IL-15 Promotes Human Myogenesis and Mitigates the Detrimental Effects of TNFα on Myotube Development
Open accessAbstract
Studies in murine cell lines and in mouse models suggest that IL-15 promotes myogenesis and may protect against the inflammation-mediated skeletal muscle atrophy which occurs in sarcopenia and cachexia. The effects of IL-15 on human skeletal muscle growth and development remain largely uncharacterised. Myogenic cultures were isolated from the skeletal muscle of young and elderly subjects. Myoblasts were differentiated for 8 d, with or without the addition of recombinant cytokines (rIL-15, rTNFα) and an IL-15 receptor neutralising antibody. Although myotubes were 19% thinner in cultures derived from elderly subjects, rIL-15 increased the thickness of myotubes (MTT) from both age groups to a similar extent. Neutralisation of the high-affinity IL-15 receptor binding subunit, IL-15rα in elderly myotubes confirmed that autocrine concentrations of IL-15 also support myogenesis. Co-incubation of differentiating myoblasts with rIL-15 and rTNFα, limited the reduction in MTT and nuclear fusion index (NFI) associated with rTNFα stimulation alone. IL-15rα neutralisation and rTNFα decreased MTT and NFI further. This, coupled with our observation that myotubes secrete IL-15 in response to TNFα stimulation supports the notion that IL-15 serves to mitigate inflammatory skeletal muscle loss. IL-15 may be an effective therapeutic target for the attenuation of inflammation-mediated skeletal muscle atrophy.
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In vitro, IL-15 has an anabolic effect by inducing myosin chain synthesis in myotubes, notably in response to TNF-α stimulation.
“In vitro, IL-15 has an anabolic effect by inducing myosin chain synthesis in myotubes [52], notably in response to TNF-α stimulation [53].”
From Main Pathogenic Mechanisms and Recent Advances in COPD Peripheral Skeletal Muscle Wasting (2023) · cites this paper as [53]
The Results section reports that IL-15 increased myosin heavy chain (MHC) protein content and that co-treatment with IL-15 partially reversed TNFα-associated myotube thinning. It does not show that IL-15 induced MHC synthesis specifically in response to TNFα; total muscle protein synthesis did not increase significantly. Page numbers were not available in our copy. (LLM, conf=0.84)
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Cites
Sarcopenia: European consensus on definition and diagnosis
Cruz-Jentoft, A. J., Baeyens, J. P., Bauer, J. M., Boirie, Y., Cederholm, T., Landi, F., Martin, F. C., Michel, J.-P., Rolland, Y., Schneider, S. M., et al. (2010) · Age and Ageing · doi:10.1093/ageing/afq034 · Cited by 11,601 · see citing works
Definition and classification of cancer cachexia: an international consensus
Fearon, K., Strasser, F., Anker, S. D., Bosaeus, I. G., Bruera, E. D., Fainsinger, R. L., Jatoi, A., Loprinzi, C. L., Macdonald, N., Mantovani, G., et al. (2011) · The Lancet Oncology · doi:10.1016/s1470-2045(10)70218-7 · Cited by 5,800 · see citing works
SUnSET, a nonradioactive method to monitor protein synthesis
Schmidt, E. K., Clavarino, G., Ceppi, M., & Pierre, P. (2009) · Nature Methods · doi:10.1038/nmeth.1314 · Cited by 1,706 · see citing works
Cloning of a T Cell Growth Factor that Interacts with the β Chain of the Interleukin-2 Receptor
Grabstein, K. H., Eisenman, J. R., Shanebeck, K. D., Rauch, C. T., Srinivasan, S., Fung, V., Beers, C., Richardson, J. S., Schoenborn, M. A., Ahdieh, M., et al. (1994) · Science · doi:10.1126/science.8178155 · Cited by 1,422 · see citing works
Human aging, muscle mass, and fiber type composition.
Evans, W. J., & Lexell, J. (1995) · The Journals of Gerontology Series A: Biological Sciences and Medical Sciences · doi:10.1093/gerona/50a.special_issue.11 · Cited by 1,308 · see citing works
Anker, S. D., Negassa, A., Coats, A. J. S., Afzal, R., Poole-Wilson, P. A., Cohn, J. N., & Yusuf, S. (2003) · The Lancet · doi:10.1016/s0140-6736(03)12892-9 · Cited by 725 · see citing works
Skeletal muscle loss: cachexia, sarcopenia, and inactivity
Evans, W. J. (2010) · American Journal of Clinical Nutrition · doi:10.3945/ajcn.2010.28608a · Cited by 724 · see citing works
Lim, S., Kim, J. H., Yoon, J. W., Kang, S. M., Choi, S. H., Park, Y. J., Kim, K. W., Lim, J. Y., Park, K. S., & Jang, H. C. (2010) · Diabetes Care · doi:10.2337/dc10-0107 · Cited by 588 · see citing works
Myomaker is a membrane activator of myoblast fusion and muscle formation
Millay, D. P., O'Rourke, J. R., Sutherland, L. B., Bezprozvannaya, S., Shelton, J. M., Bassel‐Duby, R., & Olson, E. N. (2013) · Nature · doi:10.1038/nature12343 · Cited by 580 · see citing works
Satellite-cell pool size does matter: Defining the myogenic potency of aging skeletal muscle
Shefer, G., de Mark, D. P. V., Richardson, J. B., & Yablonka‐Reuveni, Z. (2006) · Developmental Biology · doi:10.1016/j.ydbio.2006.02.022 · Cited by 506 · see citing works
Lenk, K., Schuler, G. C., & Adams, V. (2010) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1007/s13539-010-0007-1 · Cited by 492 · see citing works
Bowen, T. S., Schuler, G. C., & Adams, V. (2015) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.12043 · Cited by 429 · see citing works
Jones, S. W., Hill, R. J. W., Krasney, P. A., O'Conner, B., Peirce, N. S., & Greenhaff, P. L. (2004) · The FASEB Journal · doi:10.1096/fj.03-1228fje · Cited by 404 · see citing works
Self-citationBurton, J. D., Bamford, R. N., Peters, C., Grant, A. J., Kurys, G., Goldman, C. K., Brennan, J., Roessler, E., & Waldmann, T. A. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.11.4935 · Cited by 398 · see citing works
Zanou, N., & Gailly, P. L. (2013) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-013-1330-4 · Cited by 361 · see citing works
Satellite cells in human skeletal muscle plasticity
Snijders, T., Nederveen, J. P., McKay, B. R., Joanisse, S., Verdijk, L. B., van Loon, L. J. C., & Parise, G. (2015) · Frontiers in Physiology · doi:10.3389/fphys.2015.00283 · Cited by 359 · see citing works
Distribution of different fibre types in human skeletal muscles
Lexell, J. E., Downham, D. Y., & Sjöstróm, M. (1986) · Journal of the Neurological Sciences · doi:10.1016/0022-510x(86)90009-2 · Cited by 342 · see citing works
Lutz, C. T., & Quinn, L. S. (2012) · Aging · doi:10.18632/aging.100482 · Cited by 338 · see citing works
TNF-α regulates myogenesis and muscle regeneration by activating p38 MAPK
Chen, S., Jin, B., & Li, Y.-P. (2006) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00486.2006 · Cited by 301 · see citing works
Effect of resistance training on single muscle fiber contractile function in older men
Trappe, S. W., Williamson, D., Godard, M. P., Porter, D. A., Rowden, G., & COSTILL, D. L. (2000) · Journal of Applied Physiology · doi:10.1152/jappl.2000.89.1.143 · Cited by 270 · 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
Verdijk, L. B., Jonkers, R. A., Gleeson, B. G., Beelen, M., Meijer, K., Savelberg, H. H., Wodzig, W. K., Dendale, P., & van Loon, L. J. (2009) · The American Journal of Clinical Nutrition · doi:10.3945/ajcn.2008.26626 · Cited by 253 · see citing works
Chin, S. O., Rhee, S. Y., Chon, S., Hwang, Y.-C., Jeong, I.-K., Oh, S., Ahn, K. J., Chung, H. Y., Woo, J.-T., Kim, S.-W., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0060119 · Cited by 252 · see citing works
Measuring Protein Synthesis With SUnSET: A Valid Alternative to Traditional Techniques?
Goodman, C. A., & Hornberger, T. A. (2013) · Exercise and Sport Sciences Reviews · doi:10.1097/jes.0b013e3182798a95 · Cited by 233 · see citing works
Buch, A., Carmeli, E., Boker, L. K., Marcus, Y., Shefer, G., Kis, O., Berner, Y., & Stern, N. (2016) · Experimental Gerontology · doi:10.1016/j.exger.2016.01.008 · Cited by 227 · see citing works
IL-15, a novel T cell growth factor that shares activities and receptor components with IL-2
Giri, J. G., Anderson, D. M., Kumaki, S., Park, L. S., Grabstein, K. H., & Cosman, D. J. (1995) · Journal of Leukocyte Biology · doi:10.1002/jlb.57.5.763 · Cited by 215 · see citing works
Evidence for Nervous System Degeneration with Advancing Age
Lexell, J. E. (1997) · Journal of Nutrition · doi:10.1093/jn/127.5.1011s · Cited by 199 · see citing works
Myomaker is essential for muscle regenerationPreprint
Millay, D. P., Sutherland, L. B., Bassel‐Duby, R., & Olson, E. N. (2014) · Genes & Development · doi:10.1101/gad.247205.114 · Cited by 195 · see citing works
Muscle function in elite master weightlifters
PEARSON, S. J., YOUNG, A., MACALUSO, A., DEVITO, G., NIMMO, M. A., COBBOLD, M., & HARRIDGE, S. D. R. (2002) · Medicine & Science in Sports & Exercise · doi:10.1097/00005768-200207000-00023 · Cited by 184 · 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
Wang, D., Yin, Y., Yang, Y., Lv, P.-J., Shi, Y. Q., Lu, L., & Wei, L.-B. (2014) · International Immunopharmacology · doi:10.1016/j.intimp.2014.02.002 · Cited by 176 · see citing works
The myogenic kinome: protein kinases critical to mammalian skeletal myogenesis
Knight, J. D. R., & Kothary, R. (2011) · Skeletal Muscle · doi:10.1186/2044-5040-1-29 · Cited by 159 · see citing works
Requirement of myomaker-mediated stem cell fusion for skeletal muscle hypertrophy
Goh, Q., & Millay, D. P. (2017) · eLife · doi:10.7554/elife.20007 · Cited by 157 · see citing works
Cachexia in chronic obstructive pulmonary disease: new insights and therapeutic perspective
Sanders, K. J. C., Kneppers, A. E. M., van de Bool, C., LANGEN, R. C. J., & Schols, A. M. W. J. (2015) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.12062 · Cited by 149 · see citing works
IL-15–PI3K–AKT–mTOR: A Critical Pathway in the Life Journey of Natural Killer Cells
Ali, A. K., Nandagopal, N., & Lee, S. (2015) · Frontiers in Immunology · doi:10.3389/fimmu.2015.00355 · Cited by 145 · see citing works
Protein Supplementation during Resistance-Type Exercise Training in the Elderly
Leenders, M., Verdijk, L. B., van der Hoeven, L., van Kranenburg, J. M. X., Nilwik, R., Wodzig, W. K. W. H., Senden, J. M., KEIZER, H. A., & van Loon, L. J. C. (2013) · Medicine & Science in Sports & Exercise · doi:10.1249/mss.0b013e318272fcdb · Cited by 132 · see citing works
Association between tumor necrosis factor in serum and cachexia in patients with prostate cancer.
Nakashima, J., Tachibana, M., Ueno, M., Miyajima, A., Baba, S., & Murai, M. (1998) · PubMed · Cited by 128 · see citing works
Agley, C. C., Rowlerson, A. M., Velloso, C. P., Lazarus, N. R., & Harridge, S. D. R. (2013) · Journal of Cell Science · doi:10.1242/jcs.132563 · Cited by 119 · see citing works
Myomaker, Regulated by MYOD, MYOG and miR-140-3p, Promotes Chicken Myoblast Fusion
Luo, W., Li, E., Nie, Q., & Zhang, X. (2015) · International Journal of Molecular Sciences · doi:10.3390/ijms161125946 · Cited by 113 · see citing works
Tsintzas, K., Jewell, K., Kamran, M., Laithwaite, D., Boonsong, T., Littlewood, J. J., Macdonald, I. A., & Bennett, A. J. (2006) · The Journal of Physiology · doi:10.1113/jphysiol.2006.109892 · Cited by 111 · see citing works
Self-citationTreatment of cachexia: An overview of recent developments
von Haehling, S., & Anker, S. D. (2014) · International Journal of Cardiology · doi:10.1016/j.ijcard.2014.10.026 · Cited by 93 · see citing works
TNF-alpha, soluble TNF receptor and interleukin-6 plasma levels in the general population.
Himmerich, H., Fulda, S., Linseisen, J., Seiler, H., Wolfram, G., Himmerich, S., Gedrich, K., & Pollmächer, T. (2006) · PubMed · Cited by 87 · see citing works
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 · see citing works
Pistilli, E. E., Bogdanovich, S., Garton, F. C., Yang, N., Gulbin, J. P., Conner, J. D., Anderson, B. G., Quinn, L. S., North, K. N., Ahima, R. S., et al. (2011) · Journal of Clinical Investigation · doi:10.1172/jci44945 · Cited by 83 · see citing works
Interleukin-15 responses to aging and unloading-induced skeletal muscle atrophy
Pistilli, E. E., Siu, P. M., & Alway, S. E. (2006) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00496.2006 · Cited by 80 · see citing works
Increased IL-15 production of muscle cells in polymyositis and dermatomyositis
Sugiura, T. (2002) · International Immunology · doi:10.1093/intimm/dxf062 · Cited by 73 · see citing works
Elevated plasma levels of tumor necrosis factor in chronic heart failure with cachexia
Zhao, S., & Ling-hui, Z. (1997) · International Journal of Cardiology · doi:10.1016/s0167-5273(96)02873-2 · Cited by 71 · see citing works
Distinct actions of Akt1 and Akt2 in skeletal muscle differentiation
Rotwein, P. S., & Wilson, E. M. (2009) · Journal of Cellular Physiology · doi:10.1002/jcp.21692 · Cited by 70 · see citing works
Agley, C. C., Rowlerson, A. M., Velloso, C. P., Lazarus, N. R., & Harridge, S. D. R. (2015) · Journal of Visualized Experiments · doi:10.3791/52049 · Cited by 41 · see citing works
O’Connell, G. C., & Pistilli, E. E. (2015) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2015.02.015 · Cited by 30 · see citing works
Pawlikowski, B. T., Lee, L., Zuo, J., & Kramer, R. H. (2008) · Developmental Dynamics · doi:10.1002/dvdy.21833 · Cited by 28 · see citing works
Role of IL-15 in Sepsis-Induced Skeletal Muscle Atrophy and Proteolysis
Kim, H. C., Cho, H. Y., & Hah, Y. (2012) · Tuberculosis & respiratory diseases · doi:10.4046/trd.2012.73.6.312 · Cited by 22 · see citing works
Flagged first, then by citations
1 of the 53 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Sarcopenia during COVID-19 lockdown restrictions: long-term health effects of short-term muscle loss
Kirwan, R., McCullough, D., Butler, T., de Heredia, F. P., Davies, I. G., & Stewart, C. E. (2020) · GeroScience · doi:10.1007/s11357-020-00272-3 · Cited by 331 · see citing works
Inflammation and sarcopenia: A focus on circulating inflammatory cytokines
Pan, L., Xie, W., Fu, X., Lu, W., Jin, H., Lai, J., Zhang, A., Yu, Y., Li, Y., & Xiao, W. (2021) · Experimental Gerontology · doi:10.1016/j.exger.2021.111544 · Cited by 307 · see citing works
Inflammaging: Implications in Sarcopenia
Antuña, E., Cachán-Vega, C., Bermejo-Millo, J. C., Potes, Y., Caballero, B., Vega‐Naredo, I., Coto‐Montes, A. M., & García-González, C. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232315039 · Cited by 223 · see citing works
The interplay of immunology and cachexia in infection and cancer
Baazim, H., Antonio-Herrera, L., & Bergthaler, A. (2021) · Nature reviews. Immunology · doi:10.1038/s41577-021-00624-w · Cited by 188 · see citing works
Molecular mechanisms of exercise contributing to tissue regeneration
Chen, J.-B., Zhou, R., Feng, Y., & Cheng, L. (2022) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-01233-2 · Cited by 152 · see citing works
Experimental Models of Sarcopenia: Bridging Molecular Mechanism and Therapeutic Strategy
Mankhong, S., Kim, S., Moon, S., Kwak, H., Park, D., & Kang, J. (2020) · Cells · doi:10.3390/cells9061385 · Cited by 144 · see citing works
Interplay of skeletal muscle and adipose tissue: sarcopenic obesity.
Park, M., & Choi, K. M. (2023) · Metabolism: Clinical and Experimental · doi:10.1016/j.metabol.2023.155577 · Cited by 106 · see citing works
Muscle-to-tumor crosstalk: The effect of exercise-induced myokine on cancer progression
Huang, Q., Wu, M., Wu, X., Zhang, Y., & Xia, Y. (2022) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2022.188761 · Cited by 118 · see citing works
Searching for the link between inflammaging and sarcopenia
Wang, T. (2022) · Ageing Research Reviews · doi:10.1016/j.arr.2022.101611 · Cited by 88 · see citing works
Main Pathogenic Mechanisms and Recent Advances in COPD Peripheral Skeletal Muscle Wasting
Henrot, P., Dupin, I., Schilfarth, P., Esteves, P., Blervaque, L., Zysman, M., Gouzi, F., Hayot, M., Pomiès, P., & Berger, P. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24076454 · Cited by 85 · see citing works
“In vitro, IL-15 has an anabolic effect by inducing myosin chain synthesis in myotubes [52], notably in response to TNF-α stimulation [53].”
BackgroundSarcopenic obesity: Myokines as potential diagnostic biomarkers and therapeutic targets?
Guo, A., Li, K., & Xiao, Q. (2020) · Experimental Gerontology · doi:10.1016/j.exger.2020.111022 · Cited by 83 · see citing works
Álvarez, Á. M., DeOcesano-Pereira, C., Teixeira, C., & Moreira, V. (2020) · Cells · doi:10.3390/cells9092005 · Cited by 78 · see citing works
Cell Types Used for Cultured Meat Production and the Importance of Myokines
Shaikh, S., Lee, E. J., Ahmad, K., Ahmad, S. S., Chun, H.-J., Lim, J. H., Lee, Y., & Choi, I. (2021) · Foods · doi:10.3390/foods10102318 · Cited by 77 · see citing works
O’Leary, M. F., Wallace, G. R., Davis, E. T., Murphy, D. P., Nicholson, T. A., Bennett, A. J., Tsintzas, K., & Jones, S. W. (2018) · Scientific Reports · doi:10.1038/s41598-018-33840-x · Cited by 70 · see citing works
Self-citationCheng, Y., Lin, S., Cao, Z., Yu, R., Fan, Y., & Chen, J. (2025) · International Immunopharmacology · doi:10.1016/j.intimp.2025.114056 · Cited by 49 · see citing works
Sarcopenia and cachexia: molecular mechanisms and therapeutic interventions
Wang, T., Zhou, D., & Hong, Z. (2025) · MedComm · doi:10.1002/mco2.70030 · Cited by 46 · see citing works
Vaspin promotes insulin sensitivity in elderly muscle and is upregulated in obesity
Nicholson, T. A., Church, C., Tsintzas, K., Jones, R., Breen, L., Davis, E. T., Baker, D. J., & Jones, S. W. (2019) · Journal of Endocrinology · doi:10.1530/joe-18-0528 · Cited by 43 · see citing works
Self-citationMuscle–Brain crosstalk in cognitive impairment
Han, X., Ashraf, M., Tipparaju, S. M., & Xuan, W. (2023) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2023.1221653 · Cited by 40 · see citing works
Wilhelmsen, A., Tsintzas, K., & Jones, S. W. (2021) · GeroScience · doi:10.1007/s11357-021-00322-4 · Cited by 39 · see citing works
Self-citationEnergy metabolism and frailty: The potential role of exercise-induced myokines – A narrative review
Barros, D. G. M., Marques, E. A., Magalhães, J., & Carvalho, J. (2022) · Ageing Research Reviews · doi:10.1016/j.arr.2022.101780 · Cited by 36 · see citing works
Murphy, D. P., Nicholson, T. A., Jones, S. W., & O’Leary, M. F. (2019) · Wellcome Open Research · doi:10.12688/wellcomeopenres.15055.1 · Cited by 33 · see citing works
Self-citationHingorjo, M. R., Zehra, S., Saleem, S., & Qureshi, M. A. (2018) · Pakistan Journal of Medical Sciences · doi:10.12669/pjms.345.15516 · Cited by 29 · see citing works
Oxidative Stress, Inflammation and Connexin Hemichannels in Muscular Dystrophies
González‐Jamett, A. M., Vásquez, W., Cifuentes-Riveros, G., Martínez-Pando, R., Sáez, J. C., & Cárdenas, A. M. (2022) · Biomedicines · doi:10.3390/biomedicines10020507 · Cited by 29 · see citing works
Sarcopenia and COVID-19 Outcomes
Wang, Y., Tan, S., Yan, Q., & Gao, Y. H. (2023) · Clinical Interventions in Aging · doi:10.2147/cia.s398386 · Cited by 29 · see citing works
Talotta, R., Porrello, I., Restuccia, R., & Magaudda, L. (2021) · Clinical Rheumatology · doi:10.1007/s10067-021-05954-7 · Cited by 28 · see citing works
Xenos, D., Mancinetti, F., Mecocci, P., & Boccardi, V. (2025) · Ageing Research Reviews · doi:10.1016/j.arr.2025.102955 · Cited by 25 · see citing works
Amato, C. M., & Yao, H. H. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2103856118 · Cited by 25 · see citing works
Catitti, G., Bellis, D. D., Vespa, S., Simeone, P., Canonico, B., & Lanuti, P. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232214098 · Cited by 26 · see citing works
Liang, Z., & Zhang, L. (2026) · Frontiers in Pharmacology · doi:10.3389/fphar.2026.1733798 · Cited by 26 · see citing works
Cytokines and inflammatory mediators as promising markers of polymyositis/dermatomyositis
Cerezo, L. A., Vencovský, J., & Šenolt, L. (2020) · Current Opinion in Rheumatology · doi:10.1097/bor.0000000000000744 · Cited by 24 · see citing works
Myokines in Appetite Control and Energy Balance
Grannell, A., Kokkinos, A. D., & le Roux, C. W. (2022) · Muscles · doi:10.3390/muscles1010003 · Cited by 23 · see citing works
Wang, J., Xiang, Y., Wu, L., Zhang, C., Han, B., Cheng, Y., Tong, Y., Yan, D., & Wang, L. (2024) · European Journal of Clinical Nutrition · doi:10.1038/s41430-024-01486-w · Cited by 22 · see citing works
Visuthranukul, C., Leelahavanichkul, A., Tepaamorndech, S., Chamni, S., Mekangkul, E., & Chomtho, S. (2024) · Scientific Reports · doi:10.1038/s41598-024-61781-1 · Cited by 22 · see citing works
Satellite cell function, intramuscular inflammation and exercise in chronic kidney disease
O’Sullivan, T. F., Smith, A. C., & Watson, E. L. (2018) · Clinical Kidney Journal · doi:10.1093/ckj/sfy052 · Cited by 22 · see citing works
Webster, J. M., Sagmeister, M. S., Fenton, C. G., Seabright, A. P., Lai, Y., Jones, S. W., Filer, A. D., Cooper, M. S., Lavery, G. G., Raza, K., et al. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22157828 · Cited by 19 · see citing works
Self-citationPark, S., Park, G., Oh, S., Park, Y., Kim, Y., Kim, J., & Choi, J. (2023) · Scientific Reports · doi:10.1038/s41598-023-40800-7 · Cited by 19 · see citing works
Pinto, A. C., Tavares, P., Neves, B. M., Oliveira, P. F., Vitorino, R. M. P., Moreira‐Gonçalves, D., & Ferreira, R. M. (2024) · Journal of Molecular Medicine · doi:10.1007/s00109-024-02427-7 · Cited by 18 · see citing works
Wilhelmsen, A., Stephens, F. B., Bennett, A. J., Karagounis, L. G., Jones, S. W., & Tsintzas, K. (2023) · GeroScience · doi:10.1007/s11357-023-00956-6 · Cited by 17 · see citing works
Self-citationShen, L., Zong, Y., Zhao, J., Yang, Y., Li, L., Li, N., Gao, Y., Xie, X., Bao, Q., Jiang, L., et al. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1414387 · Cited by 17 · see citing works
Antioxidants Facilitate High–intensity Exercise IL–15 Expression in Skeletal Muscle
Pérez‐López, A., Martín-Rincón, M., Santana, A., Pérez-Suárez, I., Dorado, C., Calbet, J. A. L., & Morales‐Álamo, D. (2018) · International Journal of Sports Medicine · doi:10.1055/a-0781-2527 · Cited by 17 · see citing works
Different roles of circulating and intramuscular GDF15 as markers of skeletal muscle health
Chiariello, A., Conte, G., Rossetti, L. M., Trofarello, L., Salvioli, S., & Conte, M. (2024) · Frontiers in Endocrinology · doi:10.3389/fendo.2024.1404047 · Cited by 17 · see citing works
Alcalde‐Estévez, E., Moreno-Piedra, A., Asenjo‐Bueno, A., Martos-Elvira, M., de la Serna-Soto, M., Ruiz‐Ortega, M., Olmos, G., López‐Ongil, S., & Ruiz‐Torres, M. P. (2025) · Life Sciences · doi:10.1016/j.lfs.2025.123507 · Cited by 15 · see citing works
The inflammatory response, a mixed blessing for muscle homeostasis and plasticity
Bouredji, Z., Argaw, A., & Frenette, J. (2022) · Frontiers in Physiology · doi:10.3389/fphys.2022.1032450 · Cited by 17 · see citing works
Otero-Tarrazón, A., Perelló-Amorós, M., Jorge-Pedraza, V., Moshayedi, F., Sánchez-Moya, A., García-Pérez, I., Fernández‐Borràs, J., de la serrana, D. G., Navarro, I., Blasco, J., et al. (2023) · Frontiers in Endocrinology · doi:10.3389/fendo.2023.1101356 · Cited by 15 · see citing works
Han, L., Li, P., He, Q., Yang, C. G., Jiang, M., Wang, Y., Cao, Y., Han, X., Liu, X., & Wu, W. (2023) · Aging and Disease · doi:10.14336/ad.2023.1125 · Cited by 16 · see citing works
Kerr, A., Hart, L. M., Davis, H., Wall, A. M., Lacey, S., Franklyn‐Miller, A., Khaldi, N., & Keogh, B. (2023) · Nutrients · doi:10.3390/nu15040986 · Cited by 13 · see citing works
Hormonal, immune, and oxidative stress responses to blood flow‐restricted exercise
Hjortshoej, M. H., Aagaard, P., Storgaard, C. D., Juneja, H., Lundbye‐Jensen, J., Magnusson, S. P., & Couppé, C. (2023) · Acta Physiologica · doi:10.1111/apha.14030 · Cited by 13 · see citing works
Sharma, A. R., Chatterjee, S., Lee, Y., & Lee, S. (2023) · Aging and Disease · doi:10.14336/ad.2023.00903 · Cited by 15 · see citing works
Rients, E. L., Deters, E. L., McGill, J. L., Belknap, C. R., & Hansen, S. L. (2023) · Journal of Animal Science · doi:10.1093/jas/skac311 · Cited by 13 · see citing works
The dichotomic role of cytokines in aging
Silva, R. C. M. C. (2024) · Biogerontology · doi:10.1007/s10522-024-10152-4 · Cited by 14 · see citing works
Molecular Fingerprint of BMD Patients Lacking a Portion in the Rod Domain of Dystrophin
Capitanio, D., Moriggi, M., Barbacini, P., Torretta, E., Moroni, I., Blàsevich, F., Morandi, L. O., Mora, M., & Gelfi, C. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23052624 · Cited by 12 · see citing works
Exhausted PD-1+ TOX+ CD8+ T Cells Arise Only in Long-Term Experimental Trypanosoma cruzi Infection
Gálvez, R. I., & Jacobs, T. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.866179 · Cited by 11 · see citing works
Yoshida, S., Fujimoto, T., Takahashi, T., Sugimoto, K., Akasaka, H., Tanaka, M., Huang, Y., Yasunobe, Y., Xie, K., Ohnishi, Y., et al. (2022) · Experimental Physiology · doi:10.1113/ep090205 · Cited by 11 · see citing works
Clostridium perfringens α-toxin inhibits myogenic differentiation of C2C12 myoblasts
Takehara, M., Kobayashi, K., & Nagahama, M. (2020) · Anaerobe · doi:10.1016/j.anaerobe.2020.102265 · Cited by 9 · see citing works
Hodson, N. W., Dent, J. R., Song, Z., O’Leary, M. F., Nicholson, T. A., Jones, S. W., Murray, J. T., Jeromson, S., Hamilton, D. L., Breen, L., et al. (2020) · Experimental Physiology · doi:10.1113/ep088805 · Cited by 9 · see citing works
Self-citationModelling Skeletal Muscle Ageing and Repair In Vitro
Tarum, J., Degens, H., Turner, M. D., Stewart, C. E., Sale, C., & Santos, L. (2023) · Journal of Tissue Engineering and Regenerative Medicine · doi:10.1155/2023/9802235 · Cited by 8 · see citing works
Berciano, M. T., Gatius, A., Puente-Bedia, A., Rufino-Gómez, A., Tarabal, O., Rodríguez-Rey, J. C., Calderó, J., Lafarga, M., & Tapia, O. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms252212415 · Cited by 8 · see citing works
Immunosenescence in skeletal muscle: The role-play in cancer cachexia chessboard
Giovarelli, M., Mocciaro, E., Carnovale, C., Cervia, D., Perrotta, C., & Clementi, E. (2025) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2025.02.012 · Cited by 8 · see citing works
Lin, S., Cheng, Y., Cui, T., Yang, F., Yang, S., & Fan, Y. (2025) · Inflammation · doi:10.1007/s10753-025-02274-9 · Cited by 7 · see citing works
Cordingley, D. M., Anderson, J. E., & Cornish, S. M. (2024) · Muscles · doi:10.3390/muscles3030018 · Cited by 6 · see citing works
Wilhelmsen, A., Karagounis, L. G., Bennett, A. J., D'Amico, D. F., Fouassier, A. M., Jones, S. W., & Tsintzas, K. (2025) · Nutrition & Metabolism · doi:10.1186/s12986-025-00909-0 · Cited by 6 · see citing works
Self-citationRosqvist, F., Cedernaes, J., Mora, A. M., Fridén, M., Johansson, H.-E., Iggman, D., Larsson, A. O., Ahlström, H. K., Kullberg, J., & Risérus, U. (2024) · American Journal of Clinical Nutrition · doi:10.1016/j.ajcnut.2024.04.010 · Cited by 4 · see citing works
Park, G., Park, S., Oh, S., Choi, N., & Choi, J. (2023) · Journal of Animal Science and Technology · doi:10.5187/jast.2023.e130 · Cited by 3 · see citing works
Myokines Produced by Cultured Bovine Satellite Cells Harvested from 3- and 11-Month-Old Angus Steers
Shira, K. A., Murdoch, B. M., Thornton, K. J., Reichhardt, C. C., Becker, G. M., Chibisa, G. E., & Murdoch, G. K. (2024) · Animals · doi:10.3390/ani14050709 · Cited by 3 · see citing works
Lin, S., Cheng, Y., Chen, X., Yang, F., Fan, Y., & Yang, S. (2025) · Food Science & Nutrition · doi:10.1002/fsn3.70166 · Cited by 3 · see citing works
Lugtmeijer, C., Bowtell, J. L., & O’Leary, M. F. (2024) · Nutrients · doi:10.3390/nu16142291 · Cited by 2 · see citing works
Self-citationWelch, C., Acharjee, A., Birch, R. J., de Magalhães, J. P., Duggal, N. A., Hainsworth, A. J., Hombrebueno, J. R., Jones, S. W., Lewis, J., Mazaheri, A., et al. (2025) · BMC Geriatrics · doi:10.1186/s12877-025-06109-y · Cited by 2 · see citing works
Self-citationThe Application Value of Interleukin-10 and Interleukin-15 in Osteoporosis
Lei, T., Wang, M., Zuo, C., & Xu, H. (2021) · OALib · doi:10.4236/oalib.1107279 · Cited by 2 · see citing works
Spontaneous Alignment of Myotubes Through Myogenic Progenitor Cell Migration
Mehanna, L. E., Osborne, A. R., Peterson, C. A., & Berron, B. J. (2023) · Tissue Engineering Part A · doi:10.1089/ten.tea.2023.0177 · Cited by 1 · see citing works
Samid, M. A. A., Al‐Shanti, N., & Odeh, M. (2018) · International Conference on Cancer Care Informatics (CCI) · doi:10.1109/cancercare.2018.8618261
Interleukin-15 and creatine kinase response to high-intensity intermittent exercise training
dos Santos, T., Lira, F. S., & Antunes, B. M. (2020) · Sport Sciences for Health · doi:10.1007/s11332-020-00629-3
Deng, G., Zhu, D., Song, H., Du, Z., Xue, Y., Song, H., & Li, Y. (2023) · Research Square · doi:10.21203/rs.3.rs-3540222/v1
Shen, L., Zong, Y., Zhao, J., Yang, Y., Li, L., Li, N., Gao, Y., Xie, X., Bao, Q., Jiang, L., et al. (2024) · medRxiv · doi:10.1101/2024.02.23.24303270
Improving efficiency in the feedlot industry
Rients, E. L. (2022) · doi:10.31274/td-20240329-414
Chronic Low-Grade Inflammation and Sarcopenia
王, 锐. (2024) · Advances in Clinical Medicine · doi:10.12677/acm.2024.1461784
Improvement of cellular pattern organization and clarity through centrifugal force
Mehanna, L. E., Boyd, J. D., Remus-Williams, S., Racca, N. M., Spraggins, D. P., Grady, M. E., & Berron, B. J. (2025) · Biomedical Materials · doi:10.1088/1748-605x/ada508
Transient expression of human interleukin-15 in Nicotiana benthamiana
Mukai, Y., Taguchi, Y., & Matsuo, K. (2025) · Plant Biotechnology · doi:10.5511/plantbiotechnology.25.0711a
Humińska‐Lisowska, K., Bicakci, B., Michałowska‐Sawczyn, M., Aschenbrenner, P., September, A. V., Proia, P., & Leońska‐Duniec, A. (2025) · medRxiv · doi:10.1101/2025.11.05.25339580
A Novel Mouse Model to Identify Antigen-Specific Immune Responses in Pancreatic Cancer Cachexia
Das, A., Mukherjee, D., D’Alesio, L., Wedig, J., Lathrop, H., Schmidt, M., Guenther, A., Kaiser, M., Varghese, J., Remaily, B., et al. (2026) · Cancers · doi:10.3390/cancers18040587
Key hormones for the control of muscle mass: Myokines
Gu, H., Albrecht, E., Deng, Z., & Maak, S. (2026) · Best Practice & Research Clinical Endocrinology & Metabolism · doi:10.1016/j.beem.2026.102115
Sukocheva, O. A., Harding, D., Ow, T., & Tse, E. (2026) · Biomedicines · doi:10.3390/biomedicines14092082
The Myokine Landscape: Sources, Signaling, and Context-Dependent Actions
Casadevall, C., Ramírez-Sarmiento, A., Camps-Ubach, R., Barreiro, E., Orozco‐Levi, M., & Gea, J. (2026) · Cells · doi:10.3390/cells15181682
Lee, E. J., Ahmad, K., Shaikh, S., Lim, J. H., Ahmad, S. S., Seo, M., & Choi, I. (2026) · Food Science of Animal Resources · doi:10.1007/s44463-026-00108-2
Tambaro, F., Imbimbo, G., Coletti, D., TULLIO, R. D., Belloni, E., Nigri, G. R., Costelli, P., Muscaritoli, M., & Molfino, A. (2026) · Frontiers in Nutrition · doi:10.3389/fnut.2026.1937525
Skorkina, M., Bobylev, A. G., Belova, D., Bravyy, Y. R., Mutig, K., & Lebedeva, S. A. (2026) · Biomolecules · doi:10.3390/biom16101536
- Authors
- O’Leary, M. F., Wallace, G. R., Bennett, A. J., Tsintzas, K., & Jones, S. W.
- Affiliations
- University of Birmingham (GB)
- University of Nottingham (GB)
- Corresponding author
- Tsintzas, Kostas
- Jones, Simon W.
- Venue
- Scientific Reports
- Published
- 2017-10-11
- Volume
- 7
- Issue
- 1
- Pages
- 12997-12997
- ISSN
- 2045-2322 (ISSN-L)
- PMC
- PMC5636823
- OpenAlex
- W2762734331
- Cited by
- 85
- References
- 53
- Citations by year
- 2026: 8 · 2025: 12 · 2024: 13 · 2023: 16 · 2022: 13 · 2021: 8 · 2020: 8 · 2019: 2 · 2018: 5
- FWCI
- 1.68
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Scientific Reports (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Open Research Exeter (University of Exeter) (submittedVersion, cc-by)
- University of Birmingham Research Portal (University of Birmingham) (submittedVersion, cc-by)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Nottingham ePrints (University of Nottingham) (submittedVersion, cc-by)
- Figshare (submittedVersion, cc-by)
- Repository@Nottingham (University of Nottingham) (submittedVersion, cc-by)
- Funders
- Wellcome Trust
- Medical Research Council (MR/K00414X/1, MR/P021220/1)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Health Sciences › Medicine › Physiology › Nutrition and Health in Aging
- Health Sciences › Medicine › Rehabilitation › Exercise and Physiological Responses
- Keywords
- IL-15, myogenesis, TNF-α, skeletal muscle atrophy, sarcopenia, cachexia, IL-15 receptor alpha, inflammation, aging
- MeSH terms
- Aged, Aging, Cell Differentiation, Cells, Cultured, Female, Humans, Male, Recombinant Proteins, Tumor Necrosis Factor-alpha, Muscle Fibers, Skeletal, Gene Expression Regulation, Developmental, Interleukin-15, Muscle Development, Antibodies, Neutralizing
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