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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Figure 1 Proposed regulation of skeletal muscle size by 5’-adenosine monophosphate-activated protein kinase (AMPK). Energy stress (decreased ATP/AMP ratio; as in moderately intensive exercise) predominantly activates AMPKα2 via liver kinase B1 (LKB1), while AMPKα1 is only activated by highly-intense or prolonged exercise. Basal AMPKα1 content and activity is also increased by long-term endurance training, perhaps via Calcium/calmodulin-dependent protein kinase (CamKK) action, or other AMPK kinases. AMPKα2 stimulates catabolic processes by increasing Foxo3a, Atrogin-1 and MuRF-1 expression/activity and increasing autophagy, leading, under certain circumstance, to muscle atrophy, but has little effect on protein anabolism. AMPKα1 impairs mTOR signaling, slows protein synthesis, and blocks hypertrophy. Hypertrophic loading (i.e., resistance exercise) stimulates mechanistic target of rapamycin (mTOR) signaling, protein synthesis, and hypertrophy, but also activates AMPKα1 independent of LKB1 (perhaps via CamKK or other means), limiting the hypertrophic growth. ↑: increase expression or activity; ↓: decreased expression or activity.CC BY · PubMed Central

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Background
Allele-specific expression reveals the phenotypic differences between thin- and fat-tailed sheepPreprint
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Developing a ceRNA-based lncRNA-miRNA-mRNA regulatory network to uncover roles in skeletal muscle development
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RyR1 Is Involved in the Control of Myogenesis
Tourel, A., Reynaud-Dulaurier, R., Brocard, J., Fauré, J., Marty, I., & Petiot, A. (2025) · Cells · doi:10.3390/cells14030158 · Cited by 5
“It has been shown that AMPK activation blocks muscle proliferation and differentiation [44–48].”
Lactoferrin attenuates renal fibrosis and uremic sarcopenia in a mouse model of adenine-induced chronic kidney disease
Iwamoto, Y., Yamakoshi, S., Sekimoto, A., Hosomi, K., Toyama, T., Saito, Y., Kunisawa, J., Takahashi, N., Mishima, E., & Sato, E. (2025) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2025.110039 · Cited by 5
Melatonin Activates AMPK Pathway to Regulate the Regeneration of Slow Muscle Fibers in Skeletal Muscle Injury Repair
Xie, W., Hong, Z., Xie, Y., Hou, K., Li, S., Fang, M., Guan, Y., Zhang, Z., & Zhang, M. (2025) · The FASEB Journal · doi:10.1096/fj.202501549rr · Cited by 5
CRISPR/Cas9-mediated mstnb knockout enhances muscle growth in salt-tolerant tilapia
Yang, Z., Le, W., Sun, F., Wong, J. E. L., Lee, M., & Yue, G. H. (2026) · Aquaculture · doi:10.1016/j.aquaculture.2026.743829 · Cited by 5
Integrative Analysis of ATAC-Seq and RNA-Seq Identifies Key Genes Affecting Muscle Development in Ningxiang Pigs
Tan, W., Liu, C., Liu, J., Wen, S., Chen, Y., Ren, R., Gao, N., Ding, X., He, J., & Zhang, Y. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26062634 · Cited by 5
Effects of YAP1 on proliferation and differentiation of Hu sheep skeletal muscle satellite cells in vitro
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“aged muscle tissue through activation and proliferation.(9) In the present study, we used Hu sheep”
Method
The Effect of β-GPA on the Markers of Anabolic and Catabolic Signaling Pathways in Rat Soleus Muscle at the Initial Stage of Hindlimb Unloading
Vilchinskaya, N. A., Mochalova, E. P., Paramonova, I. I., Belova, S. P., Mirzoev, T. M., & Shenkman, E. A. (2020) · Biochemistry (Moscow) Supplement Series A Membrane and Cell Biology · doi:10.1134/s1990747819060102 · Cited by 5
Manipulating Cellular Energetics to Slow Aging of Tissues and Organs
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Aerobic exercise ameliorates skeletal muscle atrophy in atic knockout zebrafish through the oxidative phosphorylation pathway
Peng, Z., Yang, T., Xu, S., Yang, B., Zhang, Z., Ding, M., Gu, W., & Zheng, L. (2025) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2025.07.007 · Cited by 5
Dietary perennial ryegrass improves meat quality: insights into the gut-muscle axis in geese
Zulfiqar, Z., Asif, M. A., Alharbi, K., Yao, H., Zhu, X., Wang, Z., Sun, H., Cui, Y., Liu, B., Huang, S., et al. (2025) · npj Science of Food · doi:10.1038/s41538-025-00642-1 · Cited by 4
“AMPK is activated under conditions of energy stress, promoting fat oxidation and inhibiting anabolic processes like muscle protein synthesis to conserve energy 13 .”
Dual Action of Dipyridamole in Experimental Rheumatoid Arthritis: Suppression of Joint Inflammation and Upregulation of Muscle Anabolism via Adenosine and AMPK Pathways
Marco-Bonilla, M., Fresnadillo, M. J., Sánchez-Platero, I., de la Riva-Bueno, M., Huete‐Toral, F., Carracedo, G., Conde, C., Benítez, Y., Mínguez, P., Cifuentes, S. C., et al. (2025) · Arthritis & Rheumatology · doi:10.1002/art.70047 · Cited by 4
“10,21,39 Notably, A2BR activation and elevated cAMP levels are well-established positive regulators of muscle growth, hypertrophy, and physical activity.”
Integrative Analysis of Chromatin Accessibility and Transcriptional Landscape Identifies Key Genes During Muscle Development in Pigs
Zhang, D., Zhang, Q., Wu, X., Wang, L., Zhang, X., Liu, D., & Yang, X. (2024) · Cells · doi:10.3390/cells13242118 · Cited by 4
Tofogliflozin ameliorates cardiotoxin induced skeletal muscle injury and fibrosis in obesity
Bilal, M., Phuong, N. Q., Kado, T., Liu, J., Anh, L. D., Khalid, S., Aslam, M. R., Memoona, M., Nishimura, A., Igarashi, Y., et al. (2025) · Scientific Reports · doi:10.1038/s41598-025-12734-9 · Cited by 4
“Recently, it was shown that the inhibition of AMPK subunit α1 (AMPKα1) in FAPs impairs muscle repair and promotes fibrosis 13,36 .”
Transcriptome Analysis of miRNA and mRNA in Porcine Skeletal Muscle following Glaesserella parasuis Challenge
Zhou, H., Chen, X., Deng, X., Zhang, X., Zeng, X., Xu, K., & Chen, H. (2024) · Genes · doi:10.3390/genes15030359 · Cited by 4
“The regulation of skeletal muscle mass involves various molecular mechanisms, including signal transduction [12,13], transcription factors [11,12], and epigenetic modifications [14]. miRNAs are small non-coding RNAs that act as inhibitors of gene expression and play important roles in skeletal…”
Background
Whole milk protein powder separated by low-temperature nanofiltration membrane administration alleviates sepsis-induced myopathy
Li, N., Lan, J., Yang, J., & Ding, H. W. (2024) · Nutrition & Metabolism · doi:10.1186/s12986-024-00862-4 · Cited by 4
“Under conditions of nutrient deprivation, AMPK activation suppresses mTOR activity [8]. mTOR, a highly conserved nutrient-responsive regulator of cell growth in all eukaryotes, controls cell growth and metabolism in response to nutrients, growth factors, and cellular energy status (mediated by…”
Background
Hotspots and trends in liver kinase B1 research: A bibliometric analysis
Song, Y., Zhao, F., Ma, W., & Li, G. (2021) · PLoS ONE · doi:10.1371/journal.pone.0259240 · Cited by 4
LEDT and Idebenone treatment modulate autophagy and improve regenerative capacity in the dystrophic muscle through an AMPK-pathway
da Silva, H. N. M., Fernandes, E. M., Pereira, V. A., Mizobuti, D. S., Covatti, C., da Rocha, G. L., & Minatel, E. (2024) · PLoS ONE · doi:10.1371/journal.pone.0300006 · Cited by 4
LC-MS/MS based metabolomics reveals the mechanism of skeletal muscle regeneration
Lei, Y., Wang, K., Liufu, S., Chen, W., Chen, B., Liu, X., Liu, C., Liu, J., Xu, X., & Ma, H. (2025) · BMC Musculoskeletal Disorders · doi:10.1186/s12891-025-08703-y · Cited by 3
“Adenosine monophosphate-activated protein kinase (AMPK) is a protein kinase activated by Adenosine monophosphate (AMP), and both excessive activation and deficiency of AMPK can affect skeletal muscle regeneration [30].”
Energy deprivation in youth and old age
Stern, M. (2025) · Journal of Cell Science · doi:10.1242/jcs.264018 · Cited by 3
PRMT1 (protein arginine methyltransferase 1) is essential for neuromuscular junction and mitochondrial homeostasis via mitophagy regulation
Bae, J., You, C., Jeong, Y., Kim, J., Lee, J., Jeong, H., Kim, H., Vuong, T. A., Gwon, Y., Bae, G., et al. (2025) · Autophagy · doi:10.1080/15548627.2025.2551477 · Cited by 3
“These pathways are essential for regulating muscle metabolism and maintenance, especially during conditions of energetic and metabolic stress, where they help modulate muscle adaptation [46–48].”
The Role of Mammalian Target of Rapamycin (mTOR) and Adenosine Monophosphate-Activated Protein Kinase (AMPK) Signaling in Skeletal Muscle Hypertrophy: A Literature Review With Implications for Health and Disease
Jeong, S. Y. (2025) · Cureus · doi:10.7759/cureus.96018 · Cited by 5
Glutamine Supplementation and Exercise: A Narrative Review of Biochemical Mechanisms and Timing Strategies
Djordjevic, B., Stojiljković, V., Veličkov, A., Kocic, J., Milenković, J., Veljković, A., Bašić, J., & Cvetković, T. (2026) · Medicina · doi:10.3390/medicina62020329 · Cited by 4
Molecular basis of muscle wasting and emerging therapeutic strategies targeting degenerative muscle disorders
Jude, M., Rajasingh, S., Alway, S. E., & Rajasingh, J. (2026) · Experimental Cell Research · doi:10.1016/j.yexcr.2026.114969 · Cited by 4
AMPK Signalling in Heart Failure: From Metabolic Sensor to Context-Dependent Therapeutic Target
Arzouni, R., Aazar, R. F. M., Asakrieh, S., Cattan, S., & Jovanović, A. (2026) · Biomedicines · doi:10.3390/biomedicines14061362 · Cited by 4
“Although prolonged activation can maintain metabolic homeostasis under certain conditions, excessive suppression of anabolic signaling pathways may impair normal cellular growth, protein synthesis, and tissue repair [106,107].”
Global trends and hot topics in electrical stimulation of skeletal muscle research over the past decade: A bibliometric analysis
Huang, Y., Gong, Y., Liu, Y., & Lü, J.-Q. (2022) · Frontiers in Neurology · doi:10.3389/fneur.2022.991099 · Cited by 4
Impact of maternal protein supplementation during mid or late gestation on skeletal muscle energy metabolism of beef calves
Sanglard, L. P., Márquez, D. E. C., da Silva, W., Fontes, M. M. D. S., Costa, T. C., Júnior, D. T. V., Gionbelli, M. P., Serão, N. V. L., Sampaio, C. B., & Duarte, M. D. S. (2022) · Ciência Rural · doi:10.1590/0103-8478cr20210917 · Cited by 7
Comparative Transcriptome Analysis of mRNA and miRNA during the Development of Longissimus Dorsi Muscle of Gannan Yak and Tianzhu White Yak
Niu, Y., Guo, D., Wei, Y., Li, J., Bai, Y., Liu, Z., Jia, X., Chen, Z., Li, L., Shi, B., et al. (2024) · Animals · doi:10.3390/ani14152278 · Cited by 3
“For instance, the AMPK signaling pathway plays a critical role in the reparative process following muscle injury [11,12].”
BackgroundInfluential
Effect of Combining Exercise with Adipose-Derived Mesenchymal Stem Cells in Muscle Atrophy Model of Sarcopenia
Jeong, D., Kim, M.-J., & Park, C. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26020451 · Cited by 3
Molecular signaling effects of electrical stimulation of the soleus muscle during 6 days of dry immersion
Sharlo, K. A., Lvova, I. D., Vilchinskaya, N. A., Tyganov, S. A., Turtikova, O. V., Sergeeva, K. V., Bokov, R. O., Shenkman, B. S., Tomilovskaya, E., & Orlov, O. I. (2025) · Sports Medicine and Health Science · doi:10.1016/j.smhs.2025.06.002 · Cited by 3
Knockdown of Death-Associated Protein Expression Induces Global Transcriptome Changes in Proliferating and Differentiating Muscle Satellite Cells
Horton, K. A., Sporer, K. R. B., Tempelman, R. J., Malila, Y., Reed, K. M., Velleman, S. G., & Strasburg, G. M. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.01036 · Cited by 3
The role of 5′-adenosine monophosphate-activated protein kinase (AMPK) in skeletal muscle atrophy
Dang, K., Farooq, H. M. U., GAO, Y., Deng, X., & Qian, A. (2022) · Biocell · doi:10.32604/biocell.2023.023766 · Cited by 3
“…activate GTPase, which can convert GTP to GDP and can form a complex with TSC1 and TBC1D7, reducing the ability of a GTPase, Rheb, whose binding with GTP is needed for mTORC1 activity. c. AMPK can phosphorylate RAPTOR, leading to impaired mTORC1 activity mediated by 14-3-3 proteins (Thomson, 2018).”
BackgroundInfluential
Autophagy signaling in hypertrophied muscles of diabetic and control rats
Scervino, M. V. M., Fortes, M. A. S., Vitzel, K. F., de Souza, D. R., Murata, G. M., Santana, G. O., da Silva, E. B., Levada‐Pires, A. C., Kuwabara, W. M. T., Alba‐Loureiro, T. C., et al. (2023) · FEBS Open Bio · doi:10.1002/2211-5463.13677 · Cited by 3
Involvement of the AMPK Pathways in Muscle Development Disparities across Genders in Muscovy Ducks
Zhao, W., He, Y., Du, Z., Yu, X., Chen, J., Li, A., & Huang, C. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms251810132 · Cited by 3
“Once activated, phosphorylated AMPK leads to the negative feedback regulation of key lipogenic genes such as SREBP1 [10,24], CD36 [25], and CPT1A [24], thereby promoting muscle cell growth, development, and regeneration [26,27].”
Background
Ablation of LKB1 gene changes the lipid profiles of goat intramuscular fat and enhances polyunsaturated fatty acids deposition
Sha, P., Feng, X., Wang, Y., Meng, J., Deng, L., Ma, Z., Li, D., Wang, J., Zhou, Z., Zhu, J., et al. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.138268 · Cited by 2
Sirt2 deficiency aggravates intramuscular adipose tissue infiltration and impairs myogenesis with aging in male mice
Lee, E. H., Park, S., & Jeong, K. (2025) · Biogerontology · doi:10.1007/s10522-025-10238-7 · Cited by 2
“Furthermore, liver kinase B1 (LKB1), an upstream activator of AMPK, promotes myogenic differentiation by destabilizing microtubules (Mian et al. 2012; Thomson 2018).”
The regeneration model of aging and its practical implications
Dassoff, E. (2026) · Discover Medicine · doi:10.1007/s44337-025-00558-5 · Cited by 2
“Indeed, AMPK hyper-activation can blunt the proliferation and differentiation of myoblasts in culture [159].”
Gardeniae Fructus Extract Alleviates Dexamethasone-Induced Muscle Atrophy in Mice
Lee, J. A., Lee, S. H., Shin, M.-R., Park, H.-J., & Roh, S. (2022) · Journal of Medicinal Food · doi:10.1089/jmf.2022.k.0038 · Cited by 2
“21 Also, the mitochondrial dysfunction due to MA results in insufﬁcient energy supply and activation of AMPK, which promotes the expression of MuRF-1 and MAFbx/Atrogin-1, in turn accelerating muscle breakdown.”
Metformin Protects Rat Skeletal Muscle from Physical Exercise-Induced Injury
Abbadessa, G., Maniscalco, E., Grasso, L., Popara, J., Scipio, F. D., Franco, F., Mancardi, D., Pigozzi, F., Borrione, P., Berta, G. N., et al. (2023) · Biomedicines · doi:10.3390/biomedicines11092334 · Cited by 2
“Recently, it has been reported the phosphorylation of Ser2448 leads to inactivation of mTOR as part of an inhibitory feedback mechanism induced by the activated form of p70S6K, which switches off the mTOR signal [60,61].”
The impact of exercise on cardiovascular system: Molecular signaling pathway and cardiac adaptations
Toktarbay, B., Khamitova, Z. K., Zholshybek, N., Jumadilova, D., Rakhmanov, Y., Bekbossynova, M., Gaipov, A., & Salustri, A. (2023) · Journal of Clinical Medicine of Kazakhstan · doi:10.23950/jcmk/13825 · Cited by 2
Naringenin promotes the expression of oxidized myofibers via the PKA signaling pathway in C57BL/6J mice and C2C12 cells
Shi, Y., Wang, Y., Shi, X., Zhang, X., & Zhang, S. (2023) · Journal of Functional Foods · doi:10.1016/j.jff.2023.105902 · Cited by 3
Temporal expression of mitochondrial life cycle markers during acute and chronic overload of rat plantaris muscles
Hyatt, J. K., Lu, E. J., & McCall, G. E. (2024) · Frontiers in Physiology · doi:10.3389/fphys.2024.1420276 · Cited by 2
“…directed toward maintaining the mitochondrial pool by activating mitochondrial biogenesis or for another divergent pathway such as mito/autophagy (Thomson, 2018; Seabright and Lai, 2020); at a minimum, these ﬁ ndings suggest that the activation of AMPK participates in maintaining the…”
Background
A possibility of uncoupling protein 1 induction with the enhancement of myogenesis related to ruminal fermentation
Diao, Z., Jia, S., Itoyama, E., Yoshioka, H., Murakami, M., & Funaba, M. (2024) · Scientific Reports · doi:10.1038/s41598-024-81272-7 · Cited by 2
“Although the hyperactivation of AMPK by use of synthetic reagent AICAR inhibits myogenesis 33 , the physiological significance of weak phosphorylation of AMPK remains unclear.”
Unconventional myosin VI is involved in regulation of muscle energy metabolism
Wojton, D., Dymkowska, D., Matysniak, D. P., Topolewska, M., Rędowicz, M. J., & Lehka, L. (2025) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00300.2025 · Cited by 2

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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