PGC-1α protects skeletal muscle from atrophy by suppressing FoxO3 action and atrophy-specific gene transcription

By M. Sandri, Jiandie D. Lin, Christoph Handschin, Wenli Yang, Zoltan Arany, S. Lecker, A. Goldberg, B. Spiegelman. Proceedings of the National Academy of Sciences of the United States of America, 2006

1,031 citations recorded by the source corpus.

Subfields: Cell Biology, Molecular Biology, Physiology

View Paper: https://www.semanticscholar.org/paper/28d4d335503802dffd992ac3826753bb25a51568

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Cell Biology

1. M. Sandri
2. S. Schiaffino
3. M. Gibala
4. J. Hawley
5. M. MacDonald
6. B. Spiegelman
7. J. Little
8. C. Mammucari

In Molecular Biology

1. M. Sandri
2. S. Schiaffino
3. P. Bonaldo
4. A. Goldberg
5. C. Mammucari
6. J. Hawley
7. B. Spiegelman
8. D. Glass

In Physiology

1. M. Sandri
2. S. Schiaffino
3. B. Spiegelman
4. J. Hawley
5. Christoph Handschin
6. M. Gibala
7. Jun Wu
8. Carlo Reggiani

Citations in the corpus

• Cellular and molecular mechanisms of muscle atrophy (2013, positive): “…conditions (either in transgenic mice or by transfecting adult myofibers) spares muscle mass during denervation, fasting, heart failure, aging and sarcopenia – similar to the effect observed with expression of constitutively active FoxO3 (Geng et al., 2011; Sandri et al., 2006; Wenz et al., 2009).”
• Exercise, oxidative stress and hormesis. (2008, neutral): “PGC-1a is also involved in fibertype switching from glycolytic to oxidative fibers and the abundance of contractile proteins (Sandri et al., 2006).”
• A PGC-1α isoform induced by resistance training regulates skeletal muscle hypertrophy (2012, neutral): “However, gain-of-function studies with PGC1a have not shown any increase in either muscle mass or strength (Lin et al., 2002; Sandri et al., 2006; Wende et al., 2007).”
• The role of exercise and PGC1α in inflammation and chronic disease (2008, background): “For example, denervation-induced muscle atrophy, muscle damage caused by treatment with statins, and the effects of Duchenne's muscular dystrophy are greatly ameliorated when the amount of PGC1α is maintained at normal levels or increase”
• Increased muscle PGC-1α expression protects from sarcopenia and metabolic disease during aging (2009, background): “Thereby, PGC-1 links mitochondrial function to muscle integrity (7).”
• Cancer cachexia: mediators, signaling, and metabolic pathways. (2012, background): “PGC-1a is itself downregulated in muscles from tumor-bearing mice and other wasting conditions, and transgenic expression of PGC-1a rescues muscle loss in part by inhibiting Foxo3 and through the production of metabolic products.”
• Physiological adaptations to low‐volume, high‐intensity interval training in health and disease (2012, background): “Given the positive effects that a modest increase in muscle PGC-1α appears to have on oxidative capacity, anti-oxidant defence, glucose uptake, resistance to age-related sarcopenia and anti-inflammatory pathways (Sandri et al. 2006; Benton et al. 2008; Wenz et al. 2009), the increase in PGC-1α follo”
• FoxO3 coordinately activates protein degradation by the autophagic/lysosomal and proteasomal pathways in atrophying muscle cells. (2007, background): “Our prior work showed that activation of FoxO transcription factors is essential for fiber atrophy and atro-gin-1 induction upon denervation, fasting, and glucocorticoid treatment (Sandri et al., 2004, 2006).”
• Redox regulation of FoxO transcription factors (2015, background): “PGC-1α has also been shown to interact with FoxO3a to regulate antioxidant gene expression in endothelial cells and in the skeletal muscle where PGC-1α overexpression is sufficient to attenuate muscle atrophy induced by expression of a constitutively active FoxO transgene [201].”
• Long live FOXO: unraveling the role of FOXO proteins in aging and longevity (2015, background): “FOXOs act on both the upregulation of ubiquitin ligases and by controlling the composition of the proteasome (Bodine et al., 2001; Sandri et al., 2004, 2006; Stitt et al., 2004; Vilchez et al., 2012).”
• Regulation of skeletal muscle growth by the IGF1-Akt/PKB pathway: insights from genetic models (2011, background): “PGC1a transfection protects adult muscles from FoxO-dependent atrophy, and the higher levels of PGC1a in oxidative muscle fibers can explain their greater resistance to muscle atrophy [31].”
• Autophagy is required to maintain muscle mass. (2009, positive): “The control of mitochondrial function seems to be crucial for preventing a cascade of signals that lead to muscle Cell M atrophy (Sandri et al., 2006).”