대한물리의학회지 (Journal of the Korean Society of Physical Medicine)

  • 제14권2호
  • /
  • Pages.63-70
  • /
  • 2019
  • /
  • 1975-311X(pISSN)
  • /
  • 2287-7215(eISSN)
대한물리의학회 (The Korean Society of Physical Medicine)
권호 표지
DOI QR코드

DOI QR Code

Induction of Myogenic Differentiation in Myoblasts by Electrical Stimulation

  • Je, Hyeon-Jeong (Department of Physical Therapy and Rehabilitation, College of Health Science, Eulji University) ;
  • Kim, Min-Gu (Department of Physical Therapy and Rehabilitation, College of Health Science, Eulji University) ;
  • Cho, Il-Hoon (Department of Biomedical Laboratory Science, College of Health Science, Eulji University) ;
  • Kwon, Hyuck-Joon (Department of Physical Therapy and Rehabilitation, College of Health Science, Eulji University)
  • 투고 : 2019.04.04
  • 심사 : 2019.04.22
  • 발행 : 2019.05.31
PDF 다운로드
⟨ 이전 논문 다음 논문 ⟩

초록

PURPOSE: While electrical stimulation (ES) is known to be a safe and flexible tool in rehabilitation therapy, it has had limited adoption in muscle regeneration. This study was performed to investigate whether ES can induce myogenic differentiation and to clarify the mechanism underlying the effects of ES on myogenic differentiation. METHODS: This study used rat L6 cell lines as myoblasts for myogenic differentiation. Electric stimulation was applied to the cells using a C-Pace EP culture pacer (IonOptix, Westwood, Ma, USA). The gene expressions of myogenic markers were examined using qPCR and immunochemistry. RESULTS: Our study showed that ES increased the thickness and length of myotubes during myogenic differentiation. It was found that ES increased the expression of myogenic markers, such as MyoD and Myogenin, and also activated the fusion of the myoblast cells. In addition, ES suppressed the expression of small GTPases, which can explain why ES promotes myogenic differentiation. CONCLUSION: We found that ES induced myogenic differentiation by suppressing small GTPases, inhibiting cell division. We suggest that ES-based therapies can contribute to the development of safe and efficient muscle regeneration.

키워드

참고문헌

  1. Goodpaster BH, Park SW, Harris TB, et al. The loss of skeletal muscle strength, mass, and quality in older adults: the health, aging and body composition study. J Gerontol A Biol Sci Med Sci. 2006;61(10):1059-64. https://doi.org/10.1093/gerona/61.10.1059
  2. Faulkner JA, Larkin LM, Claflin DR, et al. Age-related changes in the structure and function of skeletal muscles. Clin Exp Pharmacol Physiol. 2007;34(11):1091-6. https://doi.org/10.1111/j.1440-1681.2007.04752.x
  3. Dolbow DR, Gorgey AS. Effects of use and disuse on non-paralyzed and paralyzed skeletal muscles. Aging Dis. 2016;7(1):68-80. https://doi.org/10.14336/AD.2015.0826
  4. Sacco A, Doyonnas R, Kraft P, et al. Self-renewal and expansion of single transplanted muscle stem cells. 2008;456(7221):502. https://doi.org/10.1038/nature07384
  5. Loebel C, Burdick JA. Engineering stem and stromal cell therapies for musculoskeletal tissue repair. Cell Stem Cell. 2018;22(3):325-39. https://doi.org/10.1016/j.stem.2018.01.014
  6. Florini JR, Magri KA. Effects of growth factors on myogenic differentiation. Am J Physiol. 1989;256(4 Pt 1):C701-11. https://doi.org/10.1152/ajpcell.1989.256.4.C701
  7. Herberts CA, Kwa MS, Hermsen HP. Risk factors in the development of stem cell therapy. J Transl Med. 2011;9:29. https://doi.org/10.1186/1479-5876-9-29
  8. Guilak F, Cohen DM, Estes BT, et al. Control of stem cell fate by physical interactions with the extracellular matrix. Cell Stem Cell. 2009;5(1):17-26. https://doi.org/10.1016/j.stem.2009.06.016
  9. Kshitiz, Park J, Kim P, et al. Control of stem cell fate and function by engineering physical microenvironments. Integr Biol (Camb). 2012;4(9):1008-18. https://doi.org/10.1039/c2ib20080e
  10. Bassett CA, Pawluk RJ. Electrical behavior of cartilage during loading. Science. 1972;178(4064):982-3. https://doi.org/10.1126/science.178.4064.982
  11. Foulds I, Barker A. Human skin battery potentials and their possible role in wound healing. The British Journal of Dermatology. 1983;109(5):515-22. https://doi.org/10.1111/j.1365-2133.1983.tb07673.x
  12. Smith SD, McLeod BR, Liboff AR, et al. Calcium cyclotron resonance and diatom mobility. Bioelectromagnetics. 1987;8(3):215-27. https://doi.org/10.1002/bem.2250080302
  13. Bezanilla F. How membrane proteins sense voltage. Nature Reviews Molecular Cell Biology. 2008;9:323. https://doi.org/10.1038/nrm2376
  14. Nakagawa S, Maeda S, Tsukihara T. Structural and functional studies of gap junction channels. Curr Opin Struct Biol. 2010;20(4):423-30. https://doi.org/10.1016/j.sbi.2010.05.003
  15. Nikolic N, Gorgens SW, Thoresen GH, et al. Electrical pulse stimulation of cultured skeletal muscle cells as a model for in vitro exercise - possibilities and limitations. Acta Physiol (Oxf). 2017;220(3):310-31. https://doi.org/10.1111/apha.12830
  16. Kawahara Y, Yamaoka K, Iwata M, et al. Novel electrical stimulation sets the cultured myoblast contractile function to 'on'. Pathobiology. 2006;73(6):288-94. https://doi.org/10.1159/000099123
  17. Hashimoto S, Sato F, Uemura R, et al. Effect of Pulsatile Electric Field on Cultured Muscle Cells in Vitro. 2012;10(1):1-6.
  18. Bentzinger CF, Wang YX, Rudnicki MA. Building muscle: molecular regulation of myogenesis. Cold Spring Harb Perspect Biol. 2012;4(2).
  19. Miller JB. Myogenic programs of mouse muscle cell lines: expression of myosin heavy chain isoforms, MyoD1, and myogenin. J Cell Biol. 1990;111(3):1149-59. https://doi.org/10.1083/jcb.111.3.1149
  20. Pereira-Leal JB, Seabra MCJJomb. Evolution of the Rab family of small GTP-binding proteins. 2001;313(4):889-901. https://doi.org/10.1006/jmbi.2001.5072
  21. Takai Y, Sasaki T, Matozaki TJPr. Small GTP-binding proteins. 2001;81(1):153-208. https://doi.org/10.1152/physrev.2001.81.1.153
  22. Colicelli JJSS. Human RAS superfamily proteins and related GTPases. 2004;2004(250):re13-re.
  23. Johnson DS, Chen YHJCoip. Ras family of small GTPases in immunity and inflammation. 2012;12(4):458-63. https://doi.org/10.1016/j.coph.2012.02.003
  24. Krontiris TG, Cooper GMJPotNAoS. Transforming activity of human tumor DNAs. 1981;78(2):1181-4. https://doi.org/10.1073/pnas.78.2.1181
  25. Milburn MV, Tong L, Brunger A, et al. Molecular switch for signal transduction: structural differences between active and inactive forms of protooncogenic ras proteins. 1990;247(4945):939-45. https://doi.org/10.1126/science.2406906
  26. Pylayeva-Gupta Y, Grabocka E, Bar-Sagi DJNRC. RAS oncogenes: weaving a tumorigenic web. 2011;11(11):761. https://doi.org/10.1038/nrc3106
  27. Parri M, Chiarugi PJCC, Signaling. Rac and Rho GTPases in cancer cell motility control. 2010;8(1):23. https://doi.org/10.1186/1478-811X-8-23
  28. Rousseau M, Gaugler M-H, Rodallec A, et al. RhoA GTPase regulates radiation-induced alterations in endothelial cell adhesion and migration. 2011;414(4):750-5. https://doi.org/10.1016/j.bbrc.2011.09.150
  29. Spiering D, Hodgson LJCa, migration. Dynamics of the Rho-family small GTPases in actin regulation and motility. 2011;5(2):170-80. https://doi.org/10.4161/cam.5.2.14403
  30. Wei L, Zhou W, Croissant JD, et al. RhoA signaling via serum response factor plays an obligatory role in myogenic differentiation. 1998;273(46):30287-94. https://doi.org/10.1074/jbc.273.46.30287
  31. Charrasse S, Comunale F, Grumbach Y, et al. RhoA GTPase regulates M-cadherin activity and myoblast fusion. 2006;17(2):749-59. https://doi.org/10.1091/mbc.e05-04-0284
  32. Feng H, Li Y, Yin Y, et al. Protein kinase A-dependent phosphorylation of Dock180 at serine residue 1250 is important for glioma growth and invasion stimulated by platelet derived-growth factor receptor alpha. Neuro Oncol. 2015;17(6):832-42. https://doi.org/10.1093/neuonc/nou323