Cited by 257Adipose Tissue and MetabolismMetabolism, Diabetes, and CancerMuscle Physiology and Disorders

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A role for the transcriptional coactivator PGC-1α in muscle refueling.

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Wende, Adam R., Schaeffer, Paul J., Parker, Glendon J., Zechner, Christoph, Han, Dong-Ho, Chen, May M., Hancock, Chad R., Lehman, John J., Huss, Janice M., McClain, Donald A., Holloszy, John O., Kelly, Daniel P.·2007·Journal of Biological Chemistry

DOI 10.1074/jbc.m707006200

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Abstract

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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Wu, Z., Puigserver, P., Andersson, U., Zhang, C., Adelmant, G., Mootha, V., Troy, A., Cinti, S., Lowell, B., Scarpulla, R. C., et al. (1999) · Cell · doi:10.1016/s0092-8674(00)80611-x · Cited by 4,139
A Flexible System of Enzymatic Analysis
Lowry, O. H., & Passonneau, J. V. (1972) · Elsevier eBooks · doi:10.1016/b978-0-12-457950-7.x5001-3 · Cited by 4,050
A Cold-Inducible Coactivator of Nuclear Receptors Linked to Adaptive Thermogenesis
Puigserver, P., Wu, Z., Park, C. W., Graves, R., Wright, M., & Spiegelman, B. M. (1998) · Cell · doi:10.1016/s0092-8674(00)81410-5 · Cited by 3,864
Nutrient control of glucose homeostasis through a complex of PGC-1α and SIRT1
Rodgers, J. T., Lerin, C., Haas, W., Gygi, S. P., Spiegelman, B. M., & Puigserver, P. (2005) · Nature · doi:10.1038/nature03354 · Cited by 3,160
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Lin, J., Wu, H., Tarr, P. T., Zhang, C.-Y., Wu, Z., Boss, O., Michael, L. F., Puigserver, P., Isotani, E., Olson, E. N., et al. (2002) · Nature · doi:10.1038/nature00904 · Cited by 2,546
The Failing Heart — An Engine Out of Fuel
Neubauer, S. (2007) · New England Journal of Medicine · doi:10.1056/nejmra063052 · Cited by 2,465
Metabolic control through the PGC-1 family of transcription coactivators
Lin, J., Handschin, C., & Spiegelman, B. M. (2005) · Cell Metabolism · doi:10.1016/j.cmet.2005.05.004 · Cited by 2,130
Adaptations of skeletal muscle to endurance exercise and their metabolic consequences
Holloszy, J. O., & Coyle, E. F. (1984) · Journal of Applied Physiology · doi:10.1152/jappl.1984.56.4.831 · Cited by 1,985
Coordinated reduction of genes of oxidative metabolism in humans with insulin resistance and diabetes: Potential role of PGC1 and NRF1
Patti, M. E., Butte, A. J., Crunkhorn, S., Cusi, K., Berria, R., Kashyap, S., Miyazaki, Y., Kohane, I., Costello, M., Saccone, R., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1032913100 · Cited by 1,952
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PGC-1 coactivators: inducible regulators of energy metabolism in health and disease
Finck, B. N. (2006) · Journal of Clinical Investigation · doi:10.1172/jci27794 · Cited by 1,461
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Herzig, S., Long, F., Jhala, U. S., Hedrick, S., Quinn, R., Bauer, A., Rudolph, D., Schutz, G., Yoon, C., Puigserver, P., et al. (2001) · Nature · doi:10.1038/35093131 · Cited by 1,440
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Gerhart‐Hines, Z., Rodgers, J. T., Bare, O., Lerin, C., Kim, S., Mostoslavsky, R., Alt, F. W., Wu, Z., & Puigserver, P. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601633 · Cited by 1,294
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Lehman, J. J., Barger, P. M., Kovacs, A., Saffitz, J. E., Medeiros, D. M., & Kelly, D. P. (2000) · Journal of Clinical Investigation · doi:10.1172/jci10268 · Cited by 1,285
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Baar, K., Wende, A. R., Jones, T. E., Marison, M., Nolte, L. A., Chen, M., Kelly, D. P., & Holloszy, J. O. (2002) · The FASEB Journal · doi:10.1096/fj.02-0367com · Cited by 1,020
Self-citation
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Sandri, M., Lin, J., Handschin, C., Yang, W., Arany, Z. P., Lecker, S. H., Goldberg, A. L., & Spiegelman, B. M. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0607795103 · Cited by 974
PGC-1α Deficiency Causes Multi-System Energy Metabolic Derangements: Muscle Dysfunction, Abnormal Weight Control and Hepatic Steatosis
Leone, T. C., Lehman, J. J., Finck, B. N., Schaeffer, P. J., Wende, A. R., Boudina, S., Courtois, M., Wozniak, D. F., Sambandam, N., Bernal-Mizrachi, C., et al. (2005) · PLoS Biology · doi:10.1371/journal.pbio.0030101 · Cited by 951
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Pilegaard, H., Saltin, B., & Neufer, P. D. (2003) · The Journal of Physiology · doi:10.1113/jphysiol.2002.034850 · Cited by 885
A comparison of three methods of glycogen measurement in tissues
Passonneau, J. V., & Lauderdale, V. R. (1974) · Analytical Biochemistry · doi:10.1016/0003-2697(74)90248-6 · Cited by 735
ERRα and Gabpa/b specify PGC-1α-dependent oxidative phosphorylation gene expression that is altered in diabetic muscle.
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Huss, J. M., Pineda‐Torra, I., Staels, B., Giguère, V., & Kelly, D. P. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.20.9079-9091.2004 · Cited by 498
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Douen, A. G., Ramlal, T., Rastogi, S., Bilan, P. J., Cartee, G. D., Vranić, M., Holloszy, J. O., & Klip, A. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)77362-6 · Cited by 471
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Roach, P. (2002) · Current Molecular Medicine · doi:10.2174/1566524024605761 · Cited by 468
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Schreiber, S., Knutti, D., Brogli, K., Uhlmann, T., & Kralli, A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m212923200 · Cited by 458
Endurance Training in Humans Leads to Fiber Type-Specific Increases in Levels of Peroxisome Proliferator-Activated Receptor-γ Coactivator-1 and Peroxisome Proliferator-Activated Receptor-α in Skeletal Muscle
Russell, A. P., Feilchenfeldt, J. W., Schreiber, S., Praz, M., Crettenand, A., Gobelet, C., Meier, C. A., Bell, D., Kralli, A., Giacobino, J., et al. (2003) · Diabetes · doi:10.2337/diabetes.52.12.2874 · Cited by 451
Diet, muscle glycogen, and endurance performance
Karlsson, J., & Saltin, B. (1971) · Journal of Applied Physiology · doi:10.1152/jappl.1971.31.2.203 · Cited by 440
Cardiac-specific induction of the transcriptional coactivator peroxisome proliferator-activated receptor γ coactivator-1α promotes mitochondrial biogenesis and reversible cardiomyopathy in a developmental stage-dependent manner.
Russell, L. K., Mansfield, C. M., Lehman, J. J., Kovacs, A., Courtois, M., Saffitz, J. E., Medeiros, D. M., Valencik, M. L., McDonald, J. A., & Kelly, D. P. (2004) · Circulation Research · doi:10.1161/01.res.0000117088.36577.eb · Cited by 402
PGC-1α regulates the neuromuscular junction program and ameliorates Duchenne muscular dystrophyPreprint
Handschin, C., Kobayashi, Y. M., Chin, S., Seale, P., Campbell, K. P., & Spiegelman, B. M. (2007) · Genes & Development · doi:10.1101/gad.1525107 · Cited by 365
Effects of low-intensity prolonged exercise on PGC-1 mRNA expression in rat epitrochlearis muscle
Terada, S., Goto, M., Kato, M., Kawanaka, K., Shimokawa, T., & Tabata, I. (2002) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(02)00881-1 · Cited by 354
PGC-1α Coactivates PDK4 Gene Expression via the Orphan Nuclear Receptor ERRα: a Mechanism for Transcriptional Control of Muscle Glucose Metabolism
Wende, A. R., Huss, J. M., Schaeffer, P. J., Giguère, V., & Kelly, D. P. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.24.10684-10694.2005 · Cited by 354
Self-citation
Adaptations of Skeletal Muscle to Prolonged, Intense Endurance Training
Hawley, J. A. (2002) · Clinical and Experimental Pharmacology and Physiology · doi:10.1046/j.1440-1681.2002.03623.x · Cited by 328
Starvation and diabetes increase the amount of pyruvate dehydrogenase kinase isoenzyme 4 in rat heart
Wu, P., Sato, J., Zhao, Y., Jaskiewicz, J. A., POPOV, M. K., & HARRIS, A. R. (1998) · Biochemical Journal · doi:10.1042/bj3290197 · Cited by 310
Tissue-specific regulation of metabolic pathways through the transcriptional coactivator PGC1-α
Puigserver, P. (2005) · International Journal of Obesity · doi:10.1038/sj.ijo.0802905 · Cited by 295
Exercise and gene expression: physiological regulation of the human genome through physical activity
Booth, F. W., Chakravarthy, M. V., & Spangenburg, E. E. (2002) · The Journal of Physiology · doi:10.1113/jphysiol.2002.019265 · Cited by 277
Evidence from transgenic mice that glucose transport is rate-limiting for glycogen deposition and glycolysis in skeletal muscle
Ren, J., Marshall, B. A., Gulve, E. A., Gao, J., Johnson, D. W., Holloszy, J. O., & Mueckler, M. M. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)85395-4 · Cited by 274
Effects of detraining on enzymes of energy metabolism in individual human muscle fibers
Chi, M. M., Hintz, C. S., Coyle, E. F., Martin, W. H., Ivy, J. L., Nemeth, P. M., Holloszy, J. O., & Lowry, O. H. (1983) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.1983.244.3.c276 · Cited by 271
A potential link between muscle peroxisome proliferator- activated receptor-α signaling and obesity-related diabetes
Finck, B. N., Bernal-Mizrachi, C., Han, D. H., Coleman, T., Sambandam, N., LaRiviere, L. L., Holloszy, J. O., Semenkovich, C. F., & Kelly, D. P. (2005) · Cell Metabolism · doi:10.1016/j.cmet.2005.01.006 · Cited by 270
PGC-1α mRNA expression is influenced by metabolic perturbation in exercising human skeletal muscle
Norrbom, J., Sundberg, C. J., Rundqvist, H., Kraus, W. E., Jansson, E., & Gustafsson, T. P. (2004) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00765.2003 · Cited by 263
cDNA Cloning and mRNA Analysis of PGC-1 in Epitrochlearis Muscle in Swimming-Exercised Rats
Goto, M., Terada, S., Kato, M., Katoh, M., Yokozeki, T., Tabata, I., & Shimokawa, T. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.3134 · Cited by 258
Mammalian fuel utilization during sustained exercise
Brooks, G. A. (1998) · Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology · doi:10.1016/s0305-0491(98)00025-x · Cited by 256
Suitability of 2-deoxyglucose for in vitro measurement of glucose transport activity in skeletal muscle
Hansen, P. A., Gulve, E. A., & Holloszy, J. O. (1994) · Journal of Applied Physiology · doi:10.1152/jappl.1994.76.2.979 · Cited by 233
Creatine kinase of rat heart mitochondria. The demonstration of functional coupling to oxidative phosphorylation in an inner membrane-matrix preparation.
Saks, V. A., Kuznetsov, A. V., Kupriyanov, V. V., Miceli, M. V., & Jacobus, W. E. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)39672-2 · Cited by 189
The regulation of carbohydrate and fat metabolism during and after exercise
Holloszy, J. O. (1998) · Frontiers in bioscience · doi:10.2741/a342 · Cited by 180
Self-citation
Regulation of Net Hepatic Glycogenolysis and Gluconeogenesis during Exercise: Impact of Type 1 Diabetes
Petersen, K. F., Price, T. B., & Bergeron, R. (2004) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2004-0408 · Cited by 127
Plasma Glucose Metabolism During Exercise in Humans
Coggan, A. R. (1991) · Sports Medicine · doi:10.2165/00007256-199111020-00003 · Cited by 122
The Organization of Cerebellar Cortical Circuitry Revisited: Implications for Function
BOWER, J. M. (2002) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2002.tb07562.x · Cited by 119
Diminished Hepatic Gluconeogenesis via Defects in Tricarboxylic Acid Cycle Flux in Peroxisome Proliferator-activated Receptor γ Coactivator-1α (PGC-1α)-deficient Mice
Burgess, S. C., Leone, T. C., Wende, A. R., Croce, M. A., Chen, Z., Sherry, A. D., Malloy, C. R., & Finck, B. N. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m600050200 · Cited by 111
Regulation of glucose transport in skeletal muscle 1
Barnard, R. J., & YOUNGREN, J. F. (1992) · The FASEB Journal · doi:10.1096/fasebj.6.14.1426762 · Cited by 100
Skeletal Muscle Triglycerides
Kelley, D. E. (2002) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2002.tb04271.x · Cited by 98
Distinctive Regulatory and Metabolic Properties of Glycogen-targeting Subunits of Protein Phosphatase-1 (PTG, GL, GM/RGl) Expressed in Hepatocytes
Gasa, R., Jensen, P. B., Berman, H. K., Brady, M., DePaoli-Roach, A. A., & Newgard, C. B. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m002427200 · Cited by 87
Skeletal muscle triglycerides: an aspect of regional adiposity and insulin resistance.
Kelley, D. E. (2002) · PubMed · Cited by 84
Hormonal control of glycogen synthase in rat hemidiaphragms. Effects of insulin and epinephrine on the distribution of phosphate between two cyanogen bromide fragments.
Lawrence, J. C., Hiken, J., DePaoli-Roach, A. A., & Roach, P. J. (1983) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)44514-5 · Cited by 79
Enhanced insulin-stimulated glycogen synthesis in response to insulin, metformin or rosiglitazone is associated with increased mRNA expression of GLUT4 and peroxisomal proliferator activator receptor gamma co-activator 1
Al-Khalili, L., Forsgren, M., Kannisto, K., Zierath, J. R., Lönnqvist, F., & Krook, A. (2005) · Diabetologia · doi:10.1007/s00125-005-1741-3 · Cited by 78
Muscle glycogen and metabolic regulation
Hargreaves, M. (2004) · Proceedings of The Nutrition Society · doi:10.1079/pns2004344 · Cited by 72
Measurement of gluconeogenesis in exercising men by mass isotopomer distribution analysis
Trimmer, J. K., Schwarz, J., Casazza, G. A., Horning, M. A., Rodriguez, N., & Brooks, G. A. (2002) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01050.2001 · Cited by 58
Carbohydrate and exercise
Burke, L. M., & Hawley, J. A. (1999) · Current Opinion in Clinical Nutrition and Metabolic Care · doi:10.1097/00075197-199911000-00015 · Cited by 57
Carbohydrate metabolism during prolonged exercise and recovery: interactions between pyruvate dehydrogenase, fatty acids, and amino acids
Mourtzakis, M., Saltin, B., Graham, T. E., & Pilegaard, H. (2006) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00571.2005 · Cited by 55
Regulation of glycogen synthase activity and phosphorylation by exercise
Nielsen, J. N., & Wojtaszewski, J. F. P. (2004) · Proceedings of The Nutrition Society · doi:10.1079/pns2004348 · Cited by 52
Transcription of the rat skeletal muscle hexokinase II gene is increased by acute exercise
O'Doherty, R. M., Bracy, D. P., Granner, D. K., & Wasserman, D. H. (1996) · Journal of Applied Physiology · doi:10.1152/jappl.1996.81.2.789 · Cited by 50
An Epitope Proximal to the Carboxyl Terminus of the α-Subunit is Located near the Lobe Tips of the Phosphorylase Kinase Hexadecamer
Wilkinson, D. A., Marion, T. N., Tillman, D. M., Norcum, M. T., Hainfeld, J. F., Seyer, J. M., & Carlson, G. M. (1994) · Journal of Molecular Biology · doi:10.1006/jmbi.1994.1051 · Cited by 48
Membrane cholesterol extraction decreases Na+ transport in A6 renal epithelia
Balut, C., Steels, P., Radu, M., Ameloot, M. M., Driessche, W. V., & Jans, D. (2005) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00184.2005 · Cited by 45
Highly controlled gene expression using combinations of a tissue-specific promoter, recombinant adenovirus and a tetracycline-regulatable transcription factor
Ghersa, P., Gobert, R. P., Sattonnet-Roche, P., Richards, C., Pich, E., & van Huijsduijnen, R. H. (1998) · Gene Therapy · doi:10.1038/sj.gt.3300713 · Cited by 44
Cellular mechanism of the insulin-like effect of growth hormone in adipocytes. Rapid translocation of the HepG2-type and adipocyte/muscle glucose transporters
Tanner, J.-P., Leingang, K. A., Mueckler, M. M., & Glenn, K. C. (1992) · Biochemical Journal · doi:10.1042/bj2820099 · Cited by 29

Flagged first, then by citations

Research works printed but not linked: 6

Pilegaard, 2003, J. Phys., 546, 851
Terada, 2004, Am. J. Physiol., 286, E208
Taylor, 2005, Am. J. Physiol., 289, E960
Nielsen, 2003, Acta Psych. Scand., 178, 309
Mortensen, 2006, Am. J. Physiol., 4, E807
Koval, 1998, Am. J. Physiol., 274, E304

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See all 257

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: Wende, Adam R.
Parker, Glendon J.
Zechner, Christoph
Hancock, Chad R.
McClain, Donald A.
Kelly, Daniel P.
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 2007-12
Volume: 282
Issue: 50
Pages: 36642-36651
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1074/jbc.m707006200
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: cc-by-nc-nd
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 4708 d)
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 (medical) › 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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A role for the transcriptional coactivator PGC-1α in muscle refueling.

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