIB (ActRIIB) on Smad2 and Smad3, inhibitors of Akt; conversely, mTOR inhibits Smads [17,18].”
- Mechanisms of IGF-1-Mediated Regulation of Skeletal Muscle Hypertrophy and Atrophy (2020, background): “Indeed, IGF-1 treatment of cultured myotubes blocked myostatin-mediated downregulation of Akt and myotube diameter reduction [23].”
- Exercise is the real polypill. (2013, background): “Myostatin, the first described secreted muscle factor to fulfil the criteria of a myokine, is a potent muscle-growth inhibitor (302) that acts via SMAD signaling (398) or mammalian target-of-rapamycin (mTOR) inhibition (12, 249, 271, 301, 403, 426, 476).”
- Reversal of cancer cachexia and muscle wasting by ActRIIB antagonism leads to prolonged survival. (2010, background): “Smad and FOXO signal transduction systems can influence each other’s activity (Seoane et al., 2004), and in skeletal muscle, the myostatin-Smad pathway stimulates FOXO function (Sartori et al., 2009; Trendelenburg et al., 2009).”
- Cancer cachexia: mediators, signaling, and metabolic pathways. (2012, background): “Interestingly, treatment of IGF1 can dominantly revert myostatin inhibition of Akt, suggesting that IGF1 as a drug would be helpful even in settings where myostatin or Activin are active (Trendelenburg et al., 2009).”
- Cellular and molecular mechanisms of muscle atrophy (2013, background): “The growthpromoting effects mediated by JunB in muscle resemble the effects of inhibiting the transforming grown factor-β (TGFβ) pathway (Sartori et al., 2009; Trendelenburg et al., 2009).”