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Korean Society of Computer Information (한국컴퓨터정보학회)
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The role of myokine Irisin on bone metabolism

  • Lee, Jin-Wook (Dept. of Exercise Prescription Rehabilitation, Dankook University) ;
  • Kim, Chan-Yang (graduate school, Dankook University)
  • Received : 2019.05.30
  • Accepted : 2019.08.14
  • Published : 2019.09.30
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Abstract

Several studies have recently demonstrated that skeletal muscle is an endocrine organ releasing and expressing myokines acting in an endocrine or paracrine manner. Irisin is a hormene-like myokine induced after physical exercise by muscle fibers. It was primarily recognized as a molecule able to advance the "browning response" in white adipose tissue, however, it has been recetly identified that irisin also has a fundamental role in the control of bone mass. We study evidence for its possible skeletal effects, including the fundamental role that irisin is involved in the control of bone mass, with beneficial effects on geometry and cortical mineral density. As loss of muscle mass and bone density occurs with immobility, metabolic disease and aging, future studies researching the efficacy of irisin in reversing muscle wasting and restoring bone would be important to proving irisin as a molecule that combines helpful effects for treating muscular atrophy and osteoporosis in elderly people.

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References

  1. J. Y. Reginster, C. Beaudart, F. Buckinx, and O. Bruyere, "Osteoporosis and sarcopenia: two diseases or one?," Current opinion in clinical nutrition and metabolic care, Vol. 19, No. 1, pp. 31, Jan 2015. https://doi.org/10.1097/MCO.0000000000000230
  2. D. Dunstan, “Diabetes: exercise and T2DM-move muscles more often!,” Nat. Rev. Endocrinol, Vol. 7, No. 4, pp. 189-190, March 2011. https://doi.org/10.1038/nrendo.2011.35
  3. B. Egan, and J. R. Zierath, “Exercise metabolism and the molecular regulation of skeletal muscle adaptation,” Cell Metabolism, Vol. 17, No. 2, pp. 162-184, Feb 2013. https://doi.org/10.1016/j.cmet.2012.12.012
  4. G. Colaianni, T. Mongelli, S. Colucci, S. Cinti, and M. Grano, “Crosstalk between muscle and bone via the muscle-myokine irisin,” Current osteoporosis reports, Vol. 14, No. 4, pp. 132-137, Aug 2016. https://doi.org/10.1007/s11914-016-0313-4
  5. H. H. Jones, J. D. Priest, and W. C. Hayes, “Humeral hypertrophy in response to exercise,” Journal of Bone and Joint Surgery A, Vol. 59, No. 2, pp. 204-208, 1977. https://doi.org/10.2106/00004623-197759020-00012
  6. C. M. Girgis, N. Mokbel, and D. J. Digirolamo, “ Therapies for musculoskeletal disease: can we treat two birds with one stone?,” Current osteoporosis reports, Vol. 12, No. 2, pp. 142-153, June 2014. https://doi.org/10.1007/s11914-014-0204-5
  7. C. Tagliaferri, Y. Wittrant, M. J. Davicco, S. Walrand, and V. Coxam, "Muscle and bone, two interconnected tissues," Ageing research reviews, Vol. 21, pp. 55-70, May 2015. https://doi.org/10.1016/j.arr.2015.03.002
  8. L. F. Bonewald, “Osteocytes as dynamic multifunctional cells,” Annals of the New York Academy of Sciences, Vol. 1116, No. 1, pp. 281-290, Dec 2007. https://doi.org/10.1196/annals.1402.018
  9. L. F. Bonewald, and M. L. Johnson, “Osteocytes, mechanosensing and Wnt signaling,” Bone, Vol. 42, No. 4, pp. 606-615, April 2008. https://doi.org/10.1016/j.bone.2007.12.224
  10. Y. Li, Y. Hiroi, and J. K Liao, “Notch signaling as an important mediator of cardiac repair and regeneration after myocardial infarction,” Trends in cardiovascular medicine, Vol. 20, No. 7, pp. 228-231, Oct 2010. https://doi.org/10.1016/j.tcm.2011.11.006
  11. R. S. Rainbow et al, “Muscle cell-derived factors inhibit inflammatory stimuliinduced damage in hMSC-derived chondrocytes,” Osteoarthritis and cartilage, Vol. 21, No. 7, pp. 990-998, July 2013. https://doi.org/10.1016/j.joca.2013.04.011
  12. J. N. Regan, T. Trivedi, T. A. Guise, and D. L. Waning, “The role of $TGF{\beta}$ in bone-muscle crosstalk,” Current osteoporosis reports, Vol. 15, No. 1, pp. 18-23, Feb 2017. https://doi.org/10.1007/s11914-017-0344-5
  13. P. Bostrom et al, “A PGC1-${\alpha}$-dependent myokine that drives brown-fat-like development of white fat and thermogenesis,” Nature, Vol. 481, No. 7382, pp. 463-468, Jan 2012. https://doi.org/10.1038/nature10777
  14. G. Colaianni et al, "Irisin enhances osteoblast differentiation in vitro," International journal of endocrinology, Vol. 2014, pp. 8, Jan 2014.
  15. G. Colaianni et al, “The Myokine Irisin increases cortical bone mass,” Proceedings of the National Academy of Sciences, Vol. 112, No. 39, pp. 12157-12162, Sep 2015. https://doi.org/10.1073/pnas.1516622112
  16. B. K. Pedersen, and M. A. Febbraio, “Muscles, exercise and obesity: skeletal muscle as a secretory organ,” Nature Reviews Endocrinology, Vol. 8, No. 8, pp. 457-465, Apr 2012. https://doi.org/10.1038/nrendo.2012.49
  17. N. A. Sims, "Cell-specific paracrine actions of IL-6 family cytokines from bone, marrow and muscle that control bone formation and resorption," The international journal of biochemistry & cell biology, Vol. 79, pp. 14-23, Oct 2016. https://doi.org/10.1016/j.biocel.2016.08.003
  18. S. Schnyder, and C. Handschin, "Skeletal muscle as an endocrine organ: PGC-1 alpha, myokines and exercise," Bone, Vol. 80, pp. 115-125, Nov 2015. https://doi.org/10.1016/j.bone.2015.02.008
  19. B. K. Pedersen, “Muscle as a secretory organ,” Comprehensive Physiology, Vol. 3, No. 3, pp. 1337-1362, July 2013. https://doi.org/10.1002/cphy.c120033
  20. L. F. Wu et al, “Relative abundance of mature myostatin rather than total myostatin is negatively associated with bone mineral density in Chinese,” Journal of cellular and molecular medicine, Vol. 22, No. 2, pp. 1329-1336, Dec 2017.
  21. H. Kim et al, “Irisin Mediates Effects on Bone and Fat via ${\alpha}V$ Integrin Receptors,” Cell, Vol. 175, No. 7, pp. 1756-1768, Dec 2018. https://doi.org/10.1016/j.cell.2018.10.025
  22. M. W. Berchtold, H. Brinkmeier, and M. Muntener, “Calcium ion in skeletal muscle: its crucial role for muscle function, plasticity, and disease,” Physiological reviews, Vol. 80, No. 3, pp. 1215-1265, JuL 2000. https://doi.org/10.1152/physrev.2000.80.3.1215
  23. A. P. Russell, et al, “Endurance training in humans leads to fiber type-specific increases in levels of peroxisome proliferator-activated receptor-${\gamma}$ coactivator-1 and peroxisome proliferator-activated receptor-${\alpha}$ in skeletal muscle,” Diabetes, Vol. 52, No. 12, pp. 2874-2881, Dec 2003. https://doi.org/10.2337/diabetes.52.12.2874
  24. T. G. Brock, "Weight Loss: A New Star is Irisin, 2015
  25. R. A. Vaughan, N. P. Gannon, C. M. Mermier, and C. A. Conn, "Irisin, a unique non-inflammatory myokine in stimulating skeletal muscle metabolism," Journal of physiology and biochemistry, Vol. 71, No. 4, pp. 679-689 Dec 2015. https://doi.org/10.1007/s13105-015-0433-9
  26. Y. Zhang et al, "Irisin stimulates browning of white adipocytes through mitogen-activated protein kinase p38 MAP kinase and ERK MAP kinase signaling," Diabetes, Vol. 63, No. 2, pp. 514-525 Feb 2014. https://doi.org/10.2337/db13-1106
  27. G. Colaianni et al, “Irisin prevents and restores bone loss and muscle atrophy in hind-limb suspended mice,” Scientific reports, Vol. 7, No. 1, pp. 2811, June 2017. https://doi.org/10.1038/s41598-017-02557-8
  28. X. Li et al, “Targeted deletion of the sclerostin gene in mice results in increased bone formation and bone strength,” Journal of Bone and Mineral Research, Vol. 23, No. 6, pp. 860-869, Dec 2009. https://doi.org/10.1359/jbmr.080216
  29. X. Y. Qiao et al, "Irisin promotes osteoblast proliferation and differentiation via activating the MAP kinase signaling pathways," Sci Rep, Vol. 6, No. 18732, Jan 2016.
  30. A. D. Anastasilakis et al, “Circulating irisin is associated with osteoporotic fractures in postmenopausal women with low bone mass but is not affected by either teriparatide or denosumab treatment for 3 months,” Osteoporosis international, Vol. 25, No. 5, pp. 1633-1642, May 2014. https://doi.org/10.1007/s00198-014-2673-x
  31. V. Singhal et al, “Irisin levels are lower in young amenorrheic athletes compared with eumenorrheic athletes and non-athletes and are associated with bone density and strength estimates,” PLoS ONE, Vol. 9, No. 6, pp. e100218, June 2014. https://doi.org/10.1371/journal.pone.0100218
  32. G. Colaianni et al, “Irisin levels correlate with bone mineral density in soccer players,” Journal of biological regulators and homeostatic agents, Vol. 31, No. 4-1, pp. 21-28, Oct 2017.
  33. G. Colaianni et al, “Irisin and Bone: From Preclinical Studies to the Evaluation of Its Circulating Levels in Different Populations of Human Subjects,” Cells, Vol. 8, No. 5, pp. 451, May 2019. https://doi.org/10.3390/cells8050451
  34. A. Palermo et al, “Irisin is associated with osteoporotic fractures independently of bone mineral density, body composition or daily physical activity,” Clin. Endocrinol, Vol. 82, No. 4, pp. 1615-619, Nov 2015.
  35. T. Klangjareonchai et al, "Circulating sclerostin and Irisin are related and interact with gender to influence adiposity in adults with prediabetes," Int. J. Endocrinol. Vol. 2014, Article ID 261545, 6 pages, 2014.
  36. Y. Tsuchiya, D. Ando, K. Takamatsu, and K. Goto, "Resistance exercise induces a greater irisin response than endurance exercise," Metabolism Vol. 64, No. 9, pp. 1042-1050, Sep 2015. https://doi.org/10.1016/j.metabol.2015.05.010
  37. Y. Tsuchiya, et al, "High-intensity exercise causes greater irisin response compared with low-intensity exercise under similar energy consumption," Tohoku J. Exp. Vol. 223, No. 2, pp. 135-140, 2014. https://doi.org/10.1620/tjem.233.135
  38. S. Soininen et al, "Body fat mass, lean body mass and associated biomarkers as determinants of bone mineral density in children 6-8 years of age-The Physical Activity and Nutrition in Children (PANIC) study," Bone, Vol. 108, pp. 106-114, 2018. https://doi.org/10.1016/j.bone.2018.01.003
  39. J. Y. Huh et al, "Exercise-induced irisin secretion is independent of age or fitness level and increased irisin may directly modulate muscle metabolism through AMPK activation," The Journal of Clinical Endocrinology & Metabolism, Vol. 99, No. 11, pp. E2154-E2161, Nov 2014. https://doi.org/10.1210/jc.2014-1437
  40. T. Shan, X. Liang, P. Bi, and S. Kuang, “Myostatin knockout drives browning of white adipose tissue through activating the AMPK-$PGC1{\alpha}$-Fndc5 pathway in muscle,” The FASEB Journal, Vol. 27, No. 5, pp. 1981-1989, Jan 2013. https://doi.org/10.1096/fj.12-225755
  41. M. G. MacKenzie, D. L. Hamilton, M. Pepin, A. Patton, and K. Baar, “Inhibition of myostatin signaling through Notch activation following acute resistance exercise,” PloS one, Vol. 8, No. 7, pp. e68743, July 2013. https://doi.org/10.1371/journal.pone.0068743
  42. M. N. Elkasrawy, and M. W. Hamrick, “Myostatin (GDF-8) as a key factor linking muscle mass and skeletal form,” Journal of musculoskeletal & neuronal interactions, Vol. 10, No. 1, pp. 56-63, Mar 2010.
  43. Y. Wan, “iBAT on Bone,” Endocrinology, Vol. 154, No. 8, pp. 2579-2580, Aug 2013. https://doi.org/10.1210/en.2013-1514
  44. S. Rahman et al, “Inducible brown adipose tissue, or beige fat, is anabolic for the skeleton,” Endocrinology, Vol. 154, No. 8, pp. 2687-2701, Aug 2013. https://doi.org/10.1210/en.2012-2162