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

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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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FNDC5 overexpression and irisin ameliorate glucose/lipid metabolic derangements and enhance lipolysis in obesity
Xiong, X.-Q., Chen, D., Sun, H.-J., Ding, L., Wang, J.-J., Chen, Q., Li, Y.-H., Zhou, Y.-B., Han, Y., Zhang, F., et al. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2015.06.017 · Cited by 242
Fatty acid mobilization from adipose tissue during exercise
Horowitz, J. F. (2003) · Trends in Endocrinology and Metabolism · doi:10.1016/s1043-2760(03)00143-7 · Cited by 232
Association of interleukin-15 protein and interleukin-15 receptor genetic variation with resistance exercise training responses
Riechman, S. E., Balasekaran, G., Roth, S. M., & Ferrell, R. E. (2004) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00491.2004 · Cited by 228
Effect of endurance training on skeletal muscle myokine expression in obese men: Identification of apelin as a novel myokine
Besse-Patin, A., Montastier, E., Vinel, C., Castan-Laurell, I., Louche, K., Dray, C., Daviaud, D., Mir, L., Marques, M.-A., Thalamas, C., et al. (2014) · International Journal of Obesity · doi:10.1038/ijo.2013.158 · Cited by 227 · cited 1×
“Apelin is a well-known adipokine upregulated in obese individuals undergoing an 8 week endurance training, and thus, it is identified as a novel exercise-regulated myokine and is suggested to improve muscle metabolism and function (Besse-Patin et al. 2014).”
Background
Irisin, a Novel Myokine, Regulates Glucose Uptake in Skeletal Muscle Cells via AMPK
Lee, H. J., Lee, J. O., Kim, N., Kim, J. K., Kim, H. I., Lee, Y. W., Kim, S. J., Choi, J., Oh, Y., Kim, J. H., et al. (2015) · Molecular Endocrinology · doi:10.1210/me.2014-1353 · Cited by 224
Plasma irisin levels progressively increase in response to increasing exercise workloads in young, healthy, active subjects
Daskalopoulou, S. S., Cooke, A. B., Sandoval, Y.-H. G., Mutter, A. F., Filippaios, A., Mesfum, E. T., & Mantzoros, C. S. (2014) · European Journal of Endocrinology · doi:10.1530/eje-14-0204 · Cited by 220
Role of IL-6 in Exercise Training- and Cold-Induced UCP1 Expression in Subcutaneous White Adipose Tissue
Knudsen, J. G., Murholm, M., Carey, A. L., Biensø, R. S., Basse, A. L., Allen, T. L., Hidalgo, J., Kingwell, B. A., Febbraio, M. A., Hansen, J. B., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0084910 · Cited by 219
Inhibition of myostatin in mice improves insulin sensitivity via irisin-mediated cross talk between muscle and adipose tissues
Dong, J., Dong, Y., Dong, Y., Chen, F., Mitch, W. E., & Zhang, L. (2016) · International Journal of Obesity · doi:10.1038/ijo.2015.200 · Cited by 212
Myostatin modulates adipogenesis to generate adipocytes with favorable metabolic effects
Feldman, B. J., Streeper, R. S., Farese, R. V., & Yamamoto, K. R. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0607501103 · Cited by 211
Expression and function of myostatin in obesity, diabetes, and exercise adaptation
ALLEN, D. L., HITTEL, D. S., & MCPHERRON, A. C. (2011) · Medicine & Science in Sports & Exercise · doi:10.1249/mss.0b013e3182178bb4 · Cited by 207
Adipocyte metrnl antagonizes insulin resistance through PPARγ signaling
Li, Z.-Y., Song, J., Zheng, S.-L., Fan, M.-B., Guan, Y.-F., Qu, Y., Xu, J., Wang, P., & Miao, C.-Y. (2015) · Diabetes · doi:10.2337/db15-0274 · Cited by 203
Exercise induces a marked increase in plasma follistatin: Evidence that follistatin is a contraction-induced hepatokine
Hansen, J., Brandt, C., Nielsen, A. R., Hojman, P., Whitham, M., Febbraio, M. A., Pedersen, B. K., & Plomgaard, P. (2011) · Endocrinology · doi:10.1210/en.2010-0868 · Cited by 200
Interleukin-15 stimulates adiponectin secretion by 3T3-L1 adipocytes: Evidence for a skeletal muscle-to-fat signaling pathway
QUINN, L., STRAITBODEY, L., ANDERSON, B., ARGILES, J., & HAVEL, P. (2005) · Cell Biology International · doi:10.1016/j.cellbi.2005.02.005 · Cited by 199
Exercise and BDNF reduce Aβ production by enhancing α‐secretase processing of APP
Nigam, S. M., Xu, S., Kritikou, J. S., Marosi, K., Brodin, L., & Mattson, M. P. (2017) · Journal of Neurochemistry · doi:10.1111/jnc.14034 · Cited by 193
Inhibition of myostatin protects against diet-induced obesity by enhancing fatty acid oxidation and promoting a brown adipose phenotype in mice
Zhang, C., McFarlane, C., Lokireddy, S., Masuda, S., Ge, X., Gluckman, P. D., Sharma, M., & Kambadur, R. (2012) · Diabetologia · doi:10.1007/s00125-011-2304-4 · Cited by 192
A Role for Myokines in Muscle-Bone Interactions
Hamrick, M. W. (2010) · Exercise and Sport Sciences Reviews · doi:10.1097/jes.0b013e318201f601 · Cited by 190
Transgenic expression of myostatin propeptide prevents diet-induced obesity and insulin resistance
Zhao, B., Wall, R. J., & Yang, J. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.09.044 · Cited by 186
Brain-derived neurotrophic factor improves blood glucose control and alleviates fasting hyperglycemia in C57BLKS-Lepr(db)/lepr(db) mice.
Tonra, J. R., Ono, M., Liu, X., Garcia, K., Jackson, C., Yancopoulos, G. D., Wiegand, S. J., & Wong, V. (1999) · Diabetes · doi:10.2337/diabetes.48.3.588 · Cited by 186
Anti-myostatin antibody increases muscle mass and strength and improves insulin sensitivity in old mice
Camporez, J.-P. G., Petersen, M. C., Abudukadier, A., Moreira, G. V., Jurczak, M. J., Friedman, G., Haqq, C. M., Petersen, K. F., & Shulman, G. I. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1525795113 · Cited by 184
Identification of human exercise-induced myokines using secretome analysis
Catoire, M., Mensink, M., Kalkhoven, E., Schrauwen, P., & Kersten, S. (2014) · Physiological Genomics · doi:10.1152/physiolgenomics.00174.2013 · Cited by 179
Interleukin-15 mediates reciprocal regulation of adipose and muscle mass: A potential role in body weight control
Carbó, N., López-Soriano, J., Costelli, P., Alvarez, B., Busquets, S., Baccino, F. M., Quinn, L. S., López-Soriano, F. J., & Argilés, J. M. (2001) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/s0304-4165(00)00188-4 · Cited by 174 · cited 2×
“In addition to its effects on muscle, IL-15 downregulates the accumulation of lipids in preadipocytes and reduces the WAT mass, partly through stimulation of adiponectin secretion (Carbo et al. 2001; Quinn et al. 2005), which suggests that IL-15 mediates the exerciseinduced muscle-fat crosstalk.”
Background
Exercise training increases sarcolemmal and mitochondrial fatty acid transport proteins in human skeletal muscle
Talanian, J. L., Holloway, G. P., Snook, L. A., Heigenhauser, G. J. F., Bonen, A., & Spriet, L. L. (2010) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00073.2010 · Cited by 167
Protein and exercise in the prevention of sarcopenia and aging
Naseeb, M. A., & Volpe, S. L. (2017) · Nutrition Research · doi:10.1016/j.nutres.2017.01.001 · Cited by 160
BDNF AND NGF TREATMENT IN LESIONED RATS
Lapchak, P. A., & Hefti, F. F. (1992) · Neuroreport · doi:10.1097/00001756-199205000-00007 · Cited by 156
LIF is a contraction-induced myokine stimulating human myocyte proliferation
Broholm, C., Laye, M. J., Brandt, C., Vadalasetty, R., Pilegaard, H., Pedersen, B. K., & Scheele, C. C. (2011) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01399.2010 · Cited by 155
Irisin Lowers Blood Pressure by Improvement of Endothelial Dysfunction via AMPK‐Akt‐eNOS‐NO Pathway in the Spontaneously Hypertensive Rat
Fu, J., Han, Y., Wang, J., Liu, Y., Zheng, S., Zhou, L., José, P. A., & Zeng, C. (2016) · Journal of the American Heart Association · doi:10.1161/jaha.116.003433 · Cited by 153
Irisin Inhibits Hepatic Cholesterol Synthesis via AMPK-SREBP2 Signaling
Tang, H. W., Yu, R., Liu, S., Huwatibieke, B., Li, Z., & Zhang, W. (2016) · EBioMedicine · doi:10.1016/j.ebiom.2016.02.041 · Cited by 152
Activation of AMP-Activated Protein Kinase by Interleukin-6 in Rat Skeletal Muscle
Kelly, M., Gauthier, M., Saha, A. K., & Ruderman, N. B. (2009) · Diabetes · doi:10.2337/db08-1293 · Cited by 151
BAIBA attenuates insulin resistance and inflammation induced by palmitate or a high fat diet via an AMPK–PPARδ-dependent pathway in mice
Jung, T. W., Hwang, H.-J., Hong, H. C., Yoo, H. J., Baik, S. H., & Choi, K. M. (2015) · Diabetologia · doi:10.1007/s00125-015-3663-z · Cited by 145
Upregulation of circulating IL-15 by treadmill running in healthy individuals: Is IL-15 an endocrine mediator of the beneficial effects of endurance exercise?
Tamura, Y., Watanabe, K., Kantani, T., Hayashi, J., Ishida, N., & Kaneki, M. (2011) · Endocrine Journal · doi:10.1507/endocrj.k10e-400 · Cited by 137 · cited 2×
“Although numerous studies have demonstrated that exercise alters the IL-15 concen- tration in serum (Riechman et al. 2004; Tamura et al. 2011), there are somewhat conflicting data on the effect of exercise on IL-15 protein expression and secretion from skeletal muscle, which needs to be further…”
Background
Computational reconstruction of the human skeletal muscle secretome
Bortoluzzi, S., Scannapieco, P., Cestaro, A., Danieli, G. A., & Schiaffino, S. (2005) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.20803 · Cited by 136
Protectin DX alleviates insulin resistance by activating a myokine-liver glucoregulatory axis
White, P. J., St‐Pierre, P., Charbonneau, A., Mitchell, P. L., St-Amand, E., Marcotte, B., & Marette, A. (2014) · Nature Medicine · doi:10.1038/nm.3549 · Cited by 136
SPARC Inhibits Adipogenesis by Its Enhancement of β-Catenin Signaling
Nie, J., & Sage, E. H. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m808285200 · Cited by 136
Exercise induces expression of leukaemia inhibitory factor in human skeletal muscle
Broholm, C., Mortensen, O. H., Nielsen, S., Akerstrom, T., Zankari, A., Dahl, B., & Pedersen, B. K. (2008) · The Journal of Physiology · doi:10.1113/jphysiol.2007.149781 · Cited by 132
Leptin administration activates irisin-induced myogenesis via nitric oxide-dependent mechanisms, but reduces its effect on subcutaneous fat browning in mice
Rodrı́guez, A., Becerril, S., Méndez-Giménez, L., Ramírez, B., Sáinź, N., Catalán, V., Gómez‐Ambrosi, J., & Frühbeck, G. (2014) · International Journal of Obesity · doi:10.1038/ijo.2014.166 · Cited by 130
Regulation of the Fibrosis and Angiogenesis Promoter SPARC/Osteonectin in Human Adipose Tissue by Weight Change, Leptin, Insulin, and Glucose
Kos, K., Wong, S., Tan, B. K., Gummesson, A., Jernås, M., Franck, N., Kerrigan, D. D., Nyström, F. H., Carlsson, L. M. S., Randeva, H. S., et al. (2009) · Diabetes · doi:10.2337/db09-0211 · Cited by 126
Leukemia Inhibitory Factor and Its Receptor Promote Adipocyte Differentiation via the Mitogen-activated Protein Kinase Cascade
Aubert, J., Dessolin, S., Belmonte, N., Li, M., McKenzie, F. R., Staccini-Lavenant, L., Villageois, P., Barhanin, B., Vernallis, A. B., Smith, A. G., et al. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.35.24965 · Cited by 119
Effects of (−)-epicatechin on molecular modulators of skeletal muscle growth and differentiation
Gutiérrez-Salmeán, G., Ciaraldi, T. P., Nogueira, L., Barboza, J., Taub, P. R., Hogan, M. C., Henry, R. R., Meaney, E., Villarreal, F. J., Ceballos, G. M., et al. (2013) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2013.09.007 · Cited by 113
β-aminoisobutyric acid attenuates hepatic endoplasmic reticulum stress and glucose/lipid metabolic disturbance in mice with type 2 diabetes
Shi, C.-X., Zhao, M.-X., Shu, X.-D., Xiong, X.-Q., Wang, J.-J., Gao, X.-Y., Chen, Q., Li, Y.-H., Kang, Y.-M., & Zhu, G.-Q. (2016) · Scientific Reports · doi:10.1038/srep21924 · Cited by 108
Interleukin-6 induces impairment in human subcutaneous adipogenesis in obesity-associated insulin resistance
Almuraikhy, S., Kafienah, W., Bashah, M., Diboun, I., Jaganjac, M., Al‐Khelaifi, F., Abdesselem, H., Mazloum, N. A., Alsayrafi, M., Mohamed‐Ali, V., et al. (2016) · Diabetologia · doi:10.1007/s00125-016-4031-3 · Cited by 107
Humoral Nature of the Hypoglycemic Factor of Muscular Work
Goldstein, M. S. (1961) · Diabetes · doi:10.2337/diab.10.3.232 · Cited by 105
IL-15 activates the Jak3/STAT3 signaling pathway to mediate glucose uptake in skeletal muscle cells
Krolopp, J. E., Thornton, S. M., & Abbott, M. J. (2016) · Frontiers in Physiology · doi:10.3389/fphys.2016.00626 · Cited by 104 · cited 2×
“IL-15 also modulates glucose uptake in cultured myocytes in vitro and in isolated skeletal muscle ex vivo through activation of the JAK3/ STAT3 signaling pathway (Busquets et al. 2005; Krolopp et al. 2016).”
Background
Exercise-induced increase in IL-6 level enhances GLUT4 expression and insulin sensitivity in mouse skeletal muscle
Ikeda, S., Tamura, Y., Kakehi, S., Sanada, H., Kawamori, R., & Watada, H. (2016) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.03.159 · Cited by 100
β‐Aminoisobutyric Acid Prevents Diet‐induced Obesity in Mice With Partial Leptin Deficiency
Begriche, K., Massart, J., Abbey‐Toby, A., Igoudjil, A., Lettéron, P., & Fromenty, B. (2008) · Obesity · doi:10.1038/oby.2008.337 · Cited by 99
The Matricellular Protein SPARC/Osteonectin as a Newly Identified Factor Up-regulated in Obesity
Tartare‐Deckert, S., Chavey, C., Monthouel, M.-N., Gautier, N., & OBBERGHEN, E. V. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m010634200 · Cited by 98
Irisin Controls Growth, Intracellular Ca2+ Signals, and Mitochondrial Thermogenesis in Cardiomyoblasts
Xie, C., Zhang, Y., Tran, T. D. N., Wang, H., Li, S., George, E. V., Zhuang, H., Zhang, P., Kandel, A., Lai, Y., et al. (2015) · PLoS ONE · doi:10.1371/journal.pone.0136816 · Cited by 96
The effects of brain-derived neurotrophic factor on insulin signal transduction in the liver of diabetic mice
Tsuchida, A., Nakagawa, T., Itakura, Y., Ichihara, J., Ogawa, W., Kasuga, M., Taiji, M., & Noguchi, H. (2001) · Diabetologia · doi:10.1007/s001250051661 · Cited by 91
Irisin and FNDC5: effects of 12-week strength training, and relations to muscle phenotype and body mass composition in untrained women
Ellefsen, S., Vikmoen, O., Slettaløkken, G., Whist, J. E., Nygaard, H., Hollan, I., Rauk, I., Vegge, G., Strand, T. A., Raastad, T., et al. (2014) · European Journal of Applied Physiology · doi:10.1007/s00421-014-2922-x · Cited by 91
Comparative proteomic analysis of the insulin‐induced L6 myotube secretome
Yoon, J. H., Yea, K., Kim, J., Choi, Y. S., Park, S., Lee, H., Lee, C. S., Suh, P., & Ryu, S. H. (2008) · PROTEOMICS · doi:10.1002/pmic.200800187 · Cited by 89
Interleukin-6 mediates exercise preconditioning against myocardial ischemia reperfusion injury
McGinnis, G. R., Ballmann, C. G., Peters, B. A., Nanayakkara, G., Roberts, M. D., Amin, R., & Quindry, J. C. (2015) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00850.2014 · Cited by 87
Inhibition of adipose tissue lipolysis increases intramuscular lipid and glycogen use in vivo in humans
van Loon, L. J. C., Thomason-Hughes, M., Constantin‐Teodosiu, D., Koopman, R., Greenhaff, P. L., Hardie, D. G., KEIZER, H. A., Saris, W. H. M., & Wagenmakers, A. J. M. (2005) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00092.2005 · Cited by 86
Interleukin-15 decreases proteolysis in skeletal muscle: A direct effect
Busquets, S., Figueras, M., Meijsing, S. H., Carbó, N., Quinn, L. S., Almendro, V., Argilés, J. M. A., & López-Soriano, F. J. (2005) · International Journal of Molecular Medicine · doi:10.3892/ijmm.16.3.471 · Cited by 85
A PHASE 2 RANDOMIZED STUDY INVESTIGATING THE EFFICACY AND SAFETY OF MYOSTATIN ANTIBODY LY2495655 VERSUS PLACEBO IN PATIENTS UNDERGOING ELECTIVE TOTAL HIP ARTHROPLASTY
Woodhouse, L. J., Gandhi, R., Warden, S. J., Poiraudeau, S., Myers, S. L., Benson, C., Hu, L., Ahmad, Q., Linnemeier, P., Gomez, E. V., et al. (2016) · The Journal of Frailty & Aging · doi:10.14283/jfa.2016.81 · Cited by 81
Protective effect of brain-derived neurotrophic factor on pancreatic islets in obese diabetic mice
Yamanaka, M., Itakura, Y., Inoue, T., Tsuchida, A., Nakagawa, T., Noguchi, H., & Taiji, M. (2006) · Metabolism · doi:10.1016/j.metabol.2006.04.017 · Cited by 79
Blockade of ActRIIB Signaling Triggers Muscle Fatigability and Metabolic Myopathy
Relizani, K., Mouisel, É., Giannesini, B., Hourdé, C., Patel, K., Morales-Gonzalez, S., Jülich, K., Vignaud, A., Piétri‐Rouxel, F., Fortin, D., et al. (2014) · Molecular Therapy · doi:10.1038/mt.2014.90 · Cited by 79
Inhibition of Myoblast Differentiation by Tumor Necrosis Factor α Is Mediated by c-Jun N-terminal Kinase 1 and Leukemia Inhibitory Factor
Alter, J., Rozentzweig, D., & Bengal, E. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m801379200 · Cited by 77
SOCS1, SOCS3, and PIAS1 Promote Myogenic Differentiation by Inhibiting the Leukemia Inhibitory Factor-Induced JAK1/STAT1/STAT3 Pathway
Diao, Y., Wang, X., & Wu, Z. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.00267-09 · Cited by 76
Suppression of muscle wasting by the plant‐derived compound ursolic acid in a model of chronic kidney disease
Yu, R., Chen, J., Xu, J., Cao, J., Wang, Y., Thomas, S. S., & Hu, Z. (2016) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.12162 · Cited by 73
Contraction and AICAR Stimulate IL-6 Vesicle Depletion From Skeletal Muscle Fibers In Vivo
Lauritzen, H. P. M. M., Brandauer, J., Schjerling, P., Koh, H., Treebak, J. T., Hirshman, M. F., Galbo, H., & Goodyear, L. J. (2013) · Diabetes · doi:10.2337/db12-1261 · Cited by 71
Small Molecules Dorsomorphin and LDN-193189 Inhibit Myostatin/GDF8 Signaling and Promote Functional Myoblast Differentiation
Horbelt, D., Boergermann, J. H., Chaikuad, A., Alfano, I., Williams, E., Lukonin, I., Timmel, T., Bullock, A. N., & Knaus, P. I. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.604397 · Cited by 70
Ursolic acid-induced elevation of serum irisin augments muscle strength during resistance training in men
Bang, H. S., Seo, D. Y., Chung, Y. M., Oh, K.-M., Park, J. J., Arturo, F., Jeong, S.-H., Kim, N., & Han, J. (2014) · The Korean Journal of Physiology & Pharmacology · doi:10.4196/kjpp.2014.18.5.441 · Cited by 69 · cited 1×
“In addition, natural product dihydromyricetin and ursolic acid stimulate irisin secretion (Bang et al. 2014; Zhou et al. 2015).”
Background
Leukemia inhibitory factor: A paracrine mediator of bone metabolism
Sims, N. A., & Johnson, R. W. (2012) · Growth Factors · doi:10.3109/08977194.2012.656760 · Cited by 66
Loganin possesses neuroprotective properties, restores SMN protein and activates protein synthesis positive regulator Akt/mTOR in experimental models of spinal muscular atrophy
Tseng, Y., Chen, C., Jong, Y., Chang, F., & Lo, Y. (2016) · Pharmacological Research · doi:10.1016/j.phrs.2016.05.023 · Cited by 64
Chitinase-3-like protein 1 protects skeletal muscle from TNFα-induced inflammation and insulin resistance
Görgens, S. W., Eckardt, K., Elsen, M., Tennagels, N., & Eckel, J. (2014) · Biochemical Journal · doi:10.1042/bj20131151 · Cited by 62
SPARC interacts with AMPK and regulates GLUT4 expression
Song, H., Guan, Y., Zhang, L., Li, K., & Dong, C. (2010) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2010.05.033 · Cited by 62
METRNL decreases during adipogenesis and inhibits adipocyte differentiation leading to adipocyte hypertrophy in humans
Löffler, D., Landgraf, K., Rockstroh, D., Schwartze, J. T., Dunzendorfer, H., Kiess, W., & Körner, A. (2016) · International Journal of Obesity · doi:10.1038/ijo.2016.180 · Cited by 61
Glucoregulation During Exercise: The Role of the Neuroendocrine System
Coker, R. H., & Kjaer, M. (2005) · Sports Medicine · doi:10.2165/00007256-200535070-00003 · Cited by 60
Clearance and fate of leukemia‐inhibitory factor (LIF) after injection into mice
Hilton, D. J., Nicola, N. A., Waring, P. M., & Metcalf, D. (1991) · Journal of Cellular Physiology · doi:10.1002/jcp.1041480315 · Cited by 60
Fenofibrate, a PPARα agonist, decreases atrogenes and myostatin expression and improves arthritis-induced skeletal muscle atrophy
Castillero, E., Nieto‐Bona, M. P., Fernández‐Galaz, C., Martı́n, A. I., López-Menduiña, M., Granado, M., Villanúa, M. Á., & López‐Calderón, A. (2011) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00590.2010 · Cited by 59
Exercise-mimetic AICAR transiently benefits brain function
Guerrieri, D., & van Praag, H. (2015) · Oncotarget · doi:10.18632/oncotarget.4715 · Cited by 58
Inorganic Nitrate Mimics Exercise-Stimulated Muscular Fiber-Type Switching and Myokine and γ-Aminobutyric Acid Release
Roberts, L. D., Ashmore, T., McNally, B. D., Murfitt, S. A., Fernandez, B. O., Feelisch, M., Lindsay, R., Siervo, M., Williams, E. A., Murray, A. J., et al. (2017) · Diabetes · doi:10.2337/db16-0843 · Cited by 57
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 52
Safety, Tolerability, Pharmacokinetics, and Pharmacodynamics of Domagrozumab (PF‐06252616), an Antimyostatin Monoclonal Antibody, in Healthy Subjects
Bhattacharya, I., Pawlak, S., Marraffino, S., Christensen, J., Sherlock, S. P., Alvey, C. W., Morris, C. A., Arkin, S., & Binks, M. H. (2017) · Clinical Pharmacology in Drug Development · doi:10.1002/cpdd.386 · Cited by 50
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 50
Effect of ghrelin and its analogues, BIM‐28131 and BIM‐28125, on the expression of myostatin in a rat heart failure model
Lenk, K., Palus, S., Schur, R., Datta, R., Dong, J. Z., Culler, M. D., Anker, S. D., Springer, J., Schuler, G. C., & Adams, V. (2012) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1007/s13539-012-0085-3 · Cited by 49
Protective effect of myokine IL-15 against H2O2-mediated oxidative stress in skeletal muscle cells
Li, F., Li, Y., Tang, Y., Lin, B., Kong, X., Oladele, O. A., & Yin, Y. (2014) · Molecular Biology Reports · doi:10.1007/s11033-014-3665-9 · Cited by 48
Atomoxetine Prevents Dexamethasone-Induced Skeletal Muscle Atrophy in Mice
Jesinkey, S. R., Korrapati, M. C., Rasbach, K. A., Beeson, C., & Schnellmann, R. G. (2014) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.114.217380 · Cited by 48
Building muscle, browning fat and preventing obesity by inhibiting myostatin
LeBrasseur, N. K. (2012) · Diabetologia · doi:10.1007/s00125-011-2361-8 · Cited by 46
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 45
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
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Background

See all 242

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 › Physiology (medical) › Exercise and Physiological Responses
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › 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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