Cited by 1,222Peroxisome Proliferator-Activated ReceptorsMetabolism, Diabetes, and CancerAdipose Tissue and Metabolism

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AMPK and PPARδ Agonists Are Exercise Mimetics

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Narkar, Vihang A., Downes, Michael, Yu, Ruth T., Embler, Emi, Wang, Yong-Xu, Banayo, Ester, Mihaylova, Maria M., Nelson, Michael C., Zou, Yuhua, Juguilon, Henry, Kang, Heonjoong, Shaw, Reuben J., Evans, Ronald M.·2008·Cell

DOI 10.1016/j.cell.2008.06.051PMC PMC2706130

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Abstract

The benefits of endurance exercise on general health make it desirable to identify orally active agents that would mimic or potentiate the effects of exercise to treat metabolic diseases. Although certain natural compounds, such as reseveratrol, have endurance-enhancing activities, their exact metabolic targets remain elusive. We therefore tested the effect of pathway-specific drugs on endurance capacities of mice in a treadmill running test. We found that PPARbeta/delta agonist and exercise training synergistically increase oxidative myofibers and running endurance in adult mice. Because training activates AMPK and PGC1alpha, we then tested whether the orally active AMPK agonist AICAR might be sufficient to overcome the exercise requirement. Unexpectedly, even in sedentary mice, 4 weeks of AICAR treatment alone induced metabolic genes and enhanced running endurance by 44%. These results demonstrate that AMPK-PPARdelta pathway can be targeted by orally active drugs to enhance training adaptation or even to increase endurance without exercise.

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Molinari, F., Pin, F., Gorini, S., Chiandotto, S., Pontecorvo, L., Penna, F., Rizzuto, E., Pisu, S., Musarò, A., Costelli, P., et al. (2017) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.12226 · Cited by 88
Metabolic intermediates selectively stimulate transcription factor interaction and modulate phosphate and purine pathwaysPreprint
Pinson, B., Vaur, S., Sagot, I., Coulpier, F., Lemoine, S., & Daignan‐Fornier, B. (2009) · Genes & Development · doi:10.1101/gad.521809 · Cited by 86
Activation of the AMP-Activated Protein Kinase Reduces Inflammatory Nociception
Russe, O. Q., Möser, C. V., Kynast, K. L., King-Himmelreich, T. S., Stephan, H., Geißlinger, G., & Niederberger, E. (2013) · Journal of Pain · doi:10.1016/j.jpain.2013.05.012 · Cited by 87
Postexercise whole body heat stress additively enhances endurance training-induced mitochondrial adaptations in mouse skeletal muscle
Tamura, Y., Matsunaga, Y., Masuda, H., Takahashi, Y., Takahashi, Y., Terada, S., Hoshino, D., & Hatta, H. (2014) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00525.2013 · Cited by 93
Irisin, a Link among Fatty Liver Disease, Physical Inactivity and Insulin Resistance
Arias, M., Ranchal, I., Romero‐Gómez, M., & Crespo, J. (2014) · International Journal of Molecular Sciences · doi:10.3390/ijms151223163 · Cited by 87
Diverse roles of GSK-3: Tumor promoter–tumor suppressor, target in cancer therapy
McCubrey, J. A., Davis, N. M., Abrams, S. L., Montalto, G., Cervello, M., Bäsecke, J., Libra, M., Nicoletti, F., Cocco, L., Martelli, A. M., et al. (2013) · Advances in Biological Regulation · doi:10.1016/j.jbior.2013.09.013 · Cited by 85
Resistance to type 2 diabetes mellitus: a matter of hormesis?
Kolb, H., & Eizirik, D. L. (2011) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2011.158 · Cited by 87
SIRT1 phosphorylation by AMP-activated protein kinase regulates p53 acetylation.
Lau, A. W., Liu, P., Inuzuka, H., & Gao, D. (2014) · PubMed Central · Cited by 86
Phosphoproteomics reveals conserved exercise‐stimulated signaling and AMPK regulation of store‐operated calcium entry
Nelson, M. E., Parker, B. L., Burchfield, J. G., Hoffman, N. J., Needham, E. J., Cooke, K. C., Naim, T., Sylow, L., Ling, N. X. Y., Francis, D., et al. (2019) · The EMBO Journal · doi:10.15252/embj.2019102578 · Cited by 81
Self-citation
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Chen, Z., Li, L., Wu, W., Liu, Z., Huang, Y., Yang, L., Luo, Q., Chen, J., Hou, Y., & Song, G. (2020) · Theranostics · doi:10.7150/thno.43577 · Cited by 88
Integrative and Systemic Approaches for Evaluating PPARβ/δ (PPARD) Function
Attianese, G. M. P. G., & Desvergne, B. (2015) · Nuclear Receptor Signaling · doi:10.1621/nrs.13001 · Cited by 88
Secondary brain injury after polystyrene microplastic-induced intracerebral hemorrhage is associated with inflammation and pyroptosis
Yin, K., Lu, H., Zhang, Y., Hou, L., Meng, X., Li, J., Zhao, H., & Xing, M. (2022) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2022.110180 · Cited by 89
Adenosine monophosphate–activated protein kinase in diabetic nephropathy
Kim, Y., & Park, C. W. (2016) · Kidney Research and Clinical Practice · doi:10.1016/j.krcp.2016.02.004 · Cited by 85
Molecular Nutrition Research—The Modern Way Of Performing Nutritional Science
Norheim, F., Gjelstad, I., Hjorth, M., Vinknes, K., Langleite, T., Holen, T., Jensen, J., Dalen, K., Karlsen, A., Kielland, A., et al. (2012) · Nutrients · doi:10.3390/nu4121898 · Cited by 83
Mimicking exercise: what matters most and where to next?
Hawley, J. A., Joyner, M. J., & GREEN, D. J. (2019) · The Journal of Physiology · doi:10.1113/jp278761 · Cited by 85
Aerobic exercise alleviates oxidative stress-induced apoptosis in kidneys of myocardial infarction mice by inhibiting ALCAT1 and activating FNDC5/Irisin signaling pathway
Wu, F., Li, Z., Cai, M., Xi, Y., Xu, Z., Zhang, Z., Li, H., Zhu, W., & Tian, Z. (2020) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2020.06.038 · Cited by 82
Loss of IL-15 receptor α alters the endurance, fatigability, and metabolic characteristics of mouse fast skeletal muscles
Pistilli, E. E., Bogdanovich, S., Garton, F. C., Yang, N., Gulbin, J. P., Conner, J. D., Anderson, B. G., Quinn, L. S., North, K. N., Ahima, R. S., et al. (2011) · Journal of Clinical Investigation · doi:10.1172/jci44945 · Cited by 86
The molecular basis of nutritional intervention in multiple sclerosis: A narrative review
Riccio, P. (2011) · Complementary Therapies in Medicine · doi:10.1016/j.ctim.2011.06.006 · Cited by 86
Physical Exercise Protects Against Endothelial Dysfunction in Cardiovascular and Metabolic Diseases
Gao, J., Pan, X., Li, G., Chatterjee, E., & Xiao, J. (2021) · Journal of Cardiovascular Translational Research · doi:10.1007/s12265-021-10171-3 · Cited by 84
Small-Molecule Activators of AMP-Activated Protein Kinase (AMPK), RSVA314 and RSVA405, Inhibit Adipogenesis
Vingtdeux, V., Chandakkar, P., Zhao, H., Davies, P., & Marambaud, P. (2011) · Molecular Medicine · doi:10.2119/molmed.2011.00163 · Cited by 81
Central role of nitric oxide synthase in AICAR and caffeine-induced mitochondrial biogenesis in L6 myocytes
McConell, G. K., Ng, G. P. Y., Phillips, M., Ruan, Z., Macaulay, S. L., & Wadley, G. D. (2010) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00377.2009 · Cited by 81
Skeletal muscle adiposity is associated with physical activity, exercise capacity and fibre shift in COPD
Maddocks, M. M., Shrikrishna, D., Vitoriano, S., Natanek, S. A., Tanner, R., Hart, N., Kemp, P. R., Moxham, J., Polkey, M. I., & Hopkinson, N. S. (2014) · European Respiratory Journal · doi:10.1183/09031936.00066414 · Cited by 81
PPARs and angiogenesis
Bishop‐Bailey, D. (2011) · Biochemical Society Transactions · doi:10.1042/bst20110643 · Cited by 81
PPAR-delta promotes survival of breast cancer cells in harsh metabolic conditions
Wang, X., Wang, G., Shi, Y., Sun, L., Gorczynski, R. M., Li, Y., Xu, Z., & Spaner, D. (2016) · Oncogenesis · doi:10.1038/oncsis.2016.41 · Cited by 82
α-Ketoglutarate Modulates Macrophage Polarization Through Regulation of PPARγ Transcription and mTORC1/p70S6K Pathway to Ameliorate ALI/ARDS
Liu, M., Chen, Y., Wang, S., Zhou, H., Feng, D., Wei, J., Shi, X., Wu, L., Zhang, P., Yang, H., et al. (2019) · Shock · doi:10.1097/shk.0000000000001333 · Cited by 80
Peroxisome Proliferator-Activated Receptors and Caloric Restriction—Common Pathways Affecting Metabolism, Health, and Longevity
Duszka, K., Gregor, A., Guillou, H., König, J. S., & Wahli, W. (2020) · Cells · doi:10.3390/cells9071708 · Cited by 86
Remote preconditioning provides potent cardioprotection via PI3K/Akt activation and is associated with nuclear accumulation of β-catenin
Li, J., Xuan, W., Yan, R., Tropak, M. B., Jean-st-michel, E. M., Liang, W., Gladstone, R. A., Backx, P. H., Kharbanda, R. K., & Redington, A. N. (2011) · Clinical Science · doi:10.1042/cs20100466 · Cited by 78
Methotrexate Promotes Glucose Uptake and Lipid Oxidation in Skeletal Muscle via AMPK Activation
Pirkmajer, S., Kulkarni, S. S., Tom, R. Z., Ross, F. A., Hawley, S. A., Hardie, D. G., Zierath, J. R., & Chibalin, A. (2014) · Diabetes · doi:10.2337/db14-0508 · Cited by 83

Authors: Narkar, V. A., Downes, M., Yu, R. T., Embler, E., Wang, Y.-X., Banayo, E., Mihaylova, M. M., Nelson, M. C., Zou, Y., Juguilon, H., Kang, H., Shaw, R. J., & Evans, R. M.
Affiliations: Salk Institute for Biological Studies (US)
University of Massachusetts Chan Medical School (US)
Howard Hughes Medical Institute (US)
Seoul National University (KR)
Corresponding author: Evans, Ronald M.
ORCID: Narkar, Vihang A.
Downes, Michael
Yu, Ruth T.
Mihaylova, Maria M.
Nelson, Michael C.
Kang, Heonjoong
Shaw, Reuben J.
Evans, Ronald M.
Venue: Cell
Publisher: Elsevier BV
Published: 2008-08
Volume: 134
Issue: 3
Pages: 405-415
ISSN: 0092-8674 (ISSN-L)
DOI: 10.1016/j.cell.2008.06.051
PMC: PMC2706130
OpenAlex: W2061075485
Cited by: 1,222
References: 54
Citations by year: 2026: 45 · 2025: 30 · 2024: 43 · 2023: 46 · 2022: 35 · 2021: 58 · 2020: 68 · 2019: 56 · 2018: 76 · 2017: 74 · 2016: 58 · 2015: 89 · 2014: 95 · 2013: 97 · 2012: 80
FWCI: 37.75
Type: journal article
Language: en
Update notices: erratum (2008-10-03)
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 1847 d)
doi.org/10.15223/policy-017 (stm-asf)
doi.org/10.15223/policy-037 (stm-asf)
doi.org/10.15223/policy-012 (stm-asf)
doi.org/10.15223/policy-029 (stm-asf)
doi.org/10.15223/policy-004 (stm-asf)
Locations: Cell (publishedVersion)
PubMed (publishedVersion)
PubMed Central (acceptedVersion)
Funders: Howard Hughes Medical Institute
National Cancer Institute (P30CA014195)
National Institute of Diabetes and Digestive and Kidney Diseases (R37DK057978, DK057978, R01DK057978)
National Institute of Arthritis and Musculoskeletal and Skin Diseases (F32AR053803)
Eunice Kennedy Shriver National Institute of Child Health and Human Development (R01HD027183, HD027183)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Peroxisome Proliferator-Activated Receptors
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
Health Sciences › Medicine › Physiology (medical) › Adipose Tissue and Metabolism
Keywords: AMPK agonists, PPARδ agonist, exercise mimetics, AICAR, running endurance, PGC-1α, PPARδ, metabolic adaptation, sedentary mice, metabolic disorders, treadmill running
MeSH terms: Administration, Oral, Aminoimidazole Carboxamide, Animals, Male, Mice, Inbred C57BL, Multienzyme Complexes, Physical Conditioning, Animal, Physical Endurance, Ribonucleotides, Thiazoles, Protein Serine-Threonine Kinases, Muscle, Skeletal, Biomimetics, PPAR delta, Mice, AMP-Activated Protein Kinases

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AMPK and PPARδ Agonists Are Exercise Mimetics

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