OSA's Digital Library

Optics Express

Optics Express

  • Editor: Andrew M. Weiner
  • Vol. 21, Iss. 9 — May. 6, 2013
  • pp: 11404–11414

Study of the effect of myofibrillar misalignment on the sarcomeric SHG intensity pattern

Denis Rouède, Jean-Jacques Bellanger, Gaëlle Recher, and François Tiaho  »View Author Affiliations

Optics Express, Vol. 21, Issue 9, pp. 11404-11414 (2013)

View Full Text Article

Enhanced HTML    Acrobat PDF (6375 KB)

Browse Journals / Lookup Meetings

Browse by Journal and Year


Lookup Conference Papers

Close Browse Journals / Lookup Meetings

Article Tools



We present a theoretical simulation of the sarcomeric SHG intensity pattern (SHG-IP) that takes into account myofibrillar misalignment that is experimentally observed in SHG images of proteolysed muscles. The model predicts that myofibrillar displacement results in the conversion from one peak (1P) to two peaks (2P) sarcomeric SHG-IP in agreement with experimental results. This study suggests that sarcomeric SHG-IP is a powerful tool for mapping spatial myofibrillar displacement and its related excitation-contraction disruption that could occur during muscle physiological adaptation and disease.

© 2013 OSA

OCIS Codes
(170.3880) Medical optics and biotechnology : Medical and biological imaging
(190.4160) Nonlinear optics : Multiharmonic generation
(180.4315) Microscopy : Nonlinear microscopy

ToC Category:
Medical Optics and Biotechnology

Original Manuscript: March 5, 2013
Revised Manuscript: April 19, 2013
Manuscript Accepted: April 20, 2013
Published: May 2, 2013

Virtual Issues
Vol. 8, Iss. 6 Virtual Journal for Biomedical Optics

Denis Rouède, Jean-Jacques Bellanger, Gaëlle Recher, and François Tiaho, "Study of the effect of myofibrillar misalignment on the sarcomeric SHG intensity pattern," Opt. Express 21, 11404-11414 (2013)

Sort:  Author  |  Year  |  Journal  |  Reset  


  1. P. J. Campagnola and L. M. Loew, “Second-harmonic imaging microscopy for visualizing biomolecular arrays in cells, tissues and organisms,” Nat. Biotechnol.21(11), 1356–1360 (2003). [CrossRef] [PubMed]
  2. W. R. Zipfel, R. M. Williams, and W. W. Webb, “Nonlinear magic: multiphoton microscopy in the biosciences,” Nat. Biotechnol.21(11), 1369–1377 (2003). [CrossRef] [PubMed]
  3. O. Friedrich, M. Both, C. Weber, S. Schürmann, M. D. H. Teichmann, F. von Wegner, R. H. A. Fink, M. Vogel, J. S. Chamberlain, and C. Garbe, “Microarchitecture Is Severely Compromised but Motor Protein Function is Preserved in Dystrophic mdx Skeletal Muscle,” Biophys. J.98(4), 606–616 (2010). [CrossRef] [PubMed]
  4. M. E. Llewellyn, R. P. Barretto, S. L. Delp, and M. J. Schnitzer, “Minimally invasive high-speed imaging of sarcomere contractile dynamics in mice and humans,” Nature454(7205), 784–788 (2008). [PubMed]
  5. V. Nucciotti, C. Stringari, L. Sacconi, F. Vanzi, L. Fusi, M. Linari, G. Piazzesi, V. Lombardi, and F. S. Pavone, “Probing myosin structural conformation in vivo by second-harmonic generation microscopy,” Proc. Natl. Acad. Sci. U.S.A.107(17), 7763–7768 (2010). [CrossRef] [PubMed]
  6. S. V. Plotnikov, A. M. Kenny, S. J. Walsh, B. Zubrowski, C. Joseph, V. L. Scranton, G. A. Kuchel, D. Dauser, M. Xu, C. C. Pilbeam, D. J. Adams, R. P. Dougherty, P. J. Campagnola, and W. A. Mohler, “Measurement of muscle disease by quantitative second-harmonic generation imaging,” J. Biomed. Opt.13(4), 044018 (2008). [CrossRef] [PubMed]
  7. E. Ralston, B. Swaim, M. Czapiga, W. L. Hwu, Y. H. Chien, M. G. Pittis, B. Bembi, O. Schwartz, P. Plotz, and N. Raben, “Detection and imaging of non-contractile inclusions and sarcomeric anomalies in skeletal muscle by second harmonic generation combined with two-photon excited fluorescence,” J. Struct. Biol.162(3), 500–508 (2008). [CrossRef] [PubMed]
  8. F. Tiaho, G. Recher, and D. Rouède, “Estimation of helical angles of myosin and collagen by second harmonic generation imaging microscopy,” Opt. Express15(19), 12286–12295 (2007). [CrossRef] [PubMed]
  9. G. Recher, D. Rouède, P. Richard, A. Simon, J.-J. Bellanger, and F. Tiaho, “Three distinct sarcomeric patterns of skeletal muscle revealed by SHG and TPEF Microscopy,” Opt. Express17(22), 19763–19777 (2009). [CrossRef] [PubMed]
  10. G. Recher, D. Rouède, E. Schaub, and F. Tiaho, “Skeletal muscle sarcomeric SHG patterns photo-conversion by femtosecond infrared laser,” Biomed. Opt. Express2(2), 374–384 (2011). [CrossRef] [PubMed]
  11. G. Recher, D. Rouède, C. Tascon, L. A. D’Amico, and F. Tiaho, “Double-band sarcomeric SHG pattern induced by adult skeletal muscles alteration during myofibrils preparation,” J. Microsc.241(2), 207–211 (2011). [CrossRef] [PubMed]
  12. D. Rouède, G. Recher, J. J. Bellanger, M. T. Lavault, E. Schaub, and F. Tiaho, “Modeling of Supramolecular Centrosymmetry Effect on Sarcomeric SHG Intensity Pattern of Skeletal Muscles,” Biophys. J.101(2), 494–503 (2011). [CrossRef] [PubMed]
  13. D. Rouède, J. J. Bellanger, E. Schaub, G. Recher, and F. Tiaho, “Theoretical and experimental SHG angular intensity patterns from healthy and proteolysed muscles,” Biophys. J.104(9), 1959–1968 (2013).
  14. L. S. Song, E. A. Sobie, S. McCulle, W. J. Lederer, C. W. Balke, and H. Cheng, “Orphaned ryanodine receptors in the failing heart,” Proc. Natl. Acad. Sci. U.S.A.103(11), 4305–4310 (2006). [CrossRef] [PubMed]
  15. A. R. Lyon, K. T. MacLeod, Y. Zhang, E. Garcia, G. K. Kanda, M. J. Lab, Y. E. Korchev, S. E. Harding, and J. Gorelik, “Loss of T-tubules and other changes to surface topography in ventricular myocytes from failing human and rat heart,” Proc. Natl. Acad. Sci. U.S.A.106(16), 6854–6859 (2009). [CrossRef] [PubMed]
  16. V. Dubowitz and C. A. Sewry, Muscle Biopsy: A Practical Approach, 3rd Ed. (London, 2007).
  17. R. M. Lovering, A. O’Neill, J. M. Muriel, B. L. Prosser, J. Strong, and R. J. Bloch, “Physiology, structure, and susceptibility to injury of skeletal muscle in mice lacking keratin 19-based and desmin-based intermediate filaments,” Am. J. Physiol. Cell Physiol.300(4), C803–C813 (2011). [CrossRef] [PubMed]
  18. Z. Li, M. Mericskay, O. Agbulut, G. Butler-Browne, L. Carlsson, L. E. Thornell, C. Babinet, and D. Paulin, “Desmin is essential for the tensile strength and integrity of myofibrils but not for myogenic commitment, differentiation, and fusion of skeletal muscle,” J. Cell Biol.139(1), 129–144 (1997). [CrossRef] [PubMed]
  19. M. Both, M. Vogel, O. Friedrich, F. von Wegner, T. Künsting, R. H. A. Fink, and D. Uttenweiler, “Second harmonic imaging of intrinsic signals in muscle fibers in situ,” J. Biomed. Opt.9(5), 882–892 (2004). [CrossRef] [PubMed]
  20. D. Rhee, J. M. Sanger, and J. W. Sanger, “The premyofibril - evidence for its role in myofibrillogenesis,” Cell Motil. Cytoskeleton28(1), 1–24 (1994). [CrossRef] [PubMed]
  21. J. W. Sanger, J. S. Wang, B. Holloway, A. P. Du, and J. M. Sanger, “Myofibrillogenesis in Skeletal Muscle Cells in Zebrafish,” Cell Motil. Cytoskeleton66(8), 556–566 (2009). [CrossRef] [PubMed]
  22. J. Mertz and L. Moreaux, “Second-harmonic generation by focused excitation of inhomogeneously distributed scatterers,” Opt. Commun.196(1-6), 325–330 (2001). [CrossRef]
  23. N. Prent, C. Green, C. Greenhalgh, R. Cisek, A. Major, B. Stewart, and V. Barzda, “Intermyofilament dynamics of myocytes revealed by second harmonic generation microscopy,” J. Biomed. Opt.13(4), 041318 (2008). [CrossRef] [PubMed]
  24. I. Freund, “Nonlinear diffraction,” Phys. Rev. Lett.21(19), 1404–1406 (1968). [CrossRef]
  25. I. Freund, M. Deutsch, and A. Sprecher, “Connective-tissue polarity - optical second-harmonic microscopy, crossed-beam summation, and small-angle scattering in rat-tail tendon,” Biophys. J.50(4), 693–712 (1986). [CrossRef] [PubMed]
  26. P. A. Franken and J. F. Ward, “Optical harmonics and nonlinear phenomena,” Rev. Mod. Phys.35(1), 23–39 (1963). [CrossRef]
  27. M. M. Fejer, G. A. Magel, D. H. Jundt, and R. L. Byer, “Quasi-phase-matched second harmonic generation: tuning and tolerances,” IEEE J. Quantum Electron.28(11), 2631–2654 (1992). [CrossRef]

Cited By

Alert me when this paper is cited

OSA is able to provide readers links to articles that cite this paper by participating in CrossRef's Cited-By Linking service. CrossRef includes content from more than 3000 publishers and societies. In addition to listing OSA journal articles that cite this paper, citing articles from other participating publishers will also be listed.


Fig. 1 Fig. 2 Fig. 3
Fig. 4 Fig. 5

« Previous Article  |  Next Article »

OSA is a member of CrossRef.

CrossCheck Deposited