Myokines: Metabolic regulation in obesity and type 2 diabetes
Open accessAbstract
Skeletal muscle plays a vital role in the regulation of systemic metabolism, partly through its secretion of endocrine factors which are collectively known as myokines. Altered myokine levels are associated with metabolic diseases, such as type 2 diabetes (T2D). The significance of interorgan crosstalk, particularly through myokines, has emerged as a fundamental aspect of nutrient and energy homeostasis. However, a comprehensive understanding of myokine biology in the setting of obesity and T2D remains a major challenge. In this review, we discuss the regulation and biological functions of key myokines that have been extensively studied during the past two decades, namely interleukin 6 (IL-6), irisin, myostatin (MSTN), growth differentiation factor 11 (GDF11), fibroblast growth factor 21 (FGF21), apelin, brain-derived neurotrophic factor (BDNF), meteorin-like (Metrnl), secreted protein acidic and rich in cysteine (SPARC), β-aminoisobutyric acid (BAIBA), Musclin, and Dickkopf 3 (Dkk3). Related to these, we detail the role of exercise in myokine expression and secretion together with their contributions to metabolic physiology and disease. Despite significant advancements in myokine research, many myokines remain challenging to measure accurately and investigate thoroughly. Hence, new research techniques and detection methods should be developed and rigorously tested. Therefore, developing a comprehensive perspective on myokine biology is crucial, as this will likely offer new insights into the pathophysiological mechanisms underlying obesity and T2D and may reveal novel targets for therapeutic interventions.
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Power training (PT) may amplify the myokine response, contributing to the observed reductions in body fat and improvements in body composition.
“PT, by involving intense and repeated contractions of large muscle groups, may amplify this myokine response, contributing to the observed reductions in body fat and improvements in body composition [37,38].”
From Efficacy of Power Training on Sarcopenic Obesity in Community-Dwelling Older Women: A 32-Week Randomized Clinical Trial (2025) · cites this paper as [38]
The Introduction (page unavailable) says myokines regulate adipose-tissue mass and browning, while the Conclusions say exercise affects myokine levels. The Conclusions also caution that different forms of exercise may have different effects. The paper does not establish that power training specifically amplifies the myokine response or that this response caused the cited reductions in body fat and improvements in body composition. (LLM, conf=0.85)
Experimental — accuracy not yet measuredSkeletal muscles function as an endocrine organ by releasing myokines in response to contraction, which can influence fat metabolism, reduce inflammation, and improve insulin sensitivity.
“Skeletal muscles function as an endocrine organ by releasing myokines in response to contraction, which can influence fat metabolism, reduce inflammation, and improve insulin sensitivity.”
From Efficacy of Power Training on Sarcopenic Obesity in Community-Dwelling Older Women: A 32-Week Randomized Clinical Trial (2025) · cites this paper as [38]
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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
Muscles, exercise and obesity: skeletal muscle as a secretory organ
Pedersen, B. K., & Febbraio, M. A. (2012) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2012.49 · Cited by 2,909 · see citing works
Chatterjee, S., Khunti, K., & Davies, M. J. (2017) · The Lancet · doi:10.1016/s0140-6736(17)30058-2 · Cited by 2,577 · see citing works
Transcriptional co-activator PGC-1α drives the formation of slow-twitch muscle fibres
Lin, J., Wu, H., Tarr, P. T., Zhang, C.-Y., Wu, Z., Boss, O., Michael, L. F., Puigserver, P., Isotani, E., Olson, E. N., et al. (2002) · Nature · doi:10.1038/nature00904 · Cited by 2,546 · see citing works
Self-citationAMP-activated protein kinase (AMPK) action in skeletal muscle via direct phosphorylation of PGC-1α
Jäger, S., Handschin, C., St.-Pierre, J., & Spiegelman, B. M. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0705070104 · Cited by 2,491 · 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
Satellite Cells and the Muscle Stem Cell Niche
Yin, H., Price, F., & Rudnicki, M. A. (2013) · Physiological Reviews · doi:10.1152/physrev.00043.2011 · Cited by 2,166 · see citing works
Double muscling in cattle due to mutations in the myostatin gene
McPherron, A. C., & Lee, S.-J. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.23.12457 · Cited by 2,039 · see citing works
Isolation and Characterization of a Novel Endogenous Peptide Ligand for the Human APJ Receptor
Tatemoto, K., Hosoya, M., Habata, Y., Fujii, R., Kakegawa, T., Zou, M.-X., Kawamata, Y., Fukusumi, S., Hinuma, S., Kitada, C., et al. (1998) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1998.9489 · Cited by 1,684 · see citing works
Muscle–Organ Crosstalk: The Emerging Roles of Myokines
Severinsen, M. C. K., & Pedersen, B. K. (2020) · Endocrine Reviews · doi:10.1210/endrev/bnaa016 · Cited by 1,226 · cited 3× · see citing works
“…and stress, skeletal muscle secretes myokines, which are then found to participate in physiological processes, including the metabolism of lipids and glucose, and the browning of white adipose tissue (WAT), indicating that they are important in the development of obesity and diabetes [6, 31].”
The integrative biology of type 2 diabetes
Roden, M., & Shulman, G. I. (2019) · Nature · doi:10.1038/s41586-019-1797-8 · Cited by 1,167 · see citing works
Osteonectin, a bone-specific protein linking mineral to collagen
Termine, J. D., Kleinman, H. K., Whitson, S. W., Conn, K. M., McGarvey, M. L., & Martin, G. R. (1981) · Cell · doi:10.1016/0092-8674(81)90037-4 · Cited by 1,162 · see citing works
IL-6 enhances plasma IL-1ra, IL-10, and cortisol in humans
Steensberg, A., Fischer, C. P., Keller, C., Møller, K., & Pedersen, B. K. (2003) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00074.2003 · Cited by 1,135 · 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
Interleukin-6, a Major Cytokine in the Central Nervous System
Erta, M., Quintana, A., & Hidalgo, J. (2012) · International Journal of Biological Sciences · doi:10.7150/ijbs.4679 · Cited by 1,093 · see citing works
Adipokines in health and disease
Fasshauer, M., & Blüher, M. (2015) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2015.04.014 · Cited by 1,050 · 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
Myostatin, a Negative Regulator of Muscle Growth, Functions by Inhibiting Myoblast Proliferation
Thomas, M., Langley, B., Berry, C., Sharma, M., Kirk, S., Bass, J., & Kambadur, R. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m004356200 · Cited by 1,014 · see citing works
Potter, L. R., Abbey‐Hosch, S. E., & Dickey, D. M. (2005) · Endocrine Reviews · doi:10.1210/er.2005-0014 · Cited by 1,004 · see citing works
Function and biological roles of the Dickkopf family of Wnt modulators
Niehrs, C. (2006) · Oncogene · doi:10.1038/sj.onc.1210054 · Cited by 995 · see citing works
Rao, R. R., Long, J. Z., White, J. P., Svensson, K. J., Lou, J., Lokurkar, I., Jedrychowski, M. P., Ruas, J. L., Wrann, C. D., Lo, J. C., et al. (2014) · Cell · doi:10.1016/j.cell.2014.03.065 · Cited by 973 · see citing works
Epigenetics in Human Obesity and Type 2 Diabetes
Ling, C., & Rönn, T. (2019) · Cell Metabolism · doi:10.1016/j.cmet.2019.03.009 · Cited by 965 · see citing works
Why does obesity cause diabetes?
Klein, S., Gastaldelli, A., Yki-Järvinen, H., & Scherer, P. E. (2022) · Cell Metabolism · doi:10.1016/j.cmet.2021.12.012 · Cited by 939 · see citing works
Exerkines in health, resilience and disease
Chow, L. S., Gerszten, R. E., Taylor, J. M., Pedersen, B. K., van Praag, H., Trappe, S., Febbraio, M. A., Galis, Z. S., Gao, Y., Haus, J. M., et al. (2022) · Nature Reviews Endocrinology · doi:10.1038/s41574-022-00641-2 · Cited by 927 · see citing works
Ellingsgaard, H., Hauselmann, I., Schuler, B., Habib, A. M., Baggio, L. L., Meier, D. T., Eppler, E., Bouzakri, K., Wueest, S., Muller, Y. D., et al. (2011) · Nature Medicine · doi:10.1038/nm.2513 · Cited by 922 · see citing works
Understanding the Physiology of FGF21
Fisher, F. M., & Maratos-Flier, E. (2016) · Annual Review of Physiology · doi:10.1146/annurev-physiol-021115-105339 · Cited by 912 · 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
Interleukin-6 Is an Essential Regulator of Satellite Cell-Mediated Skeletal Muscle Hypertrophy
Serrano, A. L., Baeza-Raja, B., Perdiguero, E., Jardí, M., & Muñoz-Cánoves, P. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2007.11.011 · Cited by 873 · cited 1× · see citing works
“Previous research has found that IL-6 can promote muscle hypertrophy [44, 45], lipolysis [46], and glucose uptake [47] in skeletal muscle.”
Pancreatic β-cells in type 1 and type 2 diabetes mellitus: different pathways to failure
Eizirik, D. L., Pasquali, L., & Cnop, M. (2020) · Nature Reviews Endocrinology · doi:10.1038/s41574-020-0355-7 · Cited by 854 · see citing works
Restoring systemic GDF11 levels reverses age-related dysfunction in mouse skeletal muscle
Sinha, M., Jang, Y. C., Oh, J., Khong, D., Wu, E. Y., Manohar, R., Miller, C., Regalado, S. G., Loffredo, F. S., Pancoast, J. R., et al. (2014) · Science · doi:10.1126/science.1251152 · Cited by 824 · see citing works
Irisin and FGF21 are cold-induced endocrine activators of brown fat function in humans
Lee, P., Linderman, J. D., Smith, S., Brychta, R. J., Wang, J., Idelson, C., Perron, R. M., Werner, C. D., Phan, G. Q., Kammula, U. S., et al. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2013.12.017 · Cited by 802 · see citing works
Moreno-Navarrete, J. M., Ortega, F., Serrano, M., Guerra, E., Pardo, G., Tinahones, F., Ricart, W., & Fernández-Real, J. M. (2013) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2012-2749 · Cited by 788 · see citing works
Physical activity and muscle-brain crosstalk
Pedersen, B. K. (2019) · Nature Reviews Endocrinology · doi:10.1038/s41574-019-0174-x · Cited by 772 · see citing works
Interleukin-6 stimulates lipolysis and fat oxidation in humans
van Hall, G., Steensberg, A., Sacchetti, M., Fischer, C., Keller, C., Schjerling, P., Hiscock, N., Møller, K., Saltin, B., Febbraio, M. A., et al. (2003) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2002-021687 · Cited by 767 · see citing works
Zhang, Y., Li, R., Meng, Y., Li, S., Donelan, W., Zhao, Y., Qi, L., Zhang, M., Wang, X., Cui, T., et al. (2014) · Diabetes · doi:10.2337/db13-1106 · Cited by 733 · cited 1× · see citing works
“Upregulated UCP1, a thermogenic regulator in brown adipose tissue (BAT), contributes to the induction of white-to-brown shift [64, 87].”
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 2× · see citing works
“Skeletal muscle [186] Adipose tissue [330] Liver [331] Neuronal cells [332]”
Lin, Z., Tian, H., Lam, K. S. L., Lin, S., Hoo, R. C. L., Konishi, M., Itoh, N., Wang, Y., Bornstein, S. R., Xu, A., et al. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2013.04.005 · Cited by 691 · see citing works
Extracellular Vesicles Provide a Means for Tissue Crosstalk during Exercise
Whitham, M., Parker, B. L., Friedrichsen, M. H., Hingst, J. R., Hjorth, M., Hughes, W. E., Egan, C. L., Cron, L., Watt, K. I., Kuchel, R. P., et al. (2018) · Cell Metabolism · doi:10.1016/j.cmet.2017.12.001 · Cited by 689 · see citing works
Roberts, L. D., Boström, P., O’Sullivan, J. F., Schinzel, R. T., Lewis, G. D., Dejam, A., Lee, Y.-K., Palma, M. J., Calhoun, S., Georgiadi, A., et al. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2013.12.003 · Cited by 643 · see citing works
Physiology and role of irisin in glucose homeostasis
Perakakis, N., Triantafyllou, G. A., Fernández-Real, J. M., Huh, J. Y., Park, K. H., Seufert, J., & Mantzoros, C. S. (2017) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2016.221 · Cited by 621 · see citing works
The Liver as an Endocrine Organ—Linking NAFLD and Insulin Resistance
Watt, M. J., Miotto, P. M., De Nardo, W., & Montgomery, M. K. (2019) · Endocrine Reviews · doi:10.1210/er.2019-00034 · Cited by 615 · 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
GDF11 increases with age and inhibits skeletal muscle regeneration
Egerman, M. A., Cadena, S. M., Gilbert, J. A., Meyer, A., Nelson, H. N., Swalley, S. E., Mallozzi, C., Jacobi, C., Jennings, L. L., Clay, I., et al. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.05.010 · Cited by 527 · see citing works
Circulating irisin in relation to insulin resistance and the metabolic syndrome.
Park, K., Zaichenko, L., Brinkoetter, M. T., Thakkar, B., Sahin-Efe, A., Joung, K., Tsoukas, M. A., Geladari, E., Huh, J., Dinçer, F., et al. (2013) · Journal of Clinical Endocrinology and Metabolism · doi:10.1210/jc.2013-2373 · Cited by 527 · see citing works
Apelin Stimulates Glucose Utilization in Normal and Obese Insulin-Resistant Mice
Dray, C., Knauf, C., Daviaud, D., Waget, A., Boucher, J., Buléon, M., Cani, P. D., Attané, C., Guigné, C., Carpéné, C., et al. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2008.10.003 · Cited by 522 · see citing works
The myokine irisin increases cortical bone mass
Colaianni, G., Cuscito, C., Mongelli, T., Pignataro, P., Buccoliero, C., Liu, P., Lü, P., Sartini, L., Comite, M. D., Mori, G., et al. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1516622112 · Cited by 513 · see citing works
Muscle, Bone, and Fat Crosstalk: The Biological Role of Myokines, Osteokines, and Adipokines
Kirk, B., Feehan, J., Lombardi, G., & Duque, G. (2020) · Current Osteoporosis Reports · doi:10.1007/s11914-020-00599-y · Cited by 510 · see citing works
Suppression of body fat accumulation in myostatin-deficient mice
McPherron, A. C., & Lee, S.-J. (2002) · Journal of Clinical Investigation · doi:10.1172/jci0213562 · Cited by 505 · see citing works
The role of hepatokines in metabolism
Stefan, N., & Häring, H.-U. (2013) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2012.258 · Cited by 500 · see citing works
Rapid, deep and precise profiling of the plasma proteome with multi-nanoparticle protein corona
Blume, J. E., Manning, W. C., Troiano, G., Hornburg, D., Figa, M. A., Hesterberg, L. K., Platt, T. L., Zhao, X., Cuaresma, R., Everley, P. A., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-17033-7 · Cited by 458 · see citing works
Interleukin-6 Is a Novel Factor Mediating Glucose Homeostasis During Skeletal Muscle Contraction
Febbraio, M. A., Hiscock, N., Sacchetti, M., Fischer, C. P., & Pedersen, B. K. (2004) · Diabetes · doi:10.2337/diabetes.53.7.1643 · Cited by 455 · 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
Trans-presentation of IL-6 by dendritic cells is required for the priming of pathogenic TH17 cells
Heink, S., Yogev, N., Garbers, C., Herwerth, M., Aly, L., Gasperi, C., Husterer, V., Croxford, A. L., Möller‐Hackbarth, K., Bartsch, H. S., et al. (2016) · Nature Immunology · doi:10.1038/ni.3632 · Cited by 401 · see citing works
The exerkine apelin reverses age-associated sarcopenia
Vinel, C., Lukjanenko, L., Batut, A., Deleruyelle, S., Pradère, J.-P., Le Gonidec, S., Dortignac, A., Geoffre, N., Pereira, O., Karaz, S., et al. (2018) · Nature Medicine · doi:10.1038/s41591-018-0131-6 · Cited by 398 · see citing works
Azzu, V., Vacca, M., Virtue, S., Allison, M., & Vidal-Puig, A. (2020) · Gastroenterology · doi:10.1053/j.gastro.2019.12.054 · Cited by 369 · see citing works
Huh, J. Y., Mougios, V., Kabasakalis, A., Fatouros, I., Siopi, A., Douroudos, I. I., Filippaios, A., Panagiotou, G., Park, K. H., & Mantzoros, C. S. (2014) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2014-1437 · Cited by 363 · see citing works
Hotta, Y., Nakamura, H., Konishi, M., Murata, Y., Takagi, H., Matsumura, S., Inoue, K., Fushiki, T., & Itoh, N. (2009) · Endocrinology · doi:10.1210/en.2009-0119 · Cited by 352 · 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
Ashley, E. A., Powers, J. C., Chen, M. M., Kundu, R. K., Finsterbach, T., Caffarelli, A. D., Deng, A. C., EICHHORN, J., MAHAJAN, R., & Agrawal, R. (2004) · Cardiovascular Research · doi:10.1016/j.cardiores.2004.08.018 · Cited by 345 · see citing works
Exercise Metabolism and Adaptation in Skeletal Muscle
Smith, J. A. B., Murach, K. A., Dyar, K. A., & Zierath, J. R. (2023) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-023-00606-x · Cited by 342 · see citing works
The varying faces of IL-6: from cardiac protection to cardiac failure
Fontes, J. A., Rose, N., & Čiháková, D. (2015) · Cytokine · doi:10.1016/j.cyto.2014.12.024 · Cited by 334 · see citing works
BioID: A Screen for Protein‐Protein Interactions
Roux, K. J., Kim, D. I., Burke, B. E., & May, D. G. (2018) · Current Protocols in Protein Science · doi:10.1002/cpps.51 · Cited by 334 · see citing works
A leptin–BDNF pathway regulating sympathetic innervation of adipose tissue
Wang, P., Loh, K. H., Wu, M., Morgan, D. A., Schneeberger, M., Yu, X., Chi, J., Kosse, C., Kim, D., Rahmouni, K., et al. (2020) · Nature · doi:10.1038/s41586-020-2527-y · Cited by 332 · see citing works
Cellular Localization of Interleukin 6 mRNA and Interleukin 6 Receptor mRNA in Rat Brain
Schöbitz, B., de Kloet, E. R., Sutanto, W., & Holsboer, F. (1993) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.1993.tb00210.x · Cited by 329 · see citing works
Physical activity and autoimmune diseases: Get moving and manage the disease
Sharif, Κ., Watad, ., Bragazzi, N. L., Lichtbroun, M., Amital, H., & Shoenfeld, Y. (2017) · Autoimmunity Reviews · doi:10.1016/j.autrev.2017.11.010 · Cited by 325 · see citing works
Increased secretion and expression of myostatin in skeletal muscle from extremely obese women
Hittel, D. S., Berggren, J. R., Shearer, J., Boyle, K., & Houmard, J. A. (2009) · Diabetes · doi:10.2337/db08-0943 · Cited by 324 · 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 318 · see citing works
FGF21 as Modulator of Metabolism in Health and Disease
Tezze, C., Romanello, V., & Sandri, M. (2019) · Frontiers in Physiology · doi:10.3389/fphys.2019.00419 · Cited by 313 · see citing works
A live cell reporter of exosome secretion and uptake reveals pathfinding behavior of migrating cells
Sung, B. H., von Lersner, A. K., Guerrero, J. F., Krystofiak, E., Inman, D. R., Pelletier, R., Zijlstra, A., Ponik, S. M., & Weaver, A. M. (2020) · Nature Communications · doi:10.1038/s41467-020-15747-2 · Cited by 313 · see citing works
Dietary factors, epigenetic modifications and obesity outcomes: Progresses and perspectives
Milagro, F. I., Mansego, M. L., de Miguel, C., & Martínez, J. A. (2012) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2012.06.010 · Cited by 310 · see citing works
Huh, J. Y., Dincer, F., Mesfum, E., & Mantzoros, C. S. (2014) · International Journal of Obesity · doi:10.1038/ijo.2014.42 · Cited by 309 · see citing works
Irisin: A Hope in Understanding and Managing Obesity and Metabolic Syndrome
Arhire, L. I., Mihalache, L., & Covașă, M. (2019) · Frontiers in Endocrinology · doi:10.3389/fendo.2019.00524 · Cited by 306 · see citing works
Dynamics of the skeletal muscle secretome during myoblast differentiation
Henningsen, J., Rigbolt, K. T. G., Blagoev, B., Pedersen, B. K., & Kratchmarova, I. (2010) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m110.002113 · Cited by 303 · see citing works
Interleukin 6 as an Energy Allocator in Muscle Tissue
Kistner, T. M., Pedersen, B. K., & Lieberman, D. E. (2022) · Nature Metabolism · doi:10.1038/s42255-022-00538-4 · Cited by 295 · see citing works
Chemerin and its receptors in leukocyte trafficking, inflammation and metabolism
Bondue, B., Wittamer, V., & Parmentier, M. (2011) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2011.11.004 · Cited by 294 · see citing works
Bi, J., Zhang, J., Ren, Y., Du, Z., Li, Q., Wang, Y., Wei, S., Yang, L., Zhang, J., Liu, C., et al. (2018) · Redox Biology · doi:10.1016/j.redox.2018.10.019 · Cited by 288 · see citing works
The Ever-Expanding Myokinome: Discovery Challenges and Therapeutic Implications
Whitham, M., & Febbraio, M. A. (2016) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2016.153 · Cited by 279 · see citing works
Apelin is necessary for the maintenance of insulin sensitivity
Yue, P., Jin, H. H., Aillaud, M., Deng, A. C., Azuma, J., Asagami, T., Kundu, R. K., Reaven, G. M., Quertermous, T., & Tsao, P. S. (2009) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00385.2009 · Cited by 277 · see citing works
Quantitative Fluxomics of Circulating Metabolites
Hui, S. T., Cowan, A. J., Zeng, X., Yang, L., TeSlaa, T. A., Li, X., Bartman, C., Zhang, Z., Jang, C., Wang, L., et al. (2020) · Cell Metabolism · doi:10.1016/j.cmet.2020.07.013 · Cited by 274 · see citing works
Myostatin decreases with aerobic exercise and associates with insulin resistance
HITTEL, D. S., AXELSON, M., SARNA, N., SHEARER, J., HUFFMAN, K. M., & KRAUS, W. E. (2010) · Medicine & Science in Sports & Exercise · doi:10.1249/mss.0b013e3181e0b9a8 · Cited by 271 · see citing works
Diverse biological functions of the SPARC family of proteins
Bradshaw, A. D. (2012) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2011.12.021 · Cited by 268 · see citing works
Ren, Y., Zhao, H., Yin, C., Lan, X., Wu, L., Du, X., Griffiths, H. R., & Gao, D. (2022) · Frontiers in Endocrinology · doi:10.3389/fendo.2022.873699 · Cited by 260 · see citing works
Hepatokines and metabolism: Deciphering communication from the liver
Jensen-Cody, S. O., & Potthoff, M. J. (2021) · Molecular Metabolism · doi:10.1016/j.molmet.2020.101138 · Cited by 252 · see citing works
Human and Rat Hepatic Stellate Cells Express Neurotrophins and Neurotrophin Receptors
Cassiman, D. M., Denef, C., Desmet, V. J., & Roskams, T. (2001) · Hepatology · doi:10.1053/jhep.2001.20793 · Cited by 250 · see citing works
CD81 controls beige fat progenitor cell growth and energy balance via FAK signaling
Oguri, Y., Shinoda, K., Kim, H., Alba, D. L., Bolus, W. R., Wang, Q., Brown, Z., Pradhan, R., Tajima, K., Yoneshiro, T., et al. (2020) · Cell · doi:10.1016/j.cell.2020.06.021 · Cited by 250 · see citing works
Xin, C., Liu, J., Zhang, J., Zhu, D., Wang, H., Xiong, L., Lee, Y., Ye, J., Lian, K., Xu, C., et al. (2016) · International Journal of Obesity · doi:10.1038/ijo.2015.199 · Cited by 248 · cited 2× · see citing works
“Phosphorylation of AMPK α / insulin receptor β -subunit/ERK1/2 also contributes to the regulation of these effects, which is maintained by irisin [96, 97].”
Progress and Challenges in the Biology of FNDC5 and Irisin
Maak, S., Norheim, F., Drevon, C. A., & Erickson, H. P. (2021) · Endocrine Reviews · doi:10.1210/endrev/bnab003 · Cited by 247 · see citing works
The role of exercise-induced myokines in regulating metabolism
Huh, J. Y. (2018) · Archives of Pharmacal Research · doi:10.1007/s12272-017-0994-y · Cited by 242 · see citing works
The effects of obesity on skeletal muscle regeneration
Akhmedov, D., & Berdeaux, R. (2013) · Frontiers in Physiology · doi:10.3389/fphys.2013.00371 · Cited by 241 · see citing works
Nakashima, M., Toyono, T., Akamine, A., & Joyner, A. (1999) · Mechanisms of Development · doi:10.1016/s0925-4773(98)00205-6 · Cited by 240 · see citing works
Fibroblast growth factor 21 controls mitophagy and muscle mass
Oost, L. J., Kustermann, M., Armani, A., Blaauw, B., & Romanello, V. (2019) · Journal of Cachexia, Sarcopenia and Muscle · doi:10.1002/jcsm.12409 · Cited by 231 · see citing works
Age-Associated Mitochondrial Dysfunction Accelerates Atherogenesis
Tyrrell, D. J., Blin, M. G., Song, J., Wood, S. C., Zhang, M., Beard, D. A., & Goldstein, D. R. (2019) · Circulation Research · doi:10.1161/circresaha.119.315644 · Cited by 228 · see citing works
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 2× · see citing works
“Apelin was first defined as a myokine in endurance training research for obese individuals [174].”
Attané, C., Foussal, C., Gonidec, S. L., Bénani, A., Daviaud, D., Wanecq, E., Guzmán‐Ruiz, R., Dray, C., Bézaire, V., Rancoule, C., et al. (2011) · Diabetes · doi:10.2337/db11-0100 · Cited by 226 · see citing works
Myokines in insulin resistance and type 2 diabetes
Eckardt, K., Görgens, S. W., Raschke, S., & Eckel, J. (2014) · Diabetologia · doi:10.1007/s00125-014-3224-x · Cited by 223 · see citing works
Diabetic myopathy: impact of diabetes mellitus on skeletal muscle progenitor cells
D’Souza, D. M., Al‐Sajee, D., & Hawke, T. J. (2013) · Frontiers in Physiology · doi:10.3389/fphys.2013.00379 · Cited by 223 · see citing works
Brown Adipose Tissue Controls Skeletal Muscle Function via the Secretion of Myostatin
Kong, X., Yao, T. S., Zhou, P., Kazak, L., Tenen, D. E., Lyubetskaya, A., Dawes, B. A., Tsai, L. T.-Y., Kahn, B. B., Spiegelman, B. M., et al. (2018) · Cell Metabolism · doi:10.1016/j.cmet.2018.07.004 · Cited by 223 · 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 2× · see citing works
“These results indicate that skeletal muscle can secrete FGF21, which acts on adipocytes to promote browning and regulate thermogenesis [168].”
β-aminoisobutyric Acid, l-BAIBA, Is a Muscle-Derived Osteocyte Survival Factor
Kitase, Y., Vallejo, J. A., Gutheil, W., Vemula, H., Jähn, K., Yi, J., Zhou, J., Brotto, M., & Bonewald, L. F. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.01.041 · Cited by 219 · see citing works
Boettcher, M., Machann, J., Stefan, N., Thamer, C., Häring, H., Claussen, C. D., Fritsche, A., & Schick, F. (2009) · Journal of Magnetic Resonance Imaging · doi:10.1002/jmri.21754 · Cited by 214 · see citing works
OPA1 deficiency promotes secretion of FGF21 from muscle that prevents obesity and insulin resistance
Pereira, R. O., Tadinada, S. M., Zasadny, F. M., Oliveira, K. J., Pires, K. M. P., Olvera, A., Jeffers, J., Souvenir, R., Mcglauflin, R., Seei, A., et al. (2017) · The EMBO Journal · doi:10.15252/embj.201696179 · Cited by 211 · see citing works
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 210 · see citing works
The WNT signalling pathway and diabetes mellitus
Jin, T. (2008) · Diabetologia · doi:10.1007/s00125-008-1084-y · Cited by 208 · see citing works
Quantification of GDF11 and Myostatin in Human Aging and Cardiovascular Disease
Schafer, M. J., Atkinson, E. J., Vanderboom, P. M., Kotajarvi, B. R., White, T. A., Moore, M. M., Bruce, C. J., Greason, K. L., Suri, R. M., Khosla, S., et al. (2016) · Cell Metabolism · doi:10.1016/j.cmet.2016.05.023 · Cited by 206 · see citing works
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 · see citing works
Jung, T. W., Lee, S. H., Kim, H.-C., Bang, J. S., Abd El-Aty, A. M., Hacımüftüoğlu, A., Shin, Y. K., & Jeong, J. H. (2018) · Experimental & Molecular Medicine · doi:10.1038/s12276-018-0147-5 · Cited by 203 · see citing works
Glucose Ingestion Attenuates Interleukin‐6 Release from Contracting Skeletal Muscle in Humans
Febbraio, M. A., Steensberg, A., Keller, C., Starkie, R. L., Nielsen, H. B., Krustrup, P., Ott, P., Secher, N. H., & Pedersen, B. K. (2003) · The Journal of Physiology · doi:10.1113/jphysiol.2003.042374 · Cited by 202 · 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
Musclin is an activity-stimulated myokine that enhances physical endurance
Subbotina, E., Sierra, A., Zhu, Z., Gao, Z., Koganti, S. R. K., Reyes, S., Stepniak, E., Walsh, S. A., Acevedo, M. R., Perez-Terzic, C. M., et al. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1514250112 · Cited by 198 · see citing works
SPARC: a key player in the pathologies associated with obesity and diabetes
Kos, K., & Wilding, J. P. H. (2010) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2010.18 · Cited by 193 · see citing works
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 · see citing works
A REIC Gene Shows Down-Regulation in Human Immortalized Cells and Human Tumor-Derived Cell Lines
Tsuji, T., Miyazaki, M., Sakaguchi, M., Inoue, Y., & Namba, M. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1999.2067 · Cited by 191 · see citing works
Metrnl: A secreted protein with new emerging functions
Zheng, S.-L., Li, Z.-Y., Song, J., Liu, J.-M., & Miao, C.-Y. (2016) · Acta Pharmacologica Sinica · doi:10.1038/aps.2016.9 · Cited by 190 · see citing works
Adipokines, Myokines, and Hepatokines: Crosstalk and Metabolic Repercussions
de Oliveira dos Santos, A. R., de Oliveira Zanuso, B., Miola, V. F. B., Barbalho, S. M., Santos Bueno, P. C., Flato, U. A. P., Detregiachi, C. R. P., Buchaim, D. V., Buchaim, R. L., Tofano, R. J., et al. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22052639 · Cited by 189 · see citing works
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 · see citing works
Allen, D. L., Cleary, A. S., Speaker, K. J., Lindsay, S. F., Uyenishi, J., Reed, J. M., Madden, M. C., & Mehan, R. S. (2008) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00798.2007 · Cited by 183 · see citing works
Musclin, a novel skeletal muscle-derived secretory factor
Nishizawa, H., Matsuda, M., Yamada, Y., Kawai, K., Suzuki, E., Makishima, M., Kitamura, T., & Shimomura, I. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.c400066200 · Cited by 182 · see citing works
Kumar, S., Wang, G., Zheng, N., Cheng, W., Ouyang, K., Lin, H., Liao, Y., & Liu, J. (2019) · Hypertension · doi:10.1161/hypertensionaha.118.12267 · Cited by 181 · see citing works
LeBrasseur, N. K., Schelhorn, T. M., Bernardo, B. L., Cosgrove, P. G., Loria, P. M., & Brown, T. A. (2009) · The Journals of Gerontology Series A: Biological Sciences and Medical Sciences · doi:10.1093/gerona/glp068 · Cited by 180 · see citing works
Keller, C., Steensberg, A., Hansen, A. K., Fischer, C. P., Plomgaard, P., & Pedersen, B. K. (2005) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00590.2005 · Cited by 179 · see citing works
Muscular Interleukin-6 and Its Role as an Energy Sensor
Pedersen, B. K. (2011) · Medicine & Science in Sports & Exercise · doi:10.1249/mss.0b013e31822f94ac · Cited by 175 · see citing works
Apelin and APJ regulation in adipose tissue and skeletal muscle of type 2 diabetic mice and humans
Dray, C., Debard, C., Jager, J., Disse, E., Daviaud, D., Martin, P. G. P., Attané, C., Wanecq, E., Guigné, C., Bost, F., et al. (2010) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00598.2009 · Cited by 171 · 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
Liu, W., Zhou, L., Zhou, C., Zhang, S., Jing, J., Xie, L., Sun, N., Duan, X., Jing, W., Liang, X., et al. (2016) · Nature Communications · doi:10.1038/ncomms12794 · Cited by 155 · see citing works
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 151 · see citing works
β-Aminoisobutyric Acid (α-Methyl-β-Alanine): A New Amino-Acid Obtained from Human Urine
Crumpler, H. R., Dent, C. E., Harris, H., et al. (1951) · Nature · doi:10.1038/167307a0 · Cited by 149 · see citing works
Sheikh, A. Y., Chun, H. J., Glassford, A. J., Kundu, R. K., Kutschka, I., Ardigò, D., Hendry, S. L., Wagner, R. A., Chen, M. M., Ali, Z. A., et al. (2007) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00935.2007 · Cited by 148 · see citing works
Targeting the myostatin signaling pathway to treat muscle loss and metabolic dysfunction
Lee, S. (2021) · Journal of Clinical Investigation · doi:10.1172/jci148372 · Cited by 147 · see citing works
Meng, Z.-X., Li, S., Wang, L., Ko, H. J., Lee, Y., Jung, D. Y., Okutsu, M., Yan, Z., Kim, J. K., & Lin, J. D. (2013) · Nature Medicine · doi:10.1038/nm.3144 · Cited by 146 · see citing works
Self-citationThe endocrine role of brown adipose tissue: An update on actors and actions
Gavaldà‐Navarro, A., Villarroya, J., Cereijo, R., Giralt, M., & Villarroya, F. (2021) · Reviews in Endocrine and Metabolic Disorders · doi:10.1007/s11154-021-09640-6 · Cited by 145 · see citing works
Cell type-selective secretome profiling in vivo
Wei, W., Riley, N. M., Yang, A. C., Kim, J. T., Terrell, S. M., Li, V. L., García-Contreras, M., Bertozzi, C. R., & Long, J. Z. (2020) · Nature Chemical Biology · doi:10.1038/s41589-020-00698-y · Cited by 144 · see citing works
Sesti, G., Andreozzi, F., Fiorentino, T. V., Mannino, G. C., Sciacqua, A., Marini, M. A., & Perticone, F. (2014) · Acta Diabetologica · doi:10.1007/s00592-014-0576-0 · Cited by 142 · see citing works
BDNF is a mediator of glycolytic fiber-type specification in mouse skeletal muscle
Delezie, J., Weihrauch, M., Maier, G., Tejero, R., Ham, D. J., Gill, J. F., Karrer-Cardel, B., Rüegg, M. A., Tabares, L., & Handschin, C. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1900544116 · Cited by 141 · see citing works
Simón, J., Núñez-García, M., Fernández-Tussy, P., Barbier-Torres, L., Fernández-Ramos, D., Gómez-Santos, B., Buqué, X., Lopitz-Otsoa, F., Goikoetxea-Usandizaga, N., Serrano-Maciá, M., et al. (2020) · Cell Metabolism · doi:10.1016/j.cmet.2020.01.013 · Cited by 141 · see citing works
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 · see citing works
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 · see citing works
Osteocrin, a Novel Bone-specific Secreted Protein That Modulates the Osteoblast Phenotype
Thomas, G. P., Moffatt, P., Salois, P., Gaumond, M.-H., Gingras, R., Godin, É., Miao, D., Goltzman, D., & Lanctôt, C. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m307310200 · Cited by 130 · see citing works
Chronic Exercise Training and Circulating Irisin in Adults: A Meta-Analysis
Qiu, S., Cai, X., Sun, Z., Schumann, U., Zügel, M., & Steinacker, J. M. (2015) · Sports Medicine · doi:10.1007/s40279-014-0293-4 · Cited by 129 · see citing works
Browning of white fat: does irisin play a role in humans?
Elsen, M., Raschke, S., & Eckel, J. (2014) · Journal of Endocrinology · doi:10.1530/joe-14-0189 · Cited by 128 · see citing works
Inhibition of Preadipocyte Differentiation by Myostatin Treatment in 3T3-L1 Cultures
Kim, H., Liang, L., Dean, R. G., Hausman, D. B., Hartzell, D. L., & Baile, C. A. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.4435 · Cited by 127 · see citing works
Eaton, M., Granata, C., Barry, J., Safdar, A., Bishop, D., & Little, J. P. (2018) · Journal of Sport and Health Science · doi:10.1016/j.jshs.2017.01.003 · Cited by 126 · see citing works
Begue, G., Douillard, A., Galbes, O., Rossano, B., Vernus, B., Candau, R., & Py, G. (2013) · PLoS ONE · doi:10.1371/journal.pone.0057141 · Cited by 124 · see citing works
Systemic Nutrient and Stress Signaling via Myokines and Myometabolites
Rai, M., & Demontis, F. (2016) · Annual Review of Physiology · doi:10.1146/annurev-physiol-021115-105305 · Cited by 123 · see citing works
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 121 · see citing works
Natalicchio, A., Marrano, N., Biondi, G., Spagnuolo, R., Labarbuta, R., Porreca, I., Cignarelli, A., Bugliani, M., Marchetti, P., Perrini, S., et al. (2017) · Diabetes · doi:10.2337/db17-0002 · Cited by 121 · see citing works
Beta-Aminoisobutyric Acid as a Novel Regulator of Carbohydrate and Lipid Metabolism
Tanianskii, D. A., Jarzebska, N., Birkenfeld, A. L., O’Sullivan, J. F., & Rodionov, R. N. (2019) · Nutrients · doi:10.3390/nu11030524 · Cited by 121 · see citing works
Ahuja, P., Ng, C. F., Pang, B. P. S., Chan, W. S., Tse, M. C. L., Bi, X., Kwan, H.-L. R., Brobst, D., Herlea-Pana, O., Yang, X., et al. (2022) · Autophagy · doi:10.1080/15548627.2021.1985257 · Cited by 116 · 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
FNDC5/Irisin inhibits pathological cardiac hypertrophy
Yu, Q., Kou, W., Xu, X., Zhou, S., Luan, P., Xu, X., Li, H., Zhuang, J., Wang, J., Zhao, Y., et al. (2019) · Clinical Science · doi:10.1042/cs20190016 · Cited by 115 · see citing works
Shen, G., Zhou, H.-B., Zhang, H., Chen, B., Liu, Z., Yuan, Y., Zhou, X., & Xu, Y. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2018.09.015 · Cited by 112 · see citing works
Apelin/APJ system: an emerging therapeutic target for respiratory diseases
Yan, J., Wang, A., Cao, J., & Chen, L. (2020) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03461-7 · Cited by 109 · see citing works
Kim, K.-E., Park, I., Kim, J. B., Kang, M., Choi, W. G., Shin, H., Kim, J.-S., Rhee, H., & Suh, J. M. (2021) · Nature Communications · doi:10.1038/s41467-021-25546-y · Cited by 109 · see citing works
Fournier, B., Murray, B., Gutzwiller, S., Marcaletti, S., Marcellin, D., Bergling, S., Brachat, S., Persohn, E., Pierrel, E., Bombard, F., et al. (2012) · Molecular and Cellular Biology · doi:10.1128/mcb.06575-11 · Cited by 108 · see citing works
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 · see citing works
Myokines in metabolic homeostasis and diabetes
Eckel, J. (2019) · Diabetologia · doi:10.1007/s00125-019-4927-9 · Cited by 107 · see citing works
Humoral Nature of the Hypoglycemic Factor of Muscular Work
Goldstein, M. S. (1961) · Diabetes · doi:10.2337/diab.10.3.232 · Cited by 106 · see citing works
Martínez-Sánchez, N., Sweeney, O., Sidarta-Oliveira, D., Caron, A., Stanley, S., & Domingos, A. (2022) · Neuron · doi:10.1016/j.neuron.2022.10.017 · Cited by 105 · see citing works
Control of osteocyte dendrite formation by Sp7 and its target gene osteocrin
Wang, J. S., Kamath, T., Mazur, C. M., Mirzamohammadi, F., Rotter, D., Hojo, H., Castro, C. D., Tokavanich, N., Patel, R., Govea, N., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-26571-7 · Cited by 103 · see citing works
Irisin, a fascinating field in our times
Bao, J., She, Q.-Y., Hu, P., Jia, N., & Li, A. (2022) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2022.06.003 · Cited by 102 · see citing works
Antibody–cytokine fusion proteins
Kontermann, R. E. (2012) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2012.03.001 · Cited by 101 · see citing works
Yie, J., Wang, W., Deng, L., Tam, L., Stevens, J., Chen, M. M., Li, Y., Xu, J., Lindberg, R., Hecht, R., et al. (2012) · Chemical Biology & Drug Design · doi:10.1111/j.1747-0285.2012.01325.x · Cited by 99 · see citing works
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 · see citing works
Ji, C., Chen, X., Gao, C., Jiao, L., Wang, J., Xu, G., Fu, H., Guo, X., & Zhao, Y. (2011) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-011-9361-8 · Cited by 99 · see citing works
Moffatt, P., Thomas, G. P., Sellin, K., Bessette, M.-C., Lafrenière, F., Akhouayri, O., St‐Arnaud, R., & Lanctôt, C. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m708596200 · Cited by 99 · see citing works
Global mRNA sequencing of human skeletal muscle: Search for novel exercise-regulated myokines
Pourteymour, S., Eckardt, K., Holen, T., Langleite, T. M., Lee-Ødegård, S., Jensen, J., Birkeland, K. I., Drevon, C. A., & Hjorth, M. (2017) · Molecular Metabolism · doi:10.1016/j.molmet.2017.01.007 · Cited by 99 · see citing works
Muscle-generated BDNF is a sexually dimorphic myokine that controls metabolic flexibility
Yang, X., Brobst, D., Chan, W. S., Tse, M. C. L., Herlea-Pana, O., Ahuja, P., Bi, X., Zaw, A. M., Kwong, Z. S. W., Jia, W.-H., et al. (2019) · Science Signaling · doi:10.1126/scisignal.aau1468 · Cited by 99 · see citing works
Lee, J. O., Lee, H. J., Lee, Y. W., Han, J. A., Kang, M. J., Moon, J., Shin, M.-J., Lee, H. J., Chung, J. H., Lee, J., et al. (2020) · FEBS Journal · doi:10.1111/febs.15301 · Cited by 97 · see citing works
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
A Piezo1/KLF15/IL-6 axis mediates immobilization-induced muscle atrophy
Hirata, Y., Nomura, K., Kato, D., Tachibana, Y., Niikura, T., Uchiyama, K., Hosooka, T., Fukui, T., Oe, K., Kuroda, R., et al. (2022) · Journal of Clinical Investigation · doi:10.1172/jci154611 · Cited by 96 · see citing works
Interactions between central nervous system and peripheral metabolic organs
Zeng, W., Yang, F., Shen, W. L., Zhan, C., Zheng, P., & Hu, J. (2022) · Science China Life Sciences · doi:10.1007/s11427-021-2103-5 · Cited by 96 · see citing works
Abnormal hepatic apolipoprotein B metabolism in type 2 diabetes
Vergès, B. L. (2010) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2010.01.028 · Cited by 95 · see citing works
Wolf, J., Waetzig, G. H., Chalaris, A., Reinheimer, T. M., Wege, H., Rose‐John, S., & Garbers, C. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.718551 · Cited by 95 · see citing works
El‐Ashmawy, H. M., Selim, F. O., Hosny, T., & Almassry, H. N. (2019) · Diabetes Research and Clinical Practice · doi:10.1016/j.diabres.2019.02.026 · Cited by 93 · see citing works
Baetta, R., & Banfi, C. (2019) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.119.312612 · Cited by 93 · see citing works
Chen, Y., Ye, J., Cao, L., Zhang, Y., Xia, W., & Zhu, D. (2010) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2010.09.017 · Cited by 91 · see citing works
Inhibition of the Fission Machinery Mitigates OPA1 Impairment in Adult Skeletal Muscles
Romanello, V., Scalabrin, M., Albiero, M., Blaauw, B., Scorrano, L., & Sandri, M. (2019) · Cells · doi:10.3390/cells8060597 · Cited by 91 · see citing works
Metrnl Alleviates Lipid Accumulation by Modulating Mitochondrial Homeostasis in Diabetic Nephropathy
Zhou, Y., Liu, L., Jin, B., Wu, Y., Xu, L., Chang, X., Hu, L., Wang, G., Huang, Y., Song, L., et al. (2023) · Diabetes · doi:10.2337/db22-0680 · Cited by 91 · see citing works
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 · see citing works
Dadmanesh, M., Aghajani, H., Fadaei, R., & Ghorban, K. (2018) · PLOS ONE · doi:10.1371/journal.pone.0204180 · Cited by 89 · see citing works
Irisin, an exercise-induced bioactive peptide beneficial for health promotion during aging process
Zhang, H., Wu, X., Liang, J., Kirberger, M., & Chen, N. (2022) · Ageing Research Reviews · doi:10.1016/j.arr.2022.101680 · Cited by 88 · see citing works
Neuroendocrine control of appetite and metabolism
Yoo, E.-S., Yu, J., & Sohn, J. (2021) · Experimental & Molecular Medicine · doi:10.1038/s12276-021-00597-9 · Cited by 87 · see citing works
Hepatosplanchnic clearance of interleukin-6 in humans during exercise
Febbraio, M. A., Ott, P., Nielsen, H. B., Steensberg, A., Keller, C., Krustrup, P., Secher, N. H., & Pedersen, B. K. (2003) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00134.2003 · Cited by 86 · see citing works
Skeletal muscle derived Musclin protects the heart during pathological overload
Szaroszyk, M., Kattih, B., Martín-Garrido, A., Trogisch, F. A., Dittrich, G. M., Grund, A., Abouissa, A., Derlin, K., Meier, M., Holler, T., et al. (2022) · Nature Communications · doi:10.1038/s41467-021-27634-5 · Cited by 86 · see citing works
Murata, Y., Konishi, M., & Itoh, N. (2011) · Journal of Nutrition and Metabolism · doi:10.1155/2011/981315 · Cited by 85 · see citing works
He, Y., Hakvoort, T. B. M., Köhler, E. S., Vermeulen, J. L. M., de Waart, D. R., de Theije, C. C., Have, G. A. M. T., van Eijk, H. M. H., Kunne, C., Labruyère, W. T., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.092429 · Cited by 84 · see citing works
A Strategy for Discovery of Endocrine Interactions with Application to Whole-Body Metabolism
Seldin, M. M., Koplev, S., Rajbhandari, P., Vergnes, L., Rosenberg, G. M., Meng, Y., Pan, C., Phuong, T. M. N., Gharakhanian, R., Che, N., et al. (2018) · Cell Metabolism · doi:10.1016/j.cmet.2018.03.015 · Cited by 84 · see citing works
Hjorth, M., Pourteymour, S., Görgens, S. W., Langleite, T. M., Lee, S., Holen, T., Gulseth, H. L., Birkeland, K. I., Jensen, J., Drevon, C. A., et al. (2016) · Acta Physiologica · doi:10.1111/apha.12631 · Cited by 83 · see citing works
So, W. Y., & Leung, P. S. (2016) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2016.07.022 · Cited by 83 · cited 1× · see citing works
“Ex vivo studies have found that irisin ameliorates dysregulated glucose and lipid metabolism, and improves hepatic insulin resistance and cell survival under high glucose-high insulin conditions [104].”
Parr, E. B., CAMERA, D. M., Burke, L. M., Phillips, S. M., Coffey, V. G., & Hawley, J. A. (2016) · PLoS ONE · doi:10.1371/journal.pone.0152545 · Cited by 82 · see citing works
Role of growth differentiation factor 11 in development, physiology and disease
Zhang, Y., Wei, Y. S., Liu, D., Liu, F., Li, X. A., Pan, L., Pang, Y., & Chen, D. (2017) · Oncotarget · doi:10.18632/oncotarget.20258 · Cited by 82 · 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
Suh, J., Kim, N.-K., Lee, S., Eom, J., Lee, Y., Park, J., Woo, K. M., Baek, J., Kim, J., Ryoo, H., et al. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1916034117 · Cited by 82 · see citing works
Bagheri, R., Moghadam, B. H., Church, D. D., Tinsley, G. M., Eskandari, M., Moghadam, B. H., Motevalli, M. S., Baker, J. S., Robergs, R. A., & Wong, A. (2020) · Experimental Gerontology · doi:10.1016/j.exger.2020.110869 · Cited by 81 · see citing works
Meteorin-like/Meteorin-β protects heart against cardiac dysfunction
Rupérez, C., Ferrer‐Curriu, G., Cervera-Barea, A., Florit, L., Guitart‐Mampel, M., Garrabou, G., Zamora, M., Crispi, F., Fernández‐Solà, J., Lupón, J., et al. (2021) · The Journal of Experimental Medicine · doi:10.1084/jem.20201206 · Cited by 79 · see citing works
Physical Exercise-Induced Myokines in Neurodegenerative Diseases
Lee, B., Shin, M., Park, Y., Won, S.-Y., & Cho, K. S. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22115795 · Cited by 79 · see citing works
Mechanical load regulates bone growth via periosteal Osteocrin
Watanabe‐Takano, H., Ochi, H., Chiba, A., Matsuo, A., Kanai, Y., Fukuhara, S., Ito, N., Sako, K., Miyazaki, T., Tainaka, K., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109380 · Cited by 78 · see citing works
Lattanzio, S., Santilli, F., Liani, R., Vazzana, N., Ueland, T., Fulvio, P. D., Formoso, G., Consoli, A., Aukrust, P., & Davı̀, G. (2014) · Journal of the American Heart Association · doi:10.1161/jaha.114.001000 · Cited by 77 · see citing works
A Piezo1/KLF15/IL-6 axis mediates immobilization- induced muscle atrophy
Hirata, Y., Nomura, K., 野村, 和., ノムラ, カ., Kato, D., Wake, H., 和氣, 弘., ワケ, ヒ., Ogawa, W., Hirata, Y., et al. (2022) · Institutional Repositories DataBase (IRDB) · Cited by 76 · see citing works
Stressed Liver and Muscle Call on Adipocytes with FGF21
Luo, Y., & McKeehan, W. L. (2013) · Frontiers in Endocrinology · doi:10.3389/fendo.2013.00194 · Cited by 75 · see citing works
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Obesity and Exercise: New Insights and Perspectives
James, N. M., & Stanford, K. I. (2025) · Endocrine Reviews · doi:10.1210/endrev/bnaf017 · Cited by 20 · see citing works
Polo-Ferrero, L., Martin, M. J., Puente-González, A. S., Barbero-Iglesias, F. J., González-Manzano, S., & Méndez-Sánchez, R. (2025) · Nutrients · doi:10.3390/nu17111822 · Cited by 15 · see citing works
- Authors
- Chen, Z.-T., Weng, Z.-X., Lin, J. D., & Meng, Z.-X.
- Affiliations
- Second Affiliated Hospital of Zhejiang University (CN)
- University of Michigan (US)
- Affiliated Hangzhou First People's Hospital, Westlake University, School of Medicine (CN)
- Corresponding author
- Lin, Jiandie D
- Meng, Zhuo-Xian
- Venue
- Life Metabolism
- Publisher
- Oxford University Press (OUP)
- Published
- 2024-03-02
- Volume
- 3
- Issue
- 3
- Pages
- loae006-loae006
- ISSN
- 2755-0230 (ISSN-L)
- PMC
- PMC11749576
- OpenAlex
- W4392351638
- Cited by
- 58
- References
- 346
- Citations by year
- 2026: 29 · 2025: 27 · 2024: 2
- FWCI
- 3.82
- Type
- journal article
- Language
- en
- Open access
- diamond
- doi.org
- Licence
- Locations
- Life Metabolism (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- National Key Research and Development Program of China (2018YFA0800403, 2021YFC2701903)
- National Natural Science Foundation of China (91857110, 81670740, 32000817, 82100904, 82300910)
- National Outstanding Youth Science Fund Project of National Natural Science Foundation of China (81722012)
- Zhejiang Provincial Natural Science Foundation of China (LZ21H070001, LHDMD22H02001, LHDMD24H030001)
- Innovative Institute of Basic Medical Sciences of Zhejiang University
- Fundamental Research Funds
- Topics
- Health Sciences › Medicine › Epidemiology › Adipokines, Inflammation, and Metabolic Diseases
- Health Sciences › Medicine › Rehabilitation › Exercise and Physiological Responses
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Keywords
- myokines, skeletal muscle, obesity, type 2 diabetes, interleukin-6, irisin, myostatin, GDF11, FGF21, apelin, brain-derived neurotrophic factor, Metrnl, SPARC, musclin, Dickkopf-3, physical activity, organ crosstalk, energy homeostasis, metabolic regulation
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
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