Metabolic control of muscle mitochondrial function and fatty acid oxidation through SIRT1/PGC‐1α
By Zachary Gerhart-Hines, J. T. Rodgers, Olivia Baré, C. Lerin, Seung-hee Kim, R. Mostoslavsky, F. Alt, Zhidan Wu, P. Puigserver. EMBO Journal, 2007
1,326 citations recorded by the source corpus.
Subfields: Cell Biology, Geriatrics and Gerontology, Physiology
View Paper: https://www.semanticscholar.org/paper/500ff3980696f0f6dba07372c9e5a77f7c3883da
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Citations in the corpus
- A practical model of low‐volume high‐intensity interval training induces mitochondrial biogenesis in human skeletal muscle: potential mechanisms (2010, background): “The protein content of SIRT1, an NAD+-dependent deacetylase which has been shown to deacetylate and activate PGC-1α (Cantó et al. 2009; Gerhart-Hines et al. 2007) was also elevated post-training, as was content of Tfam, a mitochondrial transcription factor which is induced by PGC-1α (Wu et al.…”
- Interdependence of AMPK and SIRT1 for metabolic adaptation to fasting and exercise in skeletal muscle (2010, background): “How SIRT1 activity is regulated is still largely unknown, even thought it has been hypothesized that NAD availability, for which SIRT1 acts as a sensor, plays a major role (Gerhart-Hines et al., 2007).”
- SIRT1 is required for AMPK activation and the beneficial effects of resveratrol on mitochondrial function (2012, background): “SIRT1 promotes mitochondrial biogenesis through deacetylation and activation of PGC-1α (Gerhart-Hines et al., 2007; Rodgers et al., 2005), a master regulator of mitochondrial biogenesis that co-activates the nuclear respiratory factors (NRF-1 and NRF-2), which induce the transcription of genes…”
- Mitochondrial dysfunction results from oxidative stress in the skeletal muscle of diet-induced insulin-resistant mice. (2008, background): “ is increased in high-fat diet fed mice (30).”
- Sirtuin 3, a New Target of PGC-1α, Plays an Important Role in the Suppression of ROS and Mitochondrial Biogenesis (2010, methodology): “cell lines from ATCC were maintained in DMEM supplemented with 10% fetal bovine serum (FBS) and antibiotics. Myotube differentiation was induced as previously reported”
- SIRTUIN 1 AND SIRTUIN 3: PHYSIOLOGICAL MODULATORS OF METABOLISM (2012, background): “SIRT1 is activated during low energy states, and therefore, it makes sense that SIRT1 would induce fatty acid oxidation as the cell shifts from glucose consumption to fatty acid oxidation (114) (FIGURE 6).”
- Exercise metabolism and the molecular regulation of skeletal muscle adaptation. (2013, background): “Enhanced SIRT activity is associated with favorable adaptations in skeletal muscle metabolism, including enhanced mitochondrial function, exercise performance, and protection against obesogenic feeding (Lagouge et al., 2006; Gerhart-Hines et al., 2007).”
- Specific SIRT1 activation mimics low energy levels and protects against diet-induced metabolic disorders by enhancing fat oxidation. (2008, background): “One of the best characterized metabolic targets of SIRT1 is PGC-1a, which is activated by SIRT1-mediated deacetylation (Gerhart-Hines et al., 2007; Lagouge et al., 2006; Rodgers et al., 2005, 2008).”
- Sirt1 and the Mitochondria (2016, background): “The group also showed that fasting induced PGC-1α deacetylation by Sirt1 in skeletal muscle, which is required for the activation of mitochondrial fatty acid oxidation genes (Gerhart-Hines et al., 2007).”
- Transcriptional control of mitochondrial biogenesis and function. (2009, background): “F or p er so na l u se o nl y. ANRV369-PH71-09 ARI 5 January 2009 14:42 Sirtuin 1 (SIRT1): NAD+-dependent protein deacetylase homologous to the yeast silent information regulator (Sir2) and implicated in caloric restriction and aging pathways Histone deacetylase (HDAC): a family of enzymes that deac”