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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High concentration of sodium fluoride in drinking water induce hypertrophy versus atrophy in mouse skeletal muscle via modulation of sarcomeric proteins
Nagendra, A. H., Najar, M. A., Bose, B., & Sudheer Shenoy, P. (2022) · Journal of Hazardous Materials · doi:10.1016/j.jhazmat.2022.128654 · Cited by 18
Sesamin Activates Skeletal Muscle FNDC5 Expression and Increases Irisin Secretion via the SIRT1 Signaling Pathway.
Kou, G.-N., Li, P., Shi, Y., Traore, S. S., Shi, X.-Y., Amoah, A., Cui, Z., & Lyu, Q. (2022) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.2c02794 · Cited by 17
Natural constituents from food sources: potential therapeutic agents against muscle wasting
Shen, S., Yu, H., Gan, L., Yang, Y., & Lin, L. (2019) · Food & Function · doi:10.1039/c9fo00912d · Cited by 20
Irisin in degenerative musculoskeletal diseases: Functions in system and potential in therapy
Wang, Y.-T., Zheng, S., Jiang, S., Luo, Y., Wu, Y., Naranmandakh, S., Li, Y., Liu, S.-G., & Xiao, W. (2024) · Pharmacological Research · doi:10.1016/j.phrs.2024.107480 · Cited by 21
Circulating irisin levels in patients with sarcopenia: a systematic review and meta-analysis
Zhang, L., Peng, Y., Kong, Y., Zhang, X., Li, Z., & Jia, H. (2024) · European Geriatric Medicine · doi:10.1007/s41999-024-01097-5 · Cited by 17
Football (soccer) match-derived hamstring muscles residual fatigue can be monitored using early rate of torque development
Cosio, P. L., Moreno-Simonet, L., Fernández, D., Lloret, M., Padullés, X., Padulles, J. M., Farrán-Codina, A., Rodas, G., & Cadefau, J. A. (2024) · European Journal of Applied Physiology · doi:10.1007/s00421-024-05694-x · Cited by 16
“…according to manufacturer’s instruction (intra-assay variability <10%; inter-assay variability <15%), owing to its protective effect against inflammatory and oxidative processes (Askari et al. 2018; Trettel et al. 2023) and promotion of muscle regeneration (Reza et al. 2017; Zhang et al. 2023).”
Exercise-mitigated sex-based differences in aging: from genetic alterations to heart performance
Börzsei, D., Priksz, D., Szabó, R., Bombicz, M., Karácsonyi, Z., Puskás, L. G., Fehér, L. Z., Radak, Z. O., Kupai, K., Berkó, A. M., et al. (2020) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00643.2020 · Cited by 16
Effects of marathon race on selected myokines and sclerostin in middle-aged male amateur runners
Śliwicka, E., Cisoń, T., Pilaczyńska-Szczȩśniak, Ł., Ziemba, A. W., & Straburzyńska‐Lupa, A. (2021) · Scientific Reports · doi:10.1038/s41598-021-82288-z · Cited by 19
An oleanolic acid derivative reduces denervation-induced muscle atrophy via activation of CNTF-mediated JAK2/STAT3 signaling pathway
Cui, W., Liu, C., Wang, J., Zhang, Y., Shen, Q., Feng, Z., Wu, J., & Li, J. (2019) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2019.172612 · Cited by 16
Adipose-derived exosomes ameliorate skeletal muscle atrophy via miR-146a-5p/IGF-1R signaling
Qin, M., Zhu, J., Xing, L., Fan, Y., Luo, J., Sun, J., Chen, T., Zhang, Y., & Xi, Q. (2024) · Journal of Nanobiotechnology · doi:10.1186/s12951-024-02983-7 · Cited by 22
Methyltransferase‐like 21e inhibits 26S proteasome activity to facilitate hypertrophy of type IIb myofibers
Wang, C., Zhang, B., Ratliff, A. C., Arlington, J., Chen, J., Xiong, Y., Yue, F., Nie, Y., Hu, K., Jin, W. L., et al. (2019) · The FASEB Journal · doi:10.1096/fj.201900582r · Cited by 16
“Myofiber size may be regulated at both cellular (myogenic differentiation and myoblast fusion) (46) and molecular (protein synthesis anddegradation) level.”
Background
Transcriptome sequencing and analysis reveals the molecular mechanism of skeletal muscle atrophy induced by denervation
Chen, X., Li, M., Chen, B., Wang, W., Zhang, L., Ji, Y., Chen, Z., Ni, X., Shen, Y., & Sun, H. (2021) · Annals of Translational Medicine · doi:10.21037/atm-21-1230 · Cited by 14
“Peripheral nerve injury leads to the loss of innervation of skeletal muscle, and then the loss of signal transmission and material exchange with nerves, resulting in a series of pathological changes, such as the reduction of cross-sectional area of muscle fibers, destruction of myofilaments and sarcomeres, degradation…”
Background
Myokine Response to Blood-Flow Restricted Resistance Exercise in Younger and Older Males in an Untrained and Resistance-Trained State: A Pilot Study
Cordingley, D. M., Anderson, J. E., & Cornish, S. M. (2022) · Journal of Science in Sport and Exercise · doi:10.1007/s42978-022-00164-2 · Cited by 18
“Although primarily known for the “browning” of white adipose tissue [78], irisin also promotes muscle hypertrophy [72] by upregulating expression of insulin-like growth factor-1 (IGF-1), down-regulating myostatin expression [41], and increasing satellite cell activation, myoblast proliferation, and myotube formation […”
Background
Crosstalk between bone and muscle in chronic kidney disease
Wong, L., & McMahon, L. P. (2023) · Frontiers in Endocrinology · doi:10.3389/fendo.2023.1146868 · Cited by 15
“Higher expression of tumour necrosis factor-alpha (TNF-a) and IL-6 were observed in the muscle of CKD patients and mice compared to healthy controls and were associated with the development of muscle atrophy (19).”
BackgroundInfluential
Irisin Protects against Loss of Trabecular Bone Mass and Strength in Adult Ovariectomized Mice by Stimulating Osteoblast Activity
Storlino, G., Dicarlo, M., Zerlotin, R., Pignataro, P., Sanesi, L., Suriano, C., Oranger, A., Mori, G., Passeri, G., Colucci, S. C., et al. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24129896 · Cited by 15
“Of note, as already demonstrated by other authors in a mouse model of denervation-induced atrophy [33], we showed here that haptoglobin, which promotes skeletal muscle hypertrophy, was significantly upregulated by irisin treatment in the ovx mouse model.”
BackgroundResult
Revisiting Skeletal Muscle Dysfunction and Exercise in Chronic Obstructive Pulmonary Disease: Emerging Significance of Myokines
Han, L., Li, P., He, Q., Yang, C. G., Jiang, M., Wang, Y., Cao, Y., Han, X., Liu, X., & Wu, W. (2023) · Aging and Disease · doi:10.14336/ad.2023.1125 · Cited by 17
MyoV: a deep learning-based tool for the automated quantification of muscle fibers
Gu, S., Wen, C., Xiao, Z., Huang, Q., Jiang, Z., Liu, H., Gao, J., Li, J., Sun, C., & Yang, N. (2023) · Briefings in Bioinformatics · doi:10.1093/bib/bbad528 · Cited by 15
“Muscle fibers are elongated, multinucleated cells originating from the fusion of numerous mononucleated muscle precursor cells known as myoblasts during embryonic and fetal development [11–13].”
Background
The role and underlying mechanisms of irisin in exercise-mediated cardiovascular protection
Guo, W., Peng, J., Su, J., Xia, J., Deng, W., Li, P., Chen, Y., Liu, G., Wang, S., & Huang, J. (2024) · PeerJ · doi:10.7717/peerj.18413 · Cited by 18
Molecular targets of exercise mimetics and their natural activators
Jang, Y. J., & Byun, S. (2021) · BMB Reports · doi:10.5483/bmbrep.2021.54.12.151 · Cited by 17
“The level of irisin positively correlates with muscle mass and muscle strength (19) and injection of irisin rescues denervation-induced loss of skeletal muscle mass by enhancing satellite cell activation and reducing protein degradation (22).”
Background
Proteoglycan Extracted from Ganoderma lucidum Ameliorated Diabetes-Induced Muscle Atrophy via the AMPK/SIRT1 Pathway In Vivo and In Vitro
Li, J., Zhang, Y., Yu, F., Pan, Y., Zhang, Z., He, Y., Yang, H., & Zhou, P. (2023) · ACS Omega · doi:10.1021/acsomega.3c03513 · Cited by 14
Exerkines and myokines in aging sarcopenia
Wang, H., He, W., Chen, P., Wang, H., Wang, H., Zhu, L., & Liu, X. (2025) · Frontiers in Endocrinology · doi:10.3389/fendo.2025.1592491 · Cited by 20
Irisin/FNDC5 influences myogenic markers on skeletal muscle following high and moderate-intensity exercise training in STZ-diabetic rats
Arabzadeh, E., Shirvani, H., Zahmatkesh, M. E., Malayeri, S. R., Meftahi, G. H., & Rostamkhani, F. (2022) · 3 Biotech · doi:10.1007/s13205-022-03253-9 · Cited by 14
Skeletal Muscle Myokine Expression in Critical Illness, Association With Outcome and Impact of Therapeutic Interventions
Vanhorebeek, I., Gunst, J., Casaer, M. P., Derese, I., Derde, S., Pauwels, L., Segers, J., Hermans, G., Gosselink, R., & den Berghe, G. V. (2023) · Journal of the Endocrine Society · doi:10.1210/jendso/bvad001 · Cited by 18
“Indeed, this treatment induced significant hypertrophy and enhanced grip strength of uninjured muscle, improved regeneration and rescued loss of muscle mass of denervation-induced injured muscle, and showed beneficial effects in hind limb ischemia–reperfusion injury [44, 45].”
RBM4a modulates the impact of PRDM16 on development of brown adipocytes through an alternative splicing mechanism
Chi, Y.-L., & Lin, J.-C. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2018.08.001 · Cited by 14
The association between sarcopenia and decorin, an exercise‐induced myokine, in patients with liver cirrhosis: a pilot study
Bekki, M., Hashida, R., Kawaguchi, T., Goshima, N., Yoshiyama, T., Otsuka, T., Koya, S., Hirota, K., Matsuse, H., Niizeki, T., et al. (2018) · JCSM Rapid Communications · doi:10.1002/j.2617-1619.2018.tb00009.x · Cited by 14
Therapeutic Targets in Amyotrophic Lateral Sclerosis: Focus on Ion Channels and Skeletal Muscle
Tarantino, N., Canfora, I., Camerino, G. M., & Pierno, S. (2022) · Cells · doi:10.3390/cells11030415 · Cited by 14
The role of irisin in exercise-induced muscle and metabolic health: a narrative review
Mohammed, S. N., Jasim, M. H., Mahmood, S. H., Saleh, E. N., & Hashemzadeh, A. (2025) · Naunyn-Schmiedeberg s Archives of Pharmacology · doi:10.1007/s00210-025-04083-1 · Cited by 13
“These effects collectively support muscle hypertrophy and strength, which can enhance functional capacity and physical performance (Reza et al. 2017).”
Influential
HIF-1α Negatively Regulates Irisin Expression Which Involves in Muscle Atrophy Induced by Hypoxia
Liu, S., Fu, P., Ning, K., Wang, R., Yang, B., Chen, J., & Xu, H. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23020887 · Cited by 14
“have found that irisin increases myogenic differentiation and myoblast fusion by activating IL-6 signaling and further improves injured skeletal muscle by promoting protein synthesis [15].”
Background
The Cellular and Molecular Signature of ALS in Muscle
Anakor, E., Duddy, W. J., & Duguez, S. (2022) · Journal of Personalized Medicine · doi:10.3390/jpm12111868 · Cited by 14
“Other examples of muscle secreted factors important for NMJ stabilization and dysregulated in ALS animal models and patients include: Insulin Like Growth Factor-1 (IGF-1) [137–140] or Glial-Cell-Line-Derived Neurotrophic Factor (GDNF) [141–145], Irisin [146] and Brain-Derived Neurotrophic Factor (BDNF) [138,147].”
Background
Effects of high-intensity interval training (HIIT) on skeletal muscle atrophy, function, and myokine profile in diabetic myopathy
Özçatal, Y., Akat, F., Tatar, Y., Fıçıcılar, H., Serdaroğlu, B., Çelikkan, F. T., & Baştuğ, M. (2023) · Cytokine · doi:10.1016/j.cyto.2023.156279 · Cited by 14
Targeting Crosstalk of Signaling Pathways among Muscles-Bone-Adipose Tissue: A Promising Therapeutic Approach for Sarcopenia
Sharma, A. R., Chatterjee, S., Lee, Y., & Lee, S. (2023) · Aging and Disease · doi:10.14336/ad.2023.00903 · Cited by 15
“Furthermore, introducing irisin in mice models also explicated irisin's capacity to induce muscle hypertrophy by the IGF-1/mTOR/Akt pathway, which simultaneously activates the synthesis of the muscle proteins [98].”
Background
Assessment of inter-individual variability in hamstring muscle recovery after a sport-specific sprint training in women and men
Cosio, P. L., Moreno-Simonet, L., Porcelli, A., Lloret, M., Padullés, X., Padulles, J. M., Farrán-Codina, A., & Cadefau, J. A. (2024) · Frontiers in Physiology · doi:10.3389/fphys.2023.1331878 · Cited by 13
Roles of Myokines and Muscle-Derived Extracellular Vesicles in Musculoskeletal Deterioration under Disuse Conditions
Zhang, J., Gao, Y., & Yan, J. (2024) · Metabolites · doi:10.3390/metabo14020088 · Cited by 15
“…myoblast proliferation and fusion [13], maintains muscle protein balance by down-regulating protein degradation and up-regulating protein synthesis [12], stimulates muscle growth by up-regulating the mRNA expression of myokines that play positive roles in skeletal muscles, such as insulin-like…”
Background
Myokines as potential mediators of changes in glucose homeostasis and muscle mass after bariatric surgery
Orioli, L., & Thissen, J. (2025) · Frontiers in Endocrinology · doi:10.3389/fendo.2025.1554617 · Cited by 17
Mst1/2 Is Necessary for Satellite Cell Differentiation to Promote Muscle Regeneration
Yang, J., Wang, K., An, Y., Wu, R., Li, J., Wang, H., & Dong, Y. (2021) · Stem Cells · doi:10.1093/stmcls/sxab010 · Cited by 13
Fndc5/irisin is regulated by myogenesis stage, irisin, muscle type and training.
Lavi, G., Horwitz, A., Einstein, O., Zipori, R., Gross, O., & Birk, R. Z. (2022) · PubMed Central · Cited by 13
Systematic Review and Meta-Analysis of Circulating Irisin Levels Following Endurance Training: Results of Continuous and Interval Training
Cosio, P. L., Peláez, M., Cadefau, J. A., & Farrán-Codina, A. (2022) · Biological Research For Nursing · doi:10.1177/10998004221142580 · Cited by 13
“Likewise, irisin has been shown to be a potent inducer of IL-6 (Reza et al., 2017), and since both myokines are released in response to muscle contraction, it is suggested that both feeds back into each other during exercise.”
BackgroundInfluential
A novel oleanolic acid derivative HA-19 ameliorates muscle atrophy via promoting protein synthesis and preventing protein degradation
Cui, W., Liu, C., Zhang, Y., Shen, Q., Feng, Z., Wang, J., Lu, S.-F., Wu, J., & Li, J. (2019) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2019.114625 · Cited by 13
Serum Irisin Level Is Positively Associated with Bone Mineral Density in Patients on Maintenance Hemodialysis
Lu, C., Wang, C., Lin, Y., Kuo, C., Lai, Y.-H., Hsu, B., & Tsai, J. (2021) · International Journal of Endocrinology · doi:10.1155/2021/8890042 · Cited by 13
“Irisin, a newly discovered myokine, which is cleaved from the precursor fibronectin type III domain-containing 5 (FNDC5), is primarily known for its modulatory role in phenotypic changes of white adipose tissue to brown adipose tissue to increase energy expenditure and improve glucose homeostasis; irisin also activate…”
Background
Muscles proteome analysis; irisin administration mimics some molecular effects of exercise in quadriceps muscle
Momenzadeh, S., Zamani, S., Tabrizi, Z. P. F., Barreiro, C., & Jami, M. (2021) · Biochimie · doi:10.1016/j.biochi.2021.06.016 · Cited by 14
Irisin-loaded electrospun core-shell nanofibers as calvarial periosteum accelerate vascularized bone regeneration by activating the mitochondrial SIRT3 pathway
Hua, X., Hou, M., Deng, L., Lv, N., Xu, Y. X., Zhu, X., Yang, H., Shi, Q., Liu, H., & He, F. (2023) · Regenerative Biomaterials · doi:10.1093/rb/rbad096 · Cited by 12
“These effects are achieved through the activation of myogenic differentiation in muscle-derived satellite stem cells and the prevention of myotube-related protein degradation [18].”
Background
Role of irisin and myostatin on sarcopenia in malnourished patients diagnosed with GLIM criteria.
de Luis, D., Primo, D., Izaola, O., & Gomez, J. J. L. (2023) · Nutrition (Burbank, Los Angeles County, Calif.) · doi:10.1016/j.nut.2023.112348 · Cited by 13
Poor bone health in Duchenne muscular dystrophy: a multifactorial problem beyond corticosteroids and loss of ambulation
Hurley-Novatny, A. C., Chang, D., Murakami, K., Wang, L., & Li, H. (2024) · Frontiers in Endocrinology · doi:10.3389/fendo.2024.1398050 · Cited by 17
Variations in Irisin, Bone Mineral Density, Bone Mineral Content, and Body Composition After Laparoscopic Bariatric Procedures in Obese Adults
Lu, C., Li, Z., Yang, J., Feng, L., Wang, C., & Shi, Q. (2019) · Journal of Clinical Densitometry · doi:10.1016/j.jocd.2019.05.002 · Cited by 12
High-velocity resistance training improves executive function in mobility-limited older adults
Feter, N., Schaun, G. Z., Smith, E. C., Cassuriaga, J., Alt, R., Redig, L., Alberton, C. L., Coombes, J. S., & Rombaldi, A. J. (2023) · Archives of Gerontology and Geriatrics · doi:10.1016/j.archger.2023.105081 · Cited by 16
Oleanolic acid alleviates obesity‐induced skeletal muscle atrophy via the PI3K /Akt signaling pathway
Sun, Y., Wei, X., Zhao, T. M., Shi, H., Hao, X., Wang, Y., Zhang, H., Yao, Z., Zheng, M., Ma, T., et al. (2024) · FEBS Open Bio · doi:10.1002/2211-5463.13780 · Cited by 11
Differential mitochondrial adaptation and FNDC5 production in brown and white adipose tissue in response to cold and obesity
Neira, G., Hernández‐Pardos, A. W., Becerril, S., Ramírez, B., Valentí, V., Moncada, R., Catalán, V., Gómez‐Ambrosi, J., Burrell, M. A., Silva, C., et al. (2024) · Obesity · doi:10.1002/oby.24132 · Cited by 11
“FNDC5/irisin exerts autocrine and paracrine actions in skeletal myofibers, promoting myogenesis and inhibiting muscle atrophy [14, 15].”
Heat acclimation defense against exertional heat stroke by improving the function of preoptic TRPV1 neurons
Li, J., Zhou, Z., Wu, Y., Zhao, J., Duan, H.-K., Peng, Y., Wang, X., Fan, Z., Yin, L., Li, M., et al. (2024) · Theranostics · doi:10.7150/thno.101422 · Cited by 15
“Irisin might be an ideal therapeutic target for not only the metabolic disease by reducing diet-induced obesity and insulin resistance [35], but also the non-metabolic diseases including sarcopenia [102], osteoporosis [103].”
Irisin suppressed the progression of TBI via modulating AMPK/MerTK/autophagy and SYK/ROS/inflammatory signaling
Zhang, K., Du, Y., Yang, S. Z., & Sun, G. (2025) · Scientific Reports · doi:10.1038/s41598-025-00066-7 · Cited by 11
“In addition, Irisin maintains musculoskeletal homeostasis by binding to integrin αVβ5 25,26 .”
Impacts of rat hindlimb Fndc5/irisin overexpression on muscle and adipose tissue metabolism
Farrash, W. F., Brook, M. S., Crossland, H., Phillips, B. E., Cegielski, J., Wilkinson, D. J., Constantin‐Teodosiu, D., Greenhaff, P. L., Smith, K., Cleasby, M. E., et al. (2020) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00034.2020 · Cited by 13
Irisin levels in the serum and cerebrospinal fluid of patients with multiple sclerosis and the expression and distribution of irisin in experimental autoimmune encephalomyelitis
Zhang, Q., Zhang, S., Zhang, L., Zhang, D., & Yang, L. (2021) · Clinical & Experimental Immunology · doi:10.1111/cei.13656 · Cited by 10
“It is reported that irisin is a promyogenic factor with the potential of myogenesis [22,23] and we speculated that the increased irisin in muscle of EAE mice may improve myodynamia; the underlying mechanism needs to be further explored.”
Background
Pancreatic Cancer‐Derived Extracellular Vesicles Enriched with miR‐223‐5p Promote Skeletal Muscle Wasting Associated with Cachexia
Xu, K., Shen, R., Zhang, L., Gao, X., Wang, X., Zhang, C., Chen, X., & Wang, X. (2025) · Advanced Science · doi:10.1002/advs.202504064 · Cited by 10
Skeletal Muscle as an Auto-, Para- and Endocrine Organ: The Role of Myokines in Muscle Metabolism and Other Metabolic Organs
Horváth, L., Pekár, M., Švagera, Z., Horká, V., Mráz, M., & Bužga, M. (2025) · Physiological Research · doi:10.33549/physiolres.935751 · Cited by 14
“In vitro activation of skeletal muscle by irisin leads to a significant proliferation of murine myoblasts and a higher concentration of activated myoblast nuclei in a dose-dependent manner, while also accelerating muscle regeneration and attenuating muscle atrophy after denervation in mice [39].”
Irisin Ameliorates Muscle Atrophy by Inhibiting the Upregulation of the Ubiquitin‒Proteasome System in Chronic Kidney Disease
Wang, S., Pan, Y., Pang, Q., & Zhang, A. (2024) · Calcified Tissue International · doi:10.1007/s00223-024-01283-4 · Cited by 10
“Interventions involving irisin could induce skeletal muscle hypertrophy and mitigate denerva-tion-induced atrophy [9].”
SIRT1 and exercise-induced bone metabolism: a regulatory nexus
Liu, L., Zhang, J., Cui, R., Wang, N., Zhang, Y., Liu, L., Zhang, X., & Liu, Q. (2025) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2025.1522821 · Cited by 11
Correlations of serum myostatin and irisin with sarcopenia and osteoporosis in rheumatoid arthritis patients: a cross-sectional study
Li, W.-J., Yin, R., Xia, X., Xing, Q.-X., & Xu, S. (2025) · Scientific Reports · doi:10.1038/s41598-025-07378-8 · Cited by 10
“Research demonstrated that increased irisin levels could promote muscle growth, while injecting irisin induced skeletal muscle hypertrophy and enhanced skeletal muscle regeneration after muscle injury 12 .”
The relationship between sarcopenia and serum irisin and TNF-α levels in newly diagnosed cancer patients
Demir, L., & Oflazoğlu, U. (2023) · Supportive Care in Cancer · doi:10.1007/s00520-023-08041-6 · Cited by 10
“Reza et al. stated that irisin improved muscle mass in atrophied mice through myogenic signalling [25].”
Background
Effects of 2-week HMB-FA supplementation with or without eccentric resistance exercise on expression of some genes related to muscle protein turnover and serum irisin and IGF-1 concentrations
Shirvani, H., Rahmati-Ahmadabad, S., Kowsari, E., Fry, H. L., Kazemi, M., & Kaviani, M. (2020) · Gene · doi:10.1016/j.gene.2020.145018 · Cited by 10
Construction of a Pichia pastoris strain efficiently secreting irisin and assessment of its bioactivity in HepG2 cells
Li, X., Duan, H., Liu, Q., Umar, M., Luo, W., Yang, X., Zhu, J., & Li, M. (2018) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2018.11.092 · Cited by 10
Treadmill exercise with nanoselenium supplementation affects the expression of Irisin/FNDC5 and semaphorin 3A in rats exposed to cigarette smoke extract
Arabzadeh, E., Shirvani, H., Masjedi, M. R., Ghanei, M., Hofmeister, M., & Rostamkhani, F. (2023) · 3 Biotech · doi:10.1007/s13205-023-03849-9 · Cited by 9
“In muscle tissue, irisin affects the differentiation of myogenic from myoblast fusion with activation of IL6 signaling (Reza et al. 2017).”
Background
Comparative Analysis of Myofiber Characteristics, Shear Force, and Amino Acid Contents in Slow- and Fast-Growing Broilers
Gu, S., Gao, J., Li, Z., Zhang, S., Wen, C., Sun, C., Yan, W., Hou, Z., Yang, N., & Li, J. (2024) · Foods · doi:10.3390/foods13243997 · Cited by 9
Soyasapogenol B prevents sarcopenia by increasing skeletal muscle mass and function through the Sirt1/PGC-1α and PI3K pathway
Ahn, B. M., Noh, Y., Lee, J. J., Park, J. H. Y., Lee, K. W., & Jang, Y. J. (2025) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2025.118316 · Cited by 9
The canonical ER stress IRE1α/XBP1 pathway mediates skeletal muscle wasting during pancreatic cancer cachexia
Joshi, A. S., da Silva, M. T., Vuong, T. A., Xu, B., Singh, R. K., & Kumar, A. (2025) · EMBO Molecular Medicine · doi:10.1038/s44321-025-00337-w · Cited by 9
“In a parallel experiment, cultured myotubes were treated with 4 μ 8C (an inhibitor of IRE1 α endonuclease activity) for 24 h followed by measuring levels of p-STAT3 protein.”
Irisin and the muscle–brain axis: Mechanisms and translational potential
Arosio, B., & Picca, A. (2026) · Experimental Gerontology · doi:10.1016/j.exger.2026.113028 · Cited by 11
Effect of single bout downhill running on the serum irisin concentrations in rats
Murao, M., Imano, T., Akiyama, J., 川上, 照., & Nakajima, M. (2019) · Growth Factors · doi:10.1080/08977194.2020.1742118 · Cited by 9
Myokine secretion following moderate-intensity endurance exercise under different environmental temperatures
Tsuchiya, Y., & Goto, K. (2021) · Cytokine · doi:10.1016/j.cyto.2021.155553 · Cited by 9
Irisin: A Potentially Fresh Insight into the Molecular Mechanisms Underlying Vascular Aging
Wang, Y., Wang, M., & Wang, Y. (2023) · Aging and Disease · doi:10.14336/ad.2023.1112 · Cited by 10
“Recombinant irisin administration or gene gain/loss of function has been used in preclinical investigations to modify irisin levels in animal and tissue engineering models [6–8].”
Irisin/FNDC5: A participant in camel metabolism
Kirat, D., Hamada, M. M. Z., Moustafa, A., & Miyasho, T. (2020) · Saudi Journal of Biological Sciences · doi:10.1016/j.sjbs.2020.10.061 · Cited by 10
Cross talk mechanisms of aerobic exercise training on obesity, type 2 diabetes, and Alzheimer's disease: the role of insulin resistance
Sousa, R. A. L. D., Magalhães, C. O. D. E., Dias, I. R., de Oliveira, L. R. S., Caria, A. C. I., & Cassilhas, R. C. (2022) · Revista da Associação Médica Brasileira · doi:10.1590/1806-9282.20211210 · Cited by 10
SMN Deficiency Induces an Early Non-Atrophic Myopathy with Alterations in the Contractile and Excitatory Coupling Machinery of Skeletal Myofibers in the SMN∆7 Mouse Model of Spinal Muscular Atrophy
Berciano, M. T., Gatius, A., Puente-Bedia, A., Rufino-Gómez, A., Tarabal, O., Rodríguez-Rey, J. C., Calderó, J., Lafarga, M., & Tapia, O. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms252212415 · Cited by 8
“It is well established that PGC-1 α activates the downstream factor FDCN5 (fibronectin type III domain containing 5), which is cleaved in the sarcolemma of skeletal myofibers to give rise to the myokine irisin [73–76].”
Combined Treatment of Metformin and Resveratrol Promotes Myogenesis Through Increased Irisin Release in C2C12 Cells
Seong, E. J., Kim, Y., Su, Z., Kang, H., & Lee, J. H. (2025) · Pharmaceutical Research · doi:10.1007/s11095-025-03834-2 · Cited by 8
“In addition, irisin induces myogenesis by activating IL-6 signaling [36], whereas IL-6 also plays a role in inducing muscle atrophy through inflammatory responses [37], so high concentrations of irisin may have induced muscle atrophy through IL-6.”
Potential effect of Irisin on sarcopenia: a systematic review
Chen, Y., Qian, M., Gao, F., Li, G., Peng, K., Sun, Q., Sun, Y., Liu, G., Ge, Y., Yang, M., et al. (2025) · BMC Musculoskeletal Disorders · doi:10.1186/s12891-025-08767-w · Cited by 8
“Experimental studies demonstrate irisin’s regenerative capacity: In murine models of muscle injury, irisin activates satellite cells and regulates protein synthesis/degradation balance, facilitating tissue repair and hypertrophy [12].”
Comprehensive Transcriptome Profiling of NAFLD- and NASH-Induced Skeletal Muscle Dysfunction
Guo, M., Xiang, L., Yao, J., Zhang, J., Zhu, S., Wang, D., Liu, C., Li, G., Wang, J., Gao, Y., et al. (2022) · Frontiers in Endocrinology · doi:10.3389/fendo.2022.851520 · Cited by 8
Biomechanical Stimulation of Muscle Constructs Influences Phenotype of Bone Constructs by Modulating Myokine Secretion
Kumar, H. S., Barnett, E. N., Fowlkes, J. L., Kalaitzoglou, E., & Annamalai, R. T. (2023) · JBMR Plus · doi:10.1002/jbm4.10804 · Cited by 8
“(48,49) Interestingly, when muscle constructs are co-cultured with bone constructs, the effect of the exercise regimens changed markedly.”
Background
Chicoric acid does not restore palmitate-induced decrease in irisin levels in PBMCs of newly diagnosed patients with T2D and healthy subjects
Sadeghabadi, Z. A., Abbasalipourkabir, R., Mohseni, R., & Ziamajidi, N. (2019) · Archives of Physiology and Biochemistry · doi:10.1080/13813455.2019.1702060 · Cited by 8
“Irisin promotes myogenesis through increasing myocyte cell proliferation and genes expression of myogenin and myonectin, as well as, inhibiting genes expression of atrophy-related markers including MAFbx and MuRF1 (Rodr ıguez et al. 2015, Reza et al. 2017).”
Background
Irisin Is Target of Sphingosine-1-Phosphate/Sphingosine-1-Phosphate Receptor-Mediated Signaling in Skeletal Muscle Cells
Pierucci, F., Chirco, A., & Meacci, E. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241310548 · Cited by 8
“The ability of irisin to modulate IL-6 signaling [18] was also mediated by SphK/S1P.”
BackgroundInfluential
The Preventive Effect of Specific Collagen Peptides against Dexamethasone-Induced Muscle Atrophy in Mice
Oh, J., Park, S. H., Kim, D. S., Choi, W., Jang, J., Rahmawati, L., Jang, W. Y., Lim, H. K., Hwang, J. Y., Gu, G. R., et al. (2023) · Molecules · doi:10.3390/molecules28041950 · Cited by 7
“Irisin causes skeletal muscle hypertrophy by activating muscle satellite cells and protein synthesis [18].”

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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