The DOI matches its Crossref record; 44 of the 44 references it cites were found in a registry or an index.
IL-15 Overexpression Promotes Endurance, Oxidative Energy Metabolism, and Muscle PPARδ, SIRT1, PGC-1α, and PGC-1β Expression in Male Mice
Open accessAbstract
Endurance exercise initiates a pattern of gene expression that promotes fat oxidation, which in turn improves endurance, body composition, and insulin sensitivity. The signals from exercise that initiate these pathways have not been completely characterized. IL-15 is a cytokine that is up-regulated in skeletal muscle after exercise and correlates with leanness and insulin sensitivity. To determine whether IL-15 can induce any of the metabolic adaptations associated with exercise, substrate metabolism, endurance, and molecular expression patterns were examined in male transgenic mice with constitutively elevated muscle and circulating IL-15 levels. IL-15 transgenic mice ran twice as long as littermate control mice in a run-to-exhaustion trial and preferentially used fat for energy metabolism. Fast muscles in IL-15 transgenic mice exhibited high expression of intracellular mediators of oxidative metabolism that are induced by exercise, including sirtuin 1, peroxisome proliferator-activated receptor (PPAR)-δ, PPAR-γ coactivator-1α, and PPAR-γ coactivator-1β. Muscle tissue in IL-15 transgenic mice exhibited myosin heavy chain and troponin I mRNA isoform expression patterns indicative of a more oxidative phenotype than controls. These findings support a role for IL-15 in induction of exercise endurance, oxidative metabolism, and skeletal muscle molecular adaptations induced by physical training.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“and augments PPARδ and PGC-1α activity, favoring mitochondrial biogenesis and FAO [84,91,126]”
From The Role of Exercise in the Interplay between Myokines, Hepatokines, Osteokines, Adipokines, and Modulation of Inflammation for Energy Substrate Redistribution and Fat Mass Loss: A Review (2020) · cites this paper as [91]
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“Exercise-inducible myokines, such as irisin [62,63], IL-6 [76,77], IL-15 [91,126], BAIBA [111], and METRNL [100], as well as the osteokine OCN [71] have been shown to directly stimulate oxidative metabolism in autocrine and endocrine ways, respectively (1).”
From The Role of Exercise in the Interplay between Myokines, Hepatokines, Osteokines, Adipokines, and Modulation of Inflammation for Energy Substrate Redistribution and Fat Mass Loss: A Review (2020) · cites this paper as [91]
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“It has been suggested to be an important modulator of body fat mass, which also actively participates in the innate immune response, playing an important role in the development and function of natural killer (NK) cells and lymphocytes (Quinn et al., 2013).”
From Physical Exercise-Induced Myokines and Muscle-Adipose Tissue Crosstalk: A Review of Current Knowledge and the Implications for Health and Metabolic Diseases (2018) · cites this paper as Quinn et al., 2013
Experimental — accuracy not yet measuredThe cited source says what the claim attributes to it.
In the citing paper
“In addition, IL-15 is directly related to muscle metabolism, or even diet-induced obesity and insulin sensitivity (Quinn et al., 2011, 2013).”
From Physical Exercise-Induced Myokines and Muscle-Adipose Tissue Crosstalk: A Review of Current Knowledge and the Implications for Health and Metabolic Diseases (2018) · cites this paper as Quinn et al., 2013
The cited source says what the claim attributes to it.
In the citing paper
“Another IL expressed by SkM with an important metabolic role is IL-15.”
From Physical Exercise-Induced Myokines and Muscle-Adipose Tissue Crosstalk: A Review of Current Knowledge and the Implications for Health and Metabolic Diseases (2018) · cites this paper as Quinn et al., 2013
The cited source says what the claim attributes to it.
In the citing paper
“The concentration of circulating IL-15 was shown to be closely related to physical exercise, in addition to increasing lipid oxidation and gene expression of peroxisome proliferator-activated receptor delta (PPARδ) in rodents when they were treated with the cytokine (Quinn et al., 2013).”
From Physical Exercise-Induced Myokines and Muscle-Adipose Tissue Crosstalk: A Review of Current Knowledge and the Implications for Health and Metabolic Diseases (2018) · cites this paper as Quinn et al., 2013
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
1 retracted
Safdar, A., Little, J. P., Stokl, A., Hettinga, B. P., Akhtar, M., & Tarnopolsky, M. A. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.211466 · Cited by 321
RetractedAnalyzing real-time PCR data by the comparative CT method
Schmittgen, T. D., & Livak, K. J. (2008) · Nature Protocols · doi:10.1038/nprot.2008.73 · Cited by 26,190
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
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
PRDM16 controls a brown fat/skeletal muscle switch
Seale, P., Bjork, B., Yang, W., Kajimura, S., Chin, S., Kuang, S., Scimè, A., Devarakonda, S., Conroe, H. M., Erdjument-Bromage, H., et al. (2008) · Nature · doi:10.1038/nature07182 · Cited by 2,347
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
PGC-1α: a key regulator of energy metabolism
Liang, H., & Ward, W. F. (2006) · AJP Advances in Physiology Education · doi:10.1152/advan.00052.2006 · Cited by 1,291
Regulation of Muscle Fiber Type and Running Endurance by PPARδ
Wang, Y.-X., Zhang, C.-L., Yu, R. T., Cho, H. K., Nelson, M. C., Bayuga-Ocampo, C. R., Ham, J., Kang, H., & Evans, R. M. (2004) · PLoS Biology · doi:10.1371/journal.pbio.0020294 · Cited by 1,089
Interleukin 15: biology and relevance to human disease
Fehniger, T. A., & Caligiuri, M. A. (2001) · Blood · doi:10.1182/blood.v97.1.14 · Cited by 976
Tanaka, T., Yamamoto, J., Iwasaki, S., Asaba, H., Hamura, H., Ikeda, Y., Watanabe, M., Magoori, K., Ioka, R. X., Tachibana, K., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0306981100 · Cited by 832
Flagged first, then by citations
Cited by
Sorted by citations
Kalinkovich, A., & Livshits, G. (2017) · Ageing Research Reviews · doi:10.1016/j.arr.2016.09.008 · Cited by 882
Li, X., Fang, P., Mai, J., Choi, E. T., Wang, H., & Yang, X. (2013) · Journal of Hematology & Oncology · doi:10.1186/1756-8722-6-19 · Cited by 860
Role of Myokines in Regulating Skeletal Muscle Mass and Function
Lee, J. H., & Jun, H.-S. (2019) · Frontiers in Physiology · doi:10.3389/fphys.2019.00042 · Cited by 432
Skeletal Muscle as an Endocrine Organ: The Role of Myokines in Exercise Adaptations
Hoffmann, C., & Weigert, C. (2017) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a029793 · Cited by 393
Leal, L. G., Lopes, M. A., & Batista, M. L. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.01307 · Cited by 382
Adipo-myokines: two sides of the same coin–mediators of inflammation and mediators of exercise
Raschke, S., & Eckel, J. (2013) · Mediators of Inflammation · doi:10.1155/2013/320724 · Cited by 296
Gonzalez-Gil, A. M., & Elizondo-Montemayor, L. (2020) · Nutrients · doi:10.3390/nu12061899 · Cited by 278
The influence of skeletal muscle on systemic aging and lifespan
Demontis, F., Piccirillo, R., Goldberg, A. L., & Perrimon, N. (2013) · Aging Cell · doi:10.1111/acel.12126 · Cited by 238
Exercise-Released Myokines in the Control of Energy Metabolism
Laurens, C., Bergouignan, A., & Moro, C. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.00091 · Cited by 159
Myostatin and its Regulation: A Comprehensive Review of Myostatin Inhibiting Strategies
Baig, M. H., Ahmad, K., Moon, J. S., Park, S.-Y., Ho Lim, J., Chun, H. J., Qadri, A. F., Hwang, Y. C., Jan, A. T., Ahmad, S. S., et al. (2022) · Frontiers in Physiology · doi:10.3389/fphys.2022.876078 · Cited by 135
Central Nervous System Delivery of Intranasal Insulin: Mechanisms of Uptake and Effects on Cognition
Salameh, T. S., Bullock, K. M., Hujoel, I. A., Niehoff, M. L., Wolden‐Hanson, T., Kim, J., Morley, J. E., Farr, S. A., & Banks, W. A. (2015) · Journal of Alzheimer s Disease · doi:10.3233/jad-150307 · Cited by 136
Mechanisms by Which Skeletal Muscle Myokines Ameliorate Insulin Resistance
Balakrishnan, R., & Thurmond, D. C. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23094636 · Cited by 143
Exercise-induced myokines and their effect on prostate cancer
Kim, J., Galvao, D. A., Newton, R. U., Gray, E. S., & Taaffe, D. R. (2021) · Nature Reviews Urology · doi:10.1038/s41585-021-00476-y · Cited by 131
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
Rowe, G. C., Safdar, A., & Arany, Z. P. (2014) · Circulation · doi:10.1161/circulationaha.113.001590 · Cited by 107
Endurance training enhances skeletal muscle interleukin-15 in human male subjects
Rinnov, A., Yfanti, C., Nielsen, S., Åkerström, T. C. A., Peijs, L., Zankari, A., Fischer, C. P., & Pedersen, B. K. (2014) · Endocrine · doi:10.1007/s12020-013-9969-z · Cited by 103
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
Shi, H., Munk, A., Nielsen, T. S., Daughtry, M. R., Larsson, L., Li, S., Høyer, K. F., Geisler, H. W., Sulek, K., Kjøbsted, R., et al. (2018) · Molecular Metabolism · doi:10.1016/j.molmet.2018.02.010 · Cited by 87
Myf6/MRF4 is a myogenic niche regulator required for the maintenance of the muscle stem cell pool
Lazure, F., Blackburn, D. M., Karam, N., Sahinyan, K., Sharanek, A., Nguyen, D., Corchado, A. H., Lepper, C., Najafabadi, H. S., Perkins, T. J., et al. (2020) · EMBO Reports · doi:10.15252/embr.201949499 · Cited by 84
Research progress of interleukin-15 in cancer immunotherapy
Cai, M., Huang, X., Huang, X., Ju, D., Zhu, Y. Z., & Li, Y. (2023) · Frontiers in Pharmacology · doi:10.3389/fphar.2023.1184703 · Cited by 83
Interleukin-15 as a myokine: Mechanistic insight into its effect on skeletal muscle metabolism
Nadeau, L., & Aguer, C. (2019) · Applied Physiology Nutrition and Metabolism · doi:10.1139/apnm-2018-0022 · Cited by 83
Ye, J. (2015) · Frontiers of Medicine · doi:10.1007/s11684-015-0377-z · Cited by 66
Cellular Metabolism on T-Cell Development and Function
Chen, H., Yang, T., Zhu, L., & Zhao, Y. X. (2014) · International Reviews of Immunology · doi:10.3109/08830185.2014.902452 · Cited by 68
Myokines: a descriptive review
Barbalho, S. M., Neto, E. V. P., Goulart, R. D. Á., Bechara, M. D., Chagas, E. F. B., Audi, M., Campos, L. M. G., Guiguer, É. L., Buchaim, R. L., Buchaim, D. V., et al. (2020) · The Journal of Sports Medicine and Physical Fitness · doi:10.23736/s0022-4707.20.10884-3 · Cited by 73
Shamsi, M. M., Chekachak, S., Soudi, S., Quinn, L. S., Ranjbar, K., Chenari, J., Yazdi, M. H., & Mahdavi, M. (2016) · Cytokine · doi:10.1016/j.cyto.2016.11.005 · Cited by 63
Exercise tolls the bell for key mediators of low-grade inflammation in dysmetabolic conditions
Guardia, L. D., & Codella, R. (2021) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2021.09.003 · Cited by 68
Nadeau, L., Patten, D. A., Caron, A., Garneau, L., Pinault-Masson, É., Foretz, M., Haddad, P., Anderson, B. G., Quinn, L. S., Jardine, K. E., et al. (2018) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2018.10.021 · Cited by 62
Bohlen, J. F., McLaughlin, S. L., Hazard-Jenkins, H. W., Infante, A. M., Montgomery, C., Davis, M. C., & Pistilli, E. E. (2018) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.12294 · Cited by 56
Quinn, K. M., Hussain, T., Kraus, F., Formosa, L. E., Lam, W. K., Dagley, M. J., Saunders, E. C., Assmus, L. M., Wynne-Jones, E., Loh, L., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-16633-7 · Cited by 56
Redirecting drug repositioning to discover innovative cosmeceuticals
Sotiropoulou, G., Zingkou, E., & Pampalakis, G. (2021) · Experimental Dermatology · doi:10.1111/exd.14299 · Cited by 53
Protective effect of myokine IL-15 against H2O2-mediated oxidative stress in skeletal muscle cells
Li, F., Li, Y., Tang, Y., Lin, B., Kong, X., Oladele, O. A., & Yin, Y. (2014) · Molecular Biology Reports · doi:10.1007/s11033-014-3665-9 · Cited by 48
Lacraz, G., Rakotoarivelo, V., Labbé, S. M., Vernier, M., Noll, C., Mayhue, M., Staňková, J., Schwertani, A. G., Grenier, G., Carpentier, A. C., et al. (2016) · PLoS ONE · doi:10.1371/journal.pone.0162995 · Cited by 47
Interleukin‐15 in obesity and metabolic dysfunction: current understanding and future perspectives
Duan, Y., Li, F., Wang, W., Guo, Q., Wen, C., Li, Y., & Yin, Y. (2017) · Obesity Reviews · doi:10.1111/obr.12567 · Cited by 47
Shamsi, M. M., Chekachak, S., Soudi, S., Gharakhanlou, R., Quinn, L. S., Ranjbar, K., Rezaei, S., Shirazi, F. J., Allahmoradi, B., Yazdi, M. H., et al. (2018) · Nutrition · doi:10.1016/j.nut.2018.05.022 · Cited by 47
Kim, O. Y., Chung, J. Y., & Song, J. (2019) · Pharmacological Research · doi:10.1016/j.phrs.2019.104411 · Cited by 48
Sun, H., & Liu, D. (2015) · Gene Therapy · doi:10.1038/gt.2014.114 · Cited by 43
Zamboni, M. M., Mazzali, G., Brunelli, A., Saatchi, T., Urbani, S., Giani, A., Rossi, A. P., Zoico, E., & Fantin, F. (2022) · Cells · doi:10.3390/cells11213361 · Cited by 47
Conner, J. D., Wolden‐Hanson, T., & Quinn, L. S. (2014) · Journal of Visualized Experiments · doi:10.3791/51846 · Cited by 43
Mitochondria Homeostasis and Oxidant/Antioxidant Balance in Skeletal Muscle—Do Myokines Play a Role?
Pang, B. P. S., Chan, W. S., & Chan, C. B. (2021) · Antioxidants · doi:10.3390/antiox10020179 · Cited by 43
Quinn, L. S., Anderson, B. G., Conner, J. D., Wolden-Hanson, T., & Marcell, T. J. (2014) · Endocrinology · doi:10.1210/en.2013-1645 · Cited by 40
Interleukin-15 Modulates Adipose Tissue by Altering Mitochondrial Mass and Activity
Barra, N. G., Palanivel, R., Denou, E., Chew, M. V., Gillgrass, A. E., Walker, T. D., Kong, J., Richards, C. D., Jordana, M., Collins, S. M., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0114799 · Cited by 40
Energy 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 41
Mitochondrial Metabolism in T-Cell Exhaustion
Li, F., Yu, F., Yin, Z., & Wang, Y. J. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26157400 · Cited by 42
Mechanisms governing the health and performance benefits of exercise
Bishop‐Bailey, D. (2013) · British Journal of Pharmacology · doi:10.1111/bph.12399 · Cited by 40
Exploring exercise-driven exerkines: unraveling the regulation of metabolism and inflammation
Zhou, N., Gong, L., Zhang, E., & Wang, X. (2024) · PeerJ · doi:10.7717/peerj.17267 · Cited by 35
Bevilacqua, A., Franco, F., Lu, Y.-T., Rahiman, N., Kao, K., Chuang, Y., Zhu, Y., Held, W., Xie, X., Gunsalus, K. C., et al. (2024) · Science Immunology · doi:10.1126/sciimmunol.adn2717 · Cited by 33
Cheng, M., Zhu, J., Ren, T., & Zhou, M. (2016) · Drug Design Development and Therapy · doi:10.2147/dddt.s102883 · Cited by 33
Hypothalamus-skeletal muscle crosstalk during exercise and its role in metabolism modulation
Ibeas, K., Herrero, L., Mera, P., & Serra, D. (2021) · Biochemical Pharmacology · doi:10.1016/j.bcp.2021.114640 · Cited by 39
IL-15Rα is a determinant of muscle fuel utilization, and its loss protects against obesity
Loro, E., Seifert, E. L., Moffat, C., Romero, F., Mishra, M. K., Sun, Z., Krajacic, P., Anokye‐Danso, F., Summer, R. S., Ahima, R. S., et al. (2015) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00505.2014 · Cited by 32
Thornton, S. M., Krolopp, J. E., & Abbott, M. J. (2016) · PPAR Research · doi:10.1155/2016/5465804 · Cited by 31
Nezhad, F. Y., Verbrugge, S. A. J., Schönfelder, M., Becker, L., de Angelis, M. H., & Wackerhage, H. (2019) · Frontiers in Physiology · doi:10.3389/fphys.2019.00262 · Cited by 30
O’Connell, G. C., & Pistilli, E. E. (2015) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2015.02.015 · Cited by 30
The paradox of aging: Aging-related shifts in T cell function and metabolism
Quinn, K. M., Moreno-Vicencio, D., & Gruta, N. L. L. (2023) · Seminars in Immunology · doi:10.1016/j.smim.2023.101834 · Cited by 28
Hingorjo, M. R., Zehra, S., Saleem, S., & Qureshi, M. A. (2018) · Pakistan Journal of Medical Sciences · doi:10.12669/pjms.345.15516 · Cited by 29
Skeletal muscle interleukin 15 promotes CD8+ T-cell function and autoimmune myositis
Huang, P.-L., Hou, M.-S., Wang, S.-W., Chang, C.-L., Liou, Y.-H., & Liao, N. (2015) · Skeletal Muscle · doi:10.1186/s13395-015-0058-2 · Cited by 32
Garcia, M. D. C., Pazos, P., Lima, L., & Diéguez, C. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19092569 · Cited by 27
Deloux, R., Tannous, C., Ferry, A., Li, Z., & Mericskay, M. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.01290 · Cited by 25
Yang, H., Luo, L.-J., Chen, W.-J., Zhao, L., Tang, C., Qi, Y., & Zhang, J. (2014) · Endocrine · doi:10.1007/s12020-014-0233-y · Cited by 22
Nikseresht, M., Ahmadi, M. H., Abdolhosein, T. K., Nikseresht, M., & Arent, S. M. (2021) · European Journal of Sport Science · doi:10.1080/17461391.2021.1895893 · Cited by 19
Duan, Z., Yang, Y., Qin, M., & Yi, X. (2024) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.70136 · Cited by 19
O’Connell, G. C., Guo, G., Stricker, J., Quinn, L. S., Ma, A. I., & Pistilli, E. E. (2014) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00704.2014 · Cited by 18
Circulating irisin levels and muscle FNDC5 mRNA expression are independent of IL-15 levels in mice
Quinn, L. S., Anderson, B. G., Conner, J. D., & Wolden‐Hanson, T. (2015) · Endocrine · doi:10.1007/s12020-015-0607-9 · Cited by 21
Morino, K., & Maegawa, H. (2020) · Journal of Diabetes Investigation · doi:10.1111/jdi.13359 · Cited by 18
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
Wang, J., Gu, J., Li, X., Sun, H., & Yang, X. (2026) · Pharmaceuticals · doi:10.3390/ph19071056 · Cited by 18
Histone Deacetylases as Modulators of the Crosstalk Between Skeletal Muscle and Other Organs
Renzini, A., D’Onghia, M., Coletti, D., & Moresi, V. (2022) · Frontiers in Physiology · doi:10.3389/fphys.2022.706003 · Cited by 15
Timofte, D. V., Tudor, R. C., Mocanu, V., & Labusca, L. S. (2024) · Nutrients · doi:10.3390/nu16234231 · Cited by 16
Phua, W. W. T., Tan, W., Yip, Y. S., Hew, I. D., Wee, J. W. K., Cheng, H. S., Leow, M. K., Wahli, W., & Tan, N. S. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21051747 · Cited by 15
Anderson, B. G., & Quinn, L. S. (2016) · Endocrinology · doi:10.1210/en.2015-1746 · Cited by 14
Jaworska, J., Laskowski, R., Ziemann, E., Żuczek, K., Lombardi, G., Antosiewicz, J., & Żurek, P. (2021) · Frontiers in Physiology · doi:10.3389/fphys.2021.627657 · Cited by 14
Huang, T., Chen, X., He, J., Zheng, P., Luo, Y., Wu, A., Yan, H., Yu, B., Chen, D., & Huang, Z. (2023) · eLife · doi:10.7554/elife.90724 · Cited by 12
Lim, J. Y., & Kim, E. (2023) · Metabolites · doi:10.3390/metabo13090979 · Cited by 13
Mitochondrial ultrastructural adaptations in fast muscles of mice lacking IL15RA
Loro, E., Bisetto, S., & Khurana, T. S. (2018) · Journal of Cell Science · doi:10.1242/jcs.218313 · Cited by 12
Kuhnen, G., Russomanno, T. G., Murgia, M., Pillon, N. J., Schönfelder, M., & Wackerhage, H. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232112933 · Cited by 12
O’Connell, G. C., Nichols, C. E., Guo, G., Croston, T. L., Thapa, D., Hollander, J. M., & Pistilli, E. E. (2015) · Mitochondrion · doi:10.1016/j.mito.2015.10.004 · Cited by 11
Short term exercise training enhances cell-mediated responses to HSV-1 vaccine in mice
Shamsi, M. M., Najedi, S., Hassan, Z. M., Isanejad, A., & Mahdavi, M. (2017) · Microbial Pathogenesis · doi:10.1016/j.micpath.2017.07.035 · Cited by 8
Loro, E., Jang, C., Quinn, W. J., Baur, J. A., Arany, Z. P., & Khurana, T. S. (2019) · Frontiers in Physiology · doi:10.3389/fphys.2019.01439 · Cited by 8
Zumbaugh, M. D., Yen, C., Bodmer, J. S., Shi, H., & Gerrard, D. E. (2021) · Frontiers in Physiology · doi:10.3389/fphys.2021.682052 · Cited by 9
Effects of interleukin-15 on autophagy regulation in the skeletal muscle of mice
Tanaka, M., Sugimoto, K., Akasaka, H., Yoshida, S., Takahashi, T., Fujimoto, T., Keyu, X., Yasunobe, Y., Yamamoto, K. I., Hirabayashi, T., et al. (2024) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00311.2023 · Cited by 7
Characteristics of Skeletal Muscle as a Secretory Organ
Aoi, W. (2017) · Springer eBooks · doi:10.1007/978-981-10-3292-9_9 · Cited by 5
Obesity, Myokines, and Metabolic Health
Malandrino, N., & Ahima, R. S. (2023) · Springer eBooks · doi:10.1007/978-3-031-40116-9_56 · Cited by 2
Kuhnen, G., Russomanno, T. G., Murgia, M., Pillon, N. J., Schönfelder, M., & Wackerhage, H. (2022) · Research Square · doi:10.21203/rs.3.rs-1519277/v1 · Cited by 2
Huang, T., Chen, X., He, J., Zheng, P., Luo, Y., Wu, A., Yan, H., Yu, B., Chen, D., & Huang, Z. (2024) · eLife · doi:10.7554/elife.90724.3 · Cited by 1
Vitamin D stimulates Il-15 synthesis in rodent muscle
Ewendt, F., Drewitz, F., Althammer, M., Eichler, C., Brandsch, C., Brey, S., Winkler, T., Wilkens, M. R., St‐Arnaud, R., Kreutz, M. P., et al. (2025) · Biochemistry and Biophysics Reports · doi:10.1016/j.bbrep.2025.101925 · Cited by 1
Lee, H. S., KIM, I., Kim, J. G., & Kim, Y.-Y. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27125204 · Cited by 1
Hu, R., Zhang, X., Hu, L., Li, X., Hu, Q., & Jin, H. (2026) · Frontiers in Medicine · doi:10.3389/fmed.2026.1868285 · Cited by 1
Two‐Way Communication Between Skeletal Muscle and Myokines
Huang, T., Zhou, S., Chen, X., Chen, D., Yu, B., & Huang, Z. (2026) · Cell Biochemistry and Function · doi:10.1002/cbf.70267 · Cited by 1
Pajari, J. (2016) · Jyväskylä University Digital Archive (University of Jyväskylä)
O’Leary, M. F. (2018) · University of Birmingham Institutional Research Archive (University of Birmingham)
The impact on high-fat diet on skeletal muscle stem cell recruitment in CD36 deficient mice
Verpoorten, S. (2019) · Repository@Hull (Worktribe) (University of Hull)
Ex-Vivo Model for Muscle Exposure to Tumor Cell Conditioned Media
Chahal, I. K. (2018) · doi:10.33915/etd.5330
Huang, T., Chen, X., He, J., Zheng, P., Luo, Y., Wu, A., Yan, H., Yu, B., Chen, D., & Huang, Z. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.07.18.549410
Obesity, Myokines, and Metabolic Health
Malandrino, N., & Ahima, R. S. (2023) · Springer eBooks · doi:10.1007/978-3-319-12125-3_56-1
Huang, T., Chen, X., He, J., Zheng, P., Luo, Y., Wu, A., Yan, H., Yu, B., Chen, D., & Huang, Z. (2023) · eLife · doi:10.7554/elife.90724.1
Huang, T., Chen, X., He, J., Zheng, P., Luo, Y., Wu, A., Yan, H., Yu, B., Chen, D., & Huang, Z. (2024) · eLife · doi:10.7554/elife.90724.2
Antonson, N. D., Hauber, M. E., Schelsky, W. M., Kallembach, C., & Fuxjager, M. J. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.10.31.621188
Leońska‐Duniec, A., Małkowska, P., & Sawczuk, M. (2026) · Genes · doi:10.3390/genes17060618
Metadata
- Authors
- Quinn, L. S., Anderson, B. G., Conner, J. D., & Wolden-Hanson, T.
- Affiliations
- University of Washington (US)
- VA Puget Sound Health Care System (US)
- Research Service (L.S.Q., J.D.C., T.W.-H.), VA Puget Sound Health Care System, Seattle, Washington 98108
- Corresponding author
- Quinn, LeBris S.
- Venue
- Endocrinology
- Publisher
- The Endocrine Society
- Published
- 2013-01-01
- Volume
- 154
- Issue
- 1
- Pages
- 232-245
- ISSN
- 0013-7227 (ISSN-L)
- 1945-7170
- PMC
- PMC3529369
- OpenAlex
- W1963939681
- Cited by
- 102
- References
- 44
- Citations by year
- 2026: 7 · 2025: 2 · 2024: 8 · 2023: 8 · 2022: 7 · 2021: 8 · 2020: 7 · 2019: 5 · 2018: 14 · 2017: 4 · 2016: 9 · 2015: 7 · 2014: 10 · 2013: 6
- FWCI
- 7.78
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Endocrinology (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- U.S. Department of Veterans Affairs (I01 BX001026)
- National Institute on Aging (R01AG024136, P30AG013280)
- National Institute of Diabetes and Digestive and Kidney Diseases (P30-DK 17047, P30DK017047)
- Topics
- Health Sciences › Medicine › Physiology (medical) › Exercise and Physiological Responses
- Health Sciences › Medicine › Physiology (medical) › Adipose Tissue and Metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Keywords
- IL-15, endurance exercise, skeletal muscle, oxidative metabolism, fat oxidation, PPARδ, SIRT1, PGC-1α, PGC-1β, transgenic mice, myosin heavy chain isoforms, troponin I isoforms, exercise adaptation, insulin sensitivity, muscle fiber type
- MeSH terms
- Peroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alpha, Animals, Energy Metabolism, Male, Mice, Transgenic, Transcription Factors, Trans-Activators, Muscle, Skeletal, Myosin Heavy Chains, Troponin I, Interleukin-15, PPAR delta, Mice, Sirtuin 1
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.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
