The DOI matches its Crossref record; 31 of the 31 references it cites were found in a registry or an index.
FGF21 is an Akt‐regulated myokine
Open accessAbstract
Fibroblast growth factor‐21 (FGF21) functions as a metabolic regulator. The FGF21 transcript is reported to be abundantly expressed in liver, but little is known about the regulation of FGF21 expression in other tissues. In this study, we show that levels of FGF21 protein expression were similar in skeletal muscle and liver from fasted mice. FGF21 transcript and protein expression were upregulated in gastrocnemius muscle of skeletal muscle‐specific Akt1 transgenic mice. Serum concentration of FGF21 was also increased by Akt1 transgene activation. In cultured skeletal muscle cells, FGF21 expression and secretion was regulated by insulin, Akt transduction and LY294002. These data indicate that skeletal muscle is a source of FGF21 and that its expression is regulated by a phosphatidylinosistol 3‐kinase (PI3‐kinase)/Akt1 signaling pathway‐dependent mechanism.
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 cited source says what the claim attributes to it.
In the citing paper
“Fibroblast growth factor-21 is regulated by insulin285 through the PI3K/Akt1 signaling pathway.286”
From Pancreatic regulation of glucose homeostasis. (2016) · cites this paper as [286]
In the citing paper
“In skeletal muscle, FGF21 expression, in healthy conditions, is almost undetectable, and therefore, the circulating FGF21 is predominantly produced and released by the liver.6, 12”
From Fibroblast growth factor 21 controls mitophagy and muscle mass (2019) · cites this paper as [6]
In the citing paper
“Starvation is one of the stress conditions known to induce FGF21 expression in the liver,8, 32 WAT,10 and skeletal muscle (Figure 2A).6”
From Fibroblast growth factor 21 controls mitophagy and muscle mass (2019) · cites this paper as [6]
In the citing paper
“Recent studies reported that skeletal muscle is not only a producer but also a target of FGF21 because it expresses the cofactor β‐klotho and the FGFRs.6, 13, 14, 17, 18, 19”
From Fibroblast growth factor 21 controls mitophagy and muscle mass (2019) · cites this paper as [6]
In the citing paper
“In contrast, muscle‐dependent systemic release of FGF21 increases with starvation, endoplasmic reticulum stress, mitochondrial dysfunction, obesity, mitochondrial myopathies, and aging.6, 13, 14, 15, 16, 17, 18, 19”
From Fibroblast growth factor 21 controls mitophagy and muscle mass (2019) · cites this paper as [6]
In the citing paper
“In skeletal muscle, FGF21 expression, in healthy conditions, is almost undetectable, and therefore, the circulating FGF21 is predominantly produced and released by the liver.6, 12”
From Fibroblast growth factor 21 controls mitophagy and muscle mass (2019) · cites this paper as [6]
In the citing paper
“(ii) FGF21 is a stress‐induced myokine, which is released under conditions of starvation, ER stress, mitochondrial dysfunction, obesity, mitochondrial myopathies, and aging.6, 13, 14, 15, 16, 17, 18”
From Fibroblast growth factor 21 controls mitophagy and muscle mass (2019) · cites this paper as [6]
In the citing paper
“For example, FGF21 production from skeletal muscle (56, 61, 103, 128), BAT (59), and cardiac tissue (143) is increased in genetic mouse models of cellular or mitochondrial stress.”
From Fibroblast Growth Factor 21: A Versatile Regulator of Metabolic Homeostasis (2018) · cites this paper as [56]
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
Cellular survival: a play in three Akts
Datta, S. R., Brunet, A., & Greenberg, M. E. (1999) · Genes & Development · doi:10.1101/gad.13.22.2905 · Cited by 4,216
Bodine, S. C., Stitt, T. N., Gonzalez, M., Kline, W. O., Stover, G. L., Bauerlein, R., Zlotchenko, E., Scrimgeour, A., Lawrence, J. C., Glass, D. J., et al. (2001) · Nature Cell Biology · doi:10.1038/ncb1101-1014 · Cited by 2,752
FGF-21 as a novel metabolic regulator
Kharitonenkov, A., Shiyanova, T. L., Koester, A., Ford, A. M., Micanovic, R., Galbreath, E. J., Sandusky, G. E., Hammond, L. J., Moyers, J. S., Owens, R. A., et al. (2005) · Journal of Clinical Investigation · doi:10.1172/jci23606 · Cited by 2,125
Self-citationInagaki, T., Dutchak, P., Zhao, G., Ding, X., Gautron, L., Parameswara, V., Li, Y., Goetz, R., Mohammadi, M., Esser, V., et al. (2007) · Cell Metabolism · doi:10.1016/j.cmet.2007.05.003 · Cited by 1,504
Badman, M. K., Pissios, P., Kennedy, A. R., Koukos, G., Flier, J. S., & Maratos-Flier, E. (2007) · Cell Metabolism · doi:10.1016/j.cmet.2007.05.002 · Cited by 1,495
HIF-independent regulation of VEGF and angiogenesis by the transcriptional coactivator PGC-1α
Arany, Z., Foo, S.-Y., Ma, Y., Ruas, J. L., Bommi-Reddy, A., Girnun, G., Cooper, M., Laznik, D., Chinsomboon, J., Rangwala, S. M., et al. (2008) · Nature · doi:10.1038/nature06613 · Cited by 1,054
Shiojima, I. (2005) · Journal of Clinical Investigation · doi:10.1172/jci24682 · Cited by 935
Identification of a novel FGF, FGF-21, preferentially expressed in the liver
Nishimura, T., Nakatake, Y., Konishi, M., & Itoh, N. (2000) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/s0167-4781(00)00067-1 · Cited by 847
Role of Myokines in Exercise and Metabolism
Pedersen, B. K., Åkerström, T. C. A., Nielsen, A. R., & Fischer, C. P. (2007) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00080.2007 · Cited by 841
The metabolic state of diabetic monkeys is regulated by fibroblast growth factor-21
Kharitonenkov, A., Wroblewski, V. J., Koester, A., Chen, Y.-F., Clutinger, C. K., Tigno, X. T., Hansen, B. C., Shanafelt, A. B., & Etgen, G. J. (2007) · Endocrinology · doi:10.1210/en.2006-1168 · Cited by 738
Self-citation
Research works printed but not linked: 1
- Wang H., 2007, Identification of a domain within PPAR gamma regulating expression of a group of genes containing FGF21 that are selectively repressed by SIRT1 in adipocytes, Mol. Cell Biol.
Cited by
Sorted by citations
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
The FGF family: biology, pathophysiology and therapy
Beenken, A., & Mohammadi, M. (2009) · Nature Reviews Drug Discovery · doi:10.1038/nrd2792 · Cited by 1,945
Chait, A., & den Hartigh, L. J. (2020) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2020.00022 · Cited by 1,529
Pancreatic regulation of glucose homeostasis.
Röder, P. V., Wu, B., Liu, Y., & Han, W. (2016) · Experimental & Molecular Medicine · doi:10.1038/emm.2016.6 · Cited by 985
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
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
Metabolic Syndrome and Insulin Resistance: Underlying Causes and Modification by Exercise Training
Roberts, C. K., Hevener, A. L., & Barnard, R. J. (2012) · Comprehensive physiology · doi:10.1002/cphy.c110062 · Cited by 966
Exercise benefits in cardiovascular disease: beyond attenuation of traditional risk factors
Fiuza-Luces, C., Santos-Lozano, A., Joyner, M., Carrera-Bastos, P., Picazo, O., Zugaza, J. L., Izquierdo, M., Ruilope, L. M., & Lucia, A. (2018) · Nature Reviews Cardiology · doi:10.1038/s41569-018-0065-1 · Cited by 803
Exercise is the real polypill.
Fiuza-Luces, C., Garatachea, N., Berger, N. A., & Lucia, A. (2013) · Physiology · doi:10.1152/physiol.00019.2013 · Cited by 791
Kim, K. H., Jeong, Y. T., Oh, H., Kim, S. H., Cho, J. M., Kim, Y.-N., Kim, S. S., Kim, D. H., Hur, K. Y., Kim, H. K., et al. (2013) · Nature Medicine · doi:10.1038/nm.3014 · Cited by 774
Pedersen, B. K. (2011) · Journal of Experimental Biology · doi:10.1242/jeb.048074 · Cited by 668
The diseasome of physical inactivity – and the role of myokines in muscle–fat cross talk
Pedersen, B. K. (2009) · The Journal of Physiology · doi:10.1113/jphysiol.2009.179515 · Cited by 631
Thermogenic Activation Induces FGF21 Expression and Release in Brown Adipose Tissue
Hondares, E., Iglesias, R., Giralt, A., Gonzalez, F. J., Giralt, M., Mampel, T., & Villarroya, F. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.215889 · Cited by 623
Suomalainen, A., Elo, J. M., Pietiläinen, K. H., Hakonen, A. H., Sevastianova, K., Korpela, M., Isohanni, P., Marjavaara, S. K., Tyni, T., Kiuru-Enari, S., et al. (2011) · The Lancet Neurology · doi:10.1016/s1474-4422(11)70155-7 · Cited by 427
The Role of Exercise-Induced Myokines in Muscle Homeostasis and the Defense against Chronic Diseases
Brandt, C., & Pedersen, B. K. (2010) · BioMed Research International · doi:10.1155/2010/520258 · Cited by 443
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
Therapeutic potential of the endocrine fibroblast growth factors FGF19, FGF21 and FGF23
Degirolamo, C., Sabbà, C., & Moschetta, A. (2016) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2015.9 · Cited by 424
Myonectin (CTRP15), a novel myokine that links skeletal muscle to systemic lipid homeostasis
Seldin, M. M., Peterson, J. M., Byerly, M. S., Wei, Z., & Wong, G. W. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.336834 · Cited by 406
Fibroblast growth factor 21 protects against cardiac hypertrophy in mice
Planavila, A., Redondo‐Angulo, I., Hondares, E., Vinciguerra, M., Munts, C., Iglesias, R., Gabrielli, L., Sitges, M., Giralt, M., van Bilsen, M., et al. (2013) · Nature Communications · doi:10.1038/ncomms3019 · Cited by 371
Exercise-induced myokines and their role in chronic diseases
Pedersen, B. K. (2011) · Brain Behavior and Immunity · doi:10.1016/j.bbi.2011.02.010 · Cited by 370
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
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 319
Flippo, K. H., & Potthoff, M. J. (2021) · Nature Metabolism · doi:10.1038/s42255-021-00354-2 · Cited by 311
Mitochondrial myopathy induces a starvation-like response
Tyynismaa, H., Carroll, C. J., Raimundo, N., Ahola-Erkkilä, S., Wenz, T., Ruhanen, H., Guse, K., Hemminki, A., Peltola-Mjøsund, K. E., Tulkki, V., et al. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq310 · Cited by 300
Berglund, E. D., Li, C. Y., Bina, H. A., Lynes, S. E., Michael, M. D., Shanafelt, A. B., Kharitonenkov, A., & Wasserman, D. H. (2009) · Endocrinology · doi:10.1210/en.2009-0221 · Cited by 297
Self-citationAdipo-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
C2C12 myoblasts release micro-vesicles containing mtDNA and proteins involved in signal transduction
Guescini, M., Guidolin, D., Vallorani, L., Casadei, L., Gioacchini, A. M., Tibollo, P., Battistelli, M., Falcieri, E., Battistin, L., Agnati, L. F., et al. (2010) · Experimental Cell Research · doi:10.1016/j.yexcr.2010.04.006 · Cited by 294
Gao, Y., Zhang, W., Zeng, L.-Q., Bai, H., Li, J., Zhou, J., Zhou, G., Fang, C., Wang, F., & Qin, X.-J. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101635 · Cited by 298
Acute Exercise Induces FGF21 Expression in Mice and in Healthy Humans
Kim, K. H., Kim, S. H., Min, Y.-K., Yang, H.-M., Lee, J.-B., & Lee, M.-S. (2013) · PLoS ONE · doi:10.1371/journal.pone.0063517 · Cited by 290
Li, Y., Wong, K., Giles, A. J., Jiang, J., Lee, J. W., Adams, A. C., Kharitonenkov, A., Yang, Q., Gao, B., Guarente, L., et al. (2013) · Gastroenterology · doi:10.1053/j.gastro.2013.10.059 · Cited by 283
Self-citationA Dozen Years of Discovery: Insights into the Physiology and Pharmacology of FGF21
Kliewer, S. A., & Mangelsdorf, D. J. (2019) · Cell Metabolism · doi:10.1016/j.cmet.2019.01.004 · Cited by 273
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
Fibroblast Growth Factor 21—Metabolic Role in Mice and Men
Staiger, H., Keuper, M., Berti, L., Hrabě de Angelis, M., & Häring, H.-U. (2017) · Endocrine Reviews · doi:10.1210/er.2017-00016 · Cited by 270
Inflammation induced loss of skeletal muscle
Londhe, P., & Guttridge, D. C. (2015) · Bone · doi:10.1016/j.bone.2015.03.015 · Cited by 276
Endocrine Crosstalk Between Skeletal Muscle and the Brain
Delezie, J., & Handschin, C. (2018) · Frontiers in Neurology · doi:10.3389/fneur.2018.00698 · Cited by 277
Fibroblast growth factor 21 protects the heart from oxidative stress
Planavila, A., Redondo‐Angulo, I., Ribas‐Aulinas, F., Garrabou, G., Casademont, J., Giralt, M., & Villarroya, F. (2014) · Cardiovascular Research · doi:10.1093/cvr/cvu263 · Cited by 265
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
Activating transcription factor 4-dependent induction of FGF21 during amino acid deprivation
De Sousa-Coelho, A. L., Marrero, P. F., & Haro, D. (2012) · Biochemical Journal · doi:10.1042/bj20111748 · Cited by 246
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
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
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
Mashili, F. L., Austin, R. L., Deshmukh, A. S., Fritz, T., Caidahl, K., Bergdahl, K., Zierath, J. R., Chibalin, A., Moller, D. E., Kharitonenkov, A., et al. (2011) · Diabetes/Metabolism Research and Reviews · doi:10.1002/dmrr.1177 · Cited by 226
Self-citationMyokines 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 234
Fibroblast Growth Factor 21: A Versatile Regulator of Metabolic Homeostasis
BonDurant, L. D., & Potthoff, M. J. (2018) · Annual Review of Nutrition · doi:10.1146/annurev-nutr-071816-064800 · Cited by 222
Edward F. Adolph Distinguished Lecture: Muscle as an endocrine organ: IL-6 and other myokines
Pedersen, B. K. (2009) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00734.2009 · Cited by 221
Metabolic adaptation in obesity and type ii diabetes: myokines, adipokines and hepatokines
Oh, K.-J., Lee, D., Kim, W., Han, B., Lee, S., & Bae, K.-H. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms18010008 · Cited by 210
The brown fat secretome: metabolic functions beyond thermogenesis
Wang, G.-X., Zhao, X.-Y., & Lin, J. D. (2015) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2015.03.002 · Cited by 212
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
Fibroblast Growth Factor-21 Is Induced in Human Skeletal Muscles by Hyperinsulinemia
Hojman, P., Pedersen, M., Nielsen, A. R., Krogh-Madsen, R., Yfanti, C., Åkerstrom, T., Nielsen, S., & Pedersen, B. K. (2009) · Diabetes · doi:10.2337/db09-0713 · Cited by 198
Inventing new medicines: The FGF21 story
Kharitonenkov, A., & Adams, A. C. (2014) · Molecular Metabolism · doi:10.1016/j.molmet.2013.12.003 · Cited by 198
Self-citationCurrent and investigational medications for the treatment of sarcopenia
Rolland, Y., Dray, C., Vellas, B., & Barreto, P. D. S. (2023) · Metabolism · doi:10.1016/j.metabol.2023.155597 · Cited by 195
Exercise-Induced Myokines With Therapeutic Potential for Muscle Wasting
Piccirillo, R. (2019) · Frontiers in Physiology · doi:10.3389/fphys.2019.00287 · Cited by 197
Skeletal muscle is an endocrine organ
Iizuka, K., Machida, T., & Hirafuji, M. (2014) · Journal of Pharmacological Sciences · doi:10.1254/jphs.14r02cp · Cited by 189
Crosstalk between adipokines and myokines in fat browning
Rodríguez, A., Becerril, S., Ezquerro, S., Méndez-Giménez, L., & Frühbeck, G. (2016) · Acta Physiologica · doi:10.1111/apha.12686 · Cited by 196
Extracellular Vesicles and Exosomes: Insights From Exercise Science
Nederveen, J. P., Warnier, G., Carlo, A. D., Nilsson, M. I., & Tarnopolsky, M. A. (2021) · Frontiers in Physiology · doi:10.3389/fphys.2020.604274 · Cited by 200
Glucose induces FGF21 mRNA expression through ChREBP activation in rat hepatocytes
Iizuka, K., Takeda, J., & Horikawa, Y. (2009) · FEBS Letters · doi:10.1016/j.febslet.2009.07.053 · Cited by 187
Identification of human exercise-induced myokines using secretome analysis
Catoire, M., Mensink, M., Kalkhoven, E., Schrauwen, P., & Kersten, S. (2014) · Physiological Genomics · doi:10.1152/physiolgenomics.00174.2013 · Cited by 179
Differential Specificity of Endocrine FGF19 and FGF21 to FGFR1 and FGFR4 in Complex with KLB
Yang, C., Jin, C., Li, X., Wang, F., McKeehan, W. L., & Luo, Y. (2012) · PLoS ONE · doi:10.1371/journal.pone.0033870 · Cited by 173
The physiology of optimizing health with a focus on exercise as medicine
Pedersen, B. K. (2019) · Annual Review of Physiology · doi:10.1146/annurev-physiol-020518-114339 · Cited by 163
Cyphert, H. A., Ge, X., Kohan, A. B., Salati, L. M., Zhang, Y., & Hillgartner, F. B. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.375907 · Cited by 162
Roles of myokines in exercise-induced improvement of neuropsychiatric function
Kim, S., Choi, J., Moon, S., Park, D., Kwak, H., & Kang, J. (2019) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-019-02253-8 · Cited by 177
Mai, K., Andres, J., Biedasek, K., Weicht, J., Bobbert, T., Sabath, M., Meinus, S., Reinecke, F., Möhlig, M., Weickert, M. O., et al. (2009) · Diabetes · doi:10.2337/db08-1775 · Cited by 159
Müller, T. D., Sullivan, L. M., Habegger, K., Yi, C., Kabra, D., Grant, E., Ottaway, N., Krishna, R., Holland, J., Hembree, J., et al. (2012) · Journal of Peptide Science · doi:10.1002/psc.2408 · Cited by 156
Christodoulides, C., Dyson, P., Sprecher, D., Tsintzas, K., & Karpe, F. (2009) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2009-0111 · Cited by 153
The Role of Mitochondria in the Pathophysiology of Skeletal Muscle Insulin Resistance
Pagel-Langenickel, I., Bao, J., Pang, L., & Sack, M. N. (2010) · Endocrine Reviews · doi:10.1210/er.2009-0003 · Cited by 154
FGF21: A Novel Regulator of Glucose and Lipid Metabolism and Whole-Body Energy Balance
Szczepańska, E., & Gietka‐Czernel, M. (2022) · Hormone and Metabolic Research · doi:10.1055/a-1778-4159 · Cited by 155
Fibroblast growth factor-21, energy balance and obesity
Giralt, M., Gavaldà‐Navarro, A., & Villarroya, F. (2015) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2015.09.018 · Cited by 150
FGF21 reloaded: challenges of a rapidly growing field
Kharitonenkov, A., & Larsen, P. J. (2010) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2010.11.003 · Cited by 147
Self-citationKim, K. H., & Lee, M.-S. (2014) · Diabetes & Metabolism Journal · doi:10.4093/dmj.2014.38.4.245 · Cited by 146
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
Li, X. (2019) · Frontiers of Medicine · doi:10.1007/s11684-019-0711-y · Cited by 143
The search for exercise factors in humans
Catoire, M., & Kersten, S. (2015) · The FASEB Journal · doi:10.1096/fj.14-263699 · Cited by 137
Liu, J., Xu, Y., Hu, Y., & Wang, G. (2014) · Metabolism · doi:10.1016/j.metabol.2014.11.009 · Cited by 139
Fibroblast Growth Factor Signaling in Metabolic Regulation
Nies, V. J. M., Sancar, G., Liu, W., van Zutphen, T., Struik, D., Yu, R. T., Atkins, A. R., Evans, R. M., Jonker, J. W., & Downes, M. (2016) · Frontiers in Endocrinology · doi:10.3389/fendo.2015.00193 · Cited by 137
Exercise-induced myokines in health and metabolic diseases
So, B., Kim, H., Kim, J., & Song, W. J. (2014) · Integrative Medicine Research · doi:10.1016/j.imr.2014.09.007 · Cited by 139
Kharitonenkov, A. (2009) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2009.07.001 · Cited by 133
Self-citationRegulation of myokine expression: Role of exercise and cellular stress
Ost, M., Coleman, V., Kasch, J., & Klaus, S. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.02.018 · Cited by 135
Acute exercise increases fibroblast growth factor 21 in metabolic organs and circulation
Tanimura, Y., Aoi, W., Takanami, Y., Kawai, Y., Mizushima, K., Naito, Y., & Yoshikawa, T. (2016) · Physiological Reports · doi:10.14814/phy2.12828 · Cited by 131
Serum FGF21 levels are associated with brown adipose tissue activity in humans
Hanssen, M. J. W., Broeders, E. P. M., Samms, R. J., Vosselman, M. J., van der Lans, A. A. J. J., Cheng, C., Adams, A. C., Lichtenbelt, W. D. V. M., & Schrauwen, P. (2015) · Scientific Reports · doi:10.1038/srep10275 · Cited by 136
Feingold, K. R., Grünfeld, C., Heuer, J. G., Gupta, A., Cramer, M. S., Zhang, T., Shigenaga, J. K., Patzek, S. M., Chan, Z. W., Moser, A. H., et al. (2012) · Endocrinology · doi:10.1210/en.2011-1496 · Cited by 130
Self-citationMechanisms 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
Bouzakri, K., Plomgaard, P., Berney, T., Donath, M. Y., Pedersen, B. K., & Halban, P. A. (2011) · Diabetes · doi:10.2337/db10-1178 · Cited by 122
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
FGF21 and Cardiac Physiopathology
Planavila, A., Redondo-Angulo, I., & Villarroya, F. (2015) · Frontiers in Endocrinology · doi:10.3389/fendo.2015.00133 · Cited by 123
FGF21 mediates the lipid metabolism response to amino acid starvation
De Sousa-Coelho, A. L., Relat, J., Hondares, E., Pérez-Martí, A., Ribas, F., Villarroya, F., Marrero, P. F., & Haro, D. (2013) · Journal of Lipid Research · doi:10.1194/jlr.m033415 · Cited by 123
Glucagon-to-insulin ratio is pivotal for splanchnic regulation of FGF-21 in humans
Hansen, J. S., Clemmesen, J. O., Secher, N. H., Hoene, M., Drescher, A., Weigert, C., Pedersen, B. K., & Plomgaard, P. (2015) · Molecular Metabolism · doi:10.1016/j.molmet.2015.06.001 · Cited by 123
Role of Osteoglycin in the Linkage between Muscle and Bone
Tanaka, K.-I., Matsumoto, E., Higashimaki, Y., Katagiri, T., Sugimoto, T., Seino, S., & Kaji, H. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.292193 · Cited by 121
Role of Exercise in the Activation of Brown Adipose Tissue
Sánchez‐Delgado, G., Martínez‐Téllez, B., Olza, J., Aguilera, C. M., Gil, Á., & Ruiz, J. R. (2015) · Annals of Nutrition and Metabolism · doi:10.1159/000437173 · Cited by 122
Molecular bases of the crosstalk between bone and muscle
Karsenty, G., & Mera, P. (2017) · Bone · doi:10.1016/j.bone.2017.04.006 · Cited by 121
Activation of Liver FGF21 in hepatocarcinogenesis and during hepatic stress
Yang, C., Lu, W., Lin, T., You, P., Ye, M., Huang, Y., Jiang, X., Wang, C., Wang, F., Lee, M., et al. (2013) · BMC Gastroenterology · doi:10.1186/1471-230x-13-67 · Cited by 117
Mitochondrial stress and mitokines in aging
Burtscher, J., Soltany, A., Visavadiya, N. P., Burtscher, M., Millet, G. P., Khoramipour, K., & Khamoui, A. V. (2023) · Aging Cell · doi:10.1111/acel.13770 · Cited by 123
Joki, Y., Ohashi, K., Yuasa, D., Shibata, R., Ito, M., Matsuo, K., Kambara, T., Uemura, Y., Hayakawa, S., Hiramatsu‐Ito, M., et al. (2015) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2015.02.081 · Cited by 114
Self-citationFGF21 Revolutions: Recent Advances Illuminating FGF21 Biology and Medicinal Properties
Kharitonenkov, A., & DiMarchi, R. D. (2015) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2015.09.007 · Cited by 114
Self-citationMuscle-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 124
Myokines in metabolic homeostasis and diabetes
Eckel, J. (2019) · Diabetologia · doi:10.1007/s00125-019-4927-9 · Cited by 113
Role of the ISR-ATF4 pathway and its cross talk with Nrf2 in mitochondrial quality control
Kasai, S., Yamazaki, H., Tanji, K., Engler, M. J., Matsumiya, T., & Itoh, K. (2018) · Journal of Clinical Biochemistry and Nutrition · doi:10.3164/jcbn.18-37 · Cited by 107
Rowe, G. C., Safdar, A., & Arany, Z. P. (2014) · Circulation · doi:10.1161/circulationaha.113.001590 · Cited by 107
Hanks, L. J., Gutiérrez, O. M., Bamman, M. M., Ashraf, A., McCormick, K. L., & Casazza, K. (2015) · Journal of Clinical & Translational Endocrinology · doi:10.1016/j.jcte.2015.02.001 · Cited by 104
Impact of Melatonin on Skeletal Muscle and Exercise
Stacchiotti, A., Favero, G., & Rodella, L. F. (2020) · Cells · doi:10.3390/cells9020288 · Cited by 116
Taniguchi, H., Tanisawa, K., Sun, X., Kubo, T., & Higuchi, M. (2015) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2015-3308 · Cited by 104
Metadata
- Authors
- Izumiya, Y., Bina, H. A., Ouchi, N., Akasaki, Y., Kharitonenkov, A., & Walsh, K.
- Affiliations
- Boston University (US)
- Eli Lilly (United States) (US)
- Corresponding author
- Walsh, Kenneth
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 2008-10-21
- Volume
- 582
- Issue
- 27
- Pages
- 3805-3810
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- PMC
- PMC2604129
- OpenAlex
- W2047726905
- Cited by
- 415
- References
- 31
- Citations by year
- 2026: 7 · 2025: 23 · 2024: 25 · 2023: 25 · 2022: 21 · 2021: 18 · 2020: 20 · 2019: 35 · 2018: 31 · 2017: 26 · 2016: 21 · 2015: 36 · 2014: 33 · 2013: 23 · 2012: 24
- FWCI
- 6.44
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- FEBS Letters (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institute on Aging (R01AG015052, R37AG015052, AG15052)
- National Heart, Lung, and Blood Institute (HL81587, HL77774, R01HL086785, P01HL081587, HL 86785, R01HL077774)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fibroblast Growth Factor Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Keywords
- FGF21, myokines, AKT1, skeletal muscle, PI3K/Akt signaling, insulin, gastrocnemius, metabolic regulation, fasting
- MeSH terms
- Phosphoinositide-3 Kinase Inhibitors, Animals, Cell Line, Chromones, Fibroblast Growth Factors, Insulin, Liver, Mice, Transgenic, Morpholines, Signal Transduction, Up-Regulation, Muscle, Skeletal, Phosphatidylinositol 3-Kinases, Protein Kinase Inhibitors, Proto-Oncogene Proteins c-akt, Mice
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