Role of Myokines in Regulating Skeletal Muscle Mass and Function
Open accessAbstract
Loss of skeletal muscle mass and strength has recently become a hot research topic with the extension of life span and an increasingly sedentary lifestyle in modern society. Maintenance of skeletal muscle mass is considered an essential determinant of muscle strength and function. Myokines are cytokines synthesized and released by myocytes during muscular contractions. They are implicated in autocrine regulation of metabolism in the muscle as well as in the paracrine/endocrine regulation of other tissues and organs including adipose tissue, the liver, and the brain through their receptors. Till date, secretome analysis of human myocyte culture medium has revealed over 600 myokines. In this review article, we summarize our current knowledge of major identified and characterized myokines focusing on their biological activity and function, particularly in muscle mass and function.
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Irisin released from muscle promotes browning of WAT, increasing non-shivering thermogenesis and energy availability during exercise.
“Irisin released from muscle promotes the browning of WAT, thereby increasing non-shivering thermogenesis and energy availability during exercise”
From Exercise-Induced Muscle–Fat Crosstalk: Molecular Mediators and Their Pharmacological Modulation for the Maintenance of Metabolic Flexibility in Aging (2025) · cites this paper as [88]
The Irisin section (page unavailable) describes muscle FNDC5 driving brown fat-like development of white fat cells and increasing thermogenesis. It does not say that this increases energy availability during exercise, and it notes that an exercise-induced rise in circulating irisin is debated. (LLM, conf=0.88)
Experimental — accuracy not yet measuredAdiponectin secreted by adipose tissue enhances insulin sensitivity by activating AMPK signaling in skeletal muscle, promoting glucose uptake and increasing FA oxidation.
“In parallel, adiponectin secreted by adipose tissue enhances insulin sensitivity by activating AMPK signaling in skeletal muscle, thereby promoting glucose uptake and increasing FA oxidation”
From Exercise-Induced Muscle–Fat Crosstalk: Molecular Mediators and Their Pharmacological Modulation for the Maintenance of Metabolic Flexibility in Aging (2025) · cites this paper as [88]
The Myonectin (CTRP15) section describes AMPK-mediated glucose uptake and fatty-acid oxidation in rat skeletal myocytes, but attributes those effects to myonectin, not adiponectin. Searches for adiponectin and the claimed adipose-tissue mechanism found no passage in our copy that addresses the claim. (LLM, conf=0.75)
Experimental — accuracy not yet measuredSome myokines exert their effect within skeletal muscle itself and are involved in the regulation of muscle mass.
“Some myokines exert their effect within skeletal muscle itself and are involved in the regulation of muscle mass (14) (Fig. 1).”
From Muscle–Organ Crosstalk: The Emerging Roles of Myokines (2020) · cites this paper as [14]
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A PGC1-α-dependent myokine that drives brown-fat-like development of white fat and thermogenesis
Boström, P., Wu, J., Jedrychowski, M. P., Korde, A., Ye, L., Lo, J. C., Rasbach, K. A., Boström, E. A., Choi, J. H., Long, J. Z., et al. (2012) · Nature · doi:10.1038/nature10777 · Cited by 4,810 · see citing works
Regulation of skeletal muscle mass in mice by a new TGF-p superfamily member
McPherron, A. C., Lawler, A. M., & Lee, S.-J. (1997) · Nature · doi:10.1038/387083a0 · Cited by 4,013 · see citing works
da Luz, A. C. D. D. S., Dias, G. P., Bevilaqua, M. C. D. N., Cocks, G. D., Gardino, P. F., Thuret, S., & Nardi, A. E. (2013) · Neuropsychobiology · doi:10.1159/000353269 · Cited by 4,012 · see citing works
Muscle as an Endocrine Organ: Focus on Muscle-Derived Interleukin-6
Pedersen, B. K., & Febbraio, M. A. (2008) · Physiological Reviews · doi:10.1152/physrev.90100.2007 · Cited by 2,388 · see citing works
Purification of a new neurotrophic factor from mammalian brain.
Barde, Y. A., Edgar, D., & Thoenen, H. (1982) · The EMBO Journal · doi:10.1002/j.1460-2075.1982.tb01207.x · Cited by 1,822 · see citing works
Skeletal muscle: A brief review of structure and function
Frontera, W. R., & Ochala, J. (2015) · Calcified Tissue International · doi:10.1007/s00223-014-9915-y · Cited by 1,758 · see citing works
Binder (2004) · doi:10.1080/08977190410001723308 · Cited by 1,481 · see citing works
Myostatin Mutation Associated with Gross Muscle Hypertrophy in a Child
Schuelke, M., Wagner, K. R., Stolz, L. E., Hübner, C., Riebel, T., Kömen, W., Braun, T., Tobin, J. F., & Lee, S.-J. (2004) · New England Journal of Medicine · doi:10.1056/nejmoa040933 · Cited by 1,399 · see citing works
Cellular and molecular mechanisms of muscle atrophy
Bonaldo, P., & Sandri, M. (2013) · Disease Models & Mechanisms · doi:10.1242/dmm.010389 · Cited by 1,284 · see citing works
Steensberg, A., van Hall, G., Osada, T., Sacchetti, M., Saltin, B., & Pedersen, B. K. (2000) · The Journal of Physiology · doi:10.1111/j.1469-7793.2000.00237.x · Cited by 1,095 · see citing works
Muscle wasting in disease: molecular mechanisms and promising therapies
Cohen, S., Nathan, J. A., & Goldberg, A. L. (2015) · Nature Reviews Drug Discovery · doi:10.1038/nrd4467 · Cited by 1,089 · see citing works
Huh, J. Y., Panagiotou, G., Mougios, V., Brinkoetter, M., Vamvini, M. T., Schneider, B. E., & Mantzoros, C. S. (2012) · Metabolism · doi:10.1016/j.metabol.2012.09.002 · Cited by 1,040 · see citing works
Carey, A. L., Steinberg, G. R., Macaulay, S. L., Thomas, W. G., Holmes, A. G., Ramm, G., Prelovsek, O., Hohnen-Behrens, C., Watt, M. J., James, D. E., et al. (2006) · Diabetes · doi:10.2337/db05-1404 · Cited by 898 · see citing works
FERRIS, L. T., WILLIAMS, J. S., & SHEN, C.-L. (2007) · Medicine & Science in Sports & Exercise · doi:10.1249/mss.0b013e31802f04c7 · Cited by 849 · see citing works
Role of Myokines in Exercise and Metabolism
Pedersen, B. K., Åkerström, T. C. A., Nielsen, A. R., & Fischer, C. P. (2007) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00080.2007 · Cited by 841 · see citing works
Kim, K. H., Jeong, Y. T., Oh, H., Kim, S. H., Cho, J. M., Kim, Y.-N., Kim, S. S., Kim, D. H., Hur, K. Y., Kim, H. K., et al. (2013) · Nature Medicine · doi:10.1038/nm.3014 · Cited by 774 · see citing works
Matthews, V. B., Åström, M.-B., Chan, M. H. S., Bruce, C. R., Krabbe, K. S., Prelovsek, O., Åkerström, T., Yfanti, C., Broholm, C., Mortensen, O. H., et al. (2009) · Diabetologia · doi:10.1007/s00125-009-1364-1 · Cited by 722 · cited 1× · see citing works
“In skeletal muscle cells, BDNF mRNA expression is increased by contraction and increased fat oxidation through activation of AMP-activated protein kinase (Matthews et al., 2009).”
BackgroundFibroblast growth factors: from molecular evolution to roles in development, metabolism and disease
Itoh, N., & Ornitz, D. M. (2010) · The Journal of Biochemistry · doi:10.1093/jb/mvq121 · Cited by 708 · see citing works
Pedersen, B. K. (2011) · Journal of Experimental Biology · doi:10.1242/jeb.048074 · Cited by 668 · see citing works
Searching for the exercise factor: is IL-6 a candidate?
Pedersen (2003) · Journal of Muscle Research and Cell Motility · doi:10.1023/a:1026070911202 · Cited by 564 · see citing works
FGF21 is an Akt‐regulated myokine
Izumiya, Y., Bina, H. A., Ouchi, N., Akasaki, Y., Kharitonenkov, A., & Walsh, K. (2008) · FEBS Letters · doi:10.1016/j.febslet.2008.10.021 · Cited by 415 · see citing works
Myonectin (CTRP15), a novel myokine that links skeletal muscle to systemic lipid homeostasis
Seldin, M. M., Peterson, J. M., Byerly, M. S., Wei, Z., & Wong, G. W. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.336834 · Cited by 406 · see citing works
Interleukin-15 biology and its therapeutic implications in cancer
Steel, J. C., Waldmann, T. A., & Morris, J. C. (2011) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2011.09.004 · Cited by 361 · see citing works
Aoi, W., Naito, Y., Takagi, T., Tanimura, Y., Takanami, Y., Kawai, Y., Sakuma, K., Hang, L. P., Mizushima, K., Hirai, Y., et al. (2013) · Gut · doi:10.1136/gutjnl-2011-300776 · Cited by 347 · see citing works
Reza, M. M., Subramaniyam, N., Sim, C. M., Ge, X., Sathiakumar, D., McFarlane, C., Sharma, M., & Kambadur, R. (2017) · Nature Communications · doi:10.1038/s41467-017-01131-0 · Cited by 335 · see citing works
Evidence against a Beneficial Effect of Irisin in Humans
Raschke, S., Elsen, M., Gassenhuber, J., Sommerfeld, M. R., Schwahn, U., Brockmann, B., Jung, R., Wisløff, U., Tjønna, A. E., Raastad, T., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0073680 · Cited by 322 · see citing works
Myostatin/activin pathway antagonism: molecular basis and therapeutic potential
Han, H. Q., Zhou, X., Mitch, W. E., & Goldberg, A. L. (2013) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2013.05.019 · Cited by 314 · see citing works
Pekkala, S., Wiklund, P. K., Hulmi, J. J., Ahtiainen, J. P., Horttanainen, M., Pöllänen, E., Mäkelä, K. A., Kainulainen, H., Häkkinen, K., Nyman, K., et al. (2013) · The Journal of Physiology · doi:10.1113/jphysiol.2013.263707 · Cited by 292 · see citing works
Interleukin-15: a novel anabolic cytokine for skeletal muscle.
Quinn, L. S., Haugk, K. L., & Grabstein, K. H. (1995) · Endocrinology · doi:10.1210/endo.136.8.7628408 · Cited by 270 · see citing works
Signaling Specificity of Interleukin-6 Action on Glucose and Lipid Metabolism in Skeletal Muscle
Al-Khalili, L., Bouzakri, K., Glund, S., Lönnqvist, F., Koistinen, H. A., & Krook, A. (2006) · Molecular Endocrinology · doi:10.1210/me.2005-0490 · Cited by 250 · see citing works
METSIS, M. L., Timmusk, T., Arenas, E., & Persson, H. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.19.8802 · Cited by 248 · see citing works
A Phase 1/2a Follistatin Gene Therapy Trial for Becker Muscular Dystrophy
Mendell, J. R., Sahenk, Z., Malik, V., Gomez, A. M., Flanigan, K. M., Lowes, L. P., Alfano, L. N., Berry, K., Meadows, E., Lewis, S., et al. (2014) · Molecular Therapy · doi:10.1038/mt.2014.200 · Cited by 246 · see citing works
IL-6 and Serum Amyloid A Synergy Mediates Angiotensin II–Induced Muscle Wasting
Zhang, L., Du, J., Hu, Z., Han, G., Delafontaine, P., García, G., & Mitch, W. E. (2009) · Journal of the American Society of Nephrology · doi:10.1681/asn.2008060628 · Cited by 241 · see citing works
Irisin-immunoreactivity in neural and non-neural cells of the rodent
Dun, S. L., Lyu, R., Chen, Y., Chang, J. K., Luo, J. J., & Dun, N. J. (2013) · Neuroscience · doi:10.1016/j.neuroscience.2013.02.050 · Cited by 236 · see citing works
Irisin Enhances Osteoblast Differentiation In Vitro
Colaianni, G., Cuscito, C., Mongelli, T., Oranger, A., Mori, G., Brunetti, G., Colucci, S., Cinti, S., & Grano, M. (2014) · International Journal of Endocrinology · doi:10.1155/2014/902186 · Cited by 236 · see citing works
Role of TGF-β signaling in inherited and acquired myopathies
Burks, T. N., & Cohn, R. D. (2011) · Skeletal Muscle · doi:10.1186/2044-5040-1-19 · Cited by 234 · see citing works
Quinn, L. S., Anderson, B. G., Drivdahl, R. H., Alvarez, B., & Argilés, J. M. (2002) · Experimental Cell Research · doi:10.1006/excr.2002.5624 · Cited by 226 · see citing works
Keipert, S., Ost, M., Johann, K., Imber, F., Jastroch, M., van Schothorst, E. M., Keijer, J., & Klaus, S. (2014) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00330.2013 · Cited by 221 · cited 1× · see citing works
“Autophagy deficiency and subsequent mitochondrial dysfunction elevates the level of FGF21 as a myokine, thereby protecting against diet-induced obesity and insulin resistance (Kim et al., 2013; Keipert et al., 2014).”
BackgroundYarrow, J. F., White, L. J., McCoy, S. C., & Borst, S. E. (2010) · Neuroscience Letters · doi:10.1016/j.neulet.2010.05.058 · Cited by 218 · see citing works
The effect of graded exercise on IL‐6 release and glucose uptake in human skeletal muscle
Helge, J. W., Stallknecht, B., Pedersen, B. K., Galbo, H., Kiens, B., & Richter, E. A. (2003) · The Journal of Physiology · doi:10.1113/jphysiol.2002.030437 · Cited by 212 · see citing works
The myokine decorin is regulated by contraction and involved in muscle hypertrophy
Kanzleiter, T., Rath, M., Görgens, S. W., Jensen, J., Tangen, D. S., Kolnes, A. J., Kolnes, K. J., Lee, S., Eckel, J., Schürmann, A., et al. (2014) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2014.06.123 · Cited by 209 · see citing works
Raschke, S., Eckardt, K., Bjørklund Holven, K., Jensen, J., & Eckel, J. (2013) · PLoS ONE · doi:10.1371/journal.pone.0062008 · Cited by 199 · see citing works
FGF21 as a Hepatokine, Adipokine, and Myokine in Metabolism and Diseases
Itoh, N. (2014) · Frontiers in Endocrinology · doi:10.3389/fendo.2014.00107 · Cited by 198 · see citing works
Lecker, S. H., Zavin, A., Cao, P., Arena, R. A., Allsup, K., Daniels, K. M., Joseph, J., Schulze, P. C., & Forman, D. E. (2012) · Circulation Heart Failure · doi:10.1161/circheartfailure.112.969543 · Cited by 197 · see citing works
Frcp1 and Frcp2, two novel fibronectin type III repeat containing genes
Teufel, A., Malik, N., Mukhopadhyay, M., & Westphal, H. (2002) · Gene · doi:10.1016/s0378-1119(02)00828-4 · Cited by 183 · see citing works
Interleukin-15 antagonizes muscle protein waste in tumour-bearing rats
Carbó, N., López‐Soriano, J., Costelli, P., Busquets, S., Alvarez, B., Baccino, F. M., Quinn, L. S., López-Soriano, F. J., & Argilés, J. M. A. (2000) · British Journal of Cancer · doi:10.1054/bjoc.2000.1299 · Cited by 181 · see citing works
Clow, C., & Jasmin, B. J. (2010) · Molecular Biology of the Cell · doi:10.1091/mbc.e10-02-0154 · Cited by 175 · see citing works
Secretome profiling of primary human skeletal muscle cells
Hartwig, S., Raschke, S., Knebel, B., Scheler, M., Irmler, M., Paßlack, W., Müller, S., Hanisch, F., Franz, T., Li, X., et al. (2013) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2013.08.004 · Cited by 168 · see citing works
Exercise and regulation of adipokine and myokine production
(2015) · Progress in Molecular Biology and Translational Science · doi:10.1016/bs.pmbts.2015.07.002 · Cited by 168 · see citing works
Block of conduction in mammalian myelinated nerve fibres by low temperatures.
Paintal, A. S. (1965) · The Journal of Physiology · doi:10.1113/jphysiol.1965.sp007686 · Cited by 162 · see citing works
Morvan, F., Rondeau, J.-M., Zou, C., Minetti, G., Scheufler, C., Scharenberg, M., Jacobi, C., Brebbia, P., Ritter, V., Toussaint, G., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1707925114 · Cited by 142 · see citing works
Busquets, S., Toledo, M., Orpí, M., Massa, D., Porta, M. M., Capdevila, E., Padilla, N., Frailis, V., López-Soriano, F. J., Han, H. Q., et al. (2011) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1007/s13539-011-0049-z · Cited by 141 · see citing works
Tamura, Y., Watanabe, K., Kantani, T., Hayashi, J., Ishida, N., & Kaneki, M. (2011) · Endocrine Journal · doi:10.1507/endocrj.k10e-400 · Cited by 137 · see citing works
Bergen, H. R., Farr, J. N., Vanderboom, P. M., Atkinson, E. J., White, T. A., Singh, R. J., Khosla, S., & LeBrasseur, N. K. (2015) · Skeletal Muscle · doi:10.1186/s13395-015-0047-5 · Cited by 137 · see citing works
Mariot, V., Joubert, R., Hourdé, C., Féasson, L., Hanna, M. G., Francesco Muntoni, A., Maisonobe, T., Servais, L., Bogni, C., Panse, R. L., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-01486-4 · Cited by 136 · see citing works
Chalkiadaki, A., Igarashi, M., Nasamu, A. S., Knezevic, J., & Guarente, L. (2014) · PLoS Genetics · doi:10.1371/journal.pgen.1004490 · Cited by 126 · see citing works
Seldin, M. M., Lei, X., Tan, S. Y., Stanson, K. P., Wei, Z., & Wong, G. W. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.500736 · Cited by 120 · see citing works
Omura, T., Sano, M., Omura, K., Hasegawa, T., Doi, M., Sawada, T., & Nagano, A. (2005) · Journal of the Peripheral Nervous System · doi:10.1111/j.1085-9489.2005.10307.x · Cited by 119 · see citing works
Pistilli, E. E., Bogdanovich, S., Goncalves, M. D., Ahima, R. S., Lachey, J. L., Seehra, J. S., & Khurana, T. S. (2011) · American Journal Of Pathology · doi:10.1016/j.ajpath.2010.11.071 · Cited by 112 · see citing works
Park, H., Kim, H. C., Zhang, D., Yeom, H., & Lim, S.-K. (2018) · Endocrine · doi:10.1007/s12020-018-1814-y · Cited by 112 · see citing works
Follistatin Gene Therapy for Sporadic Inclusion Body Myositis Improves Functional Outcomes
Mendell, J. R., Sahenk, Z., Al-Zaidy, S. A., Rodino‐Klapac, L. R., Lowes, L. P., Alfano, L. N., Berry, K., Miller, N. F., YALVAÇ, M. E., Dvorchik, I., et al. (2017) · Molecular Therapy · doi:10.1016/j.ymthe.2017.02.015 · Cited by 111 · see citing works
Park, S., Choi, J. H., Ryu, H. S., Pak, Y. K., Park, K. S., Lee, H. K., & Lee, W. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.005611 · Cited by 105 · see citing works
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 · see citing works
Quinn, L. S., Anderson, B. G., Conner, J. D., & Wolden-Hanson, T. (2013) · Endocrinology · doi:10.1210/en.2012-1773 · Cited by 102 · see citing works
Biomarkers of cancer cachexia.
Loumaye, A., & Thissen, J. (2017) · Clinical Biochemistry · doi:10.1016/j.clinbiochem.2017.07.011 · Cited by 102 · see citing works
Combined Training Reduces Subclinical Inflammation in Obese Middle-Age Men
Brunelli, D. T., Chacon‐Mikahil, M. P. T., Gáspari, A. F., Lopes, W. A., Bonganha, V., Bonfante, I. L. P., Bellotto, M. L., Libardi, C. A., & Cavaglieri, C. R. (2015) · Medicine & Science in Sports & Exercise · doi:10.1249/mss.0000000000000658 · Cited by 90 · see citing works
Whole‐body magnetic resonance imaging evaluation of facioscapulohumeral muscular dystrophy
Leung, D. G., Carrino, J. A., Wagner, K. R., & Jacobs, M. A. (2015) · Muscle & Nerve · doi:10.1002/mus.24569 · Cited by 89 · see citing works
Mighty is a novel promyogenic factor in skeletal myogenesis
Marshall, A. D., Salerno, M. S., Thomas, M., Davies, T. J., Berry, C., Dyer, K. A., Bracegirdle, J., Watson, T. J., Dziadek, M. A., Kambadur, R., et al. (2008) · Experimental Cell Research · doi:10.1016/j.yexcr.2008.01.004 · Cited by 86 · see citing works
Carson, B. P. (2017) · Frontiers in Endocrinology · doi:10.3389/fendo.2017.00097 · Cited by 83 · see citing works
The role of neurotrophins in muscle under physiological and pathological conditions
Chevrel, G., Hohlfeld, R., & Sendtner, M. (2005) · Muscle & Nerve · doi:10.1002/mus.20444 · Cited by 82 · see citing works
Functional and Morphological Improvement of Dystrophic Muscle by Interleukin 6 Receptor Blockade
Pelosi, L., Berardinelli, M. G., Pasquale, L. D., Nicoletti, C., D’Amico, A., Carvello, F., Moneta, G. M., Catizone, A., Bertini, E., Benedetti, F. D., et al. (2015) · EBioMedicine · doi:10.1016/j.ebiom.2015.02.014 · Cited by 81 · see citing works
Secreted Protein Acidic and Rich in Cysteine (SPARC) in Human Skeletal Muscle
Jørgensen, L. H., Petersson, S. J., Sellathurai, J., Andersen, D. C., Thayssen, S., Sant, D. J., Jensen, C. H., & Schrøder, H. D. (2008) · Journal of Histochemistry & Cytochemistry · doi:10.1369/jhc.2008.951954 · Cited by 80 · see citing works
Irisin, a unique non-inflammatory myokine in stimulating skeletal muscle metabolism
Vaughan, R. A., Gannon, N. P., Mermier, C. M., & Conn, C. A. (2015) · Journal of Physiology and Biochemistry · doi:10.1007/s13105-015-0433-9 · Cited by 77 · see citing works
Wada, E., Tanihata, J., Iwamura, A., Takeda, S., Hayashi, Y. K., & Matsuda, R. (2017) · Skeletal Muscle · doi:10.1186/s13395-017-0140-z · Cited by 75 · see citing works
Elevated skeletal muscle irisin precursor FNDC5 mRNA in obese OLETF rats
Roberts, M. D., Bayless, D. S., Jenkins, N. T., Padilla, J., Childs, T. E., Martin, J. S., Dalbo, V. J., Booth, F. W., Rector, R. S., & Laughlin, M. H. (2013) · Metabolism · doi:10.1016/j.metabol.2013.02.002 · Cited by 73 · see citing works
Inhibition of Myostatin Signaling through Notch Activation following Acute Resistance Exercise
MacKenzie, M. G., Hamilton, D. L., Pepin, M. E., Patton, A., & Baar, K. (2013) · PLoS ONE · doi:10.1371/journal.pone.0068743 · Cited by 72 · see citing works
Regulation of tissue crosstalk by skeletal muscle-derived myonectin and other myokines
Seldin, M. M., & Wong, G. W. (2012) · Adipocyte · doi:10.4161/adip.20877 · Cited by 70 · see citing works
Ribas, F., Villarroya, J., Hondares, E., Giralt, M., & Villarroya, F. (2014) · Biochemical Journal · doi:10.1042/bj20140403 · Cited by 69 · see citing works
Amthor, H., & Hoogaars, W. M. H. (2012) · Current Gene Therapy · doi:10.2174/156652312800840577 · Cited by 66 · see citing works
Peterson, J. M., Mart, R., & Bond, C. E. (2014) · PeerJ · doi:10.7717/peerj.605 · Cited by 64 · see citing works
Harcourt, L. J., Holmes, A. G., Gregorevic, P., Schertzer, J. D., Stupka, N., Plant, D. R., & Lynch, G. S. (2005) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)62333-4 · Cited by 63 · see citing works
Reduced serum myostatin concentrations associated with genetic muscle disease progression
Burch, P. M., Pogoryelova, O., Palandra, J., Goldstein, R., Bennett, D., Fitz, L. J., Guglieri, M., Bettolo, C. M., Straub, V. W., Evangelista, T., et al. (2017) · Journal of Neurology · doi:10.1007/s00415-016-8379-6 · Cited by 63 · see citing works
Grube, L., Dellen, R., Kruse, F., Schwender, H. R., Stühler, K., & Poschmann, G. (2018) · Journal of Proteome Research · doi:10.1021/acs.jproteome.7b00684 · Cited by 63 · see citing works
BDNF rescues myosin heavy chain IIB muscle fibers after neonatal nerve injury
Mousavi, K., Parry, D. J., & Jasmin, B. J. (2004) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00583.2003 · Cited by 61 · see citing works
Wang, X., Xiao, H., Ling-lin, L., Cheng, D., Li, X.-J., & Si, L. (2016) · Experimental Cell Research · doi:10.1016/j.yexcr.2016.06.020 · Cited by 57 · see citing works
Inhibition of the myostatin/Smad signaling pathway by short decorin-derived peptides
Shafey, N. E., Guesnon, M., Simon, F., Deprez, E., Cosette, J., Stockholm, D., Scherman, D., Bigey, P., & Kichler, A. (2016) · Experimental Cell Research · doi:10.1016/j.yexcr.2016.01.019 · Cited by 54 · see citing works
Lim, S. K., Choi, S. H., Koo, B. K., Kang, S. M., Yoon, J. W., Jang, H. C., Choi, S. M., Lee, M. G., Lee, W., Shin, H., et al. (2011) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2011-1743 · Cited by 52 · see citing works
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Al-Zaidy, S. A., Sahenk, Z., Rodino‐Klapac, L. R., Kaspar, B. K., & Mendell, J. R. (2015) · Journal of Neuromuscular Diseases · doi:10.3233/jnd-150083 · Cited by 49 · see citing works
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Anaya-Segura, M., García-Martínez, F. A., Montes‐Almanza, L., Gómez‐Díaz, B., Ávila, G., Álvarez-Maya, I., Coral‐Vázquez, R. M., Mondragón‐Terán, P., Escobar‐Cedillo, R. E., García-Calderón, N., et al. (2015) · Molecules · doi:10.3390/molecules200611154 · Cited by 42 · see citing works
Pistilli, E. E., & Alway, S. E. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.05.188 · Cited by 42 · see citing works
SPARC is up-regulated during skeletal muscle regeneration and inhibits myoblast differentiation.
Petersson, S. J., Jørgensen, L. H., Andersen, D. C., Nørgaard, R. C., Jensen, C. H., & Schrøder, H. D. (2013) · PubMed · doi:10.14670/hh-28.1451 · Cited by 40 · see citing works
Kouda, K., Furusawa, K., Sugiyama, H., Sumiya, T., Ito, T., Tajima, F., & Shimizu, K. (2011) · European Journal of Applied Physiology · doi:10.1007/s00421-011-2004-2 · Cited by 40 · see citing works
The effect of exercise induced cytokines on insulin stimulated glucose transport in C2C12 cells
Gray, S. R., & Kamolrat, T. (2011) · Cytokine · doi:10.1016/j.cyto.2011.04.019 · Cited by 40 · see citing works
Kazemi, F. (2015) · Journal of Endocrinological Investigation · doi:10.1007/s40618-015-0373-9 · Cited by 32 · see citing works
Han, D., Hsiao, M., Wang, T., Chen, S., & Yang, W. (2016) · BMC Neurology · doi:10.1186/s12883-016-0661-9 · Cited by 24 · see citing works
Pereira, E. S., Neto, W. K., Calefi, A. S., Georgetti, M., Guerreiro, L., Zocoler, C. A. S., & Gama, E. F. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.00823 · Cited by 18 · see citing works
Wide ranges of serum myostatin concentrations in Duchenne muscular dystrophy patients
Awano, H., Takeshima, Y., Okizuka, Y., et al. (2008) · Clinica Chimica Acta · doi:10.1016/j.cca.2008.01.024 · Cited by 12 · see citing works
Allen (1999) · doi:10.1002/(sici)1097-4652(199907)180:1
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Severinsen, M. C. K., & Pedersen, B. K. (2020) · Endocrine Reviews · doi:10.1210/endrev/bnaa016 · Cited by 1,226 · see citing works
“Myogenesis Some myokines exert their effect within skeletal muscle itself and are involved in the regulation of muscle mass (14) (Fig.”
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Prado, C. M., Landi, F., Chew, S. T. H., Atherton, P. J., Molinger, J., Ruck, T., & Gonzalez, M. C. (2022) · Clinical Nutrition · doi:10.1016/j.clnu.2022.07.041 · Cited by 237 · see citing works
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Walowski, C. O., Braun, W., Maisch, M. J., Jensen, B., Peine, S., Norman, K., Müller, M. J., & Bosy-Westphal, A. (2020) · Nutrients · doi:10.3390/nu12030755 · Cited by 200 · see citing works
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Herrmann, M., Engelke, K., Ebert, R., Müller-Deubert, S., Rudert, M., Ziouti, F., Jundt, F., Felsenberg, D., & Jakob, F. (2020) · Biomolecules · doi:10.3390/biom10030432 · Cited by 197 · see citing works
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Rolland, Y., Dray, C., Vellas, B., & Barreto, P. D. S. (2023) · Metabolism · doi:10.1016/j.metabol.2023.155597 · Cited by 195 · see citing works
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Laurens, C., Bergouignan, A., & Moro, C. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.00091 · Cited by 159 · see citing works
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Rome, S., Forterre, A., Mizgier, M. L., & Bouzakri, K. (2019) · Frontiers in Physiology · doi:10.3389/fphys.2019.00929 · Cited by 139 · see citing works
AlKhairi, I., Cherian, P., Abu-Farha, M., Madhoun, A. A., Nizam, R., Melhem, M., Jamal, M., Al-Sabah, S., Ali, H., Tuomilehto, J., et al. (2019) · Cells · doi:10.3390/cells8101283 · Cited by 82 · see citing works
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Guo, A., Li, K., & Xiao, Q. (2020) · Experimental Gerontology · doi:10.1016/j.exger.2020.111022 · Cited by 83 · see citing works
Bettariga, F., Taaffe, D. R., Galvão, D. A., Lopez, P., Bishop, C., Markarian, A. M., Natalucci, V., Kim, J.-S., & Newton, R. U. (2024) · Journal of Sport and Health Science · doi:10.1016/j.jshs.2024.04.005 · Cited by 83 · see citing works
“12,13 As more than 600 myokines have been identified to date, and the role of most of them remains unknown, 6 this review will focus on exercise-induced myokines with established effects on the human body, including interleukin 15 (IL-15), secreted protein acidic and rich in cysteine (SPARC),…”
BackgroundEffect of Various Exercise Regimens on Selected Exercise-Induced Cytokines in Healthy People
Domin, R., Dadej, D., Pytka, M., Zybek-Kocik, A., Ruchała, M., & Guzik, P. (2021) · International Journal of Environmental Research and Public Health · doi:10.3390/ijerph18031261 · Cited by 79 · see citing works
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Dong, Y., Yuan, H., Ma, G., & Cao, H. (2024) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-024-05331-y · Cited by 52 · see citing works
Yadav, A., Singh, A., Phogat, J., Dahuja, A., & Dabur, R. (2021) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2020.113510 · Cited by 49 · see citing works
Tero-Vescan, A., Degens, H., Matsakas, A., Ștefănescu, R., Ősz, B. E., & Slevin, M. (2025) · Pharmaceuticals · doi:10.3390/ph18081222 · Cited by 44 · see citing works
“In parallel, adiponectin secreted by adipose tissue enhances insulin sensitivity by activating AMPK signaling in skeletal muscle, thereby promoting glucose uptake and increasing FA oxidation [88].”
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Barber, T. M., Kabisch, S., Pfeiffer, A. F. H., & Weickert, M. O. (2025) · Metabolites · doi:10.3390/metabo15020085 · Cited by 19 · see citing works
“%) within fast-twitch SM compared with wild-type littermates [55].”
- Authors
- Lee, J. H., & Jun, H.-S.
- Affiliations
- Gachon University (KR)
- Corresponding author
- Lee, Jong Han
- Jun, Hee-Sook
- Venue
- Frontiers in Physiology
- Publisher
- Frontiers Media SA
- Published
- 2019-01-30
- Volume
- 10
- Pages
- 42-42
- ISSN
- 1664-042X (ISSN-L)
- PMC
- PMC6363662
- OpenAlex
- W2908684623
- Cited by
- 432
- References
- 98
- Citations by year
- 2026: 40 · 2025: 64 · 2024: 73 · 2023: 66 · 2022: 71 · 2021: 52 · 2020: 49 · 2019: 17
- FWCI
- 4.17
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Frontiers in Physiology (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
- Funders
- National Research Foundation
- Korea Health Industry Development Institute (HI14C1135)
- National Research Foundation of Korea (H I14C1135, 2017R1D1A1B03036210)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Health Sciences › Medicine › Rehabilitation › Exercise and Physiological Responses
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Muscle metabolism and nutrition
- Keywords
- myokines, skeletal muscle mass, muscle function, muscle strength, muscle atrophy, cytokines, paracrine signaling, autocrine regulation, muscle metabolism, adipose tissue, liver, brain
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