Cited by 275Muscle Physiology and DisordersMetabolism, Diabetes, and CancerMuscle metabolism and nutrition

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The Role of AMPK in the Regulation of Skeletal Muscle Size, Hypertrophy, and Regeneration

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Thomson, David M.·2018·International Journal of Molecular Sciences

DOI 10.3390/ijms19103125PMC PMC6212977

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Abstract

AMPK (5’-adenosine monophosphate-activated protein kinase) is heavily involved in skeletal muscle metabolic control through its regulation of many downstream targets. Because of their effects on anabolic and catabolic cellular processes, AMPK plays an important role in the control of skeletal muscle development and growth. In this review, the effects of AMPK signaling, and those of its upstream activator, liver kinase B1 (LKB1), on skeletal muscle growth and atrophy are reviewed. The effect of AMPK activity on satellite cell-mediated muscle growth and regeneration after injury is also reviewed. Together, the current data indicate that AMPK does play an important role in regulating muscle mass and regeneration, with AMPKα1 playing a prominent role in stimulating anabolism and in regulating satellite cell dynamics during regeneration, and AMPKα2 playing a potentially more important role in regulating muscle degradation during atrophy.

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Li, Y., Jiang, Q. L., Cao, G.-F., Yao, J., & Yan, B. (2015) · Cellular Physiology and Biochemistry · doi:10.1159/000373980 · Cited by 16,351
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Kim, J., Kundu, M., Viollet, B., & Guan, K.-L. (2011) · Nature Cell Biology · doi:10.1038/ncb2152 · Cited by 7,227
Role of AMP-Activated Protein Kinase in Mechanism of Metformin Action
Zhou, G., Myers, R., Li, Y., Chen, Y., Shen, X., Fenyk-Melody, J., Wu, M., Ventre, J., Doebber, T., Fujii, N., et al. (2001) · Journal of Clinical Investigation · doi:10.1172/jci13505 · Cited by 5,652
AMPK: guardian of metabolism and mitochondrial homeostasis
Herzig, S., & Shaw, R. J. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.95 · Cited by 4,192
AMPK Phosphorylation of Raptor Mediates a Metabolic Checkpoint
Gwinn, D. M., Shackelford, D. B., Egan, D. F., Mihaylova, M. M., Mery, A., Vasquez, D. S., Turk, B. E., & Shaw, R. J. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.03.003 · Cited by 3,849
AMPK regulates energy expenditure by modulating NAD+ metabolism and SIRT1 activity
Cantó, C., Gerhart-Hines, Z., Feige, J. N., Lagouge, M., Noriega, L., Milne, J. C., Elliott, P. J., Puigserver, P., & Auwerx, J. (2009) · Nature · doi:10.1038/nature07813 · Cited by 3,300
The mechanisms of action of metformin
Rena, G., Hardie, D. G., & Pearson, E. R. (2017) · Diabetologia · doi:10.1007/s00125-017-4342-z · Cited by 2,287
5-Aminoimidazole-4-Carboxamide Ribonucleoside. A Specific Method for Activating AMP-Activated Protein Kinase in Intact Cells?
Corton, J. M., Gillespie, J. G., Hawley, S. A., & Hardie, D. G. (1995) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1995.tb20498.x · Cited by 1,232
AICA riboside increases AMP-activated protein kinase, fatty acid oxidation, and glucose uptake in rat muscle
Merrill, G. F., Kurth, E. J., Hardie, D. G., & Winder, W. W. (1997) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.1997.273.6.e1107 · Cited by 1,048
Rheb Binds and Regulates the mTOR Kinase
Long, X., Lin, Y., Ortiz-Vega, S., Yonezawa, K., & Avruch, J. (2005) · Current Biology · doi:10.1016/j.cub.2005.02.053 · Cited by 1,005
Identification and characterization of a small molecule AMPK activator that treats key components of type 2 diabetes and the metabolic syndrome
Cool, B. L., Zinker, B. A., Chiou, W. J. H., Kifle, L., Cao, N., Perham, M., Dickinson, R., Adler, A. L., Gagné, G. D., Iyengar, R., et al. (2006) · Cell Metabolism · doi:10.1016/j.cmet.2006.05.005 · Cited by 939
Interdependence of AMPK and SIRT1 for metabolic adaptation to fasting and exercise in skeletal muscle
Cantó, C., Jiang, L. Q., Deshmukh, A. S., Mataki, C., Coste, A., Lagouge, M., Zierath, J. R., & Auwerx, J. (2010) · Cell Metabolism · doi:10.1016/j.cmet.2010.02.006 · Cited by 921
The Energy Sensor AMP-activated Protein Kinase Directly Regulates the Mammalian FOXO3 Transcription Factor
Greer, E. L., Oskoui, P. R., Banko, M. R., Maniar, J. M., Gygi, M. P., Gygi, S. P., & Brunet, A. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m705325200 · Cited by 852
AMP-activated Protein Kinase Suppresses Protein Synthesis in Rat Skeletal Muscle through Down-regulated Mammalian Target of Rapamycin (mTOR) Signaling
Bolster, D. R., Crozier, S. J., Kimball, S. R., & Jefferson, L. S. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.c200171200 · Cited by 851
Glucose Restriction Inhibits Skeletal Myoblast Differentiation by Activating SIRT1 through AMPK-Mediated Regulation of Nampt
Fulco, M., Cen, Y., Zhao, P., Hoffman, E. P., McBurney, M. W., Sauve, A. A., & Sartorelli, V. (2008) · Developmental Cell · doi:10.1016/j.devcel.2008.02.004 · Cited by 843
Metformin Increases AMP-Activated Protein Kinase Activity in Skeletal Muscle of Subjects With Type 2 Diabetes
Musi, N., Hirshman, M. F., Nygren, J., Svanfeldt, M., Bavenholm, P., Rooyackers, O., Zhou, G., Williamson, J. M., Ljunqvist, O., Efendic, S., et al. (2002) · Diabetes · doi:10.2337/diabetes.51.7.2074 · Cited by 806
An AMPK-FOXO pathway mediates longevity induced by a novel method of dietary restriction in C. elegans
Greer, E. L., Dowlatshahi, D., Banko, M. R., Villen, J., Hoang, K., Blanchard, D., Gygi, S. P., & Brunet, A. (2007) · Current Biology · doi:10.1016/j.cub.2007.08.047 · Cited by 801
Inactivation of acetyl-CoA carboxylase and activation of AMP-activated protein kinase in muscle during exercise
Winder, W. W., & Hardie, D. G. (1996) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.1996.270.2.e299 · Cited by 799
AMPK signalling in health and disease
Carling, D. (2017) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2017.01.005 · Cited by 797
Interference of strength development by simultaneously training for strength and endurance.
Hickson, R. C. (1980) · European Journal of Applied Physiology and Occupational Physiology · doi:10.1007/bf00421333 · Cited by 753
Mammalian Autophagy: How Does It Work?
Bento, C. F., Renna, M., Ghislat, G., Puri, C., Ashkenazi, A., Vicinanza, M., Menzies, F. M., & Rubinsztein, D. C. (2016) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060815-014556 · Cited by 711
TBC1D7 Is a Third Subunit of the TSC1-TSC2 Complex Upstream of mTORC1
Dibble, C. C., Elis, W., Menon, S., Qin, W., Klekota, J., Asara, J. M., Finan, P. M., Kwiatkowski, D. J., Murphy, L. O., & Manning, B. D. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.06.009 · Cited by 612
Mitochondrial fission and remodelling contributes to muscle atrophy
Romanello, V., Guadagnin, E., Gomes, L., Roder, I., Sandri, C., Petersen, Y., Milan, G., Masiero, E., Del Piccolo, P., Foretz, M., et al. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.60 · Cited by 596
Aging-associated reductions in AMP-activated protein kinase activity and mitochondrial biogenesis
Reznick, R. M., Zong, H., Li, J., Morino, K., Moore, I. K., Yu, H. J., Liu, Z.-X., Dong, J., Mustard, K. J., Hawley, S. A., et al. (2007) · Cell Metabolism · doi:10.1016/j.cmet.2007.01.008 · Cited by 555
Knockout of the α2 but Not α1 5′-AMP-activated Protein Kinase Isoform Abolishes 5-Aminoimidazole-4-carboxamide-1-β-4-ribofuranosidebut Not Contraction-induced Glucose Uptake in Skeletal Muscle
Jørgensen, S. B., Viollet, B., Andreelli, F., Frøsig, C., Birk, J. B., Schjerling, P., Vaulont, S., Richter, E. A., & Wojtaszewski, J. F. P. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m306205200 · Cited by 553
Deficiency of LKB1 in skeletal muscle prevents AMPK activation and glucose uptake during contraction
Sakamoto, K., McCarthy, A., Smith, D. P., Green, K. A., Hardie, D. G., Ashworth, A., & Alessi, D. R. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600667 · Cited by 552
The Association of AMPK with ULK1 Regulates Autophagy
Lee, J. W., Park, S., Takahashi, Y., & Wang, H.-G. (2010) · PLoS ONE · doi:10.1371/journal.pone.0015394 · Cited by 482
Selective activation of AMPK‐PGC‐1α or PKB‐TSC2‐mTOR signaling can explain specific adaptive responses to endurance or resistance training‐like electrical muscle stimulation
Atherton, P. J., Babraj, J. A., Smith, K., Singh, J., Rennie, M. J., & Wackerhage, H. (2005) · The FASEB Journal · doi:10.1096/fj.04-2179fje · Cited by 475 · cited 1×
“[116] showed that tissue-autonomous differences in signaling pathway activation may contribute to the inherent differences in gross adaptation that is observed with endurance vs.”
Background
Activation of AMP-Activated Protein Kinase Leads to the Phosphorylation of Elongation Factor 2 and an Inhibition of Protein Synthesis
Horman, S., Browne, G. J., Krause, U., Patel, J. V., Vertommen, D., Bertrand, L., Lavoinne, A., Hue, L., Proud, C. G., & Rider, M. H. (2002) · Current Biology · doi:10.1016/s0960-9822(02)01077-1 · Cited by 467
AMPKα1 Regulates Macrophage Skewing at the Time of Resolution of Inflammation during Skeletal Muscle Regeneration
Mounier, R., Théret, M., Arnold, L., Cuvellier, S., Bultot, L., Göransson, O., Sanz, N., Ferry, A., Sakamoto, K., Foretz, M., et al. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2013.06.017 · Cited by 464
Isoform‐specific and exercise intensity‐dependent activation of 5′‐AMP‐activated protein kinase in human skeletal muscle
Wojtaszewski, J. F. P., Nielsen, P., Hansen, B. F., Richter, E. A., & Kiens, B. (2000) · The Journal of Physiology · doi:10.1111/j.1469-7793.2000.t01-1-00221.x · Cited by 435
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
AMP-activated Protein Kinase and the Regulation of Autophagic Proteolysis
Meley, D., Bauvy, C., Houben-Weerts, J. H. P. M., Dubbelhuis, P. F., Helmond, M. T. J., Codogno, P., & Meijer, A. J. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m605488200 · Cited by 419
Skeletal muscle protein anabolic response to resistance exercise and essential amino acids is delayed with aging
Drummond, M. J., Dreyer, H. C., Pennings, B., Fry, C. S., Dhanani, S., Dillon, E. L., Sheffield‐Moore, M., Volpi, E., & Rasmussen, B. B. (2008) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00021.2008 · Cited by 410
AMP-activated protein kinase (AMPK) β1β2 muscle null mice reveal an essential role for AMPK in maintaining mitochondrial content and glucose uptake during exercise
O'Neill, H. M., Maarbjerg, S. J., Crane, J. D., Jeppesen, J., Jørgensen, S. B., Schertzer, J. D., Shyroka, O., Kiens, B., van Denderen, B. J., Tarnopolsky, M. A., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1105062108 · Cited by 406
Contraction-induced Changes in Acetyl-CoA Carboxylase and 5′-AMP-activated Kinase in Skeletal Muscle
Vavvas, D., Apazidis, A., Saha, A. K., Gamble, J., Patel, A., Kemp, B. E., Witters, L. A., & Ruderman, N. B. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.20.13255 · Cited by 395
A Muscle Stem Cell Support Group: Coordinated Cellular Responses in Muscle Regeneration
Wosczyna, M. N., & Rando, T. A. (2018) · Developmental Cell · doi:10.1016/j.devcel.2018.06.018 · Cited by 363
Exercise induces isoform-specific increase in 5'AMP-activated protein kinase activity in human skeletal muscle
Fujii, N., Hayashi, T., Hirshman, M. F., Smith, J. T., Habinowski, S. A., Kaijser, L., Mu, J., Ljungqvist, O., Birnbaum, M. J., Witters, L. A., et al. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.3073 · Cited by 351
Concurrent exercise training: do opposites distract?
Coffey, V. G., & Hawley, J. A. (2017) · The Journal of Physiology · doi:10.1113/jp272270 · Cited by 351 · cited 2×
“, through endurance exercise training) significantly impacts mTOR signaling and/or protein synthesis [115].”
Background
AMPK signaling in contracting human skeletal muscle: acetyl-CoA carboxylase and NO synthase phosphorylation
Chen, Z., McConell, G. K., Michell, B. J., Snow, R. J., Canny, B. J., & Kemp, B. E. (2000) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.2000.279.5.e1202 · Cited by 342
Thr2446 Is a Novel Mammalian Target of Rapamycin (mTOR) Phosphorylation Site Regulated by Nutrient Status
Cheng, S., Fryer, L. G. D., Carling, D., & Shepherd, P. R. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.c300534200 · Cited by 340
Activation of AMP-activated protein kinase inhibits protein synthesis associated with hypertrophy in the cardiac myocyte
Chan, A. Y. M., Soltys, C.-L. M., Young, M. E., Proud, C. G., & Dyck, J. R. B. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m403528200 · Cited by 331
AMPK promotes skeletal muscle autophagy through activation of forkhead FoxO3a and interaction with Ulk1
Sanchez, A. M., Csibi, A., Raibon, A., Cornille, K., Gay, S., Bernardi, H., & Candau, R. (2012) · Journal of Cellular Biochemistry · doi:10.1002/jcb.23399 · Cited by 306
Predominant α2/β2/γ3 AMPK activation during exercise in human skeletal muscle
Birk, J. B., & Wojtaszewski, J. F. P. (2006) · The Journal of Physiology · doi:10.1113/jphysiol.2006.120972 · Cited by 293
Effects of α‐AMPK knockout on exercise‐induced gene activation in mouse skeletal muscle
Jørgensen, S. B., Wojtaszewski, J. F. P., Viollet, B., Andreelli, F., Birk, J. B., Hellsten, Y., Schjerling, P., Vaulont, S., Neufer, P. D., Richter, E. A., et al. (2005) · The FASEB Journal · doi:10.1096/fj.04-3144fje · Cited by 274
The role of E3 ubiquitin-ligases MuRF-1 and MAFbx in loss of skeletal muscle mass
Rom, O., & Reznick, A. Z. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.12.031 · Cited by 271
Thienopyridone Drugs Are Selective Activators of AMP-Activated Protein Kinase β1-Containing Complexes
Scott, J. W., van Denderen, B. J. W., Jørgensen, S. B., Honeyman, J. E., Steinberg, G. R., Oakhill, J. S., Iseli, T. J., Koay, A. Z., Gooley, P. R., Stapleton, D., et al. (2008) · Chemistry & Biology · doi:10.1016/j.chembiol.2008.10.005 · Cited by 262
AMP-activated protein kinase activators can inhibit the growth of prostate cancer cells by multiple mechanisms
Xiang, X., Saha, A. K., Wen, R., Ruderman, N. B., & Luo, Z. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.06.133 · Cited by 257
Targeted ablation of TRAF6 inhibits skeletal muscle wasting in mice
Paul, P. K., Gupta, S. K., Bhatnagar, S., Panguluri, S. K., Darnay, B. G., Choi, Y., & Kumar, A. (2010) · The Journal of Cell Biology · doi:10.1083/jcb.201006098 · Cited by 234
AMPK Activation Stimulates Autophagy and Ameliorates Muscular Dystrophy in the mdx Mouse Diaphragm
Pauly, M., Daussin, F., Burelle, Y., Li, T., Godin, R., Fauconnier, J., Koechlin-Ramonatxo, C., Hugon, G., Lacampagne, A., Coisy-Quivy, M., et al. (2012) · The American Journal of Pathology · doi:10.1016/j.ajpath.2012.04.004 · Cited by 225 · cited 1×
“Furthermore, 4 weeks of AICAR treatment of mdx mice (a model for Duchenne muscular dystrophy) did not exacerbate atrophy associated with dystrophy, and actually improved muscle function, probably through enhanced autophagic clearing of damaged cell components [106], and/or promotion of a more oxidative muscle phenotyp…”
Background
AMP-activated protein kinase activity and glucose uptake in rat skeletal muscle
Musi, N., Hayashi, T., FUJII, N. L., Hirshman, M. F., Witters, L. A., & Goodyear, L. J. (2001) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.2001.280.5.e677 · Cited by 219
Possible CaMKK-dependent regulation of AMPK phosphorylation and glucose uptake at the onset of mild tetanic skeletal muscle contraction
Jensen, T. E., Rose, A. J., Jørgensen, S. B., Brandt, N., Schjerling, P., Wojtaszewski, J. F. P., & Richter, E. A. (2007) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00456.2006 · Cited by 216
AMPK regulates autophagy by phosphorylating BECN1 at threonine 388
Zhang, D., Wang, W., Sun, X., Xu, D., Wang, C., Zhang, Q., Wang, H., Luo, W., Chen, Y., Chen, H., et al. (2016) · Autophagy · doi:10.1080/15548627.2016.1185576 · Cited by 216
AMPK Activation Stimulates Myofibrillar Protein Degradation and Expression of Atrophy-Related Ubiquitin Ligases by Increasing FOXO Transcription Factors in C2C12 Myotubes
Nakashima, K., & Yakabe, Y. (2007) · Bioscience Biotechnology and Biochemistry · doi:10.1271/bbb.70057 · Cited by 208
Skeletal Muscle-Selective Knockout of LKB1 Increases Insulin Sensitivity, Improves Glucose Homeostasis, and Decreases TRB3
Koh, H.-J., Arnolds, D. E., Fujii, N., Tran, T. T., Rogers, M. J., Jessen, N., Li, Y., Liew, C. W., Ho, R. C., Hirshman, M. F., et al. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.00979-06 · Cited by 202
Keeping the home fires burning: AMP-activated protein kinase
Hardie, D. G. (2018) · Journal of The Royal Society Interface · doi:10.1098/rsif.2017.0774 · Cited by 195
5′AMP activated protein kinase expression in human skeletal muscle: effects of strength training and type 2 diabetes
Wojtaszewski, J. F. P., Birk, J. B., Frøsig, C., Holten, M., Pilegaard, H., & Dela, F. (2005) · The Journal of Physiology · doi:10.1113/jphysiol.2005.082669 · Cited by 170
The role of alterations in mitochondrial dynamics and PGC‐1α over‐expression in fast muscle atrophy following hindlimb unloading
Cannavino, J., Brocca, L., Sandri, M., Grassi, B., Bottinelli, R., & Pellegrino, M. A. (2015) · The Journal of Physiology · doi:10.1113/jphysiol.2014.286740 · Cited by 166
Whole Body Deletion of AMP-activated Protein Kinase β2 Reduces Muscle AMPK Activity and Exercise Capacity
Steinberg, G. R., O'Neill, H. M., Dzamko, N. L., Galic, S., Naim, T., Koopman, R., Jørgensen, S. B., Honeyman, J., Hewitt, K., Chen, Z.-P., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.102434 · Cited by 164
5′-AMP-activated protein kinase activity and protein expression are regulated by endurance training in human skeletal muscle
Frøsig, C., Jørgensen, S. B., Hardie, D. G., Richter, E. A., & Wojtaszewski, J. F. P. (2004) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00317.2003 · Cited by 161
Obesity Impairs Skeletal Muscle Regeneration Through Inhibition of AMPK
Fu, X., Zhu, M., Zhang, S., Foretz, M., Viollet, B., & Du, M. (2016) · Diabetes · doi:10.2337/db15-0647 · Cited by 155 · cited 1×
“WT) in both constitutive AMPKα1-KO mice, as well as in mice with AMPKα1-KO induced just before injury [137], and this is associated with decreased satellite cell number and Pax7, myogenic factor 5 (Myf5), and myogenin expression in basal muscles.”
Background
AMPK activation attenuates S6K1, 4E-BP1, and eEF2 signaling responses to high-frequency electrically stimulated skeletal muscle contractions
Thomson, D. M., Fick, C. A., & Gordon, S. E. (2008) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00915.2007 · Cited by 153
Self-citation
5′-AMP-activated protein kinase activity and subunit expression in exercise-trained human skeletal muscle
Nielsen, J. N., Mustard, K. J., Graham, D. A., Yu, H., MacDonald, C., Pilegaard, H., Goodyear, L. J., Hardie, D. G., Richter, E. A., & Wojtaszewski, J. F. P. (2003) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00642.2002 · Cited by 149
Progressive increase in human skeletal muscle AMPKα2 activity and ACC phosphorylation during exercise
Stephens, T. J., Chen, Z.-P., Canny, B. J., Michell, B. J., Kemp, B. E., & McConell, G. K. (2002) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00101.2001 · Cited by 148
AMPK‐independent pathways regulate skeletal muscle fatty acid oxidation
Dzamko, N., Schertzer, J. D., Ryall, J. G., Steel, R., Macaulay, S. L., Wee, S., Chen, Z., Michell, B. J., Oakhill, J. S., Watt, M. J., et al. (2008) · The Journal of Physiology · doi:10.1113/jphysiol.2008.159814 · Cited by 147
Skeletal muscle and heart LKB1 deficiency causes decreased voluntary running and reduced muscle mitochondrial marker enzyme expression in mice.
Thomson, D. M., Porter, B. B., Tall, J. H., Kim, H.-J., Barrow, J. R., & Winder, W. W. (2007) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00366.2006 · Cited by 146
Self-citation
Cellular energy sensing and signaling by AMP-activated protein kinase
Winder, W. W., & Thomson, D. M. (2007) · Cell Biochemistry and Biophysics · doi:10.1007/s12013-007-0008-7 · Cited by 142
Self-citation
Short‐term exercise training in humans reduces AMPK signalling during prolonged exercise independent of muscle glycogen
McConell, G. K., Lee, R. S., Chen, Z., Stepto, N. K., Huynh, N., Stephens, T. J., Canny, B. J., & Kemp, B. E. (2005) · The Journal of Physiology · doi:10.1113/jphysiol.2005.089839 · Cited by 139
AMPKα1‐LDH pathway regulates muscle stem cell self‐renewal by controlling metabolic homeostasis
Théret, M., Gsaier, L., Schaffer, B. E., Juban, G., Larbi, S. B., Weiss‐Gayet, M., Bultot, L., Collodet, C., Foretz, M., Dominique Desplanches, C., et al. (2017) · The EMBO Journal · doi:10.15252/embj.201695273 · Cited by 139
Important role for AMPKαl in limiting skeletal muscle cell hypertrophy
Mounier, R., Lantier, L., Leclerc, J., Sotiropoulos, A., Pende, M., Daegelen, D., Sakamoto, K., Foretz, M., & Viollet, B. (2009) · The FASEB Journal · doi:10.1096/fj.08-119057 · Cited by 133
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Thomson, D. M., & Gordon, S. E. (2005) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00811.2004 · Cited by 131
Self-citation
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Weeresekara, V., Panek, D. J., Broadbent, D. G., Mortenson, J. B., Mathis, A. D., Logan, G., Prince, J. T., Thomson, D. M., Thompson, J. W., & Andersen, J. L. (2014) · Molecular and Cellular Biology · doi:10.1128/mcb.00740-14 · Cited by 129
Self-citation
Inhibition of Hepatocytic Autophagy by Adenosine, Aminoimidazole-4-carboxamide Riboside, and N 6-Mercaptopurine Riboside
Samari, H. R., & Seglen, P. O. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.37.23758 · Cited by 125
The role of AMP-activated protein kinase in the coordination of skeletal muscle turnover and energy homeostasis
Sanchez, A. M. J., Candau, R. B., Csibi, A., Pagano, A. F., Raibon, A., & Bernardi, H. (2012) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00125.2012 · Cited by 122
Influence of Metformin on Glucose Intolerance and Muscle Catabolism Following Severe Burn Injury
Gore, D. C., Wolf, S. E., Sanford, A. P., Herndon, D. N., & Wolfe, R. R. (2005) · Annals of Surgery · doi:10.1097/01.sla.0000152013.23032.d1 · Cited by 114
A-769662 activates AMPK β 1 -containing complexes but induces glucose uptake through a PI3-kinase-dependent pathway in mouse skeletal muscle
Treebak, J. T., Birk, J. B., Hansen, B. F., Olsen, G. S., & Wojtaszewski, J. F. P. (2009) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00051.2009 · Cited by 112
Coordinated maintenance of muscle cell size control by AMP‐activated protein kinase
Lander, L., Mourner, R., Leclerc, J., Pende, M., Foretz, M., & Viollet, B. (2010) · The FASEB Journal · doi:10.1096/fj.10-155994 · Cited by 111
The impact of exercise and nutrition on the regulation of skeletal muscle mass
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A Ca2+–calmodulin–eEF2K–eEF2 signalling cascade, but not AMPK, contributes to the suppression of skeletal muscle protein synthesis during contractions
Rose, A. J., Alsted, T. J., Jensen, T. E., Kobberø, J. B., Maarbjerg, S., Jensen, J., & Richter, E. A. (2009) · The Journal of Physiology · doi:10.1113/jphysiol.2008.167528 · Cited by 106
Impaired overload‐induced muscle growth is associated with diminished translational signalling in aged rat fast‐twitch skeletal muscle
Thomson, D. M., & Gordon, S. E. (2006) · The Journal of Physiology · doi:10.1113/jphysiol.2006.107490 · Cited by 106
Self-citation
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McGee, S. L., Mustard, K. J., Hardie, D. G., & Baar, K. (2008) · The Journal of Physiology · doi:10.1113/jphysiol.2007.143685 · Cited by 105
Time course changes in signaling pathways and protein synthesis in C2C12myotubes following AMPK activation by AICAR
Williamson, D. L., Bolster, D. R., Kimball, S. R., & Jefferson, L. S. (2006) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00566.2005 · Cited by 100
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Fu, X., Zhu, M. J., Dodson, M. V., & Du, ‬. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.665232 · Cited by 96
Genetic impairment of AMPKα2 signaling does not reduce muscle glucose uptake during treadmill exercise in mice
Maarbjerg, S., Jørgensen, S. B., Rose, A. J., Jeppesen, J. F., Jensen, T. E., Treebak, J. T., Birk, J. B., Schjerling, P., Wojtaszewski, J. F. P., & Richter, E. A. (2009) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.90653.2008 · Cited by 95
Selective suppression of AMP-activated protein kinase in skeletal muscle: update on ‘lazy mice’
Mu, J., Barton, E. R., & Birnbaum, M. J. (2003) · Biochemical Society Transactions · doi:10.1042/bst0310236 · Cited by 93 · cited 1×
“Initial observations in dominant-negative AMPK (AMPK-DN) transgenic mice in which a dominant negative AMPKα2 subunit was overexpressed under the muscle creatine kinase promoter (expressed in heart and skeletal muscle) showed that EDL muscles tended to be larger than in wild-type (WT) mice, suggesting that AMPK might n…”
Background
AMPK inhibits myoblast differentiation through a PGC-1α-dependent mechanism
Williamson, D. L., Butler, D. C., & Alway, S. E. (2009) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.91007.2008 · Cited by 91
Evidence for control of protein synthesis in HeLa cells via the elongation rate
Nielsen, P. J., & McConkey, E. H. (1980) · Journal of Cellular Physiology · doi:10.1002/jcp.1041040302 · Cited by 90
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Olivier, S., Foretz, M., & Viollet, B. (2018) · Biochemical Pharmacology · doi:10.1016/j.bcp.2018.01.049 · Cited by 90
Considerations on mTOR regulation at serine 2448: implications for muscle metabolism studies
Figueiredo, V. C., Markworth, J. F., & Cameron‐Smith, D. (2017) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-017-2481-5 · Cited by 88
Resistance exercise-induced S6K1 kinase activity is not inhibited in human skeletal muscle despite prior activation of AMPK by high-intensity interval cycling
Apró, W., Moberg, M., Hamilton, D. L., Ekblom, B., van Hall, G., Holmberg, H.-C., & Blomstrand, E. (2015) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00486.2014 · Cited by 82
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Jeppesen, J. F., Maarbjerg, S., Jordy, A. B., Fritzen, A. M., Pehmøller, C. K., Sylow, L., Serup, A. K., Jessen, N., Thorsen, K., Prats, C., et al. (2013) · Diabetes · doi:10.2337/db12-1160 · Cited by 82
Self-citation
Exercise‐mediated modulation of autophagy in skeletal muscle
Martín-Rincón, M., Morales‐Álamo, D., & Calbet, J. A. L. (2017) · Scandinavian Journal of Medicine and Science in Sports · doi:10.1111/sms.12945 · Cited by 79
Energy Homeostasis and Cancer Prevention: The AMP-Activated Protein Kinase
Fay, J. R., Steele, V. E., & Crowell, J. A. (2009) · Cancer Prevention Research · doi:10.1158/1940-6207.capr-08-0166 · Cited by 77
Hepatic amino acid‐dependent signaling is under the control of AMP‐dependent protein kinase
Dubbelhuis, P. F., & Meijer, A. J. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)02815-6 · Cited by 76
Repression of protein synthesis and mTOR signaling in rat liver mediated by the AMPK activator aminoimidazole carboxamide ribonucleoside
Reiter, A. K., Bolster, D. R., Crozier, S. J., Kimball, S. R., & Jefferson, L. S. (2004) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00333.2004 · Cited by 76
Lkb1 Is Indispensable for Skeletal Muscle Development, Regeneration, and Satellite Cell Homeostasis
Shan, T., Zhang, P., Liang, X., Bi, P., Yue, F., & Kuang, S. (2014) · Stem Cells · doi:10.1002/stem.1788 · Cited by 74
Insulin-independent pathways mediating glucose uptake in hindlimb-suspended skeletal muscle
Hilder, T. L., Baer, L. A., Fuller, P. M., Fuller, C. A., Grindeland, R. E., Wade, C. E., & Graves, L. M. (2005) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00743.2005 · Cited by 71
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Rose, A. J., & Richter, E. A. (2008) · Journal of Applied Physiology · doi:10.1152/japplphysiol.91375.2008 · Cited by 67
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Niesler, C. U., Myburgh, K. H., & Moore, F. P. (2006) · Experimental Physiology · doi:10.1113/expphysiol.2006.034736 · Cited by 64
Rat hindlimb unloading down-regulates insulin like growth factor-1 signaling and AMP-activated protein kinase, and leads to severe atrophy of the soleus muscle
Han, B., Zhu, M. J., Ma, C., & Du, ‬. (2007) · Applied Physiology, Nutrition, and Metabolism · doi:10.1139/h07-102 · Cited by 63
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Fu, X., Zhao, J., Zhu, M. J., Foretz, M., Viollet, B., Dodson, M. V., & Du, ‬. (2013) · Molecular and Cellular Biology · doi:10.1128/mcb.01078-13 · Cited by 62
ATP depletion increases phosphorylation of elongation factor eEF2 in adult cardiomyocytes independently of inhibition of mTOR signalling
McLeod, L. E., & Proud, C. G. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)03582-2 · Cited by 61
LKB1 and the regulation of malonyl-CoA and fatty acid oxidation in muscle
Thomson, D. M., Brown, J. D., Fillmore, N., Condon, B. M., Kim, H., Barrow, J. R., & Winder, W. W. (2007) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00371.2007 · Cited by 61
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Deyhle, M. R., & Hyldahl, R. D. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.00768 · Cited by 60
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Egawa, T., Goto, A., Ohno, Y., Yokoyama, S., Ikuta, A., Suzuki, M., Sugiura, T., Ohira, Y., Yoshioka, T., Hayashi, T., et al. (2015) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00165.2015 · Cited by 59
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Sepsis and AMPK Activation by AICAR Differentially Regulate FoxO-1, -3 and -4 mRNA in Striated Muscle.
Nystrom, G. J., & Lang, C. H. (2008) · PubMed · Cited by 56
Ablation of LKB1 in the heart leads to energy deprivation and impaired cardiac function
Jessen, N., Koh, H.-J., Folmes, C. D. L., Wagg, C. S., FUJII, N. L., Løfgren, B., Wolf, C. M., Berul, C. I., Hirshman, M. F., Lopaschuk, G. D., et al. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2010.04.008 · Cited by 55
Time course of GLUT4 and AMPK protein expression in human skeletal muscle during one month of physical training
Langfort, J., Viese, M., Ploug, T., & Dela, F. (2003) · Scandinavian Journal of Medicine and Science in Sports · doi:10.1034/j.1600-0838.2003.20120.x · Cited by 54
Depressed mitochondrial biogenesis and dynamic remodeling in mouse tibialis anterior and gastrocnemius induced by 4‐week hindlimb unloading
Liu, J., Peng, Y., Cui, Z., Wu, Z., Qian, A., Shang, P., Qu, L., Li, Y., Liu, J., & Long, J. (2012) · IUBMB Life · doi:10.1002/iub.1087 · Cited by 54
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Dreyer, H. C., Glynn, E. L., Lujan, H. L., Fry, C. S., DiCarlo, S. E., & Rasmussen, B. B. (2007) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00736.2007 · Cited by 54
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Miyake, M., Takahashi, H., Kitagawa, E., Watanabe, H., Sakurada, T., Aso, H., & Yamaguchi, T. (2012) · Cell and Tissue Research · doi:10.1007/s00441-012-1422-8 · Cited by 51
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Self-citation
Skeletal muscle dysfunction in muscle-specific LKB1 knockout mice.
Thomson, D. M., Hancock, C. R., Evanson, B. G., Kenney, S. G., Malan, B. B., Mongillo, A. D., Brown, J. D., Hepworth, S., Fillmore, N., Parcell, A. C., et al. (2010) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01293.2009 · Cited by 45
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Layne, A. S., Nasrallah, S. N., South, M. A., Howell, M. E. A., McCurry, M. P., Ramsey, M. W., Stone, M. H., & Stuart, C. A. (2011) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2010-2532 · Cited by 44
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Egawa, T., Ohno, Y., Goto, A., Ikuta, A., Suzuki, M., Ohira, T., Yokoyama, S., Sugiura, T., Ohira, Y., Yoshioka, T., et al. (2013) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00495.2013 · Cited by 42
Impaired overload-induced hypertrophy in obese Zucker rat slow-twitch skeletal muscle
Paturi, S., Gutta, A. K., Kakarla, S. K., Katta, A., Arnold, E. C., Wu, M., Rice, K. M., & Blough, E. R. (2009) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00330.2009 · Cited by 42
Protein arginine methyltransferase expression, localization, and activity during disuse-induced skeletal muscle plasticity
Stouth, D. W., Manta, A., & Ljubicic, V. (2017) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00174.2017 · Cited by 42
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Luciano, T. F., Marques, S. D. O., Pieri, B. L. D. S., de Souza, D. R., ARAÚJO, L. V., Nesi, R. T., Scheffer, D. D. L., Comin, V. H., Pinho, R. A., Muller, A. P., et al. (2017) · Physiological Research · doi:10.33549/physiolres.933256 · Cited by 38
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Lessard, S. J., Rivas, D. A., So, K., Koh, H., Queiroz, A. L., Hirshman, M. F., Fielding, R. A., & Goodyear, L. J. (2015) · Journal of Clinical Investigation · doi:10.1172/jci79197 · Cited by 33
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Mian, I., Pierre-Louis, W., Dole, N. S., Gilberti, R. M., Dodge‐Kafka, K. L., & Tirnauer, J. S. (2012) · PLoS ONE · doi:10.1371/journal.pone.0031583 · Cited by 32
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Guo, Y., Meng, J., Tang, Y., Wang, T., Wei, B. K., Feng, R. M., Gong, B., Wang, H., Ji, G., & Lu, Z. (2016) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2016.04.015 · Cited by 31
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Cheng, Y., Zhang, D., Zhao, L., Li, Y., Yao, X., Wang, H., Zhang, S., Liu, W., Cao, H., Yu, S., et al. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17101695 · Cited by 30
Muscle‐specific AMPK β1β2‐null mice display a myopathy due to loss of capillary density in nonpostural muscles
Thomas, M. M., Wang, D. C., D’Souza, D. M., Krause, M. P., Layne, A. S., Criswell, D. S., O’Neill, H. M., Connor, M. K., Anderson, J. E., Kemp, B. E., et al. (2014) · The FASEB Journal · doi:10.1096/fj.13-238972 · Cited by 28
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Moore, T. M., Mortensen, X. M., Ashby, C. K., Harris, A. M., Kump, K. J., Laird, D. W., Adams, A. J., Bray, J. K., Chen, T., & Thomson, D. M. (2017) · Applied Physiology, Nutrition, and Metabolism · doi:10.1139/apnm-2016-0547 · Cited by 22
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Ferey, J. L. A., Brault, J. J., Smith, C. A. S., & Witczak, C. A. (2014) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00322.2014 · Cited by 20
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Gao, H., & Li, Y. (2018) · Physiological Reports · doi:10.14814/phy2.13606 · Cited by 19
Evidence for organic cation transporter-mediated metformin transport and 5′-adenosine monophosphate-activated protein kinase activation in rat skeletal muscles
Oshima, R., Yamada, M., Kurogi, E., Ogino, Y., Serizawa, Y., Tsuda, S., Ma, X., Egawa, T., & Hayashi, T. (2014) · Metabolism · doi:10.1016/j.metabol.2014.10.037 · Cited by 17
Effect of exhaustive ultra-endurance exercise in muscular glycogen and both Alpha1 and Alpha2 Ampk protein expression in trained rats
Tarini, V. A. F., Carnevali, L. C., Arida, R. M., Cunha, C. A., Alves, E. D. S., Seeleander, M. C. L., Schmidt, B. J., & Faloppa, F. (2012) · Journal of Physiology and Biochemistry · doi:10.1007/s13105-012-0224-5 · Cited by 15
AMP-activated protein kinase activation prevents denervation-induced decline in gastrocnemius GLUT-4
Paulsen, S. R., Rubink, D. S., & Winder, W. W. (2001) · Journal of Applied Physiology · doi:10.1152/jappl.2001.91.5.2102 · Cited by 14
Effect of LKB1 deficiency on mitochondrial content, fibre type and muscle performance in the mouse diaphragm
Brown, J. D., Hancock, C. R., Mongillo, A. D., Barton, J. B., DiGiovanni, R. A., Parcell, A. C., Winder, W. W., & Thomson, D. M. (2010) · Acta Physiologica · doi:10.1111/j.1748-1716.2010.02226.x · Cited by 12
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Shan, T., Zhang, P., Xiong, Y., Wang, Y., & Kuang, S. (2016) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2016.04.017 · Cited by 9
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Authors: Thomson, D. M.
Affiliations: Brigham Young University (US)
Corresponding author: Thomson, David M.
ORCID: Thomson, David M.
Venue: International Journal of Molecular Sciences
Publisher: MDPI AG
Published: 2018-10-11
Volume: 19
Issue: 10
Pages: 3125
ISSN: 1422-0067 (ISSN-L)
DOI: 10.3390/ijms19103125
PMC: PMC6212977
OpenAlex: W2896374260
Cited by: 267
References: 142
Citations by year: 2026: 29 · 2025: 36 · 2024: 41 · 2023: 52 · 2022: 40 · 2021: 31 · 2020: 24 · 2019: 13 · 2018: 1
FWCI: 1.68
Type: journal article
Language: en
Open access: gold
dx.doi.org
Licence: cc-by
creativecommons.org/licenses/by/4.0/ (vor)
Locations: International Journal of Molecular Sciences (publishedVersion, cc-by)
Europe PMC (PubMed Central) (publishedVersion, other-oa)
PubMed Central (publishedVersion, cc-by)
PubMed (publishedVersion)
DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
Health Sciences › Nursing › Nutrition and Dietetics › Muscle metabolism and nutrition
Keywords: AMPK, skeletal muscle growth, muscle hypertrophy, muscle atrophy, muscle regeneration, satellite cells, LKB1, AMPKα1, AMPKα2, muscle metabolism, myogenesis
MeSH terms: Animals, Energy Metabolism, Enzyme Activation, Humans, Hypertrophy, Organ Size, Regeneration, Wound Healing, Signal Transduction, Biomarkers, Muscle, Skeletal, Muscle Fibers, Skeletal, Muscle Development, AMP-Activated Protein Kinases

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The Role of AMPK in the Regulation of Skeletal Muscle Size, Hypertrophy, and Regeneration

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