The role of exercise-induced myokines in regulating metabolism

Huh, Joo Young

doi:10.1007/s12272-017-0994-y

Cited by 242Exercise and Physiological ResponsesMuscle Physiology and DisordersAdipokines, Inflammation, and Metabolic Diseases

The role of exercise-induced myokines in regulating metabolism

Huh, Joo Young·2018·Archives of Pharmacal Research

DOI 10.1007/s12272-017-0994-y

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Abstract

Exercise has beneficial effects in ameliorating metabolic disorders, and a combined therapeutic regimen of regular exercise and pharmaceutical treatment is often recommended. Exercise biology is complex and it involves various metabolic and molecular changes that translate into changes in substrate utilization, enzyme activation, and alternatively, improvement in exercise performance. Besides the effect of exercise on muscle metabolism, it has recently been discovered that contracting muscle can induce secretion of molecules called myokines. In the past few decades, a number of myokines have been discovered, such as interleukin-6, irisin, myostatin, interleukin-15, brain-derived neurotrophic factor, β-aminoisobutyric acid, meteorin-like, leukemia inhibitory factor, and secreted protein acidic and rich in cysteine, through secretome analysis. The existence of myokines has enhanced our understanding of how muscles communicate with other organs such as adipose tissue, liver, bone, and brain to exert beneficial effects of exercise at the whole body level. In this review, we focus on the role of these myokines in regulating local muscle metabolism as well as systemic metabolism in an autocrine/paracrine/endocrine fashion. The therapeutic potential of myokines and the natural or synthetic compounds known to date that regulate myokines are also discussed.

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These myokines exert beneficial physiologic and metabolic effects in skeletal muscle and distant tissues such as white adipose tissue, bone, liver, central nervous system, and immune cells to drive a systemic anti-inflammatory and insulin-sensitive state permissive for optimization of total-body energy expenditure.
“These exert beneficial physiologic and metabolic effects not only in SkM itself but also in distant tissues such as white adipose tissue (WAT), bone, liver, the central nervous system (CNS), and cells of the immune system to drive a systemic anti-inflammatory and insulin-sensitive state, permissive for optimization of total-body energy expenditure [5,7,26,27].”
From The Role of Exercise in the Interplay between Myokines, Hepatokines, Osteokines, Adipokines, and Modulation of Inflammation for Energy Substrate Redistribution and Fat Mass Loss: A Review (2020) · cites this paper as [27]
Myostatin contributes to the induction of PGC-1α, FNDC5, and irisin in skeletal muscle.
“It contributes to the induction of PGC-1α, FNDC5, and irisin in SkM [27,49,133].”
From The Role of Exercise in the Interplay between Myokines, Hepatokines, Osteokines, Adipokines, and Modulation of Inflammation for Energy Substrate Redistribution and Fat Mass Loss: A Review (2020) · cites this paper as [27]
Myostatin inhibits muscle cell growth and differentiation, and irisin stimulates the increase of muscle mass.
“It is believed that myostatin inhibits muscle cell growth and differentiation, and irisin stimulates the increase of muscle mass (42, 43).”
From Diabetes and Sarcopenic Obesity: Pathogenesis, Diagnosis, and Treatments (2020) · cites this paper as [42]

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Irisin Lowers Blood Pressure by Improvement of Endothelial Dysfunction via AMPK‐Akt‐eNOS‐NO Pathway in the Spontaneously Hypertensive Rat
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Background
Computational reconstruction of the human skeletal muscle secretome
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Protectin DX alleviates insulin resistance by activating a myokine-liver glucoregulatory axis
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Leukemia Inhibitory Factor and Its Receptor Promote Adipocyte Differentiation via the Mitogen-activated Protein Kinase Cascade
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β-aminoisobutyric acid attenuates hepatic endoplasmic reticulum stress and glucose/lipid metabolic disturbance in mice with type 2 diabetes
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Interleukin-6 induces impairment in human subcutaneous adipogenesis in obesity-associated insulin resistance
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Irisin Controls Growth, Intracellular Ca2+ Signals, and Mitochondrial Thermogenesis in Cardiomyoblasts
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The effects of brain-derived neurotrophic factor on insulin signal transduction in the liver of diabetic mice
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Irisin and FNDC5: effects of 12-week strength training, and relations to muscle phenotype and body mass composition in untrained women
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Comparative proteomic analysis of the insulin‐induced L6 myotube secretome
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Interleukin-15 decreases proteolysis in skeletal muscle: A direct effect
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Protective effect of brain-derived neurotrophic factor on pancreatic islets in obese diabetic mice
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Blockade of ActRIIB Signaling Triggers Muscle Fatigability and Metabolic Myopathy
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Inhibition of Myoblast Differentiation by Tumor Necrosis Factor α Is Mediated by c-Jun N-terminal Kinase 1 and Leukemia Inhibitory Factor
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SOCS1, SOCS3, and PIAS1 Promote Myogenic Differentiation by Inhibiting the Leukemia Inhibitory Factor-Induced JAK1/STAT1/STAT3 Pathway
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Suppression of muscle wasting by the plant‐derived compound ursolic acid in a model of chronic kidney disease
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Small Molecules Dorsomorphin and LDN-193189 Inhibit Myostatin/GDF8 Signaling and Promote Functional Myoblast Differentiation
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Ursolic acid-induced elevation of serum irisin augments muscle strength during resistance training in men
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Contraction and AICAR Stimulate IL-6 Vesicle Depletion From Skeletal Muscle Fibers In Vivo
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Chitinase-3-like protein 1 protects skeletal muscle from TNFα-induced inflammation and insulin resistance
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Loganin possesses neuroprotective properties, restores SMN protein and activates protein synthesis positive regulator Akt/mTOR in experimental models of spinal muscular atrophy
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METRNL decreases during adipogenesis and inhibits adipocyte differentiation leading to adipocyte hypertrophy in humans
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Glucoregulation During Exercise: The Role of the Neuroendocrine System
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Clearance and fate of leukemia‐inhibitory factor (LIF) after injection into mice
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Leukemia inhibitory factor: A paracrine mediator of bone metabolism
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SPARC interacts with AMPK and regulates GLUT4 expression
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Fenofibrate, a PPARα agonist, decreases atrogenes and myostatin expression and improves arthritis-induced skeletal muscle atrophy
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Exercise-mimetic AICAR transiently benefits brain function
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Inorganic Nitrate Mimics Exercise-Stimulated Muscular Fiber-Type Switching and Myokine and γ-Aminobutyric Acid Release
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Exenatide treatment increases serum irisin levels in patients with obesity and newly diagnosed type 2 diabetes.
Liu, J., Hu, Y., Zhang, H., Xu, Y., & Wang, G. (2016) · Journal of diabetes and its complications · doi:10.1016/j.jdiacomp.2016.07.020 · Cited by 51 · see citing works
Safety, Tolerability, Pharmacokinetics, and Pharmacodynamics of Domagrozumab (PF‐06252616), an Antimyostatin Monoclonal Antibody, in Healthy Subjects
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Glucocorticoid receptor positively regulates transcription of FNDC5 in the liver
Kim, H. K., Jeong, Y. J., Song, I.-S., Noh, Y. H., Seo, K. W., Kim, M., & Han, J. (2017) · Scientific Reports · doi:10.1038/srep43296 · Cited by 49 · see citing works
Protective effect of myokine IL-15 against H2O2-mediated oxidative stress in skeletal muscle cells
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Building muscle, browning fat and preventing obesity by inhibiting myostatin
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Supplementation of Magnolol Attenuates Skeletal Muscle Atrophy in Bladder Cancer-Bearing Mice Undergoing Chemotherapy via Suppression of FoxO3 Activation and Induction of IGF-1
Chen, M.-C., Chen, Y.-L., Lee, C.-F., Hung, C.-H., & Chou, T.-C. (2015) · PLOS ONE · doi:10.1371/journal.pone.0143594 · Cited by 45 · see citing works
Ionomycin, but not physiologic doses of epinephrine, stimulates skeletal muscle Interleukin-6 mRNA expression and protein release
Holmes, A. G., Watt, M. J., Carey, A. L., & Febbraio, M. A. (2004) · Metabolism · doi:10.1016/j.metabol.2004.05.015 · Cited by 44 · see citing works
Atomoxetine Prevents Dexamethasone-Induced Skeletal Muscle Atrophy in Mice
Jesinkey, S. R., Korrapati, M. C., Rasbach, K. A., Beeson, C. C., & Schnellmann, R. G. (2014) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.114.217380 · Cited by 44 · see citing works
Effects of Zidovudine, Stavudine and β-Aminoisobutyric Acid on Lipid Homeostasis in Mice: Possible Role in Human Fat Wasting
Maisonneuve, C., Igoudjil, A., Begriche, K., Lettéron, P., Guimont, M.-C., Bastin, J., Laigneau, J., Pessayre, D., & Fromenty, B. (2004) · Antiviral Therapy · doi:10.1177/135965350400900513 · Cited by 43 · see citing works
The exercise-regulated myokine chitinase-3-like protein 1 stimulates human myocyte proliferation
Görgens, S. W., Hjorth, M., Eckardt, K., Wichert, S., Norheim, F., Holen, T., Lee-Ødegård, S., Langleite, T. M., Birkeland, K. I., Stadheim, H. K., et al. (2015) · Acta Physiologica · doi:10.1111/apha.12579 · Cited by 42 · see citing works
SPARC Interacts with Actin in Skeletal Muscle in Vitro and in Vivo
Jørgensen, L. H., Jepsen, P. L., Boysen, A., Dalgaard, L. B., Hvid, L. G., Ørtenblad, N., Ravn, D., Sellathurai, J., Møller‐Jensen, J., Lochmüller, H., et al. (2016) · American Journal Of Pathology · doi:10.1016/j.ajpath.2016.10.013 · Cited by 41 · see citing works
Calcineurin activates interleukin-6 transcription in mouse skeletal muscle in vivo and in C2C12myotubes in vitro
Allen, D. L., Uyenishi, J. J., Cleary, A. S., Mehan, R. S., Lindsay, S. F., & Reed, J. M. (2009) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00325.2009 · Cited by 40 · see citing works
Rolipram-induced improvement of cognitive function correlates with changes in hippocampal CREB phosphorylation, BDNF and Arc protein levels
Zhong, Y., Zhu, Y., He, T., Li, W., Yan, H., & Miao, Y. (2015) · Neuroscience Letters · doi:10.1016/j.neulet.2015.09.023 · Cited by 39 · see citing works
Myostatin Neutralization Results in Preservation of Muscle Mass and Strength in Preclinical Models of Tumor-Induced Muscle Wasting
Smith, R. C., Cramer, M. S., Mitchell, P. J., Capen, A. R., Huber, L., Wang, R., Myers, L., Jones, B. E., Eastwood, B. J., Ballard, D. W., et al. (2015) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-14-0681 · Cited by 39 · see citing works
Dihydromyricetin stimulates irisin secretion partially via the PGC-1α pathway
Zhou, Q., Chen, K., Liu, P., Gao, Y., Zou, D., Deng, H., Huang, Y., Zhang, Q., Zhu, J., & Mi, M. (2015) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2015.05.036 · Cited by 39 · see citing works
Resveratrol Increases Serum BDNF Concentrations and Reduces Vascular Smooth Muscle Cells Contractility via a NOS-3-Independent Mechanism
Wiciński, M., Malinowski, B., Węclewicz, M. M., Grześk, E., & Grześk, G. (2017) · BioMed Research International · doi:10.1155/2017/9202954 · Cited by 39 · see citing works
β-Aminoisobutyric acid ameliorates the renal fibrosis in mouse obstructed kidneys via inhibition of renal fibroblast activation and fibrosis
Wang, H., Qian, J., Zhao, X., Xing, C., & Sun, B. (2017) · Journal of Pharmacological Sciences · doi:10.1016/j.jphs.2016.12.005 · Cited by 38 · see citing works
Formoterol treatment downregulates the myostatin system in skeletal muscle of cachectic tumour-bearing rats
Busquets, S., Toledo, M., Marmonti, E., Orpí, M., Capdevila, E., Betancourt, A., López-Soriano, F. J., & Argilés, J. M. A. (2011) · Oncology Letters · doi:10.3892/ol.2011.442 · Cited by 37 · see citing works
Translational Pharmacokinetic/Pharmacodynamic Analysis of MYO‐029 Antibody for Muscular Dystrophy
Singh, P., Rong, H., Gordi, T., Bosley, J., & Bhattacharya, I. (2016) · Clinical and Translational Science · doi:10.1111/cts.12420 · Cited by 37 · see citing works
Pharmacological inhibition of myostatin protects against skeletal muscle atrophy and weakness after anterior cruciate ligament tear
Wolfe, C. N., Gumucio, J. P., Grekin, J. A., Khouri, R. K., Russell, A. J., Bedi, A., & Mendias, C. L. (2017) · Journal of Orthopaedic Research® · doi:10.1002/jor.23537 · Cited by 36 · see citing works
Leukemia inhibitory factor increases glucose uptake in mouse skeletal muscle
Brandt, N., O’Neill, H. M., Kleinert, M., Schjerling, P., Vernet, E., Steinberg, G. R., Richter, E. A., & Jørgensen, S. B. (2015) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00313.2014 · Cited by 35 · see citing works
Formoterol decreases muscle wasting as well as inflammation in the rat model of rheumatoid arthritis
Gómez-SanMiguel, A. B., Gómez-Moreira, C., Nieto‐Bona, M. P., Fernández‐Galaz, C., Villanúa, M. Á., Martı́n, A. I., & López‐Calderón, A. (2016) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00503.2015 · Cited by 34 · see citing works
PGC-1 mediates the regulation of metformin in muscle irisin expression and function.
Yang, Z., Xu, C., Chen, Y., & Zhao, Q. (2015) · Europe PMC (PubMed Central) · Cited by 32 · see citing works
IL-15 Mediates Mitochondrial Activity through a PPARδ-Dependent-PPARα-Independent Mechanism in Skeletal Muscle Cells
Thornton, S. M., Krolopp, J. E., & Abbott, M. J. (2016) · PPAR Research · doi:10.1155/2016/5465804 · Cited by 31 · see citing works
Potential role for the VDR agonist elocalcitol in metabolic control: Evidences in human skeletal muscle cells
Antinozzi, C., Corinaldesi, C., Giordano, C., Pisano, A., Cerbelli, B., Migliaccio, S., Luigi, L. D., Stefanantoni, K., Vannelli, G. B., Minisola, S., et al. (2016) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2016.12.010 · Cited by 31 · see citing works
Taurine prevented cell cycle arrest and restored neurotrophic gene expression in arsenite-treated SH-SY5Y cells
Chou, C.-T., Lin, W., Kong, Z., Chen, S., & Hwang, D. (2013) · Amino Acids · doi:10.1007/s00726-013-1524-y · Cited by 20 · see citing works
Leptin Rapidly Induces the Expression of Metabolic and Myokine Genes in C2C12 Muscle Cells to Regulate Nutrient Partition and Oxidation
Nozhenko, Y., Rodríguez, A. M., & Palou, A. (2015) · Cellular Physiology and Biochemistry · doi:10.1159/000369678 · Cited by 19 · see citing works

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PGC-1α as a Pivotal Factor in Lipid and Metabolic Regulation
Cheng, C., Ku, H., & Lin, H. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19113447 · Cited by 434 · see citing works
Skeletal muscle atrophy: From mechanisms to treatments
Yin, L., Li, N., Jia, W., Wang, N., Liang, M., Yang, X., & Du, G. (2021) · Pharmacological Research · doi:10.1016/j.phrs.2021.105807 · Cited by 408 · see citing works
Resilience and immunity
Dantzer, R., Cohen, S., Russo, S. J., & Dinan, T. G. (2018) · Brain Behavior and Immunity · doi:10.1016/j.bbi.2018.08.010 · Cited by 313 · see citing works
Inflammation and sarcopenia: A focus on circulating inflammatory cytokines
Pan, L., Xie, W., Fu, X., Lu, W., Jin, H., Lai, J., Zhang, A., Yu, Y., Li, Y., & Xiao, W. (2021) · Experimental Gerontology · doi:10.1016/j.exger.2021.111544 · Cited by 307 · see citing works
The Role of Exercise in the Interplay between Myokines, Hepatokines, Osteokines, Adipokines, and Modulation of Inflammation for Energy Substrate Redistribution and Fat Mass Loss: A Review
Gonzalez-Gil, A. M., & Elizondo-Montemayor, L. (2020) · Nutrients · doi:10.3390/nu12061899 · Cited by 278 · see citing works
“It contributes to the induction of PGC-1α, FNDC5, and irisin in SkM [27,49,133].”
Background
Diabetes and Sarcopenic Obesity: Pathogenesis, Diagnosis, and Treatments
Wang, M., Tan, Y., Shi, Y., Wang, X., Liao, Z., & Wei, P. (2020) · Frontiers in Endocrinology · doi:10.3389/fendo.2020.00568 · Cited by 231 · see citing works
Myokines mediate the cross talk between skeletal muscle and other organs
Chen, W., Wang, L., You, W., & Shan, T. (2021) · Journal of Cellular Physiology · doi:10.1002/jcp.30033 · Cited by 162 · see citing works
Physical Exercise and Myokines: Relationships with Sarcopenia and Cardiovascular Complications
Barbalho, S. M., Flato, U. A. P., Tofano, R. J., Goulart, R. D. A., Guiguer, E. L., Detregiachi, C. R. P., Buchaim, D. V., Araújo, A. C., Buchaim, R. L., Reina, F. T. R., et al. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21103607 · Cited by 156 · see citing works
The Relevance of a Physical Active Lifestyle and Physical Fitness on Immune Defense: Mitigating Disease Burden, With Focus on COVID-19 Consequences
Filgueira, T. O., Castoldi, Â., Santos, L. E. R., de Amorim, G. J., Fernandes, M. S. D. S., Anastácio, W. D. L. D. N., Campos, E. Z., Santos, T. M., & Souto, F. O. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.587146 · Cited by 152 · see citing works
Exercise therapy for people with sarcopenic obesity: myokines and adipokines as effective actors
Alizadeh Pahlavani, H. (2022) · Frontiers in Endocrinology · doi:10.3389/fendo.2022.811751 · Cited by 145 · see citing works
“Therefore, expression and secretion of LIF protein after exercise have not been reported (78).”
Background
Multiple Roles in Neuroprotection for the Exercise Derived Myokine Irisin
Farshbaf, M. J., & Alviña, K. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.649929 · Cited by 143 · see citing works
Myokines in skeletal muscle physiology and metabolism: Recent advances and future perspectives
Das, D. K., Graham, Z. A., & Cardozo, C. P. (2020) · Acta Physiologica · doi:10.1111/apha.13367 · Cited by 129 · see citing works
Mechanisms 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
Mitochondrial dysfunction and skeletal muscle atrophy: Causes, mechanisms, and treatment strategies
Kubat, G. B., Bouhamida, E., Ülger, Ö., Türkel, İ., Pedriali, G., Ramaccini, D., Ekinci, Ö., Özerkliğ, B., Atalay, Ö., Patergnani, S., et al. (2023) · Mitochondrion · doi:10.1016/j.mito.2023.07.003 · Cited by 128 · see citing works
Inactivity and Skeletal Muscle Metabolism: A Vicious Cycle in Old Age
Rezuş, E., Burlui, A., Cardoneanu, A., Rezuș, C., Codreanu, C., Parvu, M., Zota, G. R., & Tamba, B.-I. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21020592 · Cited by 117 · see citing works
Interleukin-15 facilitates muscle regeneration through modulation of fibro/adipogenic progenitors
Kang, X., Yang, M., Shi, Y., Xie, M., Zhu, M. P., Zheng, X., Zhang, C., Ge, Z., Bian, X., Lv, J.-T., et al. (2018) · Cell Communication and Signaling · doi:10.1186/s12964-018-0251-0 · Cited by 117 · see citing works
Exercise-Induced Irisin Decreases Inflammation and Improves NAFLD by Competitive Binding with MD2
Zhu, W., Sahar, N.-E., Javaid, H. M. A., Pak, E. S., Liang, G., Wang, Y., Ha, H., & Huh, J. Y. (2021) · Cells · doi:10.3390/cells10123306 · Cited by 116 · see citing works
Self-citation
Anti-Inflammatory Effect of Muscle-Derived Interleukin-6 and Its Involvement in Lipid Metabolism
Nara, H., & Watanabe, R. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22189889 · Cited by 111 · see citing works
Risk Factors of Severe COVID-19: A Review of Host, Viral and Environmental Factors
Zsichla, L., & Müller, V. (2023) · Viruses · doi:10.3390/v15010175 · Cited by 113 · see citing works
Non-Alcoholic Fatty Liver Disease in Lean and Non-Obese Individuals: Current and Future Challenges
Kuchay, M. S., Martínez‐Montoro, J. I., Choudhary, N. S., Fernández‐García, J. C., & Ramos‐Molina, B. (2021) · Biomedicines · doi:10.3390/biomedicines9101346 · Cited by 103 · see citing works
Meteorin-like/Metrnl, a novel secreted protein implicated in inflammation, immunology, and metabolism: A comprehensive review of preclinical and clinical studies
Li, Z., Gao, Z., Sun, T., Zhang, S., Yang, S., Zheng, M., & Shen, H. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1098570 · Cited by 97 · see citing works
Exercise Inhibits NLRP3 Inflammasome Activation in Obese Mice via the Anti-Inflammatory Effect of Meteorin-like
Javaid, H. M. A., Sahar, N.-E., Zhuge, D., & Huh, J. Y. (2021) · Cells · doi:10.3390/cells10123480 · Cited by 96 · see citing works
Self-citation
Muscle-Bone Crosstalk in the Masticatory System: From Biomechanical to Molecular Interactions
Buvinic, S., Balanta‐Melo, J., Kupczik, K., Vásquez, W., Beato, C., & Toro‐Ibacache, V. (2021) · Frontiers in Endocrinology · doi:10.3389/fendo.2020.606947 · Cited by 82 · see citing works
Iron Metabolism of the Skeletal Muscle and Neurodegeneration
Hałoń, M., Borkowska, A., Herman-Antosiewicz, A., & Antosiewicz, J. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00165 · Cited by 69 · see citing works
If my muscle could talk: Myokines as a biomarker of frailty
Coelho‐Júnior, H. J., Picca, A., Calvani, R., Uchida, M. C., & Marzetti, E. (2019) · Experimental Gerontology · doi:10.1016/j.exger.2019.110715 · Cited by 69 · see citing works
Effects of Combined Resistance and Power Training on Cognitive Function in Older Women: A Randomized Controlled Trial
Coelho‐Júnior, H. J., Gonçalves, I. D. O., Sampaio, R. A. C., Sampaio, P. Y. S., Cadore, E. L., Calvani, R., Picca, A., Izquierdo, M., Marzetti, E., & Uchida, M. C. (2020) · International Journal of Environmental Research and Public Health · doi:10.3390/ijerph17103435 · Cited by 72 · see citing works
Functional role of skeletal muscle-derived interleukin-6 and its effects on lipid metabolism
Lin, W., Song, H., Shen, J., Wang, J., Yang, Y., Yang, Y., Cao, J., Xue, L., Zhao, F., Xiao, T., et al. (2023) · Frontiers in Physiology · doi:10.3389/fphys.2023.1110926 · Cited by 67 · see citing works
Irisin Exerts Inhibitory Effect on Adipogenesis Through Regulation of Wnt Signaling
Ma, E. B., Sahar, N.-E., Jeong, M., & Huh, J. Y. (2019) · Frontiers in Physiology · doi:10.3389/fphys.2019.01085 · Cited by 69 · see citing works
Self-citation
Myokines: a descriptive review
Barbalho, S. M., Neto, E. V. P., Goulart, R. D. Á., Bechara, M. D., Chagas, E. F. B., Audi, M., Campos, L. M. G., Guiguer, É. L., Buchaim, R. L., Buchaim, D. V., et al. (2020) · The Journal of Sports Medicine and Physical Fitness · doi:10.23736/s0022-4707.20.10884-3 · Cited by 67 · see citing works
Nutrients and Pathways that Regulate Health Span and Life Span
Pignatti, C., D’Adamo, S., Stefanelli, C., Flamigni, F., & Cetrullo, S. (2020) · Geriatrics · doi:10.3390/geriatrics5040095 · Cited by 64 · see citing works
Regular aerobic exercise correlates with reduced anxiety and incresed levels of irisin in brain and white adipose tissue
Uysal, N., Yüksel, O., Kızıldağ, S., Yüce, Z., Gümüş, H., Karakılıç, A., Güvendi, G., Koç, B., Kandiş, S., & Ateş, M. (2018) · Neuroscience Letters · doi:10.1016/j.neulet.2018.04.023 · Cited by 60 · see citing works
Exercise-induced Musclin determines the fate of fibro-adipogenic progenitors to control muscle homeostasis
Kang, X., Qian, J., Shi, Y.-X., Bian, X., Zhang, L., Li, G., Wang, L., Zhao, J., Dong, Z., Yang, M., et al. (2024) · Cell stem cell · doi:10.1016/j.stem.2023.12.011 · Cited by 59 · see citing works
The role of physical activity in individuals with cardiovascular risk factors: an opinion paper from Italian Society of Cardiology-Emilia Romagna-Marche and SIC-Sport
Nasi, M., Patrizi, G., Pizzi, C., Landolfo, M., Boriani, G., Dei, A., Cicero, A. F. G., Fogacci, F., Rapezzi, C., Sisca, G., et al. (2019) · Journal of Cardiovascular Medicine · doi:10.2459/jcm.0000000000000855 · Cited by 60 · see citing works
Irisin and Autophagy: First Update
Pesce, M., Ballerini, P., Paolucci, T., Puca, I., Farzaei, M. H., & Patruno, A. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21207587 · Cited by 59 · see citing works
Myokines: Metabolic regulation in obesity and type 2 diabetes
Chen, Z.-T., Weng, Z.-X., Lin, J. D., & Meng, Z.-X. (2024) · Life Metabolism · doi:10.1093/lifemeta/loae006 · Cited by 58 · see citing works
The Important Role of Adiponectin and Orexin-A, Two Key Proteins Improving Healthy Status: Focus on Physical Activity
Polito, R., Monda, V., Nigro, E., Messina, A., Maio, G. D., Giuliano, M. T., Orrù, S., Imperlini, E., Calcagno, G., Mosca, L., et al. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.00356 · Cited by 55 · see citing works
Acquired Resilience: An Evolved System of Tissue Protection in Mammals
Stone, J., Mitrofanis, J., Johnstone, D. M., Falsini, B., Bisti, S., Adam, P., Bravo‐Nuevo, A., George‐Weinstein, M., Mason, R. S., & Eells, J. T. (2018) · Dose-Response · doi:10.1177/1559325818803428 · Cited by 51 · see citing works
Long‐term effects of an oral elemental nutritional supplement on post‐gastrectomy body weight loss in gastric cancer patients (KSES002)
Kimura, Y., Nishikawa, K., Kishi, K., Inoue, K., Matsuyama, J., Akamaru, Y., Tamura, S., Kawada, J., Kawase, T., Kawabata, R., et al. (2019) · Annals of Gastroenterological Surgery · doi:10.1002/ags3.12290 · Cited by 50 · see citing works
Fibroblast growth factor 2 exacerbates inflammation in adipocytes through NLRP3 inflammasome activation
Zhuge, D., Javaid, H. M. A., Sahar, N.-E., Zhao, Y., & Huh, J. Y. (2020) · Archives of Pharmacal Research · doi:10.1007/s12272-020-01295-2 · Cited by 49 · see citing works
Self-citation
Beyond the Calorie Paradigm: Taking into Account in Practice the Balance of Fat and Carbohydrate Oxidation during Exercise?
Brun, J.-F., Myzia, J., Varlet-Marie, E., Raynaud de Mauverger, E., & Mercier, J. (2022) · Nutrients · doi:10.3390/nu14081605 · Cited by 48 · see citing works
Physiopathology of Lifestyle Interventions in Non-Alcoholic Fatty Liver Disease (NAFLD)
Carneros, D., López‐Lluch, G., & Bustos, M. (2020) · Nutrients · doi:10.3390/nu12113472 · Cited by 47 · see citing works
Protective Effect of Exercise in Pregnant Women Including Those Who Exceed Weight Gain Recommendations: A Randomized Controlled Trial
Peláez, M., Gonzalez‐Cerron, S., Montejo, R., & Barakat, R. (2019) · Mayo Clinic Proceedings · doi:10.1016/j.mayocp.2019.01.050 · Cited by 45 · see citing works
Promise of irisin to attenuate cognitive dysfunction in aging and Alzheimer’s disease
Madhu, L. N., Somayaji, Y., & Shetty, A. K. (2022) · Ageing Research Reviews · doi:10.1016/j.arr.2022.101637 · Cited by 49 · see citing works
β-aminoisobutyric acid protects against vascular inflammation through PGC-1β-induced antioxidative properties
Sawada, M., Yamamoto, H., Ogasahara, A., Tanaka, Y., & Kihara, S. (2019) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2019.06.141 · Cited by 44 · see citing works
Myokines and Microbiota: New Perspectives in the Endocrine Muscle–Gut Axis
Saponaro, F., Bertolini, A., Baragatti, R., Galfo, L., Chiellini, G., Saba, A., & D’Urso, G. (2024) · Nutrients · doi:10.3390/nu16234032 · Cited by 43 · see citing works
The Effects of Exercise on IL-6 Levels and Cognitive Performance in Patients with Schizophrenia
Gómez-Rubio, P., & Trapero, I. (2019) · Diseases · doi:10.3390/diseases7010011 · Cited by 43 · see citing works
The muscle to bone axis (and viceversa): An encrypted language affecting tissues and organs and yet to be codified?
Bosco, F., Musolino, V., Gliozzi, M., Nucera, S., Carresi, C., Zito, M. C., Scarano, F., Scicchitano, M., Reale, F., Ruga, S., et al. (2021) · Pharmacological Research · doi:10.1016/j.phrs.2021.105427 · Cited by 45 · see citing works
Exercise Improves Metabolism and Alleviates Atherosclerosis via Muscle-Derived Extracellular Vesicles
Wang, Y., Liu, Y., Zhang, S., Li, N., Xing, C., Wang, C., Wang, J., Wei, M., Yang, G., & Yuan, L. (2023) · Aging and Disease · doi:10.14336/ad.2022.1131 · Cited by 44 · see citing works
Exercise-induced BDNF promotes PPARδ-dependent reprogramming of lipid metabolism in skeletal muscle during exercise recovery
Chan, W. S., Ng, C. F., Pang, B. P. S., Hang, M., Tse, M. C. L., Iu, E. C. Y., Ooi, X. C., Yang, X., Kim, J. K., Lee, C. W., et al. (2024) · Science Signaling · doi:10.1126/scisignal.adh2783 · Cited by 43 · see citing works
Inflammatory and Oxidative Stress Markers in Skeletal Muscle of Obese Subjects
Catalán, V., Frühbeck, G., & Gómez‐Ambrosi, J. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-812504-5.00008-8 · Cited by 43 · see citing works
Muscle-Bone Crosstalk in Chronic Kidney Disease: The Potential Modulatory Effects of Exercise
Leal, D. V., Ferreira, A., Watson, E. L., Wilund, K. R., & Viana, J. L. (2021) · Calcified Tissue International · doi:10.1007/s00223-020-00782-4 · Cited by 40 · see citing works
Aerobic Exercise in the Management of Metabolic Dysfunction Associated Fatty Liver Disease
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Myokines are one of the key elements of interaction between skeletal muscles and other systems of human body necessary for adaptation to physical loads
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Authors: Huh, J. Y.
Affiliations: Chonnam National University (KR)
Corresponding author: Huh, Joo Young
ORCID: Huh, Joo Young
Venue: Archives of Pharmacal Research
Publisher: Springer Science and Business Media LLC
Published: 2017-11-25
Volume: 41
Issue: 1
Pages: 14-29
ISSN: 0253-6269 (ISSN-L)
1976-3786
DOI: 10.1007/s12272-017-0994-y
OpenAlex: W2770919725
Cited by: 242
References: 176
Citations by year: 2026: 15 · 2025: 20 · 2024: 27 · 2023: 39 · 2022: 34 · 2021: 34 · 2020: 31 · 2019: 29 · 2018: 13
FWCI: 2.72
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (unspecified)
Locations: Archives of Pharmacal Research (publishedVersion)
PubMed (publishedVersion)
Funders: National Research Foundation of Korea (2015R1C1A1A02037367)
Chonnam National University (2014-2215, 2015-3035)
Topics: Health Sciences › Medicine › Rehabilitation › Exercise and Physiological Responses
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
Health Sciences › Medicine › Epidemiology › Adipokines, Inflammation, and Metabolic Diseases
Keywords: muscle metabolism, systemic metabolism, interleukin-6, irisin, myostatin, IL-15, brain-derived neurotrophic factor, meteorin-like, leukemia inhibitory factor, SARC, metabolic disorders
MeSH terms: Aminoisobutyric Acids, Cysteine, Fibronectins, Humans, Exercise, Interleukin-6, Muscle, Skeletal, Brain-Derived Neurotrophic Factor, Interleukin-15, Myostatin

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The role of exercise-induced myokines in regulating metabolism

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