Cited by 335Muscle Physiology and DisordersExercise and Physiological ResponsesMuscle metabolism and nutrition

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Irisin is a pro-myogenic factor that induces skeletal muscle hypertrophy and rescues denervation-induced atrophy

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Reza, Musarrat Maisha, Subramaniyam, Nathiya, Sim, Chu Ming, Ge, Xiaojia, Sathiakumar, Durgalakshmi, McFarlane, Craig, Sharma, Mridula, Kambadur, Ravi·2017·Nature Communications

DOI 10.1038/s41467-017-01131-0PMC PMC5653663

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Abstract

Exercise induces expression of the myokine irisin, which is known to promote browning of white adipose tissue and has been shown to mediate beneficial effects following exercise. Here we show that irisin induces expression of a number of pro-myogenic and exercise response genes in myotubes. Irisin increases myogenic differentiation and myoblast fusion via activation of IL6 signaling. Injection of irisin in mice induces significant hypertrophy and enhances grip strength of uninjured muscle. Following skeletal muscle injury, irisin injection improves regeneration and induces hypertrophy. The effects of irisin on hypertrophy are due to activation of satellite cells and enhanced protein synthesis. In addition, irisin injection rescues loss of skeletal muscle mass following denervation by enhancing satellite cell activation and reducing protein degradation. These data suggest that irisin functions as a pro-myogenic factor in mice.

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Fig. 1 Irisin induces gene expression changes and improves myogenesis. a Image of Coomassie-stained polyacrylamide gel showing recombinant His-tagged irisin protein. Recombinant irisin protein was detected as a single band at ~15 kDa. Lane 1 shows the SeeBlue Plus 2 Pre-Stained ladder. Lanes 2, 3, and 4 show 1, 2, and 5 μl of the purified His-tagged irisin protein, respectively. b Graph representing qPCR analysis of Ucp1 expression in human subcutaneous white adipose-derived stem cells (hADSCs) after 21 days of adipogenic differentiation in the presence of DB (control) or irisin (n = 2 biological replicates). c Graph representing qPCR analysis of Ucp1 in 3T3L1 fibroblasts after 4 days of adipogenic differentiation in the presence of DB (control) or irisin (n = 3 biological replicates). Graphs displaying qPCR analysis of sox8 (d), heyL (e), haptoglobin (f), il6 (g), cxcl1 (h), and ptx3 (i) in 72 h-differentiated C2C12 myotubes treated with DB (control) or recombinant irisin protein for 0, 6, 12, 24, and 48 h. All qPCR graphs show gene expression normalized to gapdh (n = 3 biological replicates). Error bars represent mean ± SEM. Student’s t-test was performed for b and all relevant figure panels between d and i, and one-way ANOVA was peformed for c. Significance is indicated with *p < 0.05, **p < 0.01 and ***p < 0.001CC BY · PubMed Central

Fig. 2 Irisin promotes skeletal muscle differentiation. a Graph showing the absorbance readings of cells treated with DB (control) or increasing concentrations of irisin (250, 1000, and 2000 ng/ml) at 0, 24, 48, and 72 h of proliferation. Absorbance reading at 655 nm is proportional to the number of cells present and hence, indicative of myoblast proliferation. (n = 16 biological replicates). b Representative images of H&E-stained myoblasts at 0, 24, 48, 72, and 96 h of differentiation in the presence of DB (control) or irisin (250 and 1000 ng/ml). c Graph showing quantification of myotube number at 0, 24, 48, 72, and 96 h of differentiation in the presence of DB (control) or irisin (250 and 1000 ng/ml) (n = 3 biological replicates). d Graph showing quantification of fusion index at 0, 24, 48, 72, and 96 h of differentiation in the presence of DB (control) or irisin (250 and 1000 ng/ml) (n = 3 biological replicates). Graphs displaying qPCR analysis of e myomaker and f caveolin-3 expression normalized to GAPDH in differentiating myoblasts (0, 24, 48, 72, and 96 h) treated with DB (control) or irisin (1000 ng/ml) (n = 3 biological replicates). g IB analysis of MyoD, MHC, myogenin, and p21 protein levels. The levels of GAPDH were assessed as a loading control. Graphs show densitometric analysis of h MyoD, i MHC, j myogenin, and k p21 levels in arbitrary units (a.u), normalized to GAPDH (n = 3 biological replicates). Since MyoD, MHC, and myogenin IB analysis was performed on the same membrane, the same GAPDH was used to normalize the results. All IBs were performed on proteins collected from differentiating myotubes at 24, 48, 72, and 96 h treated with either DB (control) or irisin (1000 ng/ml). Error bars represent mean ± SEM. One-way ANOVA was performed for all relevant figure panels between a and d, and Student’s t-test was performed for all relevant figure panels between e and k. Significance is indicated with *p < 0.05 and **p < 0.01CC BY · PubMed Central

Fig. 3 Irisin enhances myogenesis in primary human myoblast cultures. a Representative images of H&E-stained 36C15Q primary myoblasts at 24, 48, 72, and 96 h of differentiation in the presence of DB (control) or irisin (250 and 1000 ng/ml). b Graph showing quantification of myotube number at 0, 24, 48, 72, and 96 h of differentiation in the presence of DB (control) or irisin (250 and 1000 ng/ml). c Graph showing quantification of fusion index at 0, 24, 48, 72, and 96 h of differentiation in the presence of DB (control) or irisin (250 and 1000 ng/ml) (n = 2 biological replicates). Error bars represent mean ± SEM. One-way ANOVA was performed for all relevant figure panels. Significance is indicated with *p < 0.05 and **p < 0.01CC BY · PubMed Central

Fig. 4 Irisin improves protein synthesis and reduces protein degradation. a Graph showing levels of irisin circulating in serum of mice injected with DB (control) or recombinant irisin (n = 5 mice for DB-injected group and n = 6 mice for irisin-injected group). b (i) IB analysis of Ucp1 levels. The levels of Ponceau S were assessed as a loading control. b (ii) Graph showing densitometric analysis of Ucp1 levels in arbitrary units (a.u), normalized to Ponceau S. Brown adipose tissue was used as a positive control to detect Ucp1 (n = 5 mice for DB-injected group and n = 3 mice for irisin-injected group). c Graph showing body weight change (% from initial) in mice injected with either DB or irisin protein. Graphs displaying d Gas, Quad, and BF, and e TA, EDL, and Sol muscle weights of mice injected with DB (control) or irisin. All hindlimb muscle weights were normalized to tibia length. f Graph showing the grip strength of mice (in newton; N) injected with DB (control) or irisin (n = 5 mice for DB-injected group and n = 4 mice for irisin-injected group). g Representative images of H&E-stained TA muscle from mice injected with DB (control) or irisin. Images were captured using a ×20 objective. Scale bar represents 100 μm. h Graph showing the distribution of TA myofiber CSA in mice injected with DB (control) or irisin (n = 3 mice per group). i Graph showing body weight change (% from initial) in mice injected with either DB (control) or His-tagged peptide. Graphs displaying j Gas, Quad, and BF, and k TA, EDL, and Sol muscle weights of mice injected with DB (control) or His-tagged peptide. All hindlimb muscle weights were normalized to tibia length (n = 5 mice for each treatment group). l Representative images of H&E-stained TA muscle from mice injected with DB (control) or His-tagged peptide. Images were captured using a ×20 objective. Scale bar represents 100 μm. m Graph showing the distribution of TA myofiber CSA in mice injected with DB (control) or His-tagged peptide (n = 3 mice per treatment group). Error bars represent mean ± SEM. Student’s t-test was performed for all relevant figure panels. Significance is indicated with *p < 0.05, **p < 0.01 and ***p < 0.001CC BY · PubMed Central

Fig. 5 Signalling behind irisin treatment. a IB analysis of p-Akt, p-Erk1/2, and p-Raptor protein levels. The levels of GAPDH were assessed as a loading control. Graphs show densitometric analysis of p-Akt (left), p-Raptor (middle), and p-Erk1/2 (right) levels in arbitrary units (a.u.), normalized to GAPDH (n = 3 biological replicates). Since p-Akt and p-Erk1/2 IB analysis was performed on the same membrane, the same GAPDH was used to normalize the results. b IB analysis of p-FoxO1, MuRF-1, FoxO1, and Atrogin-1 protein levels. The levels of tubulin or Ponceau S were assessed as loading controls. Graphs show densitometric analysis of pFoxO1/FoxO1 (left), Atrogin-1 (middle), and MuRF-1 (right) levels in a.u., normalized to tubulin or Ponceau S (n = 3 biological replicates). Since pFoxO1 and MuRF-1 IB analysis was performed on the same membrane, the same tubulin was used to normalize the results. All IBs were performed on proteins collected from 72 h-differentiated myotubes treated with either DB (control) or irisin (1000 ng/ml) for a further 48 h. Where necessary, intervening irrelevant bands were removed from the IBs, which is denoted by a gap between boxes in the figures. Error bars represent mean ± SEM. Student’s t-test was performed for all relevant figure panels. Significance is indicated with *p < 0.05 and **p < 0.01CC BY · PubMed Central

Fig. 6 Irisin treatment activates the IL6 pathway. Graphs displaying qPCR analysis of IL6 (a), Stat3 (b), and Socs3 (c) in proliferating myoblasts at 24, 48, and 72 h treated with DB (control) or irisin (1000 ng/ml). Graphs displaying qPCR analysis of IL6 (d), Stat3 (e), and Socs3 (f) in differentiating myoblasts at 24, 48, 72, and 96 h treated with DB (control) or irisin (1000 ng/ml). Graphs displaying qPCR analysis of IL6 (g) at 48 h treated with DB (control) or irisin (1000 ng/ml) in myoblasts transfected with IL6-specific siRNA (IL6 siRNA) or scrambled siRNA-transfected myoblasts (scramb-siRNA). All qPCR graphs show gene expression normalized to gapdh. h Representative images of H&E-stained IL6 knockdown (IL6 siRNA) and IL6-positive (scramb-siRNA) myoblasts differentiated for 72 h in the presence of DB (control) or irisin (1000 ng/ml). i Graph showing quantification of fusion index of IL6-knockdown (IL6 siRNA) and IL6-positive (scramb-siRNA) myoblasts differentiated for 72 h in the presence of DB (control) or irisin (1000 ng/ml). j Graph showing quantification of myotube number of IL6-knockdown (IL6 siRNA) and IL6-positive (scramb-siRNA) myoblasts differentiated for 72 h in the presence of DB (control) or irisin (1000 ng/ml) (n = 3 biological replicates for all experiments in this figure). Error bars represent mean ± SEM. Student’s t-test was performed for all figure panels between a and f, and two-way ANOVA was performed for all relevant figure panels between g and j. Significance is indicated with *p < 0.05, **p < 0.01 and ***p < 0.001CC BY · PubMed Central

Fig. 7 Irisin improves regeneration of skeletal muscle. a Representative images of MyoD immunostaining of TA muscle sections from DB (control)- or irisin-injected mice at day 2 and day 3 post notexin injury. Images were captured using a ×40 objective. Scale bar represents 100 μm. Nuclei were counterstained with DAPI. White asterisks denote MyoD-positive cells. Linear brightness and contrast of ‘Merge’ panel was adjusted to visualize MyoD+ cells without altering the interpretation of results in any way. b Graph displaying the percentage of MyoD-positive cells in TA muscle sections from DB (control)- or irisin-injected mice at day 2 (n = 3 mice for both groups) and day 3 (n = 2 mice for control group and n = 3 mice for irisin-injected group) post notexin injury. c Representative images of MyoD and Pax7 immunostaining of primary satellite cell cultures treated with either DB (Control) or irisin (1000 ng/ml) for 24 h. Linear brightness and contrast of “Dapi”, “Pax7”, and “MyoD” panels was adjusted to visualize the positively stained nuclei without altering the interpretation of results in any way. Images were captured using a ×10 objective. Scale bar represents 100 μm. Graphs displaying the percentage of d quiescent (Pax7+/MyoD−), e proliferating (Pax7+/MyoD+), and f committed (Pax7−/MyoD+) satellite cells present following treatment with either DB (control) or increasing concentrations of irisin (250, 700, and 1000 ng/ml) for 24 h (n = 2 biological replicates). g Representative images of H&E-stained TA muscle at day 10 post notexin injury from mice injected with either DB (control) or irisin. Images were captured using a ×20 objective. Scale bar represents 100 μm. h Graphs showing the distribution of TA myofiber cross-sectional area (CSA) and the i percentage of myofibers with 1, 2, 3, or 4 centrally placed nuclei at day 10 post notexin injury from mice injected with either DB (control) or irisin (2.5 μg/g of body weight) (n = 3 mice for both groups). Error bars represent mean ± SEM. Student’s t-test was performed for b, h, i, and one-way ANOVA was performed for d–f. Significance is indicated with *p < 0.05, **p < 0.01 and ***p < 0.001CC BY · PubMed Central

Fig. 8 Irisin rescues denervation-induced loss of muscle mass. a Graph showing average body weight (g) of mice injected with either DB (control) or irisin (2.5 μg/g body weight) three times a week, 1 week prior to, and 2 weeks post transection of the sciatic nerve. Body weights were measured prior to injection. b Graph showing the percentage change in body weight (from initial) in mice injected with either DB (control) or irisin pre and post sciatic nerve transection (n = 6 mice for both groups). c Graph displaying average TA, EDL, Gas, and Sol muscle weights of denervated mice injected with either DB (control) or irisin pre and post sciatic nerve transection. All hindlimb muscle weights were normalized to tibia length (n = 5 mice for DB-injected group and 6 mice for irisin-injected group). d Representative images of H&E-stained TA muscle from non-denervated and denervated mice injected with either DB (control) or irisin. e Histogram and f line graph showing the distribution of TA myofiber CSA in non-denervated and denervated mice injected with either DB (control) or irisin. g Graph displaying the average total cross-sectional area of TA muscles from denervated mice injected with either DB (control) or irisin (n = 3 mice for both groups). Error bars represent mean ± SEM. Student’s t-test was performed for all relevant figure panels. Significance is indicated with *p < 0.05 and **p < 0.01CC BY · PubMed Central

Fig. 9 Irisin treatment rescues denervation-induced muscle atrophy. a Representative images of MyoD immunostaining of TA muscle sections from denervated mice injected with either DB (control) or irisin. Images were captured using a ×20 objective. Scale bar represents 100 μm. Nuclei were counterstained with DAPI. White asterisks denote MyoD-positive cells. Linear brightness and contrast of ‘Merge’ panel was adjusted to visualize MyoD+ nuclei without altering the interpretation of results in any way. b Graph displaying the percentage of MyoD-positive cells in TA muscle sections from denervated mice injected with either DB (control) or irisin pre and post sciatic nerve transection. c IB analysis of Atrogin-1 protein levels in Gas muscle from non-denervated mice injected with DB (control) and denervated mice injected with either DB (control) or irisin. The levels of GAPDH were assessed as a loading control. Arrow indicates Atrogin-1 band. d Graph shows densitometric analysis of Atrogin-1 levels in arbitrary units (a.u), normalized to GAPDH. e IB analysis of MuRF-1 protein levels in Gas muscle from non-denervated mice injected with DB (control) or denervated mice injected with either DB (control) or irisin. The levels of GAPDH were assessed as a loading control. f Graph shows densitometric analysis of MuRF-1 levels in a.u, normalized to GAPDH (n = 3 biological replicates). Error bars represent mean ± SEM. Student’s t-test was performed for b and one-way ANOVA was performed for d and f. Significance is indicated with *p < 0.05 and **p < 0.01CC BY · PubMed Central

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“American Type Culture Collection (ATCC) murine C2C12 myoblasts (Yaffe and Saxel, 1977)40 were maintained in proliferation medium, consisting of Dulbecco’s modified Eagle’s medium (DMEM) (Invitrogen, Carlsbad, CA, USA), 10% fetal bovine serum (HyClone, Thermo Scientific, USA), and 1% penicillin/…”
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Rommel, C., Bodine, S. C., Clarke, B. A., Rossman, R., Nunez, L., Stitt, T. N., Yancopoulos, G. D., & Glass, D. J. (2001) · Nature Cell Biology · doi:10.1038/ncb1101-1009 · Cited by 1,583
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Huh, J. Y., Panagiotou, G., Mougios, V., Brinkoetter, M., Vamvini, M. T., Schneider, B. E., & Mantzoros, C. S. (2012) · Metabolism · doi:10.1016/j.metabol.2012.09.002 · Cited by 1,040
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Handgrip strength is associated with cognitive function in older patients with stage 3-5 chronic kidney disease: results from the NHANES
Zhang, J., Wang, P., Pang, Q., Wang, S., & Zhang, A. (2024) · Scientific Reports · doi:10.1038/s41598-024-60869-y · Cited by 9
“Skeletal muscle exercise induces expression of the myokine irisin, which linked to skeletal muscle mass and strength 32,33 .”
Background
Irisin promotes tilapia muscle cell growth and amino acid uptake via IGF-1 signaling
Deng, W., Xu, M., Dong, R., Yan, Y., & Jiang, Q. (2024) · Journal of Endocrinology · doi:10.1530/joe-24-0122 · Cited by 5
Exploring the Impact of Astaxanthin Supplementation in Conjunction with a 12-Week CrossFit Training Regimen on Selected Adipo-Myokines Levels in Obese Males
Moqaddam, M. A., Nemati, M., Dara, M. M., Hoteit, M., Sadek, Z., Ramezani, A., Rand, M. K., Daloii, A. A., Pashaei, Z., Almaqhawi, A., et al. (2024) · Nutrients · doi:10.3390/nu16172857 · Cited by 5
“Additionally, this 12-week exercise training supplemented with AST resulted in divergent findings in adipo-myokiness such that the plasma levels of DNC and FST were elevated while three members of the TGF-β family including activin A, MST, and TGF-β 1 were diminished.”
Method
Systemic effect of combined functional overload and endurance-type swimming exercise on whole body metabolism in mice
Shirai, T., Uemichi, K., Iwai, R., Shinkai, H., Iwata, T., Tanimura, R., Sugiyama, S., & Takemasa, T. (2025) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00433.2024 · Cited by 6
Elevated Expression of ADAM10 in Skeletal Muscle of Patients with Idiopathic Inflammatory Myopathies Could Be Responsible for FNDC5/Irisin Unbalance
Zerlotin, R., Fornaro, M., Errede, M., Pignataro, P., Suriano, C., Ruggieri, M., Colucci, S. C., Iannone, F., Grano, M., & Colaianni, G. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24032469 · Cited by 5
“and plays a pro-myogenic role by rescuing denervation-induced atrophy [36].”
Background
Serum Irisin Levels Are Positively Correlated with Physical Activity Capacity in Hemodialysis Patients
Fan, Z., Wu, F., Wang, P., Wu, L., Zhang, J., Li, W., Pang, Q., & Zhang, A. (2025) · Kidney & Blood Pressure Research · doi:10.1159/000543214 · Cited by 4
“In addition, irisin injection reportedly induces skeletal muscle hypertrophy and enhances the regenerative capacity of skeletal muscles after muscle injury [28].”
Neuromuscular and biochemical responses of the hamstrings to a Flywheel Russian belt Deadlift in women and men
Cosio, P. L., Moreno-Simonet, L., Mechó, S., Foix, X. D. B., Lloret, M., Padullés, X., Padulles, J. M., Farrán-Codina, A., Rodas, G., & Cadefau, J. A. (2025) · Journal of Sports Sciences · doi:10.1080/02640414.2025.2461939 · Cited by 4
“…protection against inflammation, oxidative and apoptosis processes (Askari et al., 2018), but also plays a key role in musculoskeletal disorders by upregulating the expression of pro-myogenic factors, stimulating satellite cell activation and ameliorating protein degradation (Reza et al., 2017).”
Exercise-induced myokines in metabolic regulation: mechanisms, mimetics, and translational potential
Aslam, M. A., Lee, J., Bowen, T. S., & Huh, J. Y. (2026) · Archives of Pharmacal Research · doi:10.1007/s12272-026-01624-x · Cited by 7
“…FNDC5/irisin is enriched in slow-twitch fibers and early myogenesis, participating in a positive regulatory loop involving PGC1α during myogenic differentiation (Lavi et al. 2022), and promotes muscle growth through IL-6-mediated myoblast differentiation, fusion, and hypertrophy (Reza et al. 2017).”
Androgen action on myogenesis throughout the lifespan; comparison with neurogenesis
Barsky, S. T., & Monks, D. A. (2023) · Frontiers in Neuroendocrinology · doi:10.1016/j.yfrne.2023.101101 · Cited by 6
Loss of Myostatin Shapes the Transcriptomic and Epigenetic Landscapes Across Multiple Muscle Types in Cattle
Hai, C., Liu, X., Bai, C., Su, G., Yang, L., & Li, G. (2025) · Current Issues in Molecular Biology · doi:10.3390/cimb47060431 · Cited by 4
Upregulation of CCL5/RANTES Gene Expression in the Diaphragm of Mice with Cholestatic Liver Disease
Morales, V., González, A., & Cabello‐Verrugio, C. (2023) · Advances in experimental medicine and biology · doi:10.1007/978-3-031-26163-3_11 · Cited by 4
Impact of Human Recombinant Irisin on Tissue-Engineered Skeletal Muscle Structure and Function
Nguyen, M. H., Kennedy, C. S., Wroblewski, O. M., Su, E. Y., Hwang, D. H., & Larkin, L. M. (2023) · Tissue Engineering Part A · doi:10.1089/ten.tea.2023.0187 · Cited by 4
“24,25 Speciﬁcally, Sat3 has been shown to be a component of the skeletal muscle repair pathway.”
Research Progress on the Effects of Different Exercise Modes on the Secretion of Exerkines After Spinal Cord Injury
Li, Q., Li, C., & Zhang, X. (2024) · Cellular and molecular neurobiology · doi:10.1007/s10571-024-01497-y · Cited by 5
“Irisin has been shown to function in an autocrine manner to promote skeletal muscle hypertrophy and rescue denervation-induced muscle atrophy (Reza et al., 2017b).”
Background
Myokines: A potential key factor in development, treatment, and biomarker of sarcopenia
Aoi, W. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-822146-4.00006-5 · Cited by 4
Mild heat stimulation facilitates muscle hypertrophy in C2C12 and mouse satellite cells through myokine release to the culture medium
Hayashi, S., & Yonekura, S. (2022) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2022.10.018 · Cited by 4
Expression analysis of irisin during different development stages of skeletal muscle in mice
Yan, Y., Ding, Y., Wen, P., Li, Y., Ge, Y., Ma, P., Yuan, J., Zhang, P., Zhu, Z., Luo, X., et al. (2022) · Gene Expression Patterns · doi:10.1016/j.gep.2022.119287 · Cited by 4
Comparison of the effectiveness of zero-profile device and plate cage construct in the treatment of one-level cervical disc degenerative disease combined with moderate to severe paraspinal muscle degeneration
Abudouaini, H., Xu, H., Yang, J.-S., Yi, M., Lin, K., & Wang, S. (2023) · Frontiers in Endocrinology · doi:10.3389/fendo.2023.1283795 · Cited by 4
From use of omics to systems biology: Identifying therapeutic targets for amyotrophic lateral sclerosis
Castelli, L. M., Vasta, R., Allen, S. P., Waller, R., Chiò, A., Traynor, B. J., & Kirby, J. (2024) · International review of neurobiology · doi:10.1016/bs.irn.2024.02.001 · Cited by 4
Pharmacological effects of denervated muscle atrophy due to metabolic imbalance in different periods
Qiu, J., CHANG, Y., LIANG, W., LIN, M., Xu, H., XU, W., ZHU, Q., ZHANG, H., & ZHANG, Z. (2023) · Biocell · doi:10.32604/biocell.2023.031043 · Cited by 3
Dual Roles of Adipose Tissue in Skeletal Muscle Regeneration: Pro‐Regenerative Versus Maladaptive
Lu, C., Lu, F., & Cai, J. (2026) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.70269 · Cited by 3
“Irisin, secreted by both muscle and adipose tissue, promotes regeneration and fibre growth by activating satellite cells and protein synthesis [37].”
Immunometabolic mechanisms of osteosarcopenic obesity: chronic inflammation, trained immunity, and systemic immune dysregulation
Jiang, H., Zhang, Y., Luo, Z., Tang, X., 赫一佑, & Hao, G. (2026) · Frontiers in Immunology · doi:10.3389/fimmu.2026.1808488 · Cited by 5
“Irisin, another exercise-responsive myokine, activates MuSCs and increases protein synthesis, promoting myogenesis and myoblast fusion by upregulating myogenic growth genes, thereby inducing hypertrophy and improving muscle regeneration (41).”
Spinal Irisin Gene Delivery Attenuates Burn Injury-Induced Muscle Atrophy by Promoting Axonal Myelination and Innervation of Neuromuscular Junctions
Wu, S., Lu, I., Yang, S., Hsieh, C.-F., Chai, C., Tai, M., & Huang, S. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232415899 · Cited by 3
“As a promyogenic factor, recombinant irisin rescues denervation-induced atrophy when intraperitoneally injected after notexin-induced neuronal damage [42].”
Background
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
Skeletal Muscle-Derived Stem Cell Transplantation Accelerates the Recovery of Peripheral Nerve Gap Injury under 50% and 100% Allogeneic Compatibility with the Swine Leucocyte Antigen
Tamaki, T., Natsume, T., Katoh, A., Shigenari, A., Shiina, T., Nakajima, N., Saito, K., Fukuzawa, T., Otake, M., Enya, S., et al. (2024) · Biomolecules · doi:10.3390/biom14080939 · Cited by 3
“However, denervation is a serious event for the motor system [42,43], and if not reinnervated, the downstream muscles might develop cord-like features.”
Background
Linking Circulating Irisin and Type 2 Diabetes: A Systematic Review and Meta‐Analysis
Aminov, E., Folan, P., & Pisconti, A. (2025) · JCSM Communications · doi:10.1002/rco2.70000 · Cited by 5
“Moreover, irisin rescues skeletal muscle atrophy in a model of muscle denervation [43], further stressing its importance as a myokine with both paracrine and autocrine activity.”
Impact of myokines on chronic liver diseases: exploring the effects of metabolic dysfunction-associated steatotic liver disease (MASLD) on skeletal muscle. A narrative review
Aguirre, F. S., Valero‐Breton, M., Cabrera, D., Peñailillo, L., Otero, C., Fredes, C., & Cabello‐Verrugio, C. (2025) · European Journal of Translational Myology · doi:10.4081/ejtm.2025.13365 · Cited by 4
“17,80 The expression and secretion of Irisin from skeletal muscles have been debated in recent years due to inconsistencies in results regarding the levels of this myokine in response to exercise.”
Influential
Local and systemic transcriptomic responses from acute exercise induced muscle damage of the human knee extensors
Kirk, E. A., Castellani, C. A., Doherty, T. J., Rice, C. L., & Singh, S. M. (2022) · Physiological Genomics · doi:10.1152/physiolgenomics.00146.2021 · Cited by 3
Preconditioning intensive training ameliorates reduction of transcription biofactors of PGC1α-pathway in paretic muscle due to cerebral ischemia
Abbasian, S., Ravasi, A. A., Haghighi, A. H., Aydın, S., Delbari, A., & Aydın, S. (2022) · Biotechnic & Histochemistry · doi:10.1080/10520295.2022.2098535 · Cited by 4
“FNDC5/irisin participates in development of muscle hypertrophy, strength, and performance (Reza et al. 2017b; Planella-Farrugia et al. 2019).”
Background
Irisin; a myokine with therapeutic and diagnostic potential in clinical dentistry
Saleem, A., & Ghafoor, S. (2023) · Journal of the Pakistan Medical Association · doi:10.47391/jpma.8360 · Cited by 3
Novel Aspects of Follistatin/Transforming Growth Factor-β (TGF-β) Signaling in Adipose Tissue Metabolism: Implications in Metabolic Health
Pervin, S., Wilson, N. Y. A. H., Reddy, S. T., & Singh, R. (2019) · IntechOpen eBooks · doi:10.5772/intechopen.88294 · Cited by 3
Die parakrine und endokrine Funktion der Muskulatur
Heitkamp, H. (2023) · MMW - Fortschritte der Medizin · doi:10.1007/s15006-023-2493-z · Cited by 2
Enriched environment improves memory function by promoting synaptic remodeling in vascular dementia rats
Lin, S., Wang, C.-J., Yang, P., Li, B., Wu, Y., & Ya, K.-W. (2025) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2025.111262 · Cited by 2
“This transcriptional coactivator induces the expression of FNDC5, which, upon cleavage at the C-terminus, facilitates the release of irisin (Jodeiri Farshbaf et al., 2016; Reza et al., 2017).”
X-Linked Hypophosphatemia: Role of Fibroblast Growth Factor 23 on Human Skeletal Muscle-Derived Cells
Falsetti, I., Palmini, G., Donati, S., Aurilia, C., Zonefrati, R., di Filippo, L., Giustina, A., Giannini, S., Arcidiacono, G., Iantomasi, T., et al. (2025) · Calcified Tissue International · doi:10.1007/s00223-025-01415-4 · Cited by 2
Therapeutic Potential of Irisin in Neurodegenerative Diseases
Muzaffar, S., Tyagi, A., & Pugazhenthi, S. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms262311348 · Cited by 5
“In mice, irisin injection induces significant muscle hypertrophy and enhances grip strength in uninjured muscle, while also improving muscle regeneration and hypertrophy following skeletal muscle injury [46].”
Therapeutic potential of exerkines in neurodegenerative and mental disorders: a narrative review
Yang, S., Sang, H.-W., Kim, S., Cho, E., Choi, Y., Kang, D., Jang, Y. C., Park, D.-H., Kwak, H., & Yook, J. S. (2026) · Frontiers in Physiology · doi:10.3389/fphys.2026.1793043 · Cited by 2
Protective effects of irisin in sarcopenia: a promising treatment
Chen, Y., Li, G., Gao, F., Li, R., Yang, M., Ge, Y., & Wu, X. (2026) · Journal of Orthopaedic Translation · doi:10.1016/j.jot.2026.101090 · Cited by 2
“(1) upregulation of myogenic growth factors (2) stimulation of myoblast differentiation and fusion (3) promotion of muscle regeneration (4) induction of hypertrophy These effects of irisin may be due to activation of satellite cells and enhancement of protein synthesis [19].”
Influential
The crossroads between osteosarcopenia and intrinsic capacity—a narrative review
Neto, N. J., Hajj‐Boutros, G., Lok, W., Borda, M. G., Prokopidis, K., Rammal, H., Rivas, D., Samhat, H., Baltasar‐Fernandez, I., Imani, M., et al. (2026) · The Journals of Gerontology Series A · doi:10.1093/gerona/glag102 · Cited by 2
“228 229-231 These deficits are exacerbated by elevated catabolic cytokines and myokines, including myostatin, P3NP, TNF-α , IL-6, and CRP, which further impair force generation and accelerate functional decline.”
Influential
Bone, muscle, and sarcopenia
Beavers, K. M., Serra, M. C., Weaver, A. A., & Houston, D. K. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-813073-5.00035-6 · Cited by 3
Identification of Potential miRNA‐mRNA Regulatory Network in Denervated Muscular Atrophy by Bioinformatic Analysis
Wang, J., Liu, Y., Zhang, Y., Liu, B., & Wei, Z. (2022) · BioMed Research International · doi:10.1155/2022/6042591 · Cited by 2
“Skeletal muscle atrophy can lead to poor functional status, reduced quality of life, and adverse impacts on life prognosis in patients, placing a heavy burden on families and society [3, 4].”
Electrical Stimulation‐Induced Muscle Damage Alters Hippocampal BDNF Signaling
Wirtz, J., Chaney, R., Cefis, M., Méloux, A., Wang, Y., Lemaire‐Ewing, S., Quirié, A., Delezie, J., Gouspillou, G., Prigent‐Tessier, A., et al. (2025) · European Journal of Neuroscience · doi:10.1111/ejn.70235 · Cited by 1
A Pilot Study Investigating the Impact of High Altitude on Myostatin and Irisin Levels
Rathor, R., Suryakumar, G., & Singh, S. N. (2024) · Defence Life Science Journal · doi:10.14429/dlsj.9.19449 · Cited by 1
Construction, Purification, and Biological Characterization of Plant-Made Human Recombinant Irisin
Ma, E. B., Min, K., Park, M., Kang, H., Choi, B.-H., Sohn, E., & Huh, J. Y. (2024) · Drug Targets and Therapeutics · doi:10.58502/dtt.23.0019 · Cited by 1
Irisin: muscle’s novel player in endoplasmic reticulum stress and disease
Pinto, J. R., Bhat, K. D., Bose, B., & Sudheer Shenoy, P. (2025) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-025-05225-y · Cited by 1
“Reza et al. found that by stimulating IL-6 signalling in animals, irisin caused skeletal muscle hypertrophy and mitigated denervation-induced atrophy [72].”
Influential
Crustacean endocrinology
Mykles, D. L., Musgrove, L., & Ventura, T. (2025) · Elsevier eBooks · doi:10.1016/b978-0-323-95424-2.00009-1 · Cited by 1
miR-320-3p regulates apelin and TGF-β/SMAD3 signaling in hypobaric hypoxia exposed rats to induce skeletal muscle atrophy
Mondal, S., Srivastava, S., Srivastava, S., Rathor, R., & Suryakumar, G. (2025) · Journal of Physiology and Biochemistry · doi:10.1007/s13105-025-01100-y · Cited by 1
Evaluation of irisin levels in plasma, skeletal muscle, and brain tissues after voluntary or regular exercise in adolescent male rats exposed to chronic social isolation
Arslankiran, A., Demirtas, H., Açıkgöz, B., Dalkiran, B., Kıray, A., Aksu, İ., Kıray, M., & Dayı, A. (2025) · Biologia Futura · doi:10.1007/s42977-025-00287-x · Cited by 1
“Early studies on the autocrine role of irisin in muscle metabolism and hypertrophy demonstrated that irisin promotes myoblast fusion, stimulates genes associated with muscle growth, and contributes to muscle growth and hypertrophy in response to physical activity (Huh et al. 2014; Reza et al. 2017).”
Circulating Muscle Markers for Sarcopenia in Peritoneal Dialysis
Xu, L., Ng, J. K., Fung, W. W., Chan, G. C., Chow, K., & Szeto, C. (2025) · International Journal of Nephrology · doi:10.1155/ijne/8817404 · Cited by 2
“Irisin and insulin-like growth factor 1 (IGF-1) are pro-myogenic [38, 39]; reduction in these factors correlates with decreased muscle growth [40, 41].”
Design of debunking the frailty–sarcopenia–ADT axis in metastatic prostate cancer with multicomponent exercise: the FIERCE trial protocol
Wilson, R. L., Vulczak, A., Morgans, A. K., Norris, M. K., Greer, J., VOTTA, J. L., Vamvini, M. T., Einstein, D. J., Uno, H., Rosenthal, M. H., et al. (2025) · Frontiers in Sports and Active Living · doi:10.3389/fspor.2025.1602123 · Cited by 1
Myokine Levels in Relation to Bone Markers and Adipokines in Children with Prader–Willi Syndrome During Growth Hormone Therapy and Dietary Intervention
Gajewska, J., Chełchowska, M., Szamotulska, K., Strucińska, M., Klemarczyk, W., & Ambroszkiewicz, J. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms262210822 · Cited by 1
“It is known that irisin is an important pro-myogenic factor that stimulates genes related to muscle growth in humans and exerts a beneficial effect on glucose and lipid metabolism, ensuring the maintenance of homeostasis of the musculoskeletal system [23,27].”
Irisin regulates the phosphorylation of glucocorticoid receptor Ser212 and Ser234 and mediates glucocorticoid-induced muscle atrophy in mice
Yang, J., Zhang, P., An, Y., Tan, S., Sun, S., Liu, Y., Zhu, L., Wang, H., Gao, T., & Dong, Y. (2025) · Communications Biology · doi:10.1038/s42003-025-09203-4 · Cited by 2
“Other studies have demonstrated that irisin signi ﬁ cantly inhibits MuRF-1 and Atrogin-1 protein levels in differentiated myotubes 34 .”
Influential
GABA induces myokine irisin release from skeletal muscle
Fan, L., Liao, Y., WANG, Z., Ni, Y., CUI, Q., Wang, Y., Zhang, L., Ye, H., Sun, X., Li, Y., et al. (2026) · Life Sciences · doi:10.1016/j.lfs.2025.124181 · Cited by 1
Exercise modality–dependent non-hypertrophic anabolic adaptations in skeletal muscle of rats with type 2 diabetes
Zhang, Y.-D., Zhao, X.-X., & Liu, X. (2026) · Frontiers in Physiology · doi:10.3389/fphys.2026.1773632 · Cited by 1
“Experimental studies further suggest that irisin may exert pro-myogenic or anti-atrophic effects under certain pathological conditions (Reza et al., 2017).”
Integrin αVβ5 regulates myoblast proliferation and differentiation in sarcopenia mice treated with FNDC5 gene delivery
Gao, G., Wang, Q., Zhang, Y., Shao, M., Liang, Y., Zhou, S., & Lu, S. (2026) · Skeletal Muscle · doi:10.1186/s13395-026-00420-x · Cited by 1
“Although many studies have shown that the product of FNDC5 gene, irisin promotes myogenic differentiation of C2C12 myoblasts [8, 22], the long-term therapeutic application involving FNDC5 gene delivery in C2C12 cells is still limited.”
Crosstalk in the kidney-muscle axis: myokines and muscle-relevant mediators in chronic kidney disease-associated sarcopenia
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
“Experimental work suggested that irisin can promote myogenesis and muscle protein synthesis while reducing protein breakdown, thereby attenuating muscle atrophy [100].”
Role of Kidney Injury Molecule-1 Expression, Wnt Proteins (Beta- catenin) and Endogenous Irisin in a Rat Model of Renal fibrosis: Renoprotective Effect of Metformin
Mohamed, M., & Eladl, A. K. (2020) · Bulletin of Egyptian Society for Physiological Sciences · doi:10.21608/besps.2020.30771.1062 · Cited by 1
Prospective effects of cholecalciferol supplementation on irisin levels in sedentary postmenopausal women: A pilot study
Aquila, L. P. D., Morales, A., Moreira, P., Cendoroglo, M. S., Elias, R. M., & Dalboni, M. A. (2023) · Journal of Clinical & Translational Endocrinology · doi:10.1016/j.jcte.2023.100324 · Cited by 1
Correlation of sarcopenia and depression: common risk factors and pathogenetic mechanisms
Мамутовна, М. Э., Yafarova, A. A., Sheptulina, A. F., Yakovleva, P. O., & Drapkina, O. M. (2023) · Russian Journal of Preventive Medicine · doi:10.17116/profmed20232611157 · Cited by 1
Role of irisin in physical activity, sarcopenia-associated type 2 diabetes, and cardiovascular complications
Berković, M. C., Cigrovski, V., & Ružić, L. (2025) · World Journal of Methodology · doi:10.5662/wjm.v15.i4.105462 · Cited by 4
“In rodent models, irisin's myogenic role was shown through the induction of skeletal muscle hypertrophy and at the same time attenuation of atrophy by activating interleukin (IL)-6, satellite cells, and protein synthesis[23].”
Potential Role of Novel Myokine in Rats-Induced Metabolic Syndrome
(2021) · Biointerface Research in Applied Chemistry · doi:10.33263/briac123.33053315 · Cited by 1
Effect of Creatine Supplementation on the Muscular Inflammation and Muscle Atrophy in High-Fat High-Fructose Fed Obese Growing Rats
Oh, S. (2022) · International Journal of Biomedical Investigation · doi:10.31531/2581-4745.1000139
“[33] reported that irisin induced skeletal muscle hypertrophy and attenuated denervationinduced muscle atrophy by IL-6 signaling in rodents and these effects due to activation of muscle satellite cells and elevation of protein synthesis.”
Background
Irisin recovers osteoarthritic chondrocytes: a muscle-cartilage cross-talk boosted by physical activityPreprint
Vadalà, G., Giacomo, G. D., Ambrosio, L., Cannata, F., Cicione, C., Papalia, R., & Denaro, V. (2020) · doi:10.21203/rs.3.rs-20856/v1 · Cited by 1
Biomechanical Stimulation of Muscles Influences Bone Phenotype by Modulating Myokine SecretionPreprint
Kumar, H. S., Barnett, E. N., Kalaitzoglou, E., Fowlkes, J. L., & Annamalai, R. T. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.10.05.510953 · Cited by 1
Are circulating levels of the myokine irisin linked to type 2 diabetes? A systematic review and meta-analysisPreprint
Aminov, E., Folan, P., & Pisconti, A. (2024) · bioRxiv · doi:10.1101/2024.06.29.601052 · Cited by 2
“Moreover, irisin rescues skeletal muscle atrophy in a model of muscle denervation (Reza et al., 2017), further stressing its importance as a myokine with both paracrine and autocrine activity.”
Background
Nuclear localized Akt limits skeletal muscle derived fibrotic signaling
Guadagnin, E., Bagchi, D., Sinha, I., & Neppl, R. L. (2018) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2018.11.202
Acute and chronic effects of exercise on irisin in healthy adults
Jafari, M., & Ravasi, A. A. (2021) · فصلنامه علوم پزشکی دانشگاه آزاد اسلامی واحد پزشکی تهران · doi:10.52547/iau.31.2.135
Identification of Potential miRNA-mRNA Regulatory Network in Denervated Muscular Atrophy by Bioinformatics AnalysisPreprint
Wang, J., Liu, Y., Zhang, Y., Liu, B., & Wei, Z. (2021) · Research Square · doi:10.21203/rs.3.rs-864617/v1
Expression Analysis of Irisin During Different Differentiation Stages of Skeletal Muscle CellsPreprint
Yan, Y., Yang, D. C., Wen, P., Li, Y., Ge, Y., Ma, P., Yuan, J., Zhang, P., Zhu, Z., Luo, X., et al. (2021) · Research Square · doi:10.21203/rs.3.rs-1021410/v1
“and insulin resistance(12-15), but also plays a key role in metabolic regulation such as inflammation, hippocampal neurogenesis, and senescence(6).”
Background
Faculty Opinions recommendation of Origin and Function of Stress-Induced IL-6 in Murine Models.
Lynch, L. (2021) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.738227474.793583818
Irisin/FNDC5: A Novel Player in Musculoskeletal Health
(2020) · Journal of Human Physiology · doi:10.31829/2691-5391/jhp2020-3(1)-107
Identification of Potential miRNA-mRNA Regulatory Network in Denervated Muscular Atrophy by Bioinformatics AnalysisPreprint
Wang, J., Liu, Y., Zhang, Y., Liu, B., & Wei, Z. (2022) · Research Square · doi:10.21203/rs.3.rs-864617/v3
Identification of Potential miRNA-mRNA Regulatory Network in Denervated Muscular Atrophy by Bioinformatics AnalysisPreprint
Wang, J., Liu, Y., Zhang, Y., Liu, B., & Wei, Z. (2021) · Research Square · doi:10.21203/rs.3.rs-864617/v2
Muscle Hormones
Rodríguez, A. M., Bonet, M. L., & Ribot, J. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-813814-4.00026-2
A Traditional Review of the Slimming Myokine: Current Approaches to FNDC5/Irisin
Altay, D. U. (2022) · Turkiye Klinikleri Journal of Medical Sciences · doi:10.5336/medsci.2022-89253
Obesity, inflammation and muscle weakness
Hasselgren, P.-O. J. (2022) · Elsevier eBooks · doi:10.1016/b978-0-323-90960-0.00014-x · Cited by 1
Salivary and serum irisin in healthy adults before and after exercise
Missaglia, S., Tommasini, E., Vago, P., Pecci, C., Galvani, C., Silvestrini, A., Mordente, A., & Tavian, D. (2023) · European Journal of Translational Myology · doi:10.4081/ejtm.2022.11093

Authors: Reza, M. M., Subramaniyam, N., Sim, C. M., Ge, X., Sathiakumar, D., McFarlane, C., Sharma, M., & Kambadur, R.
Affiliations: Nanyang Technological University (SG)
Agency for Science, Technology and Research (SG)
National University of Singapore (SG)
Corresponding author: Kambadur, Ravi
ORCID: Reza, Musarrat Maisha
McFarlane, Craig
Venue: Nature Communications
Publisher: Springer Science and Business Media LLC
Published: 2017-10-24
Volume: 8
Issue: 1
Pages: 1104-1104
ISSN: 2041-1723 (ISSN-L)
DOI: 10.1038/s41467-017-01131-0
PMC: PMC5653663
OpenAlex: W2765141291
Cited by: 335
References: 43
Citations by year: 2026: 33 · 2025: 50 · 2024: 47 · 2023: 48 · 2022: 54 · 2021: 37 · 2020: 29 · 2019: 27 · 2018: 9 · 2017: 1
FWCI: 7.38
Type: journal article
Language: en
Open access: gold
doi.org
Licence: cc-by
creativecommons.org/licenses/by/4.0 (tdm)
creativecommons.org/licenses/by/4.0 (vor)
Locations: Nature Communications (publishedVersion, cc-by)
PubMed Central (publishedVersion, cc-by)
PubMed (publishedVersion)
UEA Digital Repository (University of East Anglia) (acceptedVersion)
ResearchOnline - JCU (James Cook University) (submittedVersion)
RePEc: Research Papers in Economics (submittedVersion)
DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
DR-NTU (Nanyang Technological University) (submittedVersion, cc-by)
Funders: Agency for Science, Technology and Research
Nanyang Technological University
Medical Research Council
National Medical Research Council
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
Health Sciences › Medicine › Physiology (medical) › Exercise and Physiological Responses
Health Sciences › Nursing › Nutrition and Dietetics › Muscle metabolism and nutrition
Keywords: irisin, myokines, skeletal muscle hypertrophy, denervation-induced atrophy, satellite cells, myogenesis, myoblast fusion, IL-6 signaling, muscle regeneration, skeletal muscle injury, protein synthesis, protein degradation
MeSH terms: Animals, Atrophy, Denervation, Fibronectins, Humans, Hypertrophy, Male, Mice, Inbred C57BL, Stem Cells, Interleukin-6, Muscle, Skeletal, Muscle Fibers, Skeletal, Muscle Development, Mice, Adipose Tissue, White

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Irisin is a pro-myogenic factor that induces skeletal muscle hypertrophy and rescues denervation-induced atrophy

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