A role for the transcriptional coactivator PGC-1α in muscle refueling.
Open accessAbstract
The transcriptional coactivator peroxisome proliferator-activated receptor gamma coactivator-1alpha (PGC-1alpha) has been identified as an inducible regulator of mitochondrial function. Skeletal muscle PGC-1alpha expression is induced post-exercise. Therefore, we sought to determine its role in the regulation of muscle fuel metabolism. Studies were performed using conditional, muscle-specific, PGC-1alpha gain-of-function and constitutive, generalized, loss-of-function mice. Forced expression of PGC-1alpha increased muscle glucose uptake concomitant with augmentation of glycogen stores, a metabolic response similar to post-exercise recovery. Induction of muscle PGC-1alpha expression prevented muscle glycogen depletion during exercise. Conversely, PGC-1alpha-deficient animals exhibited reduced rates of muscle glycogen repletion post-exercise. PGC-1alpha was shown to increase muscle glycogen stores via several mechanisms including stimulation of glucose import, suppression of glycolytic flux, and by down-regulation of the expression of glycogen phosphorylase and its activating kinase, phosphorylase kinase alpha. These findings identify PGC-1alpha as a critical regulator of skeletal muscle fuel stores.
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High-level overexpression of PGC-1α may reduce insulin sensitivity via reduced glycolysis and/or glucose oxidation or myofibrillar disruption/myopathy, potentially limiting exercise tolerance.
“By contrast, highlevel overexpression of PGC-1␣ may actually reduce insulin sensitivity via reduced glycolysis and/or glucose oxidation (265) or myofibrillar disruption/myopathy, potentially limiting exercise tolerance.”
From The role of mitochondria in the pathogenesis of type 2 diabetes (2010) · cites this paper as [265]
In these animals, both muscle glucose uptake and glycogen deposition were increased.
“In these animals, both muscle glucose uptake and glycogen deposition were increased.”
From The role of mitochondria in the pathogenesis of type 2 diabetes (2010) · cites this paper as [265]
Inducible overexpression of PGC-1α in skeletal muscle results in increased mitochondrial density and a robust increase in expression of OXPHOS genes and genes necessary for fatty acid oxidation.
“Inducible overexpression of PGC-1␣ in skeletal muscle ( 265) results in increased mitochondrial density and a robust increase in expression of OXPHOS genes and genes necessary for fatty acid oxidation.”
From The role of mitochondria in the pathogenesis of type 2 diabetes (2010) · cites this paper as [265]
Although low-intensity exercise performance did not differ in this model, high-performance exercise was impaired, in parallel with failure to mobilize stored glycogen.
“Although low-intensity exercise performance did not differ in this model, high-performance exercise was impaired, in parallel with failure to mobilize stored glycogen.”
From The role of mitochondria in the pathogenesis of type 2 diabetes (2010) · cites this paper as [265]
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RetractedMolecular Mechanisms Underlying Cardiac Adaptation to Exercise
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“Targeted disruption of PGC-1a and the related PGC-1b in skeletal muscle markedly alters mitochondrial function and diminishes exercise performance (Wende et al., 2007; Zechner et al., 2010).”
Zechner, C., Lai, L., Zechner, J. F., Geng, T., Yan, Z., Rumsey, J. W., Collia, D., Chen, Z., Wozniak, D. F., Leone, T. C., et al. (2010) · Cell Metabolism · doi:10.1016/j.cmet.2010.11.008 · Cited by 274 · see citing works
“SDH stains were performed as described previously (Wende et al., 2007).”
BackgroundMethodFerraro, E., Giammarioli, A. M., Chiandotto, S., Spoletini, I., & Rosano, G. M. C. (2014) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5773 · Cited by 265 · see citing works
Mechanisms Modulating Skeletal Muscle Phenotype
Blaauw, B., Schiaffino, S., & Reggiani, C. (2013) · Comprehensive physiology · doi:10.1002/cphy.c130009 · Cited by 278 · see citing works
PGC-1 coactivators and skeletal muscle adaptations in health and disease
Arany, Z. P. (2008) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2008.07.018 · Cited by 244 · see citing works
PGC-1α-mediated adaptations in skeletal muscle
Olesen, J., Kiilerich, K., & Pilegaard, H. (2010) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-010-0834-0 · Cited by 244 · see citing works
“PGC-1α-mediated regulation also affects skeletal muscle glycogen levels, because glycogen levels were shown to be reduced in PGC-1α KO mice [32] and be elevated in PGC1α overexpression mice [7, 63].”
BackgroundInfluentialBenton, C. R., Nickerson, J. G., Lally, J., Han, X.-X., Holloway, G. P., Glatz, J. F. C., Luiken, J. J. F. P., Graham, T. E., Heikkila, J. J., & Bonen, A. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m704332200 · Cited by 214 · see citing works
Insulin-Like Growth Factor I Receptor Signaling Is Required for Exercise-Induced Cardiac Hypertrophy
Kim, J., Wende, A. R., Sena, S., Theobald, H. A., Soto, J. E., Sloan, C., Wayment, B. E., Litwin, S. E., Holzenberger, M., LeRoith, D., et al. (2008) · Molecular Endocrinology · doi:10.1210/me.2008-0265 · Cited by 215 · see citing works
“We therefore determined levels of peroxisome proliferator-activated receptor- coactivator-1 (PGC-1 ), which mediates the exercise-induced increase in mitochondrial function in the heart (17) and postexercise glycogen accumulation in skeletal muscle (21).”
BackgroundMethodRegulation by exercise of skeletal muscle content of mitochondria and GLUT4.
Holloszy, J. O. (2008) · PubMed · Cited by 202 · see citing works
p53 Improves Aerobic Exercise Capacity and Augments Skeletal Muscle Mitochondrial DNA Content
Park, J., Wang, P., Matsumoto, T., Sung, H. J., Ma, W., Choi, J. W., Anderson, S. A., Leary, S. C., Balaban, R. S., Kang, J., et al. (2009) · Circulation Research · doi:10.1161/circresaha.109.205310 · Cited by 200 · see citing works
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
“Although recent studies have identified an important physiological role of PGC-1 in skeletal muscle responses to exercise (19, 20) the underlying mechanisms remain unclear.”
BackgroundLuo, Z., Ma, L., Zhao, Z., He, H., Yang, D., Feng, X., Ma, S., Chen, X., Zhu, T., Cao, T., et al. (2011) · Cell Research · doi:10.1038/cr.2011.205 · Cited by 191 · 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
“…both GLUT4 expression and mitochondrial biogenesis can be regulated by PGC-1α (Michael et al. 2001; Handschin et al. 2003; Handschin et al. 2007; Wende et al. 2007), and AMPK-dependent signalling induces PGC-1α expression and activation (Zong et al. 2002; Jäger et al. 2007), our central…”
BackgroundGao, S., McMillan, R. P., Zhu, Q., Lopaschuk, G. D., Hulver, M. W., & Butler, A. A. (2015) · Molecular Metabolism · doi:10.1016/j.molmet.2015.01.005 · Cited by 191 · see citing works
Dominy, J. E., Lee, Y., Gerhart‐Hines, Z., & Puigserver, P. (2009) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2009.11.023 · Cited by 192 · see citing works
“The second proposed mechanism involves a PGC-1α-induced increase in the expression of pyruvate dehydrogenase kinase-4 [16,19,20], a negative regulator of pyruvate dehydrogenase, which abates the entry of glucose-derived pyruvate into the TCA cycle.”
BackgroundInfluentialRangwala, 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
Bishop, D. J., Granata, C., & Eynon, N. (2013) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.10.012 · Cited by 191 · see citing works
“, mitochondrial content) should be coupled with measurements of mitochondrial function to more accurately determine whether the observed changes are adaptive or maladaptive [22].”
BackgroundPhilp, A., Chen, A., Lan, D., Meyer, G. A., Murphy, A. N., Knapp, A. E., Olfert, I. M., McCurdy, C. E., Marcotte, G. R., Hogan, M. C., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.261685 · Cited by 184 · see citing works
Tadaishi, M., Miura, S., Kai, Y., Kano, Y., Oishi, Y., & Ezaki, O. (2011) · PLoS ONE · doi:10.1371/journal.pone.0028290 · Cited by 164 · see citing works
“Regarding mechanisms of decreased carbohydrate utilization in skeletal muscles during exercise in PGC-1α-b transgenic mice, inhibition of glycogenolysis and glycolysis was indicated. There was no increase in blood lactate concentration in PGC-1α-b transgenic mice at exhaustion, suggesting that muscle glycogen usage wa…”
MethodPGC-1α, glucose metabolism and type 2 diabetes mellitus
Wu, H., Deng, X., Shi, Y., Su, Y., Wei, J., & Duan, H. (2016) · Journal of Endocrinology · doi:10.1530/joe-16-0021 · Cited by 157 · see citing works
Pharmacotherapy of type 2 diabetes: An update and future directions
DeMarsilis, A. J., Reddy, N., Boutari, C., Filippaios, A., Sternthal, E., Katsiki, N., & Mantzoros, C. S. (2022) · Metabolism · doi:10.1016/j.metabol.2022.155332 · Cited by 161 · see citing works
Sarcopenic obesity: molecular clues to a better understanding of its pathogenesis?
Kob, R., Bollheimer, L. C., Bertsch, T., Fellner, C., Djukic, M., Sieber, C. C., & Fischer, B. E. (2015) · Biogerontology · doi:10.1007/s10522-014-9539-7 · Cited by 151 · see citing works
“Transcription factor PGC-1a decreases ROS formation (St-Pierre et al. 2006), equilibrates lipid oxidation and synthesis with direct effects on IMCL levels (Espinoza et al. 2010) and promotes mitochondrial biogenesis (Wende et al. 2007).”
BackgroundMiura, S., Kai, Y., Kamei, Y., & Ezaki, O. (2008) · Endocrinology · doi:10.1210/en.2008-0466 · Cited by 150 · see citing works
Maurya, S. K., Bal, N. C., Sopariwala, D. H., Pant, M., Rowland, L. A., Shaikh, S. A., & Periasamy, M. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.636878 · Cited by 146 · see citing works
Normal adaptations to exercise despite protection against oxidative stress
Higashida, K., Kim, S. H., Higuchi, M., Holloszy, J. O., & Han, D.-H. (2011) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00655.2010 · Cited by 148 · see citing works
The nuclear receptor PPARβ/δ programs muscle glucose metabolism in cooperation with AMPK and MEF2
Gan, Z., Burkart-Hartman, E. M., Han, D.-H., Finck, B., Leone, T. C., Smith, E. Y., Ayala, J. E., Holloszy, J., & Kelly, D. P. (2011) · Genes & Development · doi:10.1101/gad.178434.111 · Cited by 138 · see citing works
“…activity of the PPARs is regulated at multiple levels, including availability of activating ligands (endogenous FA/lipid moieties) and coactivators such as PPARg coactivator-1a (PGC-1a) (Desvergne and Wahli 1999; Vega et al. 2000; Wende et al. 2007; Madrazo and Kelly 2008; Schupp and Lazar 2010).”
Self-citationSummermatter, S., Santos, G., Pérez‐Schindler, J., & Handschin, C. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1212976110 · Cited by 137 · see citing works
Mitochondrial turnover in the heart
Gottlieb, R. A., & Gustafsson, Å. B. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2010.11.017 · Cited by 135 · see citing works
“Overexpression of PGC1α is sufficient to drive mitochondrial biogenesis [7].”
BackgroundSkeletal Muscle Abnormalities in Heart Failure
Kinugawa, S., Takada, S., Matsushima, S., Okita, K., & Tsutsui, H. (2015) · International Heart Journal · doi:10.1536/ihj.15-108 · Cited by 136 · see citing works
Gouspillou, G., Sgarioto, N., Norris, B. A., Barbat‐Artigas, S., Aubertin‐Leheudre, M., Morais, J. A., Burelle, Y., Taivassalo, T., & Hepple, R. T. (2014) · PLoS ONE · doi:10.1371/journal.pone.0103044 · Cited by 133 · 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
Agudelo, L. Z., Ferreira, D. M. S., Dadvar, S., Červenka, I., Ketscher, L., Izadi, M., Zhengye, L., Furrer, R., Handschin, C., Venckūnas, T., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-10712-0 · Cited by 127 · see citing works
Exercise-induced skeletal muscle signaling pathways and human athletic performance
Camera, D. M., Smiles, W. J., & Hawley, J. A. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.02.007 · Cited by 128 · see citing works
PGC-1α is Dispensable for Exercise-Induced Mitochondrial Biogenesis in Skeletal Muscle
Rowe, G. C., El‐Khoury, R., Patten, I. S., Rustin, P., & Arany, Z. P. (2012) · PLoS ONE · doi:10.1371/journal.pone.0041817 · Cited by 127 · see citing works
“PGC-1a potently induces mitochondrial biogenesis in skeletal muscle [11,12,13], and PGC-1a expression in skeletal muscle is strongly induced by exercise.”
BackgroundSarcolipin Signaling Promotes Mitochondrial Biogenesis and Oxidative Metabolism in Skeletal Muscle
Maurya, S. K., Herrera, J. L., Sahoo, S. K., Reis, F. C. G., Vega, R. B., Kelly, D. P., & Periasamy, M. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.08.036 · Cited by 129 · see citing works
“The fiber typing was done using the antibodies MHC-I (red, BA-D5), MHC-IIA (yellow, 2F7), MHC2x (black, unstained), and MHC2b (green, 10F5) from Developmental Studies Hybridoma Bank (East Iowa City, IA) (Wende et al., 2007).”
MethodMechanisms by Which Skeletal Muscle Myokines Ameliorate Insulin Resistance
Balakrishnan, R., & Thurmond, D. C. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23094636 · Cited by 132 · see citing works
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The many roles of PGC-1α in muscle — recent developments
Chan, M. C., & Arany, Z. P. (2014) · Metabolism · doi:10.1016/j.metabol.2014.01.006 · Cited by 125 · see citing works
“Conversely, PGC-1α KO mice have reduced basal glycogen storage, delayed replenishment of glycogen stores after exercise, and therefore reduced exercise capacity due to insufficient glycogen available during exercise[36].”
BackgroundInfluentialOlesen, J., Gliemann, L., Biensø, R., Schmidt, J., Hellsten, Y., & Pilegaard, H. (2014) · The Journal of Physiology · doi:10.1113/jphysiol.2013.270256 · Cited by 119 · see citing works
“…muscle of young mice (Leick et al. 2008; Geng et al. 2010), other studies have emphasized a role of PGC-1α in basal mitochondrial function (Lin et al. 2002, 2004; Handschin et al. 2007; Wende et al. 2007) and exercise training-induced mitochondrial adaptations (Geng et al. 2010; Leick et al. 2010).”
BackgroundThe metabolic modulator PGC-1α in cancer.
Bost, F., & Kaminski, L. (2019) · Europe PMC (PubMed Central) · Cited by 119 · see citing works
Summermatter, S., Baum, O., Santos, G., Hoppeler, H. H., & Handschin, C. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.145995 · Cited by 114 · see citing works
Endurance capacity of mice selectively bred for high voluntary wheel running
Meek, T. H., Lonquich, B. P., Hannon, R. M., & Garland, T. (2009) · Journal of Experimental Biology · doi:10.1242/jeb.028886 · Cited by 114 · see citing works
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The PGC-1 cascade as a therapeutic target for heart failure
Schilling, J. D., & Kelly, D. P. (2010) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2010.09.021 · Cited by 105 · see citing works
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The role of PGC‐1 coactivators in aging skeletal muscle and heart
Dillon, L. M., Rebelo, A. P., & Moraes, C. T. (2012) · IUBMB Life · doi:10.1002/iub.608 · Cited by 116 · see citing works
Leick, L., Fentz, J., Biensø, R. S., Knudsen, J. G., Jeppesen, J. F., Kiens, B., Wojtaszewski, J. F. P., & Pilegaard, H. (2010) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00648.2009 · Cited by 101 · see citing works
Coordination of mitochondrial biogenesis by PGC-1α in human skeletal muscle: A re-evaluation
Islam, H., Edgett, B. A., & Gurd, B. J. (2018) · Metabolism · doi:10.1016/j.metabol.2017.11.001 · Cited by 99 · see citing works
PGC-1α Improves Glucose Homeostasis in Skeletal Muscle in an Activity-Dependent Manner
Summermatter, S., Shui, G., Maag, D., Santos, G., Wenk, M. R., & Handschin, C. (2012) · Diabetes · doi:10.2337/db12-0291 · Cited by 96 · see citing works
Trausch‐Azar, J. S., Leone, T. C., Kelly, D. P., & Schwartz, A. L. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.131615 · Cited by 92 · see citing works
Benton, C. R., Wright, D. C., & Bonen, A. (2008) · Applied Physiology, Nutrition, and Metabolism · doi:10.1139/h08-074 · Cited by 91 · see citing works
Cardiac adaptation to exercise training in health and disease
Seo, D. Y., Kwak, H., Kim, A. H., Park, S. H., Heo, J., Kim, H. K., Ko, J. R., Lee, S. J., Bang, H. S., Sim, J. W., et al. (2019) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-019-02266-3 · Cited by 91 · see citing works
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Mitochondrial remodeling: Rearranging, recycling, and reprogramming
Gottlieb, R. A., & Bernstein, D. (2016) · Cell Calcium · doi:10.1016/j.ceca.2016.04.006 · Cited by 86 · see citing works
“Overexpression of PGC-1α is sufficient to drive mitochondrial biogenesis (56).”
BackgroundRegulation of Mitochondrial Biogenesis and GLUT4 Expression by Exercise
Holloszy, J. O. (2011) · Comprehensive physiology · doi:10.1002/cphy.c100052 · Cited by 96 · see citing works
Regulation of Hypoxia-Inducible Genes by PGC-1α
Shoag, J., & Arany, Z. (2010) · Arteriosclerosis, Thrombosis, and Vascular Biology · doi:10.1161/atvbaha.108.181636 · Cited by 96 · see citing works
Supruniuk, E., Mikłosz, A., & Chabowski, A. (2017) · Frontiers in Physiology · doi:10.3389/fphys.2017.00923 · Cited by 83 · see citing works
“The concomitant growth in cellular PGC-1α and FAT/CD36 amount was also confirmed in other studies with skeletal musclerestrictedmurine PGC-1α transgenic models (Wende et al., 2007; Choi et al., 2008).”
ResultImmune and Neuroprotective Effects of Physical Activity on the Brain in Depression
Phillips, C., & Fahimi, A. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00498 · Cited by 83 · see citing works
“…that enable cells modulate mitochondrial biogenesis, cellular respiration rates, and energy substrate uptake and utilization—changes that are particularly important for contractile and metabolic adaptations in skeletal muscle (Puigserver and Spiegelman, 2003; Wende et al., 2007; Scarpulla, 2008).”
BackgroundPGC-1α in Disease: Recent Renal Insights into a Versatile Metabolic Regulator
Chambers, J. M., & Wingert, R. A. (2020) · Cells · doi:10.3390/cells9102234 · Cited by 77 · see citing works
“This relationship between PGC-1α and glucose in skeletal muscles is extended to the process of glucose disposal [30,36].”
BackgroundExercise-induced PGC-1α transcriptional factors in skeletal muscle
Jung, S., & Kim, K. (2014) · Integrative Medicine Research · doi:10.1016/j.imr.2014.09.004 · Cited by 76 · see citing works
Wende, A. R., Schell, J. C., Ha, C., Pepin, M. E., Khalimonchuk, O., Schwertz, H., Pereira, R. O., Brahma, M. K., Tuinei, J., Contreras‐Ferrat, A. E., et al. (2020) · Diabetes · doi:10.2337/db19-1057 · Cited by 75 · see citing works
Oldham, S. (2011) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2010.11.002 · Cited by 75 · see citing works
“PGC-1 controls mitochondrial biogenesis and functions in a necessary and sufficient fashion that is essential for cardiac physiology [74].”
BackgroundMultifaceted roles of miR-1s in repressing the fetal gene program in the heart
Wei, Y., Peng, S., Wu, M., Sachidanandam, R., Tu, Z., Zhang, S., Falce, C., Sobie, E. A., Lebeche, D., & Zhao, Y. B. (2014) · Cell Research · doi:10.1038/cr.2014.12 · Cited by 72 · see citing works
Bonen, A. (2009) · Applied Physiology, Nutrition, and Metabolism · doi:10.1139/h09-008 · Cited by 70 · see citing works
Xu, R., Andrés‐Mateos, E., Mejı́as, R., MacDonald, E. M., Leinwand, L. A., Merriman, D. K., Fink, R., & Cohn, R. D. (2013) · Experimental Neurology · doi:10.1016/j.expneurol.2013.01.005 · Cited by 67 · see citing works
“By activating Nrf-1 and MEF-2A, PGC-1α coordinates the increase of GLUT4, which is associated with enhanced insulin-stimulated glucose transport (Baar et al., 2003; Wende et al., 2007).”
BackgroundPGC-1α and exercise intensity dependent adaptations in mouse skeletal muscle
Brandt, N., Dethlefsen, M. M., Bangsbo, J., & Pilegaard, H. (2017) · PLoS ONE · doi:10.1371/journal.pone.0185993 · Cited by 68 · see citing works
Regulatory circuitry of TWEAK‐Fn14 system and PGC‐1α in skeletal muscle atrophy program
Hindi, S. M., Mishra, V. K., Bhatnagar, S., Tajrishi, M. M., Ogura, Y., Yan, Z., Burkly, L. C., Zheng, T. S., & Kumar, A. (2013) · The FASEB Journal · doi:10.1096/fj.13-242123 · Cited by 68 · see citing works
Role of PGC-1α in exercise and fasting-induced adaptations in mouse liver
Haase, T. N., Ringholm, S., Leick, L., Biensø, R. S., Kiilerich, K., Johansen, S., Nielsen, M. M., Wojtaszewski, J. F., Hidalgo, J., Pedersen, P. A., et al. (2011) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00775.2010 · Cited by 66 · see citing works
García, M., Pujol, A., Ruzo, A., Riu, E., Ruberte, J., Arbós, A., Serafin, A. M., Albella, B., Felíu, J. E., & Bosch, F. (2009) · PLoS Genetics · doi:10.1371/journal.pgen.1000615 · Cited by 66 · see citing works
“Moreover, PGC-1a up-regulation was probably responsible for the increased expression of GLUT-4 and HK-II in skeletal muscle of Pfkm mice [28].”
BackgroundMitoTimer: a novel protein for monitoring mitochondrial turnover in the heart
Gottlieb, R. A., & Stotland, A. B. (2014) · Journal of Molecular Medicine · doi:10.1007/s00109-014-1230-6 · Cited by 63 · see citing works
Margolis, L. M., & Pasiakos, S. M. (2013) · Advances in Nutrition · doi:10.3945/an.113.004572 · Cited by 63 · see citing works
Skeletal muscle and beyond: the role of exercise as a mediator of systemic mitochondrial biogenesis
Little, J. P., Safdar, A., Benton, C. R., & Wright, D. C. (2011) · Applied Physiology, Nutrition, and Metabolism · doi:10.1139/h11-076 · Cited by 62 · see citing works
Targets and delivery methods for therapeutic angiogenesis in peripheral artery disease
Ouma, G. O., Jonas, R., Usman, M. H., & Mohler, E. R. (2012) · Vascular Medicine · doi:10.1177/1358863x12438270 · Cited by 55 · see citing works
Muscle–brain crosstalk mediated by exercise-induced myokines - insights from experimental studies
Kostka, M., Morys, J., Małecki, A., & Nowacka-Chmielewska, M. M. (2024) · Frontiers in Physiology · doi:10.3389/fphys.2024.1488375 · Cited by 68 · see citing works
Takikita, S., Schreiner, C., Baum, R., Xie, T., Ralston, E., Plotz, P. H., & Raben, N. (2010) · PLoS ONE · doi:10.1371/journal.pone.0015239 · Cited by 60 · see citing works
“This increase in muscle glycogen stores in skeletal muscle of PGC-1a transgenic mice was also due to the inhibition of glycolysis and down-regulation of glycogen phosphorylase, the enzyme responsible for the degradation of glycogen in the cytoplasm [37].”
BackgroundEspinoza, D., Boros, L. G., Crunkhorn, S., Gami, H., & Patti, M. (2009) · The FASEB Journal · doi:10.1096/fj.09-133728 · Cited by 60 · see citing works
“The net effect of PGC-1 activity in skeletal muscle is to increase mitochondrial biogenesis and oxidative phosphorylation (11), promote fiber type switching to more oxidative type I, IIA (6), or IIX fibers (7), and increase glucose uptake and glycogen storage (12), mediated in part via increased expression of the gluc…”
BackgroundWarren, B. E., Lou, P., Lucchinetti, E., Zhang, L., Clanachan, A. S., Affolter, A., Hersberger, M., Zaugg, M., & Lemieux, H. (2014) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00511.2013 · Cited by 55 · see citing works
Son, J. S., Chae, S. A., Wang, H., Chen, Y., Iniguez, A. B., de Avila, J. M., Jiang, Z., Zhu, M.-J., & Du, . (2020) · Cell Reports · doi:10.1016/j.celrep.2020.108461 · Cited by 56 · see citing works
“…is enhanced by endurance exercise training, which stimulates mitochondrial biogenesis and switches muscle fiber type composition (Lin et al., 2002; Wende et al., 2007) that is accompanied with switching from carbohydrates to lipids as the major source of energy during endurance exercise (Cantó…”
BackgroundLeMoine, C. M. R., Craig, P. M., Dhekney, K., Kim, J. J., & McClelland, G. B. (2009) · Journal of Comparative Physiology B · doi:10.1007/s00360-009-0398-5 · Cited by 57 · see citing works
“Besides its role in regulating mitochondrial content, PGC-1 has recently been associated with other homeostatic responses in muscles, including orchestrating reestablishment of glycogen stores, and regulating fatty acid oxidation (Lee et al. 2006; Wende et al. 2007 ); both crucial for skeletal muscle recovery from exe…”
BackgroundPost-natal induction of PGC-1α protects against severe muscle dystrophy independently of utrophin
Chan, M. C., Rowe, G. C., Raghuram, S., Patten, I. S., Farrell, C., & Arany, Z. P. (2014) · Skeletal Muscle · doi:10.1186/2044-5040-4-2 · Cited by 57 · see citing works
Davis, R. V. N., Lamont, S., Rothschild, M., Persia, M., Ashwell, C., & Schmidt, C. (2015) · PLoS ONE · doi:10.1371/journal.pone.0122525 · Cited by 56 · see citing works
“Peroxisome proliferator-activated receptor γ co-activator 1-α (PPARGC1A) is a transcriptional co-activator enriched in the D6 Ross 708 samples that promotes myoblast proliferation, mitochondrial biogenesis, and lipid transport, along with fatty acid and glucose oxidation [40–42].”
Background
- Authors
- Wende, A. R., Schaeffer, P. J., Parker, G. J., Zechner, C., Han, D.-H., Chen, M. M., Hancock, C. R., Lehman, J. J., Huss, J. M., McClain, D. A., Holloszy, J. O., & Kelly, D. P.
- Affiliations
- Washington University in St. Louis (US)
- University of Utah (US)
- Corresponding author
- Kelly, Daniel P.
- ORCID
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2007-12
- Volume
- 282
- Issue
- 50
- Pages
- 36642-36651
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2130246533
- Cited by
- 257
- References
- 69
- Citations by year
- 2026: 2 · 2025: 8 · 2024: 5 · 2023: 6 · 2022: 7 · 2021: 9 · 2020: 10 · 2019: 10 · 2018: 15 · 2017: 18 · 2016: 14 · 2015: 10 · 2014: 26 · 2013: 23 · 2012: 17
- FWCI
- 13.42
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (5p60dk020579-35)
- National Institute on Aging (R01AG000425)
- National Heart, Lung, and Blood Institute (T32HL007275)
- National Institute of Diabetes and Digestive and Kidney Diseases (R01DK045416, P60-DK-020579, P30DK056341, P30DK052574, R01DK074700)
- Topics
- Health Sciences › Medicine › Physiology › Adipose Tissue and Metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Keywords
- PGC-1α, glycogen stores, glucose uptake, post-exercise recovery, mitochondrial biogenesis, glycogen phosphorylase, glycolytic flux, glucose transport
- MeSH terms
- Peroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alpha, Animals, Glucose, Glycogen, Mice, Transgenic, Mitochondria, Muscle, Muscle Proteins, Phosphorylase Kinase, Transcription Factors, Trans-Activators, Muscle, Skeletal, Glycogen Phosphorylase, Mice
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