PERAN PENTING MIOKIN MELALUI LATIHAN FISIK PADA LANJUT USIA
Keywords:
Miokin, lanjut usiaSynopsis
Miokin adalah peptida yang diproduksi, diekspresikan, dan dilepaskan oleh otot yang dapat bekerja secara autokrin, parakrin atau endokrin. Otot skeletal merupakan organ terbesar dalam tubuh manusia, sehingga miokin yang diproduksi melalui kontraksi otot membuka suatu paradigma baru mengenai peran sentral otot dalam mengatur metabolisme dan fungsi organ lainnya. Beberapa penelitian menujukkan bahwa miokin yang diinduksi melalui latihan fisik memiliki efek “polypill” dengan manfaat yang sangat luas bukan hanya mencegah sarkopenia, namun juga dalam penyakit kronik dan degeneratif.
Downloads
References
Afzali, A.M., Müntefering, T., Wiendl, H., Meuth, S.G., Ruck, T., 2018. Skeletal muscle cells actively shape (auto)immune responses. Autoimmunity Reviews 17, 518–529. https://doi.org/10.1016/j.autrev.2017.12.005
Aguilar‐Agon, K.W., Capel, A.J., Martin, N.R.W., Player, D.J., Lewis, M.P., 2019. Mechanical loading stimulates hypertrophy in tissue‐engineered skeletal muscle: Molecular and phenotypic responses. J Cell Physiol 234, 23547–23558. https://doi.org/10.1002/jcp.28923
Ahima, R.S., Park, H.-K., 2015. Connecting Myokines and Metabolism. Endocrinol Metab 30, 235. https://doi.org/10.3803/EnM.2015.30.3.235
Al-Khalili, L., Bouzakri, K., Glund, S., Lönnqvist, F., Koistinen, H.A., et al., 2006. Signaling Specificity of Interleukin-6 Action on Glucose and Lipid Metabolism in Skeletal Muscle. Molecular Endocrinology 20, 3364–3375. https://doi.org/10.1210/me.2005-0490
Angulo, J., El Assar, M., Álvarez-Bustos, A., Rodríguez-Mañas, L., 2020. Physical activity and exercise: Strategies to manage frailty. Redox Biology 35, 101513. https://doi.org/10.1016/j.redox.2020.101513
Aoi, W., Naito, Y., Takagi, T., Tanimura, Y., Takanami, Y., et a., 2013. A novel myokine, secreted protein acidic and rich in cysteine (SPARC), suppresses colon tumorigenesis via regular exercise. Gut 62, 882–889. https://doi.org/10.1136/gutjnl-2011-300776
Arnold, A.-S., Egger, A., Handschin, C., 2011. PGC-1α and Myokines in the Aging Muscle – A Mini-Review. Gerontology 57, 37–43. https://doi.org/10.1159/000281883
Arrieta, H., Hervás, G., Rezola-Pardo, C., Ruiz-Litago, F., Iturburu, M., et al., 2019. Serum Myostatin Levels Are Higher in Fitter, More Active, and Non-Frail Long-Term Nursing Home Residents and Increase after a Physical Exercise Intervention. Gerontology 65, 229–239. https://doi.org/10.1159/000494137
Aryana, I.G.P.S., Hapsari, A.A.A.R., Kuswardhani, R.A.T., 2018. Myokine Regulation as Marker of Sarcopenia in Elderly. Mol Cell Biomed Sci 2, 38. https://doi.org/10.21705/mcbs.v2i2.32
Aryana, Suka, 2020. Myostatin tinggi dan irisin, interleukin 15, dan rasio interleukin 15 / myostatin rendah merupakan faktor risiko sarkopenia pada lanjut usia.
Attie, K.M., Borgstein, N.G., Yang, Y., Condon, C.H., Wilson, D.M., et al., 2013. A single ascending-dose study of muscle regulator ace-031 in healthy volunteers: ACE-031 Single-Dose Study. Muscle Nerve 47, 416–423. https://doi.org/10.1002/mus.23539
Badan Pusat Statistik, 2018. Statistik Penduduk Lanjut Usia. Jakarta.
Bano, G., Trevisan, C., Carraro, S., Solmi, M., Luchini, C., et al., 2017. Inflammation and sarcopenia: A systematic review and meta-analysis. Maturitas 96, 10–15. https://doi.org/10.1016/j.maturitas.2016.11.006
Becic, T., Studenik, C., Hoffmann, G., 2018. Exercise Increases Adiponectin and Reduces Leptin Levels in Prediabetic and Diabetic Individuals: Systematic Review and Meta-Analysis of Randomized Controlled Trials. Medical Sciences 6, 97. https://doi.org/10.3390/medsci6040097
Becker, C., Lord, S.R., Studenski, S.A., Warden, S.J., Fielding, R.A., et al., 2015. Myostatin antibody (LY2495655) in older weak fallers: a proof-of-concept, randomised, phase 2 trial. The Lancet Diabetes & Endocrinology 3, 948–957. https://doi.org/10.1016/S2213-8587(15)00298-3
Belizário, J.E., Fontes-Oliveira, C.C., Borges, J.P., Kashiabara, J.A., Vannier, E., 2016. Skeletal muscle wasting and renewal: a pivotal role of myokine IL-6. SpringerPlus 5, 619. https://doi.org/10.1186/s40064-016-2197-2
Bernardi, M., Moreau, R., Angeli, P., Schnabl, B., Arroyo, V., 2015. Mechanisms of decompensation and organ failure in cirrhosis: From peripheral arterial vasodilation to systemic inflammation hypothesis. Journal of Hepatology 63, 1272–1284. https://doi.org/10.1016/j.jhep.2015.07.004
Borello, U., Berarducci, B., Murphy, P., Bajard, L., Buffa, V., et al., 2006. The Wnt/β-catenin pathway regulates Gli-mediated Myf5 expression during somitogenesis. Development 133, 3723–3732. https://doi.org/10.1242/dev.02517
Bowser, M., Herberg, S., Arounleut, P., Shi, X., Fulzele, S., et al., 2013. Effects of the activin A–myostatin–follistatin system on aging bone and muscle progenitor cells. Experimental Gerontology 48, 290–297. https://doi.org/10.1016/j.exger.2012.11.004
Brandt, C., Pedersen, B.K., 2010. The Role of Exercise-Induced Myokines in Muscle Homeostasis and the Defense against Chronic Diseases. Journal of Biomedicine and Biotechnology 2010, 1–6. https://doi.org/10.1155/2010/520258
Broholm, C. and Pedersen, B.K, 2010. Leukaemia Inhibitory Factor—An Exercise Induced Myokine. Exercise Immunology Review 77–85.
Broholm, C., Laye, M.J., Brandt, C., Vadalasetty, R., Pilegaard, H., et al., 2011. LIF is a contraction-induced myokine stimulating human myocyte proliferation. Journal of Applied Physiology 111, 251–259. https://doi.org/10.1152/japplphysiol.01399.2010
Camporez, J.-P.G., Petersen, M.C., Abudukadier, A., Moreira, G.V., Jurczak, M.J., et al., 2016. Anti-myostatin antibody increases muscle mass and strength and improves insulin sensitivity in old mice. Proc. Natl. Acad. Sci. U.S.A. 113, 2212–2217. https://doi.org/10.1073/pnas.1525795113
Cani, P.D., Jordan, B.F., 2018. Gut microbiota-mediated inflammation in obesity: a link with gastrointestinal cancer. Nat Rev Gastroenterol Hepatol 15, 671–682. https://doi.org/10.1038/s41575-018-0025-6
Carbó, N., López-Soriano, J., Costelli, P., Busquets, S., Alvarez, B., et al., 2000. Interleukin-15 antagonizes muscle protein waste in tumour-bearing rats. Br J Cancer 83, 526–531. https://doi.org/10.1054/bjoc.2000.1299
Carlson, M.E., Hsu, M., Conboy, I.M., 2008. Imbalance between pSmad3 and Notch induces CDK inhibitors in old muscle stem cells. Nature 454, 528–532. https://doi.org/10.1038/nature07034
Chang J, 2014. Irisin as a Biomarker of Sarcopenia [degree of Doctor of Philosophy].
Chang, J.S., Kim, T.H., Nguyen, T.T., Park, K.-S., Kim, N., Kong, I.D., 2017. Circulating irisin levels as a predictive biomarker for sarcopenia: A cross-sectional community-based study: Irisin as a biomarker for sarcopenia. Geriatr Gerontol Int 17, 2266–2273. https://doi.org/10.1111/ggi.13030
Chen, N., Li, Q., Liu, J., Jia, S., 2016. Irisin, an exercise-induced myokine as a metabolic regulator: an updated narrative review: Irisin as a Metabolic Regulator. Diabetes Metab Res Rev 32, 51–59. https://doi.org/10.1002/dmrr.2660
Chew, J., Tay, L., Lim, J.P., Leung, B.P., Yeo, A., et al., 2019. Serum Myostatin and IGF-1 as Gender-Specific Biomarkers of Frailty and Low Muscle Mass in Community-Dwelling Older Adults. J Nutr Health Aging 23, 979–986. https://doi.org/10.1007/s12603-019-1255-1
Choi, H.Y., Kim, S., Park, J.W., Lee, N.S., Hwang, S.Y., et al., 2014. Implication of Circulating Irisin Levels with Brown Adipose Tissue and Sarcopenia in Humans. The Journal of Clinical Endocrinology & Metabolism 99, 2778–2785. https://doi.org/10.1210/jc.2014-1195
Choi, K.M., Kim, J.H., Cho, G.J., Baik, S.H., Park, H.S., et al., 2007. Effect of exercise training on plasma visfatin and eotaxin levels. eur j endocrinol 157, 437–442. https://doi.org/10.1530/EJE-07-0127
Ciechanover, A., Kwon, Y.T., 2015. Degradation of misfolded proteins in neurodegenerative diseases: therapeutic targets and strategies. Exp Mol Med 47, e147–e147. https://doi.org/10.1038/emm.2014.117
Cooper, R., Kuh, D., Cooper, C., Gale, C.R., Lawlor, D.A., et al, 2011. Objective measures of physical capability and subsequent health: a systematic review. Age and Ageing 40, 14–23. https://doi.org/10.1093/ageing/afq117
Cornelissen, V.A., Smart, N.A., 2013. Exercise Training for Blood Pressure: A Systematic Review and Meta‐analysis. JAHA 2, e004473. https://doi.org/10.1161/JAHA.112.004473
Cruz-Jentoft, A.J., Bahat, G., Bauer, J., Boirie, Y., Bruyère, O., et al., 2019. Sarcopenia: revised European consensus on definition and diagnosis. Age and Ageing 48, 16–31. https://doi.org/10.1093/ageing/afy169
Cypess, A.M., Lehman, S., Williams, G., Tal, I., Rodman, D., et al., 2009. Identification and Importance of Brown Adipose Tissue in Adult Humans. N Engl J Med 360, 1509–1517. https://doi.org/10.1056/NEJMoa0810780
Dalle, S., Rossmeislova, L., Koppo, K., 2017. The Role of Inflammation in Age-Related Sarcopenia. Front. Physiol. 8, 1045. https://doi.org/10.3389/fphys.2017.01045
de Sire, A., Baricich, A., Renò, F., Cisari, C., Fusco, N., Invernizzi, M., 2020. Myostatin as a potential biomarker to monitor sarcopenia in hip fracture patients undergoing a multidisciplinary rehabilitation and nutritional treatment: a preliminary study. Aging Clin Exp Res 32, 959–962. https://doi.org/10.1007/s40520-019-01436-8
Delgado-Calle, J., Sato, A.Y., Bellido, T., 2017. Role and mechanism of action of sclerostin in bone. Bone 96, 29–37. https://doi.org/10.1016/j.bone.2016.10.007
Demontis, F., Piccirillo, R., Goldberg, A.L., Perrimon, N., 2013. Mechanisms of skeletal muscle aging: insights from Drosophila and mammalian models. Disease Models & Mechanisms dmm.012559. https://doi.org/10.1242/dmm.012559
Didangelos, A., Yin, X., Mandal, K., Baumert, M., Jahangiri, M., Mayr, M., 2010. Proteomics Characterization of Extracellular Space Components in the Human Aorta. Molecular & Cellular Proteomics 9, 2048–2062. https://doi.org/10.1074/mcp.M110.001693
Dupont, J., Dedeyne, L., Dalle, S., Koppo, K., Gielen, E., 2019. The role of omega-3 in the prevention and treatment of sarcopenia. Aging Clin Exp Res 31, 825–836. https://doi.org/10.1007/s40520-019-01146-1
Duzova, H., 2012. Skeletal Muscle, Myokines and Health. Med-Science 1, 211. https://doi.org/10.5455/medscience.2012.01.8023
E. Serafini, E. Marzetti, R. Calvani, A. Picca, M. Tosato, R. B, et al, 2019. Review : Nutritional approach to sarcopenia. JGG 67, 52–61.
Elkina, Y., von Haehling, S., Anker, S.D., Springer, J., 2011. The role of myostatin in muscle wasting: an overview. J Cachexia Sarcopenia Muscle 2, 143–151. https://doi.org/10.1007/s13539-011-0035-5
Elley, C.R., Gupta, A.K., Webster, R., Selak, V., Jun, M., et al., 2012. The Efficacy and Tolerability of ‘Polypills’: Meta-Analysis of Randomised Controlled Trials. PLoS ONE 7, e52145. https://doi.org/10.1371/journal.pone.0052145
Evenhuis, H.M., Hermans, H., Hilgenkamp, T.I.M., Bastiaanse, L.P., Echteld, M.A., 2012. Frailty and Disability in Older Adults with Intellectual Disabilities: Results from the Healthy Ageing and Intellectual Disability Study. Journal of the American Geriatrics Society 60, 934–938. https://doi.org/10.1111/j.1532-5415.2012.03925.x
Farmawati, A., Kitajima, Y., Nedachi, T., Sato, M., Kanzaki, M., et al., 2013. Characterization of contraction-induced IL-6 up-regulation using contractile C2C12 myotubes. Endocr J 60, 137–147. https://doi.org/10.1507/endocrj.EJ12-0316
Febbraio, M.A., Pedersen, B.K., 2002. Muscle‐derived interleukin‐6: mechanisms for activation and possible biological roles. FASEB j. 16, 1335–1347. https://doi.org/10.1096/fj.01-0876rev
Fiuza-Luces, C., Garatachea, N., Berger, N.A., Lucia, A., 2013. Exercise is the Real Polypill. Physiology 28, 330–358. https://doi.org/10.1152/physiol.00019.2013
Fryer, L.G.D., Foufelle, F., Barnes, K., Baldwin, S.A., Woods, A., et al., 2002. Characterization of the role of the AMP-activated protein kinase in the stimulation of glucose transport in skeletal muscle cells. Biochemical Journal 363, 167–174. https://doi.org/10.1042/bj3630167
Ghanemi, A., Yoshioka, M., St-Amand, J., 2020. Secreted Protein Acidic and Rich in Cysteine: Metabolic and Homeostatic Properties beyond the Extracellular Matrix Structure. Applied Sciences 10, 2388. https://doi.org/10.3390/app10072388
Glund, S., Deshmukh, A., Long, Y.C., Moller, T., Koistinen, H.A., et al., 2007. Interleukin-6 Directly Increases Glucose Metabolism in Resting Human Skeletal Muscle. Diabetes 56, 1630–1637. https://doi.org/10.2337/db06-1733
Gray, S.R., Kamolrat, T., 2011. The effect of exercise induced cytokines on insulin stimulated glucose transport in C2C12 cells. Cytokine 55, 221–228. https://doi.org/10.1016/j.cyto.2011.04.019
Han, H.Q., Zhou, X., Mitch, W.E., Goldberg, A.L., 2013. Myostatin/activin pathway antagonism: Molecular basis and therapeutic potential. The International Journal of Biochemistry & Cell Biology 45, 2333–2347. https://doi.org/10.1016/j.biocel.2013.05.019
Harber, M.P., Crane, J.D., Dickinson, J.M., Jemiolo, B., Raue, U., et al., 2009. Protein synthesis and the expression of growth-related genes are altered by running in human vastus lateralis and soleus muscles. American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 296, R708–R714. https://doi.org/10.1152/ajpregu.90906.2008
Hashizume, M., Hayakawa, N., Suzuki, M., Mihara, M., 2009. IL-6/sIL-6R trans-signalling, but not TNF-α induced angiogenesis in a HUVEC and synovial cell co-culture system. Rheumatol Int 29, 1449–1454. https://doi.org/10.1007/s00296-009-0885-8
He, C., Bassik, M.C., Moresi, V., Sun, K., Wei, Y., et al., 2012. Exercise-induced BCL2-regulated autophagy is required for muscle glucose homeostasis. Nature 481, 511–515. https://doi.org/10.1038/nature10758
He, C., Sumpter, Jr., R., Levine, B., 2012. Exercise induces autophagy in peripheral tissues and in the brain. Autophagy 8, 1548–1551. https://doi.org/10.4161/auto.21327
Hittel, D.S., Axelson, M., Sarna, N., Shearer, J., Huffman, K.M., et al., 2010. Myostatin Decreases with Aerobic Exercise and Associates with Insulin Resistance. Medicine & Science in Sports & Exercise 42, 2023–2029. https://doi.org/10.1249/MSS.0b013e3181e0b9a8
Hjorth, M., Pourteymour, S., Görgens, S.W., Langleite, T.M., Lee, S., et al., 2016. Myostatin in relation to physical activity and dysglycaemia and its effect on energy metabolism in human skeletal muscle cells. Acta Physiol 217, 45–60. https://doi.org/10.1111/apha.12631
Hojman, P., Pedersen, M., Nielsen, A.R., Krogh-Madsen, R., Yfanti, C., et al., 2009. Fibroblast Growth Factor-21 Is Induced in Human Skeletal Muscles by Hyperinsulinemia. Diabetes 58, 2797–2801. https://doi.org/10.2337/db09-0713
Huang, C., Wang, Y., Li, X., Ren, L., Zhao, J., et al., 2020. Clinical features of patients infected with 2019 novel coronavirus in Wuhan, China. The Lancet 395, 497–506. https://doi.org/10.1016/S0140-6736(20)30183-5
Huh, J.Y., Panagiotou, G., Mougios, V., Brinkoetter, M., Vamvini, et al., 2012. FNDC5 and irisin in humans: I. Predictors of circulating concentrations in serum and plasma and II. mRNA expression and circulating concentrations in response to weight loss and exercise. Metabolism 61, 1725–1738. https://doi.org/10.1016/j.metabol.2012.09.002
Hunt, L.C., Anthea Coles, C., Gorman, C.M., Tudor, E.M., Smythe, G.M., et al., 2011. Alterations in the expression of leukemia inhibitory factor following exercise: comparisons between wild-type and mdx muscles. PLoS Curr 3, RRN1277. https://doi.org/10.1371/currents.RRN1277
Inoue, A., Cheng, X.W., Huang, Z., Hu, L., Kikuchi, R., et al., 2017. Exercise restores muscle stem cell mobilization, regenerative capacity and muscle metabolic alterations via adiponectin/AdipoR1 activation in SAMP10 mice: Exercise ameliorate muscle regeneration. Journal of Cachexia, Sarcopenia and Muscle 8, 370–385. https://doi.org/10.1002/jcsm.12166
Irie, K., Ejiri, S., Sakakura, Y., Shibui, T., Yajima, T., 2008. Matrix Mineralization as a Trigger for Osteocyte Maturation. J Histochem Cytochem. 56, 561–567. https://doi.org/10.1369/jhc.2008.950527
Jacquemin, V., Butler-Browne, G.S., Furling, D., Mouly, V., 2007. IL-13 mediates the recruitment of reserve cells for fusion during IGF-1-induced hypertrophy of human myotubes. Journal of Cell Science 120, 670–681. https://doi.org/10.1242/jcs.03371
Jin, Q., Qiao, C., Li, Jianbin, Xiao, B., Li, Juan, Xiao, X., 2019. A GDF11/myostatin inhibitor, GDF11 propeptide-Fc, increases skeletal muscle mass and improves muscle strength in dystrophic mdx mice. Skeletal Muscle 9, 16. https://doi.org/10.1186/s13395-019-0197-y
Jin, Y., Sumsuzzman, D., Choi, J., Kang, H., Lee, S.-R., et al., 2018. Molecular and Functional Interaction of the Myokine Irisin with Physical Exercise and Alzheimer’s Disease. Molecules 23, 3229. https://doi.org/10.3390/molecules23123229
Jonsdottir, I.H., Schjerling, P., Ostrowski, K., Asp, S., Richter, E.A., Pedersen, B.K., 2000. Muscle contractions induce interleukin‐6 mRNA production in rat skeletal muscles. The Journal of Physiology 528, 157–163. https://doi.org/10.1111/j.1469-7793.2000.00157.x
Jouliaekaza, D., Cabello, G., 2007. The myostatin gene: physiology and pharmacological relevance. Current Opinion in Pharmacology 7, 310–315. https://doi.org/10.1016/j.coph.2006.11.011
K. Panati, Y. Suneetha, V.R. Narala, 2016. Irisin/FNDC5 – An updated review. Eur Rev Med Pharmacol Sci 20, 689–697.
Kang, X., Yang, M., Shi, Y., Xie, M., Zhu, M., et al., 2018. Interleukin-15 facilitates muscle regeneration through modulation of fibro/adipogenic progenitors. Cell Commun Signal 16, 42. https://doi.org/10.1186/s12964-018-0251-0
Karstoft, K., Pedersen, B.K., 2016. Skeletal muscle as a gene regulatory endocrine organ. Current Opinion in Clinical Nutrition & Metabolic Care 19, 270–275. https://doi.org/10.1097/MCO.0000000000000283
Kelly, D.P., 2012. Irisin, Light My Fire. Science 336, 42–43. https://doi.org/10.1126/science.1221688
Kelly, M., Keller, C., Avilucea, P.R., Keller, P., Luo, Z., et al., 2004. AMPK activity is diminished in tissues of IL-6 knockout mice: the effect of exercise. Biochemical and Biophysical Research Communications 320, 449–454. https://doi.org/10.1016/j.bbrc.2004.05.188
Kementerian Kesehatan RI, 2016. Infodatin Lanjut Usia (lansia). In Pusat Data dan Informasi Kementerian Kesehatan RI.
Kerr, A., Syddall, H.E., Cooper, C., Turner, G.F., Briggs, R.S., Sayer, A.A., 2006. Does admission grip strength predict length of stay in hospitalised older patients? Age and Ageing 35, 82–84. https://doi.org/10.1093/ageing/afj010
Kim, J.A., Roh, E., Hong, S., Lee, Y.-B., Kim, et al., 2019. Association of serum sclerostin levels with low skeletal muscle mass: The Korean Sarcopenic Obesity Study (KSOS). Bone 128, 115053. https://doi.org/10.1016/j.bone.2019.115053
Kirkwood, T.B.L., 2008. A systematic look at an old problem. Nature 451, 644–647. https://doi.org/10.1038/451644a
Knaepen, K., Goekint, M., Heyman, E.M., Meeusen, R., 2010. Neuroplasticity – Exercise-Induced Response of Peripheral Brain-Derived Neurotrophic Factor: A Systematic Review of Experimental Studies in Human Subjects. Sports Medicine 40, 765–801. https://doi.org/10.2165/11534530-000000000-00000
Konopka, A.R., Douglass, M.D., Kaminsky, L.A., Jemiolo, B., Trappe, T.A., Trappe, S., et al., 2010. Molecular Adaptations to Aerobic Exercise Training in Skeletal Muscle of Older Women. The Journals of Gerontology Series A: Biological Sciences and Medical Sciences 65A, 1201–1207. https://doi.org/10.1093/gerona/glq109
Konopka, A.R., Wolff, C.A., Suer, M.K., Harber, M.P., 2018. Relationship between intermuscular adipose tissue infiltration and myostatin before and after aerobic exercise training. American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 315, R461–R468. https://doi.org/10.1152/ajpregu.00030.2018
Koopman, R., Saris, W.H.M., Wagenmakers, A.J.M., van Loon, L.J.C., 2007. Nutritional Interventions to Promote Post-Exercise Muscle Protein Synthesis: Sports Medicine 37, 895–906. https://doi.org/10.2165/00007256-200737100-00005
Krause, M., Milne, K., Hawke, T., 2019. Adiponectin—Consideration for its Role in Skeletal Muscle Health. IJMS 20, 1528. https://doi.org/10.3390/ijms20071528
Krolopp, J.E., Thornton, S.M., Abbott, M.J., 2016. IL-15 Activates the Jak3/STAT3 Signaling Pathway to Mediate Glucose Uptake in Skeletal Muscle Cells. Front. Physiol. 7. https://doi.org/10.3389/fphys.2016.00626
Kurdiova, T., Balaz, M., Vician, M., Maderova, D., Vlcek, M., et al., 2014. Effects of obesity, diabetes and exercise on Fndc5 gene expression and irisin release in human skeletal muscle and adipose tissue: in vivo and in vitro studies: Human Fndc5 /irisin in prediabetes, type 2 diabetes and exercise. The Journal of Physiology 592, 1091–1107. https://doi.org/10.1113/jphysiol.2013.264655
Lancaster, G.I., Febbraio, M.A., 2014. The immunomodulating role of exercise in metabolic disease. Trends in Immunology 35, 262–269. https://doi.org/10.1016/j.it.2014.02.008
Leal, L.G., Lopes, M.A., Batista, M.L., 2018. Physical Exercise-Induced Myokines and Muscle-Adipose Tissue Crosstalk: A Review of Current Knowledge and the Implications for Health and Metabolic Diseases. Front. Physiol. 9, 1307. https://doi.org/10.3389/fphys.2018.01307
LeBrasseur, N.K., Schelhorn, T.M., Bernardo, B.L., Cosgrove, P.G., et al., 2009. Myostatin Inhibition Enhances the Effects of Exercise on Performance and Metabolic Outcomes in Aged Mice. The Journals of Gerontology Series A: Biological Sciences and Medical Sciences 64A, 940–948. https://doi.org/10.1093/gerona/glp068
Lee, H.J., Lee, J.O., Kim, N., Kim, J.K., Kim, H.I., et al., 2015. Irisin, a Novel Myokine, Regulates Glucose Uptake in Skeletal Muscle Cells via AMPK. Molecular Endocrinology 29, 873–881. https://doi.org/10.1210/me.2014-1353
Lee, S.-J., 2004. Regulation of muscle mass by myostatin. Annu. Rev. Cell Dev. Biol. 20, 61–86. https://doi.org/10.1146/annurev.cellbio.20.012103.135836
Li, X., Ominsky, M.S., Niu, Q.-T., Sun, N., Daugherty, B., D et al., 2008. Targeted Deletion of the Sclerostin Gene in Mice Results in Increased Bone Formation and Bone Strength. J Bone Miner Res 23, 860–869. https://doi.org/10.1359/jbmr.080216
Li, Y., Zhang, Y., Dorweiler, B., Cui, D., Wang, T., Woo, C.W., et al., 2008. Extracellular Nampt Promotes Macrophage Survival via a Nonenzymatic Interleukin-6/STAT3 Signaling Mechanism. Journal of Biological Chemistry 283, 34833–34843. https://doi.org/10.1074/jbc.M805866200
Liguori, I., Russo, G., Aran, L., Bulli, G., Curcio, F., et al., 2018. Sarcopenia: assessment of disease burden and strategies to improve outcomes. CIA Volume 13, 913–927. https://doi.org/10.2147/CIA.S149232
Louis, E., Raue, U., Yang, Y., Jemiolo, B., Trappe, S., 2007. Time course of proteolytic, cytokine, and myostatin gene expression after acute exercise in human skeletal muscle. Journal of Applied Physiology 103, 1744–1751. https://doi.org/10.1152/japplphysiol.00679.2007
Luo, L., Lu, A.-M., Wang, Y., Hong, A., Chen, Y., et al., 2013. Chronic resistance training activates autophagy and reduces apoptosis of muscle cells by modulating IGF-1 and its receptors, Akt/mTOR and Akt/FOXO3a signaling in aged rats. Experimental Gerontology 48, 427–436. https://doi.org/10.1016/j.exger.2013.02.009
Lutz, C.T., Quinn, L.S., 2012. Sarcopenia, obesity, and natural killer cell immune senescence in aging: Altered cytokine levels as a common mechanism. Aging 4, 535–546. https://doi.org/10.18632/aging.100482
Madaro, L., Passafaro, M., Sala, D., Etxaniz, U., Lugarini, F., et al., 2018. Denervation-activated STAT3–IL-6 signalling in fibro-adipogenic progenitors promotes myofibres atrophy and fibrosis. Nat Cell Biol 20, 917–927. https://doi.org/10.1038/s41556-018-0151-y
Magarò, M.S., Bertacchini, J., Florio, F., Zavatti, M., Potì, F., Cavani, F., et al., 2021. Identification of Sclerostin as a Putative New Myokine Involved in the Muscle-to-Bone Crosstalk. Biomedicines 9, 71. https://doi.org/10.3390/biomedicines9010071
Mahtani, K.R., McManus, J., Nunan, D., 2015. Physical activity and obesity editorial: is exercise pointless or was it a pointless exercise? Br J Sports Med 49, 969–970. https://doi.org/10.1136/bjsports-2015-095005
Manolagas, S.C., 2014. Wnt signaling and osteoporosis. Maturitas 78, 233–237. https://doi.org/10.1016/j.maturitas.2014.04.013
Marzetti, E., Carter, C.S., Wohlgemuth, S.E., Lees, H.A., Giovannini, S., et al., 2009. Changes in IL-15 expression and death-receptor apoptotic signaling in rat gastrocnemius muscle with aging and life-long calorie restriction. Mechanisms of Ageing and Development 130, 272–280. https://doi.org/10.1016/j.mad.2008.12.008
Marzetti, E., Privitera, G., Simili, V., Wohlgemuth, S.E., Aulisa, L., et al., 2010. Multiple Pathways to the Same End: Mechanisms of Myonuclear Apoptosis in Sarcopenia of Aging. The Scientific World JOURNAL 10, 340–349. https://doi.org/10.1100/tsw.2010.27
Matsakas, A., Bozzo, C., Cacciani, N., Caliaro, F., Reggiani, C., et al., 2006. Effect of swimming on myostatin expression in white and red gastrocnemius muscle and in cardiac muscle of rats: Myostatin expression in response to exercise and training. Experimental Physiology 91, 983–994. https://doi.org/10.1113/expphysiol.2006.033571
McFarlane, C., Plummer, E., Thomas, M., Hennebry, A., Ashby, M., et al., 2006. Myostatin induces cachexia by activating the ubiquitin proteolytic system through an NF-κB-independent, FoxO1-dependent mechanism. J. Cell. Physiol. 209, 501–514. https://doi.org/10.1002/jcp.20757
Mitchell, W.K., Williams, J., Atherton, P., Larvin, M., Lund, J., Narici, M., 2012. Sarcopenia, Dynapenia, and the Impact of Advancing Age on Human Skeletal Muscle Size and Strength; a Quantitative Review. Front. Physio. 3. https://doi.org/10.3389/fphys.2012.00260
Mitochondrial Fission and Fusion in Human Diseases, 2014. . N Engl J Med 370, 1073–1074. https://doi.org/10.1056/NEJMc1316254
Morissette, M.R., Stricker, J.C., Rosenberg, M.A., Buranasombati, C., Levitan, E.B., et al., 2009. Effects of myostatin deletion in aging mice. Aging Cell 8, 573–583. https://doi.org/10.1111/j.1474-9726.2009.00508.x
Mraz, M., Haluzik, M., 2014. The role of adipose tissue immune cells in obesity and low-grade inflammation. Journal of Endocrinology 222, R113–R127. https://doi.org/10.1530/JOE-14-0283
Murphy, K.T., Koopman, R., Naim, T., Léger, B., Trieu, J., Ibebunjo, C., et al., 2010. Antibody‐directed myostatin inhibition in 21‐mo‐old mice reveals novel roles for myostatin signaling in skeletal muscle structure and function. FASEB j. 24, 4433–4442. https://doi.org/10.1096/fj.10-159608
Nadeau, L., Aguer, C., 2019. Interleukin-15 as a myokine: mechanistic insight into its effect on skeletal muscle metabolism. Appl. Physiol. Nutr. Metab. 44, 229–238. https://doi.org/10.1139/apnm-2018-0022
Nakamura, S.K., Nakano, S., Miyoshi, T., Yamanouchi, K., Matsuwaki, T., Nishihara, M., 2012. Age-related resistance of skeletal muscle-derived progenitor cells to SPARC may explain a shift from myogenesis to adipogenesis. Aging 4, 40–48. https://doi.org/10.18632/aging.100426
Narici, M.V., Maganaris, C.N., 2006. Adaptability of elderly human muscles and tendons to increased loading. J Anatomy 208, 433–443. https://doi.org/10.1111/j.1469-7580.2006.00548.x
Negaresh, R., Ranjbar, R., Baker, J., Habibi, A., Mokhtarzade, M., et al., 2019. Skeletal muscle hypertrophy, insulin-like growth factor 1, myostatin and follistatin in healthy and sarcopenic elderly men: The effect of whole-body resistance training. Int J Prev Med 10, 29. https://doi.org/10.4103/ijpvm.IJPVM_310_17
Nelke, C., Dziewas, R., Minnerup, J., Meuth, S.G., Ruck, T., 2019. Skeletal muscle as potential central link between sarcopenia and immune senescence. EBioMedicine 49, 381–388. https://doi.org/10.1016/j.ebiom.2019.10.034
Nie, J., Sage, E.H., 2009. SPARC functions as an inhibitor of adipogenesis. J. Cell Commun. Signal. 3, 247–254. https://doi.org/10.1007/s12079-009-0064-4
Nielsen, A.R., Pedersen, B.K., 2007. The biological roles of exercise-induced cytokines: IL-6, IL-8, and IL-15. Appl. Physiol. Nutr. Metab. 32, 833–839. https://doi.org/10.1139/H07-054
Nieman, D.C., Henson, D.A., Gojanovich, G., Mark Davis, J., Angela Murphy, E., et al., 2006. Influence of Carbohydrate on Immune Function Following 2 h Cycling. Research in Sports Medicine 14, 225–237. https://doi.org/10.1080/15438620600854793
Nishizawa, H., Matsuda, M., Yamada, Y., Kawai, K., Suzuki, E., et al., 2004. Musclin, a Novel Skeletal Muscle-derived Secretory Factor. Journal of Biological Chemistry 279, 19391–19395. https://doi.org/10.1074/jbc.C400066200
Nixon, R.A., 2020. The aging lysosome: An essential catalyst for late-onset neurodegenerative diseases. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 1868, 140443. https://doi.org/10.1016/j.bbapap.2020.140443
Novack, G.V., Galeano, P., Castaño, E.M., Morelli, L., 2020. Mitochondrial Supercomplexes: Physiological Organization and Dysregulation in Age-Related Neurodegenerative Disorders. Front. Endocrinol. 11, 600. https://doi.org/10.3389/fendo.2020.00600
Nunan, D., Mahtani, K.R., Roberts, N., Heneghan, C., 2013. Physical activity for the prevention and treatment of major chronic disease: an overview of systematic reviews. Syst Rev 2, 56. https://doi.org/10.1186/2046-4053-2-56
Offord, N.J., Witham, M.D., 2017. The emergence of sarcopenia as an important entity in older people. Clin Med 17, 363–366. https://doi.org/10.7861/clinmedicine.17-4-363
Ogawa, S., Yakabe, M., Akishita, M., 2016. Age-related sarcopenia and its pathophysiological bases. Inflamm Regener 36, 17. https://doi.org/10.1186/s41232-016-0022-5
ONU, 2015. World population, ageing. Suggested Citation: United Nations, Department of Economic and Social Affairs, Population Division.
Osborn, O., Olefsky, J.M., 2012. The cellular and signaling networks linking the immune system and metabolism in disease. Nat Med 18, 363–374. https://doi.org/10.1038/nm.2627
Ostrowski, K., Rohde, T., Zacho, M., Asp, S., Pedersen, B.K., 1998. Evidence that interleukin-6 is produced in human skeletal muscle during prolonged running. The Journal of Physiology 508, 949–953. https://doi.org/10.1111/j.1469-7793.1998.949bp.x
Paris, M.T., Bell, K.E., Mourtzakis, M., 2020. Myokines and adipokines in sarcopenia: understanding cross-talk between skeletal muscle and adipose tissue and the role of exercise. Current Opinion in Pharmacology 52, 61–66. https://doi.org/10.1016/j.coph.2020.06.003
Park, D.C., Yeo, S.G., 2013. Aging. Korean J Audiol 17, 39. https://doi.org/10.7874/kja.2013.17.2.39
Patidar, M., Yadav, N., Dalai, S.K., 2016. Interleukin 15: A key cytokine for immunotherapy. Cytokine & Growth Factor Reviews 31, 49–59. https://doi.org/10.1016/j.cytogfr.2016.06.001
Pattyn, N., Cornelissen, V.A., Eshghi, S.R.T., Vanhees, L., 2013. The Effect of Exercise on the Cardiovascular Risk Factors Constituting the Metabolic Syndrome: A Meta-Analysis of Controlled Trials. Sports Med 43, 121–133. https://doi.org/10.1007/s40279-012-0003-z
Payne, A.M., Jimenez-Moreno, R., Wang, Z.-M., Messi, M.L., Delbono, O., 2009. Role of Ca2+, membrane excitability, and Ca2+ stores in failing muscle contraction with aging. Experimental Gerontology 44, 261–273. https://doi.org/10.1016/j.exger.2008.09.013
Pedersen, B.K., 2013. Muscle as a Secretory Organ, in: Terjung, R. (Ed.), Comprehensive Physiology. Wiley, pp. 1337–1362. https://doi.org/10.1002/cphy.c120033
Pedersen, B.K., 2006. The anti-inflammatory effect of exercise: its role in diabetes and cardiovascular disease control. Essays in Biochemistry 42, 105–117. https://doi.org/10.1042/bse0420105
Pedersen, B.K., Febbraio, M.A., 2012. Muscles, exercise and obesity: skeletal muscle as a secretory organ. Nat Rev Endocrinol 8, 457–465. https://doi.org/10.1038/nrendo.2012.49
Pedersen, B.K., Febbraio, M.A., 2008. Muscle as an Endocrine Organ: Focus on Muscle-Derived Interleukin-6. Physiological Reviews 88, 1379–1406. https://doi.org/10.1152/physrev.90100.2007
Peng, L.-N., Lee, W.-J., Liu, L.-K., Lin, M.-H., Chen, L.-K., 2018. Healthy community-living older men differ from women in associations between myostatin levels and skeletal muscle mass: Myotatin levels and skeletal muscle mass. Journal of Cachexia, Sarcopenia and Muscle 9, 635–642. https://doi.org/10.1002/jcsm.12302
Pérez‐López, A., McKendry, J., Martin‐Rincon, M., Morales‐Alamo, D., Pérez‐Köhler, B., et al., 2018. Skeletal muscle IL ‐15/ IL ‐15Rα and myofibrillar protein synthesis after resistance exercise. Scandinavian Med Sci Sports 28, 116–125. https://doi.org/10.1111/sms.12901
Pesce, M., Ballerini, P., Paolucci, T., Puca, I., Farzaei, M.H., Patruno, A., 2020. Irisin and Autophagy: First Update. IJMS 21, 7587. https://doi.org/10.3390/ijms21207587
Pickering, M.-E., Simon, M., Sornay-Rendu, E., Chikh, K., Carlier, M.-C., et al., 2017. Serum Sclerostin Increases After Acute Physical Activity. Calcif Tissue Int 101, 170–173. https://doi.org/10.1007/s00223-017-0272-5
Pistilli, E.E., Devaney, J.M., Gordish-Dressman, H., Bradbury, M.K., Seip, R.L., et al., 2008. Interleukin-15 and interleukin-15Rα SNPs and associations with muscle, bone, and predictors of the metabolic syndrome. Cytokine 43, 45–53. https://doi.org/10.1016/j.cyto.2008.04.008
Poole, K.E.S., Van Bezooijen, R.L., Loveridge, N., Hamersma, H., et al., 2005. Sclerostin is a delayed secreted product of osteocytes that inhibits bone formation. FASEB j. 19, 1842–1844. https://doi.org/10.1096/fj.05-4221fje
Potthoff, M.J., Inagaki, T., Satapati, S., Ding, X., He, T., et al., 2009. FGF21 induces PGC-1α and regulates carbohydrate and fatty acid metabolism during the adaptive starvation response. Proc. Natl. Acad. Sci. U.S.A. 106, 10853–10858. https://doi.org/10.1073/pnas.0904187106
Pratesi, A., 2013. Skeletal muscle: an endocrine organ. CCMBM. https://doi.org/10.11138/ccmbm/2013.10.1.011
Purwita Wijaya Laksmi, Siti Setiati, Tirza Z Tamin, Pradana Soewondo, Wasilah Rochmah, et al, 2017. Effect of Metformin on Handgrip Strength, Gait Speed, Myostatin Serum Level, and Health-related Quality of Life: A Double Blind Randomized Controlled Trial among Non-diabetic Pre-frail Elderly Patients. Acta medica Indonesiana 49, 118–127.
Quinn, L.S., Anderson, B.G., Strait-Bodey, L., Stroud, A.M., Argilés, J.M., 2009. Oversecretion of interleukin-15 from skeletal muscle reduces adiposity. American Journal of Physiology-Endocrinology and Metabolism 296, E191–E202. https://doi.org/10.1152/ajpendo.90506.2008
Reid, K.F., Fielding, R.A., 2012. Skeletal Muscle Power: A Critical Determinant of Physical Functioning in Older Adults. Exercise and Sport Sciences Reviews 40, 4–12. https://doi.org/10.1097/JES.0b013e31823b5f13
Riechman, S.E., Balasekaran, G., Roth, S.M., Ferrell, R.E., 2004. Association of interleukin-15 protein and interleukin-15 receptor genetic variation with resistance exercise training responses. Journal of Applied Physiology 97, 2214–2219. https://doi.org/10.1152/japplphysiol.00491.2004
Rivera-Brown, A.M., Frontera, W.R., 2012. Principles of Exercise Physiology: Responses to Acute Exercise and Long-term Adaptations to Training. PM&R 4, 797–804. https://doi.org/10.1016/j.pmrj.2012.10.007
Rosen, E.D., Spiegelman, B.M., 2006. Adipocytes as regulators of energy balance and glucose homeostasis. Nature 444, 847–853. https://doi.org/10.1038/nature05483
Rosengren, B.E., Ribom, E.L., Nilsson, J.-A., Mallmin, H., Ljunggren, O., et al., 2012. Inferior physical performance test results of 10,998 men in the MrOS Study is associated with high fracture risk. Age and Ageing 41, 339–344. https://doi.org/10.1093/ageing/afs010
Roth, S.M., Martel, G.F., Ferrell, R.E., Metter, E.J., Hurley, B.F., et al., 2003. Myostatin Gene Expression is Reduced in Humans with Heavy-Resistance Strength Training: A Brief Communication. Exp Biol Med (Maywood) 228, 706–709. https://doi.org/10.1177/153537020322800609
Ruderman, N.B., Keller, C., Richard, A.-M., Saha, A.K., Luo, Z., Xiang, X., et al., 2006. Interleukin-6 Regulation of AMP-Activated Protein Kinase. Diabetes 55, S48–S54. https://doi.org/10.2337/db06-S007
Sakuma, K., Aoi, W., Yamaguchi, A., 2017. Molecular mechanism of sarcopenia and cachexia: recent research advances. Pflugers Arch - Eur J Physiol 469, 573–591. https://doi.org/10.1007/s00424-016-1933-3
Sakuma, K., Aoi, W., Yamaguchi, A., 2014. The Intriguing Regulators of Muscle Mass in Sarcopenia and Muscular Dystrophy. Front. Aging Neurosci. 6. https://doi.org/10.3389/fnagi.2014.00230
Sanchis-Gomar, F., Perez-Quilis, C., 2014. The p38–PGC-1α–irisin–betatrophin axis: Exploring new pathways in insulin resistance. Adipocyte 3, 67–68. https://doi.org/10.4161/adip.27370
Sandrini, L., Ieraci, A., Amadio, P., Zarà, M., Mitro, N., et al., 2019. Physical Exercise Affects Adipose Tissue Profile and Prevents Arterial Thrombosis in BDNF Val66Met Mice. Cells 8, 875. https://doi.org/10.3390/cells8080875
Sartori, R., Milan, G., Patron, M., Mammucari, C., Blaauw, B., et al., 2009. Smad2 and 3 transcription factors control muscle mass in adulthood. American Journal of Physiology-Cell Physiology 296, C1248–C1257. https://doi.org/10.1152/ajpcell.00104.2009
Schaper, F., Rose-John, S., 2015. Interleukin-6: Biology, signaling and strategies of blockade. Cytokine & Growth Factor Reviews 26, 475–487. https://doi.org/10.1016/j.cytogfr.2015.07.004
Schnyder, S., Handschin, C., 2015. Skeletal muscle as an endocrine organ: PGC-1α, myokines and exercise. Bone 80, 115–125. https://doi.org/10.1016/j.bone.2015.02.008
Seldin, M.M., Peterson, J.M., Byerly, M.S., Wei, Z., Wong, G.W., 2012. Myonectin (CTRP15), a Novel Myokine That Links Skeletal Muscle to Systemic Lipid Homeostasis. Journal of Biological Chemistry 287, 11968–11980. https://doi.org/10.1074/jbc.M111.336834
Setiati, S., Dwimartutie, N, 2014. Buku Ajar Ilmu Penyakit Dalam Jilid III Edisi VI. Jakarta: InternaPublishing 3719–27.
Setiati, S, Rizka, A., 2004. Sarkopenia. In Buku Ajar Ilmu Penyakit Dalam, 3rd ed. Balai Penerbit FKUI, Jakarta.
Silva Vasconcelos, E. da, Fernanda Salla, R., 2018. Role of interleukin-6 and interleukin-15 in exercise. MOJI 6. https://doi.org/10.15406/moji.2018.06.00185
Siriett, V., Platt, L., Salerno, M.S., Ling, N., Kambadur, R., et al., 2006. Prolonged absence of myostatin reduces sarcopenia. J. Cell. Physiol. 209, 866–873. https://doi.org/10.1002/jcp.20778
So, B., Kim, H.-J., Kim, J., Song, W., 2014. Exercise-induced myokines in health and metabolic diseases. Integrative Medicine Research 3, 172–179. https://doi.org/10.1016/j.imr.2014.09.007
Spangenburg, E.E., Booth, F.W., 2006. Leukemia inhibitory factor restores the hypertrophic response to increased loading in the LIF(−/−) mouse. Cytokine 34, 125–130. https://doi.org/10.1016/j.cyto.2006.05.001
Tamura, Y., Watanabe, K., Kantani, T., Hayashi, J., Ishida, N., Kaneki, M., 2011. Upregulation of circulating IL-15 by treadmill running in healthy individuals: Is IL-15 an endocrine mediator of the beneficial effects of endurance exercise? Endocr J 58, 211–215. https://doi.org/10.1507/endocrj.K10E-400
Tarkowski, M., Ferraris, L., Martone, S., Strambio de Castillia, F., Misciagna, D., et al., 2012. Expression of Interleukin-15 and Interleukin-15Rα in Monocytes of HIV Type 1-Infected Patients with Different Courses of Disease Progression. AIDS Research and Human Retroviruses 28, 693–701. https://doi.org/10.1089/aid.2010.0317
Taylor, D., 2014. Physical activity is medicine for older adults: Table 1. Postgrad Med J 90, 26–32. https://doi.org/10.1136/postgradmedj-2012-131366
ten Dijke, P., Krause, C., de Gorter, D.J.J., Löwik, C.W.G.M., van Bezooijen, R.L., 2008. Osteocyte-Derived Sclerostin Inhibits Bone Formation: Its Role in Bone Morphogenetic Protein and Wnt Signaling. Journal of Bone and Joint Surgery 90, 31–35. https://doi.org/10.2106/JBJS.G.01183
Tiedemann, A., Sherrington, C., Lord, S.R., 2013. The role of exercise for fall prevention in older age. Motriz: rev. educ. fis. 19, 541–547. https://doi.org/10.1590/S1980-65742013000300002
Tieland, M., Trouwborst, I., Clark, B.C., 2018. Skeletal muscle performance and ageing: Skeletal muscle performance and ageing. Journal of Cachexia, Sarcopenia and Muscle 9, 3–19. https://doi.org/10.1002/jcsm.12238
Tortora GJ, Derrickson B, 2012. Principles of Anatomy and Physiology. Wiley.
Trendelenburg, A.U., Meyer, A., Rohner, D., Boyle, J., Hatakeyama, S., Glass, D.J., 2009. Myostatin reduces Akt/TORC1/p70S6K signaling, inhibiting myoblast differentiation and myotube size. American Journal of Physiology-Cell Physiology 296, C1258–C1270. https://doi.org/10.1152/ajpcell.00105.2009
Tu, X., Delgado-Calle, J., Condon, K.W., Maycas, M., Zhang, H., et al., 2015. Osteocytes mediate the anabolic actions of canonical Wnt/β-catenin signaling in bone. Proc Natl Acad Sci USA 112, E478–E486. https://doi.org/10.1073/pnas.1409857112
Vandervoort, A.A., 2002. Aging of the human neuromuscular system. Muscle Nerve 25, 17–25. https://doi.org/10.1002/mus.1215
Vaughan, R.A., Gannon, N.P., Barberena, M.A., Garcia-Smith, R., Bisoffi, M., Mermier, C.M., et al., 2014. Characterization of the metabolic effects of irisin on skeletal muscle in vitro. Diabetes Obes Metab 16, 711–718. https://doi.org/10.1111/dom.12268
Verdijk, L.B., Snijders, T., Drost, M., Delhaas, T., Kadi, F., van Loon, L.J.C., 2014. Satellite cells in human skeletal muscle; from birth to old age. AGE 36, 545–557. https://doi.org/10.1007/s11357-013-9583-2
Wagner, K.R., Fleckenstein, J.L., Amato, A.A., Barohn, R.J., Bushby, K., et al., 2008. A phase I/IItrial of MYO-029 in adult subjects with muscular dystrophy. Ann Neurol. 63, 561–571. https://doi.org/10.1002/ana.21338
Waldmann, T.A., 2006. The biology of interleukin-2 and interleukin-15: implications for cancer therapy and vaccine design. Nat Rev Immunol 6, 595–601. https://doi.org/10.1038/nri1901
Wall, B.T., van Loon, L.J., 2013. Nutritional strategies to attenuate muscle disuse atrophy. Nutr Rev 71, 195–208. https://doi.org/10.1111/nure.12019
Welc, S.S., Flores, I., Wehling-Henricks, M., Ramos, J., Wang, Y., et al., 2019. Targeting a therapeutic LIF transgene to muscle via the immune system ameliorates muscular dystrophy. Nat Commun 10, 2788. https://doi.org/10.1038/s41467-019-10614-1
White, T.A., LeBrasseur, N.K., 2014. Myostatin and Sarcopenia: Opportunities and Challenges - A Mini-Review. Gerontology 60, 289–293. https://doi.org/10.1159/000356740
Whitmer, R.A., Gustafson, D.R., Barrett-Connor, E., Haan, M.N., Gunderson, E.P., et al., 2008. Central obesity and increased risk of dementia more than three decades later. Neurology 71, 1057–1064. https://doi.org/10.1212/01.wnl.0000306313.89165.ef
Wilkes, J.J., Lloyd, D.J., Gekakis, N., 2009. Loss-of-Function Mutation in Myostatin Reduces Tumor Necrosis Factor α Production and Protects Liver Against Obesity-Induced Insulin Resistance. Diabetes 58, 1133–1143. https://doi.org/10.2337/db08-0245
Wolfman, N.M., McPherron, A.C., Pappano, W.N., Davies, M.V., Song, K., et al, 2003. Activation of latent myostatin by the BMP-1/tolloid family of metalloproteinases. Proc. Natl. Acad. Sci. U.S.A. 100, 15842–15846. https://doi.org/10.1073/pnas.2534946100
Wrann, C.D., White, J.P., Salogiannnis, J., Laznik-Bogoslavski, D., Wu, J., et al., 2013. Exercise Induces Hippocampal BDNF through a PGC-1α/FNDC5 Pathway. Cell Metabolism 18, 649–659. https://doi.org/10.1016/j.cmet.2013.09.008
Yalcin, A., Silay, K., Balik, A.R., Avcioğlu, G., Aydin, A.S., 2018. The relationship between plasma interleukin-15 levels and sarcopenia in outpatient older people. Aging Clin Exp Res 30, 783–790. https://doi.org/10.1007/s40520-017-0848-y
Yang, H., Chang, J., Chen, W., Zhao, L., Qu, B., et al., 2013. Treadmill exercise promotes interleukin 15 expression in skeletal muscle and interleukin 15 receptor alpha expression in adipose tissue of high-fat diet rats. Endocrine 43, 579–585. https://doi.org/10.1007/s12020-012-9809-6
Yang, W., Zhang, Y., Li, Y., Wu, Z., Zhu, D., 2007. Myostatin Induces Cyclin D1 Degradation to Cause Cell Cycle Arrest through a Phosphatidylinositol 3-Kinase/AKT/GSK-3β Pathway and Is Antagonized by Insulin-like Growth Factor 1. Journal of Biological Chemistry 282, 3799–3808. https://doi.org/10.1074/jbc.M610185200
Yarasheski KE, Bhasin S, Sinha-Hikim I, Pak-Loduca J, Gonzalez-Cadavid NF, 2002. Serum myostatin-immunoreactive protein is increased in 60-92 year old women and men with muscle wasting. The Journal of Nutrition, Health & Aging 6, 343–348.
Ye, J., 2015. Beneficial metabolic activities of inflammatory cytokine interleukin 15 in obesity and type 2 diabetes. Front. Med. 9, 139–145. https://doi.org/10.1007/s11684-015-0377-z
Yoon, J.H., Kim, J., Song, P., Lee, T.G., Suh, P.-G., et al., 2012. Secretomics for skeletal muscle cells: A discovery of novel regulators? Advances in Biological Regulation 52, 340–350. https://doi.org/10.1016/j.jbior.2012.03.001
Zhong, S., Chen, C., Thompson, L., 2007. Sarcopenia of ageing: functional, structural and biochemical alterations. Rev. bras. fisioter. 11. https://doi.org/10.1590/S1413-35552007000200002
Zhou, Y., Hellberg, M., Hellmark, T., Höglund, P., Clyne, N., 2021. Muscle mass and plasma myostatin after exercise training: a substudy of Renal Exercise (RENEXC)—a randomized controlled trial. Nephrology Dialysis Transplantation 36, 95–103. https://doi.org/10.1093/ndt/gfz210
Downloads
Published
Categories
License

This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.






