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BioMed Research International
Volume 2015, Article ID 676575, 17 pages
http://dx.doi.org/10.1155/2015/676575
Review Article

Noncoding RNAs, Emerging Regulators of Skeletal Muscle Development and Diseases

1Department of Orthopaedic Surgery, The Second Affiliated Hospital, Chongqing Medical University, 76 Linjiang Road, Chongqing 400010, China
2Department of Cardiology, Boston Children’s Hospital, Harvard Medical School, 320 Longwood Avenue, Boston, MA 02115, USA

Received 15 December 2014; Revised 16 February 2015; Accepted 19 February 2015

Academic Editor: Wanda Lattanzi

Copyright © 2015 Mao Nie et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Linked References

  1. E. S. Lander, L. M. Linton, B. Birren et al., “Initial sequencing and analysis of the human genome,” Nature, vol. 409, no. 6822, pp. 860–921, 2001. View at Publisher · View at Google Scholar
  2. D. P. Bartel, “MicroRNAs: genomics, biogenesis, mechanism, and function,” Cell, vol. 116, no. 2, pp. 281–297, 2004. View at Publisher · View at Google Scholar · View at Scopus
  3. J. L. Rinn and H. Y. Chang, “Genome regulation by long noncoding RNAs,” Annual Review of Biochemistry, vol. 81, pp. 145–166, 2012. View at Publisher · View at Google Scholar · View at Scopus
  4. S. B. P. Chargé and M. A. Rudnicki, “Cellular and molecular regulation of muscle regeneration,” Physiological Reviews, vol. 84, no. 1, pp. 209–238, 2004. View at Publisher · View at Google Scholar · View at Scopus
  5. J. Dhawan and T. A. Rando, “Stem cells in postnatal myogenesis: molecular mechanisms of satellite cell quiescence, activation and replenishment,” Trends in Cell Biology, vol. 15, no. 12, pp. 666–673, 2005. View at Publisher · View at Google Scholar · View at Scopus
  6. S. Kuang and M. A. Rudnicki, “The emerging biology of satellite cells and their therapeutic potential,” Trends in Molecular Medicine, vol. 14, no. 2, pp. 82–91, 2008. View at Publisher · View at Google Scholar · View at Scopus
  7. T. Braun and M. Gautel, “Transcriptional mechanisms regulating skeletal muscle differentiation, growth and homeostasis,” Nature Reviews Molecular Cell Biology, vol. 12, no. 6, pp. 349–361, 2011. View at Publisher · View at Google Scholar · View at Scopus
  8. C. F. Bentzinger, Y. X. Wang, and M. A. Rudnicki, “Building muscle: molecular regulation of myogenesis,” Cold Spring Harbor Perspectives in Biology, vol. 4, no. 2, 2012. View at Publisher · View at Google Scholar · View at Scopus
  9. E. Berardi, D. Annibali, M. Cassano, S. Crippa, and M. Sampaolesi, “Molecular and cell-based therapies for muscle degenerations: a road under construction,” Frontiers in Physiology, vol. 5, article 119, 2014. View at Publisher · View at Google Scholar · View at Scopus
  10. T. E. Callis, Z. Deng, J.-F. Chen, and D.-Z. Wang, “Muscling through the microRNA world,” Experimental Biology and Medicine, vol. 233, no. 2, pp. 131–138, 2008. View at Publisher · View at Google Scholar · View at Scopus
  11. M. Sharma, P. K. Juvvuna, H. Kukreti, and C. McFarlane, “Mega roles of microRNAs in regulation of skeletal muscle health and disease,” Frontiers in Physiology, vol. 5, article 239, 2014. View at Publisher · View at Google Scholar
  12. M. V. Neguembor, M. Jothi, and D. Gabellini, “Long noncoding RNAs, emerging players in muscle differentiation and disease,” Skeletal Muscle, vol. 4, no. 1, article 8, 2014. View at Publisher · View at Google Scholar · View at Scopus
  13. X. Cai, C. H. Hagedorn, and B. R. Cullen, “Human microRNAs are processed from capped, polyadenylated transcripts that can also function as mRNAs,” RNA, vol. 10, no. 12, pp. 1957–1966, 2004. View at Publisher · View at Google Scholar · View at Scopus
  14. R. I. Gregory, K.-P. Yan, G. Amuthan et al., “The Microprocessor complex mediates the genesis of microRNAs,” Nature, vol. 432, no. 7014, pp. 235–240, 2004. View at Publisher · View at Google Scholar · View at Scopus
  15. A. M. Denli, B. B. J. Tops, R. H. A. Plasterk, R. F. Ketting, and G. J. Hannon, “Processing of primary microRNAs by the Microprocessor complex,” Nature, vol. 432, no. 7014, pp. 231–235, 2004. View at Publisher · View at Google Scholar · View at Scopus
  16. Y. Lee, C. Ahn, J. Han et al., “The nuclear RNase III Drosha initiates microRNA processing,” Nature, vol. 425, no. 6956, pp. 415–419, 2003. View at Publisher · View at Google Scholar · View at Scopus
  17. T. P. Chendrimada, R. I. Gregory, E. Kumaraswamy et al., “TRBP recruits the Dicer complex to Ago2 for microRNA processing and gene silencing,” Nature, vol. 436, no. 7051, pp. 740–744, 2005. View at Publisher · View at Google Scholar · View at Scopus
  18. W. Filipowicz, S. N. Bhattacharyya, and N. Sonenberg, “Mechanisms of post-transcriptional regulation by microRNAs: are the answers in sight?” Nature Reviews Genetics, vol. 9, no. 2, pp. 102–114, 2008. View at Publisher · View at Google Scholar · View at Scopus
  19. R. A. Espinoza-Lewis and D. Z. Wang, “MicroRNAs in Heart Development,” Current Topics in developmental biology, vol. 100, pp. 279–317, 2012. View at Publisher · View at Google Scholar · View at Scopus
  20. J. Krol, I. Loedige, and W. Filipowicz, “The widespread regulation of microRNA biogenesis, function and decay,” Nature Reviews Genetics, vol. 11, no. 9, pp. 597–610, 2010. View at Publisher · View at Google Scholar · View at Scopus
  21. D. P. Bartel, “MicroRNAs: target recognition and regulatory functions,” Cell, vol. 136, no. 2, pp. 215–233, 2009. View at Publisher · View at Google Scholar · View at Scopus
  22. N. Liu and E. N. Olson, “MicroRNA regulatory networks in cardiovascular development,” Developmental Cell, vol. 18, no. 4, pp. 510–525, 2010. View at Publisher · View at Google Scholar · View at Scopus
  23. E. M. Small and E. N. Olson, “Pervasive roles of microRNAs in cardiovascular biology,” Nature, vol. 469, no. 7330, pp. 336–342, 2011. View at Publisher · View at Google Scholar · View at Scopus
  24. E. Bernstein, S. Y. Kim, M. A. Carmell et al., “Dicer is essential for mouse development,” Nature Genetics, vol. 35, no. 3, pp. 215–217, 2003. View at Publisher · View at Google Scholar
  25. J. R. O'Rourke, S. A. Georges, H. R. Seay et al., “Essential role for Dicer during skeletal muscle development,” Developmental Biology, vol. 311, no. 2, pp. 359–368, 2007. View at Publisher · View at Google Scholar · View at Scopus
  26. J.-F. Chen, E. M. Mandel, J. M. Thomson et al., “The role of microRNA-1 and microRNA-133 in skeletal muscle proliferation and differentiation,” Nature Genetics, vol. 38, no. 2, pp. 228–233, 2006. View at Publisher · View at Google Scholar · View at Scopus
  27. L. P. Lim, N. C. Lau, P. Garrett-Engele et al., “Microarray analysis shows that some microRNAs downregulate large numbers of-target mRNAs,” Nature, vol. 433, no. 7027, pp. 769–773, 2005. View at Publisher · View at Google Scholar · View at Scopus
  28. Y. Zhao, E. Samal, and D. Srivastava, “Serum response factor regulates a muscle-specific microRNA that targets Hand2 during cardiogenesis,” Nature, vol. 436, no. 7048, pp. 214–220, 2005. View at Publisher · View at Google Scholar · View at Scopus
  29. M. Lagha, T. Sato, L. Bajard et al., “Regulation of skeletal muscle stem cell behavior by Pax3 and Pax7,” Cold Spring Harbor Symposia on Quantitative Biology, vol. 73, pp. 307–315, 2008. View at Publisher · View at Google Scholar · View at Scopus
  30. A. H. Williams, N. Liu, E. van Rooij, and E. N. Olson, “MicroRNA control of muscle development and disease,” Current Opinion in Cell Biology, vol. 21, no. 3, pp. 461–469, 2009. View at Publisher · View at Google Scholar · View at Scopus
  31. A. Antoniou, N. P. Mastroyiannopoulos, J. B. Uney, and L. A. Phylactou, “MiR-186 inhibits muscle cell differentiation through myogenin regulation,” The Journal of Biological Chemistry, vol. 289, no. 7, pp. 3923–3935, 2014. View at Publisher · View at Google Scholar · View at Scopus
  32. I. Naguibneva, M. Ameyar-Zazoua, A. Polesskaya et al., “The microRNA miR-181 targets the homeobox protein Hox-A11 during mammalian myoblast differentiation,” Nature Cell Biology, vol. 8, no. 3, pp. 278–284, 2006. View at Publisher · View at Google Scholar · View at Scopus
  33. J.-F. Chen, Y. Tao, J. Li et al., “microRNA-1 and microRNA-206 regulate skeletal muscle satellite cell proliferation and differentiation by repressing Pax7,” The Journal of Cell Biology, vol. 190, no. 5, pp. 867–879, 2010. View at Publisher · View at Google Scholar · View at Scopus
  34. K. Goljanek-Whysall, D. Sweetman, M. Abu-Elmagd et al., “MicroRNA regulation of the paired-box transcription factor Pax3 confers robustness to developmental timing of myogenesis,” Proceedings of the National Academy of Sciences of the United States of America, vol. 108, no. 29, pp. 11936–11941, 2011. View at Publisher · View at Google Scholar · View at Scopus
  35. H. Hirai, M. Verma, S. Watanabe, C. Tastad, Y. Asakura, and A. Asakura, “MyoD regulates apoptosis of myoblasts through microRNA-mediated down-regulation of Pax3,” Journal of Cell Biology, vol. 191, no. 2, pp. 347–365, 2010. View at Publisher · View at Google Scholar · View at Scopus
  36. N. Liu, A. H. Williams, Y. Kim et al., “An intragenic MEF2-dependent enhancer directs muscle-specific expression of microRNAs 1 and 133,” Proceedings of the National Academy of Sciences of the United States of America, vol. 104, no. 52, pp. 20844–20849, 2007. View at Publisher · View at Google Scholar · View at Scopus
  37. C. G. Crist, D. Montarras, G. Pallafacchina et al., “Muscle stem cell behavior is modified by microRNA-27 regulation of Pax3 expression,” Proceedings of the National Academy of Sciences of the United States of America, vol. 106, no. 32, pp. 13383–13387, 2009. View at Publisher · View at Google Scholar · View at Scopus
  38. B. K. Dey, J. Gagan, and A. Dutta, “miR-206 and -486 induce myoblast differentiation by downregulating Pax7,” Molecular and Cellular Biology, vol. 31, no. 1, pp. 203–214, 2011. View at Publisher · View at Google Scholar · View at Scopus
  39. C. G. Crist, D. Montarras, and M. Buckingham, “Muscle satellite cells are primed for myogenesis but maintain quiescence with sequestration of Myf5 mRNA targeted by microRNA-31 in mRNP granules,” Cell Stem Cell, vol. 11, no. 1, pp. 118–126, 2012. View at Publisher · View at Google Scholar · View at Scopus
  40. U. Huebscher, C. C. Kuenzle, and S. Spadari, “Variation of DNA polymerases-alpha, -beta. and -gamma during perinatal tissue growth and differentiation,” Nucleic Acids Research, vol. 4, no. 8, pp. 2917–2929, 1977. View at Publisher · View at Google Scholar · View at Scopus
  41. H. K. Kim, Y. S. Lee, U. Sivaprasad, A. Malhotra, and A. Dutta, “Muscle-specific microRNA miR-206 promotes muscle differentiation,” Journal of Cell Biology, vol. 174, no. 5, pp. 677–687, 2006. View at Publisher · View at Google Scholar · View at Scopus
  42. N. Liu, S. Bezprozvannaya, A. H. Williams et al., “microRNA-133a regulates cardiomyocyte proliferation and suppresses smooth muscle gene expression in the heart,” Genes and Development, vol. 22, no. 23, pp. 3242–3254, 2008. View at Publisher · View at Google Scholar · View at Scopus
  43. T. Sato, T. Yamamoto, and A. Sehara-Fujisawa, “miR-195/497 induce postnatal quiescence of skeletal muscle stem cells,” Nature Communications, vol. 5, article 4597, 2014. View at Publisher · View at Google Scholar
  44. S. Sarkar, B. K. Dey, and A. Dutta, “MiR-322/424 and -503 are induced during muscle differentiation and promote cell cycle quiescence and differentiation by down-regulation of Cdc25A,” Molecular Biology of the Cell, vol. 21, no. 13, pp. 2138–2149, 2010. View at Publisher · View at Google Scholar · View at Scopus
  45. G. Caretti, M. Di Padova, B. Micales, G. E. Lyons, and V. Sartorelli, “The Polycomb Ezh2 methyltransferase regulates muscle gene expression and skeletal muscle differentiation,” Genes and Development, vol. 18, no. 21, pp. 2627–2638, 2004. View at Publisher · View at Google Scholar · View at Scopus
  46. T. I. Lee, R. G. Jenner, L. A. Boyer et al., “Control of developmental regulators by Polycomb in human embryonic stem cells,” Cell, vol. 125, no. 2, pp. 301–313, 2006. View at Google Scholar
  47. A. H. Juan, R. M. Kumar, J. G. Marx, R. A. Young, and V. Sartorelli, “Mir-214-dependent regulation of the polycomb protein Ezh2 in skeletal muscle and embryonic stem cells,” Molecular Cell, vol. 36, no. 1, pp. 61–74, 2009. View at Publisher · View at Google Scholar · View at Scopus
  48. F. W. Chung and R. L. Tellam, “MicroRNA-26a targets the histone methyltransferase enhancer of Zeste homolog 2 during myogenesis,” The Journal of Biological Chemistry, vol. 283, no. 15, pp. 9836–9843, 2008. View at Publisher · View at Google Scholar · View at Scopus
  49. B. K. Dey, J. Gagan, Z. Yan, and A. Dutta, “miR-26a is required for skeletal muscle differentiation and regeneration in mice,” Genes and Development, vol. 26, no. 19, pp. 2180–2191, 2012. View at Publisher · View at Google Scholar · View at Scopus
  50. L. Zhou, L. Wang, L. Lu, P. Jiang, H. Sun, and H. Wang, “A novel target of microRNA-29, Ring1 and YY1-binding protein (Rybp), negatively regulates skeletal myogenesis,” The Journal of Biological Chemistry, vol. 287, no. 30, pp. 25255–25265, 2012. View at Publisher · View at Google Scholar · View at Scopus
  51. H. Wang, R. Garzon, H. Sun et al., “NF-kappaB-YY1-miR-29 regulatory circuitry in skeletal myogenesis and rhabdomyosarcoma,” Cancer Cell, vol. 14, no. 5, pp. 369–381, 2008. View at Publisher · View at Google Scholar · View at Scopus
  52. W. Wei, H.-B. He, W.-Y. Zhang et al., “MiR-29 targets Akt3 to reduce proliferation and facilitate differentiation of myoblasts in skeletal muscle development,” Cell Death and Disease, vol. 4, no. 6, article e668, 2013. View at Publisher · View at Google Scholar · View at Scopus
  53. P. Seale, B. Bjork, W. Yang et al., “PRDM16 controls a brown fat/skeletal muscle switch,” Nature, vol. 454, no. 7207, pp. 961–967, 2008. View at Publisher · View at Google Scholar · View at Scopus
  54. M. Trajkovski, K. Ahmed, C. C. Esau, and M. Stoffel, “MyomiR-133 regulates brown fat differentiation through Prdm16,” Nature Cell Biology, vol. 14, no. 12, pp. 1330–1335, 2012. View at Publisher · View at Google Scholar · View at Scopus
  55. H. Yin, A. Pasut, V. D. Soleimani et al., “MicroRNA-133 controls brown adipose determination in skeletal muscle satellite cells by targeting Prdm16,” Cell Metabolism, vol. 17, no. 2, pp. 210–224, 2013. View at Publisher · View at Google Scholar · View at Scopus
  56. R. Derynck and R. J. Akhurst, “Differentiation plasticity regulated by TGF-beta family proteins in development and disease,” Nature Cell Biology, vol. 9, no. 9, pp. 1000–1004, 2007. View at Publisher · View at Google Scholar · View at Scopus
  57. Z. Huang, X. Chen, B. Yu, J. He, and D. Chen, “MicroRNA-27a promotes myoblast proliferation by targeting myostatin,” Biochemical and Biophysical Research Communications, vol. 423, no. 2, pp. 265–269, 2012. View at Publisher · View at Google Scholar · View at Scopus
  58. C. McFarlane, A. Vajjala, H. Arigela et al., “Negative auto-regulation of myostatin expression is mediated by Smad3 and MicroRNA-27,” PLoS ONE, vol. 9, no. 1, Article ID e87687, 2014. View at Publisher · View at Google Scholar · View at Scopus
  59. Q. Sun, Y. Zhang, G. Yang et al., “Transforming growth factor-beta-regulated miR-24 promotes skeletal muscle differentiation,” Nucleic Acids Research, vol. 36, no. 8, pp. 2690–2699, 2008. View at Publisher · View at Google Scholar · View at Scopus
  60. B. K. Dey, K. Pfeifer, and A. Dutta, “The H19 long noncoding RNA gives rise to microRNAs miR-675-3p and miR-675-5p to promote skeletal muscle differentiation and regeneration,” Genes and Development, vol. 28, no. 5, pp. 491–501, 2014. View at Publisher · View at Google Scholar · View at Scopus
  61. A. H. Williams, G. Valdez, V. Moresi et al., “MicroRNA-206 delays ALS progression and promotes regeneration of neuromuscular synapses in mice,” Science, vol. 326, no. 5959, pp. 1549–1554, 2009. View at Publisher · View at Google Scholar · View at Scopus
  62. J. M. Toivonen, R. Manzano, S. Oliván et al., “MicroRNA-206: a potential circulating biomarker candidate for amyotrophic lateral sclerosis,” PLoS ONE, vol. 9, no. 2, Article ID e89065, 2014. View at Publisher · View at Google Scholar
  63. C. Anderson, H. Catoe, and R. Werner, “MIR-206 regulates connexin43 expression during skeletal muscle development,” Nucleic Acids Research, vol. 34, no. 20, pp. 5863–5871, 2006. View at Publisher · View at Google Scholar · View at Scopus
  64. M. I. Rosenberg, S. A. Georges, A. Asawachaicharn, E. Analau, and S. J. Tapscott, “MyoD inhibits Fstl1 and Utrn expression by inducing transcription of miR-206,” Journal of Cell Biology, vol. 175, no. 1, pp. 77–85, 2006. View at Publisher · View at Google Scholar · View at Scopus
  65. S. Schiaffino and C. Reggiani, “Fiber types in mammalian skeletal muscles,” Physiological Reviews, vol. 91, no. 4, pp. 1447–1531, 2011. View at Publisher · View at Google Scholar · View at Scopus
  66. S. M. Hughes, M. M.-Y. Chi, O. H. Lowry, and K. Gundersen, “Myogenin induces a shift of enzyme activity from glycolytic to oxidative metabolism in muscles of transgenic mice,” Journal of Cell Biology, vol. 145, no. 3, pp. 633–642, 1999. View at Google Scholar · View at Scopus
  67. E. van Rooij, D. Quiat, B. A. Johnson et al., “A family of microRNAs encoded by myosin genes governs myosin expression and muscle performance,” Developmental Cell, vol. 17, no. 5, pp. 662–673, 2009. View at Publisher · View at Google Scholar · View at Scopus
  68. E. van Rooij, L. B. Sutherland, X. Qi, J. A. Richardson, J. Hill, and E. N. Olson, “Control of stress-dependent cardiac growth and gene expression by a microRNA,” Science, vol. 316, no. 5824, pp. 575–579, 2007. View at Publisher · View at Google Scholar · View at Scopus
  69. D. Quiat, K. A. Voelker, J. Pei et al., “Concerted regulation of myofiber-specific gene expression and muscle performance by the transcriptional repressor Sox6,” Proceedings of the National Academy of Sciences of the United States of America, vol. 108, no. 25, pp. 10196–10201, 2011. View at Publisher · View at Google Scholar · View at Scopus
  70. N. Hagiwara, B. Ma, and A. Ly, “Slow and fast fiber isoform gene expression is systematically altered in skeletal muscle of the Sox6 mutant, p100H,” Developmental Dynamics, vol. 234, no. 2, pp. 301–311, 2005. View at Publisher · View at Google Scholar · View at Scopus
  71. N. Hagiwara, M. Yeh, and A. Liu, “Sox6 is required for normal fiber type differentiation of fetal skeletal muscle in mice,” Developmental Dynamics, vol. 236, no. 8, pp. 2062–2076, 2007. View at Publisher · View at Google Scholar · View at Scopus
  72. J. J. McCarthy, K. A. Esser, C. A. Peterson, and E. E. Dupont-Versteegden, “Evidence of MyomiR network regulation of beta-myosin heavy chain gene expression during skeletal muscle atrophy,” Physiological Genomics, vol. 39, no. 3, pp. 219–226, 2009. View at Publisher · View at Google Scholar · View at Scopus
  73. H. C. Dreyer, S. Fujita, E. L. Glynn, M. J. Drummond, E. Volpi, and B. B. Rasmussen, “Resistance exercise increases leg muscle protein synthesis and mTOR signalling independent of sex,” Acta Physiologica, vol. 199, no. 1, pp. 71–81, 2010. View at Publisher · View at Google Scholar · View at Scopus
  74. D. L. Mayhew, J. S. Kim, J. M. Cross, A. A. Ferrando, and M. M. Bamman, “Translational signaling responses preceding resistance training-mediated myofiber hypertrophy in young and old humans,” Journal of Applied Physiology, vol. 107, no. 5, pp. 1655–1662, 2009. View at Publisher · View at Google Scholar · View at Scopus
  75. A. L. Baggish, A. Hale, R. B. Weiner et al., “Dynamic regulation of circulating microRNA during acute exhaustive exercise and sustained aerobic exercise training,” The Journal of Physiology, vol. 589, no. 16, pp. 3983–3994, 2011. View at Publisher · View at Google Scholar · View at Scopus
  76. P. K. Davidsen, I. J. Gallagher, J. W. Hartman et al., “High responders to resistance exercise training demonstrate differential regulation of skeletal muscle microRNA expression,” Journal of Applied Physiology, vol. 110, no. 2, pp. 309–317, 2011. View at Publisher · View at Google Scholar · View at Scopus
  77. M. B. Hudson, M. E. Woodworth-Hobbs, B. Zheng et al., “miR-23a is decreased during muscle atrophy by a mechanism that includes calcineurin signaling and exosome-mediated export,” The American Journal of Physiology—Cell Physiology, vol. 306, no. 6, pp. C551–C558, 2014. View at Publisher · View at Google Scholar · View at Scopus
  78. W. Aoi, Y. Naito, K. Mizushima et al., “The microRNA miR-696 regulates PGC-1α in mouse skeletal muscle in response to physical activity,” The American Journal of Physiology—Endocrinology and Metabolism, vol. 298, no. 4, pp. E799–E806, 2010. View at Publisher · View at Google Scholar · View at Scopus
  79. A. Safdar, A. Abadi, M. Akhtar, B. P. Hettinga, and M. A. Tarnopolsky, “miRNA in the regulation of skeletal muscle adaptation to acute endurance exercise in C57BI/6J male mice,” PLoS ONE, vol. 4, no. 5, Article ID e5610, 2009. View at Publisher · View at Google Scholar · View at Scopus
  80. S. Wada, Y. Kato, M. Okutsu et al., “Translational suppression of atrophic regulators by MicroRNA-23a integrates resistance to skeletal muscle atrophy,” The Journal of Biological Chemistry, vol. 286, no. 44, pp. 38456–38465, 2011. View at Publisher · View at Google Scholar · View at Scopus
  81. J. Xu, R. Li, B. Workeneh, Y. Dong, X. Wang, and Z. Hu, “Transcription factor FoxO1, the dominant mediator of muscle wasting in chronic kidney disease, is inhibited by microRNA-486,” Kidney International, vol. 82, no. 4, pp. 401–411, 2012. View at Publisher · View at Google Scholar · View at Scopus
  82. J. Y. Kim, Y. K. Park, K. P. Lee et al., “Genome-wide profiling of the microRNA-mRNA regulatory network in skeletal muscle with aging,” Aging (Albany NY), vol. 6, no. 7, pp. 524–544, 2014. View at Google Scholar
  83. M. J. Drummond, J. J. McCarthy, C. S. Fry, K. A. Esser, and B. B. Rasmussen, “Aging differentially affects human skeletal muscle microRNA expression at rest and after an anabolic stimulus of resistance exercise and essential amino acids,” The American Journal of Physiology—Endocrinology and Metabolism, vol. 295, no. 6, pp. E1333–E1340, 2008. View at Publisher · View at Google Scholar · View at Scopus
  84. M. W. Hamrick, S. Herberg, P. Arounleut et al., “The adipokine leptin increases skeletal muscle mass and significantly alters skeletal muscle miRNA expression profile in aged mice,” Biochemical and Biophysical Research Communications, vol. 400, no. 3, pp. 379–383, 2010. View at Publisher · View at Google Scholar · View at Scopus
  85. I. Eisenberg, A. Eran, I. Nishino et al., “Distinctive patterns of microRNA expression in primary muscular disorders,” Proceedings of the National Academy of Sciences of the United States of America, vol. 104, no. 43, pp. 17016–17021, 2007. View at Publisher · View at Google Scholar · View at Scopus
  86. K. E. Davies and K. J. Nowak, “Molecular mechanisms of muscular dystrophies: old and new players,” Nature Reviews Molecular Cell Biology, vol. 7, no. 10, pp. 762–773, 2006. View at Publisher · View at Google Scholar · View at Scopus
  87. F. Rahimov and L. M. Kunkel, “The cell biology of disease: cellular and molecular mechanisms underlying muscular dystrophy,” The Journal of Cell Biology, vol. 201, no. 4, pp. 499–510, 2013. View at Publisher · View at Google Scholar
  88. E. P. Hoffman, R. H. Brown Jr., and L. M. Kunkel, “Dystrophin: the protein product of the Duchenne muscular dystrophy locus,” Cell, vol. 51, no. 6, pp. 919–928, 1987. View at Publisher · View at Google Scholar · View at Scopus
  89. Y. Matsuzaka, S. Kishi, Y. Aoki et al., “Three novel serum biomarkers, miR-1, miR-133a, and miR-206 for Limb-girdle muscular dystrophy, Facioscapulohumeral muscular dystrophy, and Becker muscular dystrophy,” Environmental Health and Preventive Medicine, vol. 19, no. 6, pp. 452–458, 2014. View at Publisher · View at Google Scholar
  90. L. Jeanson-Leh, J. Lameth, S. Krimi et al., “Serum profiling identifies novel muscle miRNA and cardiomyopathy-related miRNA biomarkers in golden retriever muscular dystrophy dogs and duchenne muscular dystrophy patients,” The American Journal of Pathology, vol. 184, no. 11, pp. 2885–2898, 2014. View at Publisher · View at Google Scholar
  91. H. Mizuno, A. Nakamura, Y. Aoki et al., “Identification of muscle-specific MicroRNAs in serum of muscular dystrophy animal models: promising novel blood-based markers for muscular dystrophy,” PLoS ONE, vol. 6, no. 3, Article ID e18388, 2011. View at Publisher · View at Google Scholar · View at Scopus
  92. J. J. McCarthy, K. A. Esser, and F. H. Andrade, “MicroRNA-206 is overexpressed in the diaphragm but not the hindlimb muscle of mdx mouse,” American Journal of Physiology: Cell Physiology, vol. 293, no. 1, pp. C451–C457, 2007. View at Publisher · View at Google Scholar · View at Scopus
  93. Z. Deng, J.-F. Chen, and D.-Z. Wang, “Transgenic overexpression of miR-133a in skeletal muscle,” BMC Musculoskeletal Disorders, vol. 12, article 115, 2011. View at Publisher · View at Google Scholar · View at Scopus
  94. D. Cacchiarelli, I. Legnini, J. Martone et al., “miRNAs as serum biomarkers for Duchenne muscular dystrophy,” The EMBO Molecular Medicine, vol. 3, no. 5, pp. 258–265, 2011. View at Publisher · View at Google Scholar · View at Scopus
  95. I. T. Zaharieva, M. Calissano, M. Scoto et al., “Dystromirs as serum biomarkers for monitoring the disease severity in Duchenne muscular dystrophy,” PLoS ONE, vol. 8, no. 11, Article ID e80263, 2013. View at Publisher · View at Google Scholar · View at Scopus
  96. K. Endo, H. Weng, Y. Naito et al., “Classification of various muscular tissues using miRNA profiling,” Biomedical Research, vol. 34, no. 6, pp. 289–299, 2013. View at Publisher · View at Google Scholar · View at Scopus
  97. M. S. Alexander, J. C. Casar, N. Motohashi et al., “MicroRNA-486–dependent modulation of DOCK3/PTEN/AKT signaling pathways improves muscular dystrophy–associated symptoms,” Journal of Clinical Investigation, vol. 124, no. 6, pp. 2651–2667, 2014. View at Publisher · View at Google Scholar
  98. L. Wang, L. Zhou, P. Jiang et al., “Loss of miR-29 in myoblasts contributes to dystrophic muscle pathogenesis,” Molecular Therapy, vol. 20, no. 6, pp. 1222–1233, 2012. View at Publisher · View at Google Scholar · View at Scopus
  99. M. S. Alexander, G. Kawahara, N. Motohashi et al., “MicroRNA-199a is induced in dystrophic muscle and affects WNT signaling, cell proliferation, and myogenic differentiation,” Cell Death and Differentiation, vol. 20, no. 9, pp. 1194–1208, 2013. View at Publisher · View at Google Scholar · View at Scopus
  100. D. Cacchiarelli, T. Incitti, J. Martone et al., “MiR-31 modulates dystrophin expression: new implications for Duchenne muscular dystrophy therapy,” The EMBO Reports, vol. 12, no. 2, pp. 136–141, 2011. View at Publisher · View at Google Scholar · View at Scopus
  101. N. Liu, S. Bezprozvannaya, J. M. Shelton et al., “Mice lacking microRNA 133a develop dynamin 2-dependent centronuclear myopathy,” The Journal of Clinical Investigation, vol. 121, no. 8, pp. 3258–3268, 2011. View at Publisher · View at Google Scholar · View at Scopus
  102. M. Bitoun, A.-C. C. Durieux, B. Prudhon et al., “Dynamin 2 mutations associated with human diseases impair clathrin-mediated receptor endocytosis,” Human Mutation, vol. 30, no. 10, pp. 1419–1427, 2009. View at Publisher · View at Google Scholar · View at Scopus
  103. A.-C. Durieux, B. Prudhon, P. Guicheney, and M. Bitoun, “Dynamin 2 and human diseases,” Journal of Molecular Medicine, vol. 88, no. 4, pp. 339–350, 2010. View at Publisher · View at Google Scholar · View at Scopus
  104. G. Merlino and L. J. Helman, “Rhabdomyosarcoma—working out the pathways,” Oncogene, vol. 18, no. 38, pp. 5340–5348, 1999. View at Publisher · View at Google Scholar · View at Scopus
  105. M. Wachtel, T. Runge, I. Leuschner et al., “Subtype and prognostic classification of rhabdomyosarcoma by immunohistochemistry,” Journal of Clinical Oncology, vol. 24, no. 5, pp. 816–822, 2006. View at Publisher · View at Google Scholar · View at Scopus
  106. E. Missiaglia, C. J. Shepherd, S. Patel et al., “MicroRNA-206 expression levels correlate with clinical behaviour of rhabdomyosarcomas,” British Journal of Cancer, vol. 102, no. 12, pp. 1769–1777, 2010. View at Publisher · View at Google Scholar · View at Scopus
  107. R. Taulli, F. Bersani, V. Foglizzo et al., “The muscle-specific microRNA miR-206 blocks human rhabdomyosarcoma growth in xenotransplanted mice by promoting myogenic differentiation,” The Journal of Clinical Investigation, vol. 119, no. 8, pp. 2366–2378, 2009. View at Publisher · View at Google Scholar · View at Scopus
  108. D. Yan, X. D. Dong, X. Chen et al., “MicroRNA-1/206 targets c-met and inhibits rhabdomyosarcoma development,” Journal of Biological Chemistry, vol. 284, no. 43, pp. 29596–29604, 2009. View at Google Scholar · View at Scopus
  109. X. Li, Y. Li, L. Zhao et al., “Circulating muscle-specific miRNAs in Duchenne muscular dystrophy patients,” Molecular Therapy—Nucleic Acids, vol. 3, no. 7, p. e177, 2014. View at Publisher · View at Google Scholar
  110. C. Chen, K. Wang, J. Chen et al., “In vitro evidence suggests that miR-133a-mediated regulation of uncoupling protein 2 (UCP2) is an indispensable step in myogenic differentiation,” The Journal of Biological Chemistry, vol. 284, no. 8, pp. 5362–5369, 2009. View at Publisher · View at Google Scholar · View at Scopus
  111. N. Liu, A. H. Williams, J. M. Maxeiner et al., “microRNA-206 promotes skeletal muscle regeneration and delays progression of Duchenne muscular dystrophy in mice,” Journal of Clinical Investigation, vol. 122, no. 6, pp. 2054–2065, 2012. View at Publisher · View at Google Scholar · View at Scopus
  112. L. Wang, X. Chen, Y. Zheng et al., “MiR-23a inhibits myogenic differentiation through down regulation of fast myosin heavy chain isoforms,” Experimental Cell Research, vol. 318, no. 18, pp. 2324–2334, 2012. View at Publisher · View at Google Scholar · View at Scopus
  113. L. Zhou, L. Wang, L. Lu, P. Jiang, H. Sun, and H. Wang, “Inhibition of miR-29 by TGF-beta-Smad3 signaling through dual mechanisms promotes transdifferentiation of mouse myoblasts into myofibroblasts,” PLoS ONE, vol. 7, no. 3, Article ID e33766, 2012. View at Publisher · View at Google Scholar · View at Scopus
  114. C. E. Winbanks, B. Wang, C. Beyer et al., “TGF-beta regulates miR-206 and miR-29 to control myogenic differentiation through regulation of HDAC4,” The Journal of Biological Chemistry, vol. 286, no. 16, pp. 13805–13814, 2011. View at Publisher · View at Google Scholar · View at Scopus
  115. A. S. Qadir, K. M. Woo, H.-M. Ryoo, T. Yi, S. U. Song, and J.-H. Baek, “MiR-124 inhibits myogenic differentiation of mesenchymal stem cells via targeting Dlx5,” Journal of Cellular Biochemistry, vol. 115, no. 9, pp. 1572–1581, 2014. View at Publisher · View at Google Scholar
  116. Y. Ge, Y. Sun, and J. Chen, “IGF-II is regulated by microRNA-125b in skeletal myogenesis,” Journal of Cell Biology, vol. 192, no. 1, pp. 69–81, 2011. View at Publisher · View at Google Scholar · View at Scopus
  117. N. Motohashi, M. S. Alexander, Y. Shimizu-Motohashi, J. A. Myers, G. Kawahara, and L. M. Kunkel, “Regulation of IRS1/Akt insulin signaling by microRNA-128a during myogenesis,” Journal of Cell Science, vol. 126, no. 12, pp. 2678–2691, 2013. View at Publisher · View at Google Scholar · View at Scopus
  118. J. Zhang, Z.-Z. Ying, Z.-L. Tang, L.-Q. Long, and K. Li, “MicroRNA-148a promotes myogenic differentiation by targeting the ROCK1 gene,” Journal of Biological Chemistry, vol. 287, no. 25, pp. 21093–21101, 2012. View at Publisher · View at Google Scholar · View at Scopus
  119. N. Khanna, Y. Ge, and J. Chen, “MicroRNA-146b promotes myogenic differentiation and modulates multiple gene targets in muscle cells,” PLoS ONE, vol. 9, no. 6, Article ID e100657, 2014. View at Publisher · View at Google Scholar
  120. H. Y. Seok, M. Tatsuguchi, T. E. Callis, A. He, W. T. Pu, and D.-Z. Wang, “miR-155 inhibits expression of the MEF2A protein to repress skeletal muscle differentiation,” The Journal of Biological Chemistry, vol. 286, no. 41, pp. 35339–35346, 2011. View at Publisher · View at Google Scholar · View at Scopus
  121. L. Jia, Y. F. Li, G. F. Wu et al., “MiRNA-199a-3p regulates C2C12 myoblast differentiation through IGF-1/AKT/mTOR signal pathway,” International Journal of Molecular Sciences, vol. 15, no. 1, pp. 296–308, 2014. View at Publisher · View at Google Scholar
  122. W. Luo, H. Wu, Y. Ye et al., “The transient expression of miR-203 and its inhibiting effects on skeletal muscle cell proliferation and differentiation,” Cell Death and Disease, vol. 5, no. 7, p. e1347, 2014. View at Publisher · View at Google Scholar
  123. B. Yan, J.-T. Guo, C.-D. Zhu, L.-H. Zhao, and J.-L. Zhao, “miR-203b: a novel regulator of MyoD expression in tilapia skeletal muscle,” Journal of Experimental Biology, vol. 216, no. 3, pp. 447–451, 2013. View at Publisher · View at Google Scholar · View at Scopus
  124. Y. Feng, J.-H. Cao, X.-Y. Li, and S.-H. Zhao, “Inhibition of miR-214 expression represses proliferation and differentiation of C2C12 myoblasts,” Cell Biochemistry and Function, vol. 29, no. 5, pp. 378–383, 2011. View at Publisher · View at Google Scholar · View at Scopus
  125. S.-B. Tan, J. Li, X. Chen et al., “Small molecule inhibitor of myogenic microRNAs leads to a discovery of miR-221/222-myoD-myomiRs regulatory pathway,” Chemistry & Biology, vol. 21, no. 10, pp. 1265–1270, 2014. View at Publisher · View at Google Scholar
  126. B. Cardinalli, L. Castellani, P. Fasanaro et al., “Microrna-221 and microrna-222 modulate differentiation and maturation of skeletal muscle cells,” PLoS ONE, vol. 4, no. 10, Article ID e7607, 2009. View at Publisher · View at Google Scholar · View at Scopus
  127. Y. Chen, D. W. Melton, J. A. L. Gelfond, L. M. McManus, and P. K. Shireman, “MiR-351 transiently increases during muscle regeneration and promotes progenitor cell proliferation and survival upon differentiation,” Physiological Genomics, vol. 44, no. 21, pp. 1042–1051, 2012. View at Publisher · View at Google Scholar · View at Scopus
  128. J. Gagan, B. K. Dey, R. Layer, Z. Yan, and A. Dutta, “MicroRNA-378 targets the myogenic repressor MyoR during myoblast differentiation,” The Journal of Biological Chemistry, vol. 286, no. 22, pp. 19431–19438, 2011. View at Publisher · View at Google Scholar · View at Scopus
  129. T. H. Cheung, N. L. Quach, G. W. Charville et al., “Maintenance of muscle stem-cell quiescence by microRNA-489,” Nature, vol. 482, no. 7386, pp. 524–528, 2012. View at Publisher · View at Google Scholar · View at Scopus
  130. S. Crippa, M. Cassano, G. Messina et al., “miR669a and miR669q prevent skeletal muscle differentiation in postnatal cardiac progenitors,” Journal of Cell Biology, vol. 193, no. 7, pp. 1197–1212, 2011. View at Publisher · View at Google Scholar · View at Scopus
  131. Y. Chen, J. Gelfond, L. M. McManus, and P. K. Shireman, “Temporal microRNA expression during in vitro myogenic progenitor cell proliferation and differentiation: regulation of proliferation by miR-682,” Physiological Genomics, vol. 43, no. 10, pp. 621–630, 2011. View at Publisher · View at Google Scholar · View at Scopus
  132. V. Dormoy-Raclet, A. Cammas, B. Celona et al., “HuR and miR-1192 regulate myogenesis by modulating the translation of HMGB1 mRNA,” Nature Communications, vol. 4, article 2388, 2013. View at Publisher · View at Google Scholar · View at Scopus
  133. C.-Y. Lin, J.-S. Chen, M.-R. Loo, C.-C. Hsiao, W.-Y. Chang, and H.-J. Tsai, “MicroRNA-3906 regulates fast muscle differentiation through modulating the target gene homer-1b in zebrafish embryos,” PLoS ONE, vol. 8, no. 7, Article ID e70187, 2013. View at Publisher · View at Google Scholar · View at Scopus
  134. I. Ulitsky and D. P. Bartel, “XLincRNAs: genomics, evolution, and mechanisms,” Cell, vol. 154, no. 1, pp. 26–46, 2013. View at Publisher · View at Google Scholar · View at Scopus
  135. T. Derrien, R. Johnson, G. Bussotti et al., “The GENCODE v7 catalog of human long noncoding RNAs: analysis of their gene structure, evolution, and expression,” Genome Research, vol. 22, no. 9, pp. 1775–1789, 2012. View at Publisher · View at Google Scholar · View at Scopus
  136. M. Guttman and J. L. Rinn, “Modular regulatory principles of large non-coding RNAs,” Nature, vol. 482, no. 7385, pp. 339–346, 2012. View at Publisher · View at Google Scholar · View at Scopus
  137. P. J. Batista and H. Y. Chang, “Long noncoding RNAs: cellular address codes in development and disease,” Cell, vol. 152, no. 6, pp. 1298–1307, 2013. View at Publisher · View at Google Scholar · View at Scopus
  138. F. de Santa, I. Barozzi, F. Mietton et al., “A large fraction of extragenic RNA Pol II transcription sites overlap enhancers,” PLoS Biology, vol. 8, no. 5, 2010. View at Publisher · View at Google Scholar · View at Scopus
  139. T.-K. Kim, M. Hemberg, J. M. Gray et al., “Widespread transcription at neuronal activity-regulated enhancers,” Nature, vol. 465, no. 7295, pp. 182–187, 2010. View at Publisher · View at Google Scholar · View at Scopus
  140. U. A. Orom and R. Shiekhattar, “XLong noncoding RNAs usher in a new era in the biology of enhancers,” Cell, vol. 154, no. 6, pp. X1190–1193, 2013. View at Publisher · View at Google Scholar · View at Scopus
  141. N. Hah, S. Murakami, A. Nagari, C. G. Danko, and W. Lee Kraus, “Enhancer transcripts mark active estrogen receptor binding sites,” Genome Research, vol. 23, no. 8, pp. 1210–1223, 2013. View at Publisher · View at Google Scholar · View at Scopus
  142. F. Lai, U. A. Orom, M. Cesaroni et al., “Activating RNAs associate with Mediator to enhance chromatin architecture and transcription,” Nature, vol. 494, no. 7438, pp. 497–501, 2013. View at Publisher · View at Google Scholar · View at Scopus
  143. M. T. Y. Lam, H. Cho, H. P. Lesch et al., “Rev-Erbs repress macrophage gene expression by inhibiting enhancer-directed transcription,” Nature, vol. 498, no. 7455, pp. 511–515, 2013. View at Publisher · View at Google Scholar · View at Scopus
  144. W. Li, D. Notani, Q. Ma et al., “Functional roles of enhancer RNAs for oestrogen-dependent transcriptional activation,” Nature, vol. 498, no. 7455, pp. 516–520, 2013. View at Publisher · View at Google Scholar · View at Scopus
  145. C. A. Melo, J. Drost, P. J. Wijchers et al., “eRNAs are required for p53-dependent enhancer activity and gene transcription,” Molecular Cell, vol. 49, no. 3, pp. 524–535, 2013. View at Publisher · View at Google Scholar · View at Scopus
  146. U. A. Ørom, T. Derrien, M. Beringer et al., “Long noncoding RNAs with enhancer-like function in human cells,” Cell, vol. 143, no. 1, pp. 46–58, 2010. View at Publisher · View at Google Scholar · View at Scopus
  147. K. C. Wang, Y. W. Yang, B. Liu et al., “A long noncoding RNA maintains active chromatin to coordinate homeotic gene expression,” Nature, vol. 472, no. 7341, pp. 120–126, 2011. View at Publisher · View at Google Scholar · View at Scopus
  148. K. Mousavi, H. Zare, S. Dell'Orso et al., “eRNAs promote transcription by establishing chromatin accessibility at defined genomic loci,” Molecular Cell, vol. 51, no. 5, pp. 606–617, 2013. View at Publisher · View at Google Scholar · View at Scopus
  149. A. C. Mueller, M. A. Cichewicz, B. K. Dey et al., “MUNC: a lncRNA that induces the expression of pro-myogenic genes in skeletal myogenesis,” Molecular and Cellular Biology, 2014. View at Publisher · View at Google Scholar
  150. L. Lu, K. Sun, X. Chen et al., “Genome-wide survey by ChIP-seq reveals YY1 regulation of lincRNAs in skeletal myogenesis,” EMBO Journal, vol. 32, no. 19, pp. 2575–2588, 2013. View at Publisher · View at Google Scholar · View at Scopus
  151. S. T. da Rocha, C. A. Edwards, M. Ito, T. Ogata, and A. C. Ferguson-Smith, “Genomic imprinting at the mammalian Dlk1-Dio3 domain,” Trends in Genetics, vol. 24, no. 6, pp. 306–316, 2008. View at Publisher · View at Google Scholar · View at Scopus
  152. J. Zhao, T. K. Ohsumi, J. T. Kung et al., “Genome-wide identification of polycomb-associated RNAs by RIP-seq,” Molecular Cell, vol. 40, no. 6, pp. 939–953, 2010. View at Publisher · View at Google Scholar · View at Scopus
  153. Y. Zhou, P. Cheunsuchon, Y. Nakayama et al., “Activation of paternally expressed genes and perinatal death caused by deletion of the Gtl2 gene,” Development, vol. 137, no. 16, pp. 2643–2652, 2010. View at Publisher · View at Google Scholar · View at Scopus
  154. G. Caretti, R. L. Schiltz, F. J. Dilworth et al., “The RNA helicases p68/p72 and the noncoding RNA SRA are coregulators of MyoD and skeletal muscle differentiation,” Developmental Cell, vol. 11, no. 4, pp. 547–560, 2006. View at Publisher · View at Google Scholar · View at Scopus
  155. R. B. Lanz, N. J. McKenna, S. A. Onate et al., “A steroid receptor coactivator, SRA, functions as an RNA and is present in an SRC-1 complex,” Cell, vol. 97, no. 1, pp. 17–27, 1999. View at Publisher · View at Google Scholar · View at Scopus
  156. F. Hubé, G. Velasco, J. Rollin, D. Furling, and C. Francastel, “Steroid receptor RNA activator protein binds to and counteracts SRA RNA-mediated activation of MyoD and muscle differentiation,” Nucleic Acids Research, vol. 39, no. 2, pp. 513–525, 2011. View at Publisher · View at Google Scholar · View at Scopus
  157. E. Emberley, G.-J. Huang, M. K. Hamedani et al., “Identification of new human coding steroid receptor RNA activator isoforms,” Biochemical and Biophysical Research Communications, vol. 301, no. 2, pp. 509–515, 2003. View at Publisher · View at Google Scholar · View at Scopus
  158. S. Khosla, A. Aitchison, R. Gregory, N. D. Allen, and R. Feil, “Parental allele-specific chromatin configuration in a boundary-imprinting-control element upstream of the mouse H19 gene,” Molecular and Cellular Biology, vol. 19, no. 4, pp. 2556–2566, 1999. View at Google Scholar · View at Scopus
  159. R. L. Davis, H. Weintraub, and A. B. Lassar, “Expression of a single transfected cDNA converts fibroblasts to myoblasts,” Cell, vol. 51, no. 6, pp. 987–1000, 1987. View at Publisher · View at Google Scholar · View at Scopus
  160. A. Gabory, H. Jammes, and L. Dandolo, “The H19 locus: role of an imprinted non-coding RNA in growth and development,” BioEssays, vol. 32, no. 6, pp. 473–480, 2010. View at Publisher · View at Google Scholar · View at Scopus
  161. T. Forne, J. Oswald, W. Dean et al., “Loss of the maternal H19 gene induces changes in Igf2 methylation in both cis and trans,” Proceedings of the National Academy of Sciences of the United States of America, vol. 94, no. 19, pp. 10243–10248, 1997. View at Publisher · View at Google Scholar · View at Scopus
  162. M. A. Ripoche, C. Kress, F. Poirier, and L. Dandolo, “Deletion of the H19 transcription unit reveals the existence of a putative imprinting control element,” Genes and Development, vol. 11, no. 12, pp. 1596–1604, 1997. View at Publisher · View at Google Scholar · View at Scopus
  163. S. Runge, F. C. Nielsen, J. Nielsen, J. Lykke-Andersen, U. M. Wewer, and J. Christiansen, “H19 RNA binds four molecules of insulin-like growth factor II mRNA-binding protein,” The Journal of Biological Chemistry, vol. 275, no. 38, pp. 29562–29569, 2000. View at Publisher · View at Google Scholar · View at Scopus
  164. A. N. Kallen, X.-B. Zhou, J. Xu et al., “The Imprinted H19 LncRNA Antagonizes Let-7 MicroRNAs,” Molecular Cell, vol. 52, no. 1, pp. 101–112, 2013. View at Publisher · View at Google Scholar · View at Scopus
  165. M. Cesana, D. Cacchiarelli, I. Legnini et al., “A long noncoding RNA controls muscle differentiation by functioning as a competing endogenous RNA,” Cell, vol. 147, no. 2, pp. 358–369, 2011. View at Publisher · View at Google Scholar · View at Scopus
  166. I. Legnini, M. Morlando, A. Mangiavacchi, A. Fatica, and I. Bozzoni, “A feedforward regulatory loop between HuR and the long noncoding RNA linc-MD1 controls early phases of myogenesis,” Molecular Cell, vol. 53, no. 3, pp. 506–514, 2014. View at Publisher · View at Google Scholar · View at Scopus
  167. A. Kapusta, Z. Kronenberg, V. J. Lynch et al., “Transposable elements are major contributors to the origin, diversification, and regulation of vertebrate long noncoding RNAs,” PLoS Genetics, vol. 9, no. 4, Article ID e1003470, 2013. View at Publisher · View at Google Scholar · View at Scopus
  168. C. Carrieri, L. Cimatti, M. Biagioli et al., “Long non-coding antisense RNA controls Uchl1 translation through an embedded SINEB2 repeat,” Nature, vol. 491, no. 7424, pp. 454–457, 2012. View at Publisher · View at Google Scholar · View at Scopus
  169. C. Gong and L. E. Maquat, “LncRNAs transactivate STAU1-mediated mRNA decay by duplexing with 3′ UTRs via Alu eleme,” Nature, vol. 470, no. 7333, pp. 284–288, 2011. View at Publisher · View at Google Scholar · View at Scopus
  170. J. Wang, C. Gong, and L. E. Maquat, “Control of myogenesis by rodent SINE-containing lncRNAs,” Genes and Development, vol. 27, no. 7, pp. 793–804, 2013. View at Publisher · View at Google Scholar · View at Scopus
  171. T. Gutschner, M. Hämmerle, M. Eißmann et al., “The noncoding RNA MALAT1 is a critical regulator of the metastasis phenotype of lung cancer cells,” Cancer Research, vol. 73, no. 3, pp. 1180–1189, 2013. View at Publisher · View at Google Scholar · View at Scopus
  172. V. Tripathi, Z. Shen, A. Chakraborty et al., “Long noncoding RNA MALAT1 controls cell cycle progression by regulating the expression of oncogenic transcription factor B-MYB,” PLoS Genetics, vol. 9, no. 3, Article ID e1003368, 2013. View at Publisher · View at Google Scholar · View at Scopus
  173. V. Tripathi, J. D. Ellis, Z. Shen et al., “The nuclear-retained noncoding RNA MALAT1 regulates alternative splicing by modulating SR splicing factor phosphorylation,” Molecular Cell, vol. 39, no. 6, pp. 925–938, 2010. View at Publisher · View at Google Scholar · View at Scopus
  174. L. Yang, C. Lin, W. Liu et al., “NcRNA- and Pc2 methylation-dependent gene relocation between nuclear structures mediates gene activation programs,” Cell, vol. 147, no. 4, pp. 773–788, 2011. View at Google Scholar · View at Scopus
  175. M. Thomas, B. Langley, C. Berry et al., “Myostatin, a negative regulator of muscle growth, functions by inhibiting myoblast proliferation,” Journal of Biological Chemistry, vol. 275, no. 51, pp. 40235–40243, 2000. View at Publisher · View at Google Scholar · View at Scopus
  176. R. Watts, V. L. Johnsen, J. Shearer, and D. S. Hittel, “Myostatin-induced inhibition of the long noncoding RNA Malat1 is associated with decreased myogenesis,” The American Journal of Physiology—Cell Physiology, vol. 304, no. 10, pp. C995–C1001, 2013. View at Publisher · View at Google Scholar · View at Scopus
  177. M. Bovolenta, D. Erriquez, E. Valli et al., “The DMD locus harbours multiple long non-coding RNAs which orchestrate and control transcription of muscle dystrophin mRNA isoforms,” PLoS ONE, vol. 7, no. 9, Article ID e45328, 2012. View at Publisher · View at Google Scholar · View at Scopus
  178. T. H. T. Tran, Z. Zhang, M. Yagi et al., “Molecular characterization of an X(p21.2;q28) chromosomal inversion in a Duchenne muscular dystrophy patient with mental retardation reveals a novel long non-coding gene on Xq28,” Journal of Human Genetics, vol. 58, no. 1, pp. 33–39, 2013. View at Publisher · View at Google Scholar · View at Scopus
  179. M. M. O. Tonini, M. R. Passos-Bueno, A. Cerqueira, S. R. Matioli, R. Pavanello, and M. Zatz, “Asymptomatic carriers and gender differences in facioscapulohumeral muscular dystrophy (FSHD),” Neuromuscular Disorders, vol. 14, no. 1, pp. 33–38, 2004. View at Publisher · View at Google Scholar · View at Scopus
  180. C. Wijmenga, L. A. Sandkuijl, P. Moerer et al., “Genetic linkage map of facioscapulohumeral muscular dystrophy and five polymorphic loci on chromosome 4q35-qter,” The American Journal of Human Genetics, vol. 51, no. 2, pp. 411–415, 1992. View at Google Scholar · View at Scopus
  181. J. E. Hewitt, R. Lyle, L. N. Clark et al., “Analysis of the tandem repeat locus D4Z4 associated with facioscapulohumeral muscular dystrophy,” Human Molecular Genetics, vol. 3, no. 8, pp. 1287–1295, 1994. View at Publisher · View at Google Scholar · View at Scopus
  182. J. C. T. van Deutekom, C. Wijmenga, E. A. E. van Tienhoven et al., “FSHD associated DNA rearrangements are due to deletions of integral copies of a 3.2 kb tandemly repeated unit,” Human Molecular Genetics, vol. 2, no. 12, pp. 2037–2042, 1993. View at Publisher · View at Google Scholar · View at Scopus
  183. C. Wijmenga, J. E. Hewitt, L. A. Sandkuijl et al., “Chromosome 4q DNA rearrangements associated with facioscapulohumeral muscular dystrophy,” Nature Genetics, vol. 2, no. 1, pp. 26–30, 1992. View at Publisher · View at Google Scholar · View at Scopus
  184. D. S. Cabianca, V. Casa, B. Bodega et al., “A long ncRNA links copy number variation to a polycomb/trithorax epigenetic switch in fshd muscular dystrophy,” Cell, vol. 149, no. 4, pp. 819–831, 2012. View at Publisher · View at Google Scholar · View at Scopus
  185. D. M. Anderson, K. M. Anderson, C.-L. Chang et al., “A micropeptide encoded by a putative long noncoding RNA regulates muscle performance,” Cell, vol. 160, no. 4, pp. 595–606, 2015. View at Publisher · View at Google Scholar