Abstract

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

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  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).
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    [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]
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    [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]
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    [CrossRef] [PubMed]
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    [CrossRef] [PubMed]
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    [CrossRef] [PubMed]
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    [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]

2013 (1)

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).

2011 (4)

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]

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]

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]

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]

2010 (2)

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]

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]

2009 (3)

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]

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]

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]

2008 (4)

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]

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]

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]

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]

2007 (1)

2006 (1)

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]

2004 (1)

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]

2003 (2)

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]

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]

2001 (1)

J. Mertz and L. Moreaux, “Second-harmonic generation by focused excitation of inhomogeneously distributed scatterers,” Opt. Commun.196(1-6), 325–330 (2001).
[CrossRef]

1997 (1)

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]

1994 (1)

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]

1992 (1)

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]

1986 (1)

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]

1968 (1)

I. Freund, “Nonlinear diffraction,” Phys. Rev. Lett.21(19), 1404–1406 (1968).
[CrossRef]

1963 (1)

P. A. Franken and J. F. Ward, “Optical harmonics and nonlinear phenomena,” Rev. Mod. Phys.35(1), 23–39 (1963).
[CrossRef]

Adams, D. J.

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]

Agbulut, O.

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]

Babinet, C.

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]

Balke, C. W.

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]

Barretto, R. P.

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]

Barzda, V.

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]

Bellanger, J. J.

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).

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]

Bellanger, J.-J.

Bembi, B.

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]

Bloch, R. J.

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]

Both, M.

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]

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]

Butler-Browne, G.

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]

Byer, R. L.

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]

Campagnola, P. J.

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]

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]

Carlsson, L.

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]

Chamberlain, J. S.

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]

Cheng, H.

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]

Chien, Y. H.

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]

Cisek, R.

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]

Czapiga, M.

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]

D’Amico, L. A.

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]

Dauser, D.

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]

Delp, S. L.

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]

Deutsch, M.

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]

Dougherty, R. P.

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]

Du, A. P.

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]

Fejer, M. M.

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]

Fink, R. H. A.

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]

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]

Franken, P. A.

P. A. Franken and J. F. Ward, “Optical harmonics and nonlinear phenomena,” Rev. Mod. Phys.35(1), 23–39 (1963).
[CrossRef]

Freund, I.

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]

I. Freund, “Nonlinear diffraction,” Phys. Rev. Lett.21(19), 1404–1406 (1968).
[CrossRef]

Friedrich, O.

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]

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]

Fusi, L.

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]

Garbe, C.

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]

Garcia, E.

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]

Gorelik, J.

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]

Green, C.

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]

Greenhalgh, C.

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]

Harding, S. E.

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]

Holloway, B.

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]

Hwu, W. L.

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]

Joseph, C.

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]

Jundt, D. H.

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]

Kanda, G. K.

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]

Kenny, A. M.

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]

Korchev, Y. E.

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]

Kuchel, G. A.

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]

Künsting, T.

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]

Lab, M. J.

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]

Lavault, M. T.

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]

Lederer, W. J.

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]

Li, Z.

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]

Linari, M.

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]

Llewellyn, M. E.

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]

Loew, L. M.

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]

Lombardi, V.

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]

Lovering, R. M.

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]

Lyon, A. R.

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]

MacLeod, K. T.

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]

Magel, G. A.

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]

Major, A.

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]

McCulle, S.

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]

Mericskay, M.

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]

Mertz, J.

J. Mertz and L. Moreaux, “Second-harmonic generation by focused excitation of inhomogeneously distributed scatterers,” Opt. Commun.196(1-6), 325–330 (2001).
[CrossRef]

Mohler, W. A.

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]

Moreaux, L.

J. Mertz and L. Moreaux, “Second-harmonic generation by focused excitation of inhomogeneously distributed scatterers,” Opt. Commun.196(1-6), 325–330 (2001).
[CrossRef]

Muriel, J. M.

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]

Nucciotti, V.

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]

O’Neill, A.

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]

Paulin, D.

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]

Pavone, F. S.

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]

Piazzesi, G.

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]

Pilbeam, C. C.

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]

Pittis, M. G.

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]

Plotnikov, S. V.

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]

Plotz, P.

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]

Prent, N.

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]

Prosser, B. L.

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]

Raben, N.

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]

Ralston, E.

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]

Recher, G.

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).

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]

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]

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]

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]

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]

Rhee, D.

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]

Richard, P.

Rouède, D.

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).

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]

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]

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]

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]

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]

Sacconi, L.

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]

Sanger, J. M.

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]

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]

Sanger, J. W.

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]

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]

Schaub, E.

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).

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]

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]

Schnitzer, M. J.

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]

Schürmann, S.

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]

Schwartz, O.

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]

Scranton, V. L.

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]

Simon, A.

Sobie, E. A.

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]

Song, L. S.

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]

Sprecher, A.

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]

Stewart, B.

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]

Stringari, C.

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]

Strong, J.

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]

Swaim, B.

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]

Tascon, C.

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]

Teichmann, M. D. H.

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]

Thornell, L. E.

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]

Tiaho, F.

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).

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]

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]

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]

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]

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]

Uttenweiler, D.

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]

Vanzi, F.

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]

Vogel, M.

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]

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]

von Wegner, F.

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]

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]

Walsh, S. J.

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]

Wang, J. S.

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]

Ward, J. F.

P. A. Franken and J. F. Ward, “Optical harmonics and nonlinear phenomena,” Rev. Mod. Phys.35(1), 23–39 (1963).
[CrossRef]

Webb, W. W.

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]

Weber, C.

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]

Williams, R. M.

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]

Xu, M.

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]

Zhang, Y.

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]

Zipfel, W. R.

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]

Zubrowski, B.

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]

Am. J. Physiol. Cell Physiol. (1)

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]

Biomed. Opt. Express (1)

Biophys. J. (4)

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]

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).

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]

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]

Cell Motil. Cytoskeleton (2)

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]

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]

IEEE J. Quantum Electron. (1)

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]

J. Biomed. Opt. (3)

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]

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]

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]

J. Cell Biol. (1)

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]

J. Microsc. (1)

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]

J. Struct. Biol. (1)

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]

Nat. Biotechnol. (2)

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]

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]

Nature (1)

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]

Opt. Commun. (1)

J. Mertz and L. Moreaux, “Second-harmonic generation by focused excitation of inhomogeneously distributed scatterers,” Opt. Commun.196(1-6), 325–330 (2001).
[CrossRef]

Opt. Express (2)

Phys. Rev. Lett. (1)

I. Freund, “Nonlinear diffraction,” Phys. Rev. Lett.21(19), 1404–1406 (1968).
[CrossRef]

Proc. Natl. Acad. Sci. U.S.A. (3)

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]

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]

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]

Rev. Mod. Phys. (1)

P. A. Franken and J. F. Ward, “Optical harmonics and nonlinear phenomena,” Rev. Mod. Phys.35(1), 23–39 (1963).
[CrossRef]

Other (1)

V. Dubowitz and C. A. Sewry, Muscle Biopsy: A Practical Approach, 3rd Ed. (London, 2007).

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Figures (5)

Fig. 1
Fig. 1

SHG images and experimental SHG-IPs. (a) SHG image at the middle (z = 0μm) of a z-stack of muscle tissue that experienced 30% elongation induced 3 hours mild-proteolysis. Horizontal lines at y = 0 μm, y = 3 μm and y = - 3 μm are ROIs for SHG-IP of (d). (b) Corresponding xz view obtained at y = 0 μm. Note that horizontal full lines localized SHG images of Fig. 2(a). (c) Corresponding yz view obtained at x = 0 μm. As SHG signal originates from the A-band, note the I-band to A-band transition from left to right. (d) SHG-IPs obtained along lines y = 0 μm, y = 3 μm and y = −3 μm of (a). (e) 3-D view of the pitchforlike SHG pattern. Scale bars are 2.5 μm.

Fig. 2
Fig. 2

SHG images and experimental/theoretical SHG-IPs. (a) SHG images are obtained at different z positions of the z-stack of Fig. 1. Note that each SHG image is labeled by its z position in the xz section of Fig. 1(b) and that z = 0 corresponds to the middle of the z-stack. (b) Experimental SHG-IPs are full lines and theoretical ones are dotted lines in white color (m = 150 nm for all myofibrils) and yellow color (m = 320 nm for the two myofibrils bordering the region of myofibrillar displacement in x direction and m = 150 nm for other myofibrils). Note that a diagram representing segments of 8 myofibrils is shown in the xz plane of each panel with a series of 4 sarcomeres consisting of A-bands (red and blue color accounting for polarity inversion) alternating with I-bands (dark color). Thin band with grey color at the center of each A-band corresponds to the M-band region of size m with antiparallel overlapping of myosin thick filaments where no SHG signal is produced (see also the schematic view of a sarcomere in the inset of Fig. 3). Each experimental SHG-IP is obtained along the horizontal line in the corresponding image of (a). Each theoretical SHG-IP is obtained from the corresponding myofibrillar schematic view and for a laser focus position along the horizontal line at the middle of each panel. Sarcomere size is L=2.5μm and it corresponds to the experimental mean value. SHG-IPs are drawn with arbitrary units. Scale bars are 2.5 μm.

Fig. 3
Fig. 3

Theoretical SHG-IPs as a function of sarcomere size L and myofibrillar displacement Δ . Each of the (9 × 6) panels is a schematic diagram of 6 segments of myofibrils that are adjacent and parallel respectively along z and x directions. For each panel, upper half of myofibrils are displaced from the lower half in x direction by Δ . Each myofibril is shown with a series of 4 sarcomeres consisting of A-bands (red and blue color accounting for polarity inversion) alternating with I-bands (dark color). Thin band with grey color at the center of each A-band corresponds to the M-band region of size m = 150 nm with antiparallel overlapping of myosin thick filaments where no SHG signal is produced. A schematic view of the sarcomere is shown in inset (upper left corner). Theoretical SHG-IP, obtained for a laser beam focalized along the horizontal line at the middle of each panel, is plotted (full lines) with arbitrary units. Note also the scale in μm at the bottom of each column.

Fig. 4
Fig. 4

Experimental SHG, TPEF α-actinin images and SHG-IPs from post-mortem proteolysed muscle. (a) SHG. (b) TPEF. (c) Merge of (a) and (b). Note that the images are from 24 hours post-mortem proteolysed and contracted muscle (L = 1.8 μm). Note also that red and green colors in (c) are respectively SHG and TPEF images. (d) SHG-IPs along indicated dotted lines of (a) and (b). (e) SHG image from 30% elongated 3 hours mild proteolysed muscle (L = 3.1 μm). (f) SHG-IP along indicated dotted line of (e). Scale bars are 2 μm.

Fig. 5
Fig. 5

Wave vector diagrams representing well aligned (a) and misaligned (b) sarcomeres. Laser beam is focused (PSF in white color) at the transition between two regions of inverse polarity as shown by the red and blue color transition. (a) Polarity inversion is along x direction. Mean distance between charges of opposite polarity within the PSF is 1 2 ×1.81 w xy . Optical path difference between harmonic waves emitted at θ angle is δ= 1 2 ×1.81 w xy ×sin(θ) . (b) Polarity inversion is along z direction. Mean distance d between charges of opposite polarity within the PSF is d= 1 2 ×1.81 w z .

Equations (4)

Equations on this page are rendered with MathJax. Learn more.

I 2ω  (r)= ω 4 r 2 c 4 χ 15 2 I ω 2 ×( 1 sin 2 θ cos 2 φ )×  | f g f (θ,φ) | 2
g f (θ,φ)= e i ( k x 2ω x+ k y 2ω y+ k z 2ω z ) × M f (x,y,z)× e 2 x 2 + y 2 w xy 2 2 z 2 w z 2 +2iξ k z ω z dxdydz.
g f (θ,φ)=u× n c xn f e 1 8 w xy 2   ( k x 2ω G xn ) 2 × n c yn f e 1 8 w xy 2   ( k y 2ω G yn ) 2 × n c zn f e 1 8 w z 2 ( k z 2ω 2ξ k z ω G zn ) 2
| c f xn    = 2i πn sin( 1 4 G xn (Am) )×sin( 1 4 G xn (A+m) )×exp(i G xn Δ x f ),n,n0 =0,n=0 c f ηn    = 1 πn sin( 1 2 G ηn η )×exp(i G ηn Δ f η ),n,n0,η=y,z = η L η 1 ,n=0,η=y,z .

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