Dietary stimulators of the PGC-1 superfamily and mitochondrial biosynthesis in skeletal muscle. A mini-review

Resveratrol improves health and survival of mice on a high-calorie diet

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Mechanisms controlling mitochondrial biogenesis and respiration through the thermogenic coactivator PGC-1

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Resveratrol Improves Mitochondrial Function and Protects against Metabolic Disease by Activating SIRT1 and PGC-1α

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AMP-activated protein kinase (AMPK) action in skeletal muscle via direct phosphorylation of PGC-1α

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Butyrate improves insulin sensitivity and increases energy expenditure in mice

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Coordinated reduction of genes of oxidative metabolism in humans with insulin resistance and diabetes: Potential role of <i>PGC1</i> and <i>NRF1</i>

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Control of hepatic gluconeogenesis through the transcriptional coactivator PGC-1

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Mechanism of Action of Fibrates on Lipid and Lipoprotein Metabolism

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Cellular and molecular mechanisms of metformin: an overview

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SIRT1 is required for AMPK activation and the beneficial effects of resveratrol on mitochondrial function

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Will All Americans Become Overweight or Obese? Estimating the Progression and Cost of the US Obesity Epidemic

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Insulin-regulated hepatic gluconeogenesis through FOXO1–PGC-1α interaction

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CREB regulates hepatic gluconeogenesis through the coactivator PGC-1

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Calorie Restriction-like Effects of 30 Days of Resveratrol Supplementation on Energy Metabolism and Metabolic Profile in Obese Humans

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Metabolic control of mitochondrial biogenesis through the PGC-1 family regulatory network

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The Coactivator PGC-1 Cooperates with Peroxisome Proliferator-Activated Receptor α in Transcriptional Control of Nuclear Genes Encoding Mitochondrial Fatty Acid Oxidation Enzymes

Vega, R. B., Huss, J. M., & Kelly, D. P. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.5.1868-1876.2000 · Cited by 1,195 · see citing works

Regulation of Muscle Fiber Type and Running Endurance by PPARδ

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HIF-independent regulation of VEGF and angiogenesis by the transcriptional coactivator PGC-1α

Arany, Z., Foo, S.-Y., Ma, Y., Ruas, J. L., Bommi-Reddy, A., Girnun, G., Cooper, M., Laznik, D., Chinsomboon, J., Rangwala, S. M., et al. (2008) · Nature · doi:10.1038/nature06613 · Cited by 1,054 · see citing works

AMP kinase is required for mitochondrial biogenesis in skeletal muscle in response to chronic energy deprivation

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Efficacy of a green tea extract rich in catechin polyphenols and caffeine in increasing 24-h energy expenditure and fat oxidation in humans

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Interdependence of AMPK and SIRT1 for metabolic adaptation to fasting and exercise in skeletal muscle

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Molecular mechanisms of insulin resistance in humans and their potential links with mitochondrial dysfunction

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Activation of the human mitochondrial transcriptionfactor A gene by nuclear respiratory factors: a potential regulatory linkbetween nuclear and mitochondrial gene expression in organellebiogenesis.

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Reduced mitochondrial density and increased IRS-1 serine phosphorylation in muscle of insulin-resistant offspring of type 2 diabetic parents

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Cytokine Stimulation of Energy Expenditure through p38 MAP Kinase Activation of PPARγ Coactivator-1

Puigserver, P., Rhee, J., Lin, J., Wu, Z., Yoon, J. C., Zhang, C.-Y., Krauss, S., Mootha, V. K., Lowell, B. B., & Spiegelman, B. M. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00390-2 · Cited by 732 · see citing works

An autoregulatory loop controls peroxisome proliferator-activated receptor γ coactivator 1α expression in muscle

Handschin, C., Rhee, J., Lin, J., Tarr, P. T., & Spiegelman, B. M. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1232352100 · Cited by 729 · see citing works

Control of mitochondrial transcription specificity factors (TFB1M and TFB2M) by nuclear respiratory factors (NRF-1 and NRF-2) and PGC-1 family coactivators

Gleyzer, N., Vercauteren, K., & Scarpulla, R. C. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.4.1354-1366.2005 · Cited by 711 · see citing works

Activation of AMP-activated protein kinase increases mitochondrial enzymes in skeletal muscle

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ERRα and Gabpa/b specify PGC-1α-dependent oxidative phosphorylation gene expression that is altered in diabetic muscle.

Mootha, V. K., Handschin, C., Arlow, D., Xie, X., St. Pierre, J., Sihag, S., Yang, W., Altshuler, D., Puigserver, P., Patterson, N., et al. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0401401101 · Cited by 688 · see citing works

Regulation of mitochondrial biogenesis in skeletal muscle by CaMK

Wu, H., Kanatous, S. B., Thurmond, F. A., Gallardo, T., Isotani, E., Bassel-Duby, R., & Williams, R. S. (2002) · Science · doi:10.1126/science.1071163 · Cited by 684 · see citing works

The estrogen-related receptor α (ERRα) functions in PPARγ coactivator 1α (PGC-1α)-induced mitochondrial biogenesis

Schreiber, S., Emter, R., Hock, M. B., Knutti, D., Cardenas, J., Podvinec, M., Oakeley, E. J., & Kralli, A. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0308686101 · Cited by 657 · see citing works

Antidiabetic actions of a non-agonist PPARγ ligand blocking Cdk5-mediated phosphorylation

Choi, J. H., Banks, A. S., Kamenecka, T. M., Busby, S. A., Chalmers, M. J., Kumar, N., Kuruvilla, D. S., Shin, Y., He, Y., Bruning, J. B., et al. (2011) · Nature · doi:10.1038/nature10383 · Cited by 541 · see citing works

Exercise-induced mitochondrial biogenesis begins before the increase in muscle PGC-1α expression.

Wright, D. C., Han, D.-H., Garcia-Roves, P. M., Geiger, P. C., Jones, T. E., & Holloszy, J. O. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m606116200 · Cited by 488 · see citing works

Diet and exercise signals regulate SIRT3 and activate AMPK and PGC-1α in skeletal muscle

Palacios, O. M., Carmona, J. J., Michan, S., Chen, K. Y., Manabe, Y., III, J. L. W., Goodyear, L. J., & Tong, Q. (2009) · Aging · doi:10.18632/aging.100075 · Cited by 487 · see citing works

Brief intense interval exercise activates AMPK and p38 MAPK signaling and increases the expression of PGC-1α in human skeletal muscle

Gibala, M. J., McGee, S. L., Garnham, A. P., Howlett, K. F., Snow, R. J., & Hargreaves, M. (2009) · Journal of Applied Physiology · doi:10.1152/japplphysiol.90880.2008 · Cited by 427 · see citing works

β2 Adrenergic Receptor Activation

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NRF-1: a trans-activator of nuclear-encoded respiratory genes in animal cells.

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Polyunsaturated fatty acids of marine origin upregulate mitochondrial biogenesis and induce β-oxidation in white fat

Flachs, P., Horakova, O., Brauner, P., Rossmeisl, M., Pecina, P., Franssen-van Hal, N., Ruzickova, J., Sponarova, J., Drahota, Z., Vlcek, C., et al. (2005) · Diabetologia · doi:10.1007/s00125-005-1944-7 · Cited by 388 · see citing works

Transcriptional activators and coactivators in the nuclear control of mitochondrial function in mammalian cells.

Scarpulla, R. (2002) · Gene · doi:10.1016/s0378-1119(01)00809-5 · Cited by 371 · see citing works

Dietary L-arginine supplementation reduces fat mass in Zucker diabetic fatty rats

Fu, W. J., Haynes, T. E., Kohli, R., Hu, J., Shi, W., Spencer, T. E., Carroll, R. J., Meininger, C. J., & Wu, G. (2005) · The Journal of Nutrition · doi:10.1093/jn/135.4.714 · Cited by 353 · see citing works

Statin-induced myopathy: a review and update

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Calcium Induces Increases in Peroxisome Proliferator-activated Receptor γ Coactivator-1α and Mitochondrial Biogenesis by a Pathway Leading to p38 Mitogen-activated Protein Kinase Activation

Wright, D. C., Geiger, P. C., Han, D.-H., Jones, T. E., & Holloszy, J. O. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m611252200 · Cited by 309 · see citing works

Skeletal muscle NAMPT is induced by exercise in humans

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A Tissue-Specific Coactivator of Steroid Receptors, Identified in a Functional Genetic Screen

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Role of calcium and AMP kinase in the regulation of mitochondrial biogenesis and GLUT4 levels in muscle

Ojuka, E. O. (2004) · Proceedings of The Nutrition Society · doi:10.1079/pns2004339 · Cited by 271 · see citing works

Regulation of the transcriptional coactivator PGC-1 via MAPK-sensitive interaction with a repressor

Knutti, D., Kressler, D., & Kralli, A. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.171184698 · Cited by 271 · see citing works

Role of AMPK in skeletal muscle metabolic regulation and adaptation in relation to exercise

Jørgensen, S. B., Richter, E. A., & Wojtaszewski, J. F. P. (2006) · The Journal of Physiology · doi:10.1113/jphysiol.2006.109942 · Cited by 261 · see citing works

Raising Ca2+ in L6 myotubes mimics effects of exercise on mitochondrial biogenesis in muscle

Ojuka, E., Jones, T. E., Han, D.-H., Chen, M. M., & Holloszy, J. (2003) · The FASEB Journal · doi:10.1096/fj.02-0951com · Cited by 258 · see citing works

Effectiveness of Metformin on Weight Loss in Non-Diabetic Individuals with Obesity

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Opposite effects of statins on mitochondria of cardiac and skeletal muscles: a ‘mitohormesis’ mechanism involving reactive oxygen species and PGC-1

Bouitbir, J., Charles, A.-L., Echaniz-Laguna, A., Kindo, M., Daussin, F., Auwerx, J., Piquard, F., Geny, B., & Zoll, J. (2012) · European Heart Journal · doi:10.1093/eurheartj/ehr224 · Cited by 256 · see citing works

Dual control of mitochondrial biogenesis by sirtuin 1 and sirtuin 3

Brenmoehl, J., & Hoeflich, A. (2013) · Mitochondrion · doi:10.1016/j.mito.2013.04.002 · Cited by 240 · see citing works

SIRT1 Controls the Transcription of the Peroxisome Proliferator-activated Receptor-γ Co-activator-1α (PGC-1α) Gene in Skeletal Muscle through the PGC-1α Autoregulatory Loop and Interaction with MyoD

Amat, R., Planavila, A., Chen, S. L., Iglesias, R., Giralt, M., & Villarroya, F. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.022749 · Cited by 218 · see citing works

A fundamental system of cellular energy homeostasis regulated by PGC-1α

Rohas, L. M., St‐Pierre, J., Uldry, M., Jäger, S., Handschin, C., & Spiegelman, B. M. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0702683104 · Cited by 210 · see citing works

Metformin increases the PGC-1α protein and oxidative enzyme activities possibly via AMPK phosphorylation in skeletal muscle in vivo

Suwa, M., Egashira, T., Nakano, H., Sasaki, H., & Kumagai, S. (2006) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00255.2006 · Cited by 210 · see citing works

Expression of the thermogenic nuclear hormone receptor coactivator PGC-1α is reduced in the adipose tissue of morbidly obese subjects

Semple, R. K., Crowley, V. C., Sewter, C. P., Laudes, M., Christodoulides, C., Considine, R. V., Vidal-Puig, A., & O'Rahilly, S. (2004) · International Journal of Obesity · doi:10.1038/sj.ijo.0802482 · Cited by 203 · see citing works

Regulation by exercise of skeletal muscle content of mitochondria and GLUT4.

Holloszy, J. O. (2008) · PubMed · Cited by 202 · see citing works

Exercise and adrenaline increase PGC‐1α mRNA expression in rat adipose tissue

Sutherland, L., Bomhof, M. R., Capozzi, L., Basaraba, S. A. U., & Wright, D. C. (2009) · The Journal of Physiology · doi:10.1113/jphysiol.2008.165464 · Cited by 201 · see citing works

Estrogen-related Receptor γ Is a Key Regulator of Muscle Mitochondrial Activity and Oxidative Capacity

Rangwala, S. M., Wang, X., Calvo, J. A., Lindsley, L., Zhang, Y., Deyneko, G., Beaulieu, V., Gao, J., Turner, G. M., & Markovits, J. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.125401 · Cited by 192 · see citing works

PGC-1α is coupled to HIF-1α-dependent gene expression by increasing mitochondrial oxygen consumption in skeletal muscle cells

O’Hagan, K., Cocchiglia, S., Zhdanov, A. V., Tambuwala, M. M., Cummins, E. P., Monfared, M. M., Agbor, T. A., Garvey, J., Papkovsky, D. B., Taylor, C. T., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0808801106 · Cited by 191 · see citing works

Subjects With Early-Onset Type 2 Diabetes Show Defective Activation of the Skeletal Muscle PGC-1α/Mitofusin-2 Regulatory Pathway in Response to Physical Activity

Hernández-Alvarez, M. I., Thabit, H., Burns, N., Shah, S., Brema, I., Hatunic, M., Finucane, F., Liesa, M., Chiellini, C., Naon, D., et al. (2010) · Diabetes Care · doi:10.2337/dc09-1305 · Cited by 189 · see citing works

Nitric oxide and AMPK cooperatively regulate PGC-1α in skeletal muscle cells

Lira, V. A., Brown, D. L., Lira, A. K., Kavazis, A. N., Soltow, Q. A., Zeanah, E. H., & Criswell, D. S. (2010) · The Journal of Physiology · doi:10.1113/jphysiol.2010.194035 · Cited by 185 · see citing works

An Increase in Murine Skeletal Muscle Peroxisome Proliferator-Activated Receptor-γ Coactivator-1α (PGC-1α) mRNA in Response to Exercise Is Mediated by β-Adrenergic Receptor Activation

Miura, S., Kawanaka, K., Kai, Y., Tamura, M., Goto, M., Shiuchi, T., Minokoshi, Y., & Ezaki, O. (2007) · Endocrinology · doi:10.1210/en.2006-1646 · Cited by 183 · see citing works

Role of AMPKα2 in basal, training-, and AICAR-induced GLUT4, hexokinase II, and mitochondrial protein expression in mouse muscle

Jørgensen, S. B., Treebak, J. T., Viollet, B., Schjerling, P., Vaulont, S., Wojtaszewski, J. F. P., & Richter, E. A. (2006) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00243.2006 · Cited by 176 · see citing works

Sirtuin 1-mediated Effects of Exercise and Resveratrol on Mitochondrial Biogenesis

Menzies, K. J., Singh, K., Saleem, A., & Hood, D. A. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.431155 · Cited by 167 · see citing works

Leucine modulation of mitochondrial mass and oxygen consumption in skeletal muscle cells and adipocytes

Sun, X., & Zemel, M. B. (2009) · Nutrition & Metabolism · doi:10.1186/1743-7075-6-26 · Cited by 166 · see citing works

Evaluation of the safety and efficacy of sibutramine, orlistat and metformin in the treatment of obesity

Gökçel, A., Gümürdülü, Y., Karakose, H., Ertörer, M. E., Tanaci, N., Tütüncü, N. B., & Guvener, N. D. (2002) · Diabetes Obesity and Metabolism · doi:10.1046/j.1463-1326.2002.00181.x · Cited by 164 · see citing works

Skeletal Muscle-Specific Expression of PGC-1α-b, an Exercise-Responsive Isoform, Increases Exercise Capacity and Peak Oxygen Uptake

Tadaishi, M., Miura, S., Kai, Y., Kano, Y., Oishi, Y., & Ezaki, O. (2011) · PLoS ONE · doi:10.1371/journal.pone.0028290 · Cited by 163 · see citing works

The PPARβ/δ Activator GW501516 Prevents the Down-Regulation of AMPK Caused by a High-Fat Diet in Liver and Amplifies the PGC-1α-Lipin 1-PPARα Pathway Leading to Increased Fatty Acid Oxidation

Barroso, E., Rodríguez‐Calvo, R., Serrano, L., Astudillo, A. M., Balsinde, J., Palomer, X., & Vázquez‐Carrera, M. (2011) · Endocrinology · doi:10.1210/en.2010-1468 · Cited by 162 · see citing works

Improved skeletal muscle oxidative enzyme activity and restoration of PGC-1α and PPARβ/δ gene expression upon rosiglitazone treatment in obese patients with type 2 diabetes mellitus

Mensink, M., Hesselink, M. K. C., Russell, A. P., Schaart, G., Sels, J.-P., & Schrauwen, P. (2007) · International Journal of Obesity · doi:10.1038/sj.ijo.0803567 · Cited by 160 · see citing works

Selected Contribution: Effects of contractile activity on mitochondrial transcription factor A expression in skeletal muscle

Gordon, J. W., Rungi, A. A., Inagaki, H., & Hood, D. A. (2001) · Journal of Applied Physiology · doi:10.1152/jappl.2001.90.1.389 · Cited by 160 · see citing works

Nuclear receptors, mitochondria and lipid metabolism

Alaynick, W. A. (2008) · Mitochondrion · doi:10.1016/j.mito.2008.02.001 · Cited by 157 · see citing works

PGC-1β-Regulated mitochondrial biogenesis and function in myotubes is mediated by NRF-1 and ERRα

Shao, D., Liu, Y., Liu, X., Zhu, L., Cui, Y., Cui, A., Qiao, A., Kong, X., Liu, Y. U., Chen, Q., et al. (2010) · Mitochondrion · doi:10.1016/j.mito.2010.05.012 · Cited by 155 · see citing works

Pioglitazone stimulates AMP-activated protein kinase signalling and increases the expression of genes involved in adiponectin signalling, mitochondrial function and fat oxidation in human skeletal muscle in vivo: a randomised trial

Coletta, D. K., Sriwijitkamol, A., Wajcberg, E., Tantiwong, P., Li, M., Prentki, M., Murthy, M. S., Jenkinson, C. P., Cersósimo, E., Musi, N., et al. (2009) · Diabetologia · doi:10.1007/s00125-008-1256-9 · Cited by 148 · see citing works

Reduced Expression of FOXC2 and Brown Adipogenic Genes in Human Subjects with Insulin Resistance

Yang, X., Enerbäck, S., & Smith, U. (2003) · Obesity Research · doi:10.1038/oby.2003.163 · Cited by 145 · see citing works

PPARδ Agonism Activates Fatty Acid Oxidation via PGC-1α but Does Not Increase Mitochondrial Gene Expression and Function

Kleiner, S., Nguyen-Tran, V., Baré, O., Huang, X., Spiegelman, B., & Wu, Z. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.008797 · Cited by 143 · see citing works

Influence of fish oil on skeletal muscle mitochondrial energetics and lipid metabolites during high-fat diet

Lanza, I. R., Blachnio-Zabielska, A., Johnson, M. L., Schimke, J. M., Jakaitis, D. R., Lebrasseur, N. K., Jensen, M. D., Sreekumaran Nair, K., & Zabielski, P. (2013) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00584.2012 · Cited by 135 · see citing works

Assessing mitochondria biogenesis

Medeiros, D. M. (2008) · Methods · doi:10.1016/j.ymeth.2008.09.026 · Cited by 135 · see citing works

Skeletal Muscle Reprogramming by Activation of Calcineurin Improves Insulin Action on Metabolic Pathways

Ryder, J. W., Bassel‐Duby, R., Olson, E. N., & Zierath, J. R. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m304510200 · Cited by 130 · see citing works

Synergistic effects of leucine and resveratrol on insulin sensitivity and fat metabolism in adipocytes and mice

Bruckbauer, A., Zemel, M. B., Thorpe, T., Akula, M. R., Stuckey, A. C., Osborne, D., Martin, E. B., Kennel, S. J., & Wall, J. S. (2012) · Nutrition & Metabolism · doi:10.1186/1743-7075-9-77 · Cited by 128 · see citing works

Leucine and Calcium Regulate Fat Metabolism and Energy Partitioning in Murine Adipocytes and Muscle Cells

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PGC-1α Integrates Insulin Signaling, Mitochondrial Regulation, and Bioenergetic Function in Skeletal Muscle

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