Abstract

The far-field optical imaging of mitochondria of live cells without the use of any label is demonstrated. It uses a highly sensitive photothermal method and has a resolution comparable to confocal fluorescence setups. The morphological states of mitochondria were followed under different physiological treatments, and the role of cytochrome c was ruled out as the main origin of the photothermal signals. This label free optical method provides a high contrast imaging of live mitochondria and should find many applications in biosciences.

©2007 Optical Society of America

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  1. D. J. Stephens and V. J. Allan, “Light microscopy techniques for live cell imaging,” Science 300, 82–86 (2003).
    [Crossref] [PubMed]
  2. J. R. Gledhill and J. E. Walker, “Inhibition in F1-ATPase from bovine heart mitochondria,” Biochem. J. 386, 591 (2005).
    [Crossref]
  3. L. Scorrano, V. Petronilli, R. Colonna, F. Di Lisa, and P. Bernardi, “Chloromethyltetramethylrosamine (Mitotracker Orange) induces the mitochondrial permeability transition and inhibits respiratory complex I. Implications for the mechanism of cytochrome c release,” J Biol. Chem 274, 24657–24663 (1999).
    [Crossref] [PubMed]
  4. J. F. Buckman, H. Hernandez, G. J. Kress, T. V. Votyakova, S. Pal, and I. J. Reynolds, “MitoTracker labeling in primary neuronal and astrocytic cultures: influence of mitochondrial membrane potential and oxidants,” J. Neurosci. Method. 104, 165 (2001).
    [Crossref]
  5. S. DiMauro, “Mitochondrial myopathies,” Curr Opin Rheumatol 18, 636–641 (2006).
    [Crossref] [PubMed]
  6. P. L. Gourley, J. K. Hendricks, A. E. McDonald, R. G. Copeland, K. E. Barrett, C. R. Gourley, K. K. Singh, and R. K. Naviaux, “Mitochondrial correlation microscopy and nanolaser spectroscopy - new tools for biophotonic detection of cancer in single cells,” Technol. Cancer Res Treat 4, 585–592 (2005).
    [PubMed]
  7. S. Berciaud, L. Cognet, G. A. Blab, and B. Lounis, “Photothermal Heterodyne Imaging of Individual Nonfluorescent Nanoclusters and Nanocrystals,” Phys Rev Lett 93, 257402 (2004).
    [Crossref]
  8. M. A. Van Dijk, A. L. Tchebotareva, M. Orrit, M. Lippitz, S. Berciaud, D. Lasne, L. Cognet, and B. Lounis, “Absorption and scattering microscopy of single metal nanoparticles,” Phys. Chem. Chem. Phys. 8, 3486 (2006).
    [Crossref] [PubMed]
  9. S. Berciaud, D. Lasne, G. A. Blab, L. Cognet, and B. Lounis, “Photothermal Heterodyne Imaging of Individual Metallic Nanoparticles: Theory versus Experiments,” Phys. Rev. B 73, 045424 (2006).
    [Crossref]
  10. G. A. Blab, L. Cognet, S. Berciaud, I. Alexandre, D. Husar, J. Remacle, and B. Lounis, “Optical readout of gold nanoparticle-based DNA microarrays without silver enhancement,” Biophys. J. 90 (2006).
    [Crossref]
  11. E. Tamaki, K. Sato, M. Tokeshi, K. Sato, M. Aihara, and T. Kitamori, “Single-cell analysis by a scanning thermal lens microscope with a microchip: direct monitoring of cytochrome c distribution during apoptosis process,” Anal Chem 74, 1560–1564 (2002).
    [Crossref] [PubMed]
  12. V. P. Zharov, V. Galitovskiy, C. S. Lyle, and T. C. Chambers, “Superhigh-sensitivity photothermal monitoring of individual cell response to antitumor drug,” J Biomed Opt 11, 064034 (2006).
    [Crossref]
  13. L. A. Ligon and O. Steward, “Movement of mitochondria in the axons and dendrites of cultured hippocampal neurons,” J. Comp. Neurol. 427, 340–350 (2000).
    [Crossref] [PubMed]
  14. C. Hoppel and C. Cooper, “The action of digitonin on rat liver mitochondria. The effects on enzyme content,” Biochem. J. 107, 367–375 (1968).
    [PubMed]
  15. A. E. Vercesi, C. F. Bernardes, M. E. Hoffmann, F. R. Gadelha, and R. Docampo, “Digitonin permeabilization does not affect mitochondrial function and allows the determination of the mitochondrial membrane potential of Trypanosoma cruzi in situ,” J Biol Chem 266, 14431–14434 (1991).
    [PubMed]
  16. R. Rizzuto, M. Brini, P. Pizzo, M. Murgia, and T. Pozzan, “Chimeric green fluorescent protein as a tool for visualizing subcellular organelles in living cells,” Curr. Biol. 5, 635 (1995).
    [Crossref] [PubMed]
  17. R. M. Kluck, E. Bossy-Wetzel, D. R. Green, and D. D. Newmeyer, “The release of cytochrome c from mitochondria: a primary site for Bcl-2 regulation of apoptosis,” Science 275, 1132–1136 (1997).
    [Crossref] [PubMed]
  18. J. Yang, X. Liu, K. Bhalla, C. N. Kim, A. M. Ibrado, J. Cai, T. I. Peng, D. P. Jones, and X. Wang, “Prevention of apoptosis by Bcl-2: release of cytochrome c from mitochondria blocked,” Science 275, 1129–1132 (1997).
    [Crossref] [PubMed]
  19. J. C. Goldstein, N. J. Waterhouse, P. Juin, G. I. Evan, and D. R. Green, “The coordinate release of cytochrome c during apoptosis is rapid, complete and kinetically invariant,” Nat Cell Biol 2, 156–162 (2000).
    [Crossref] [PubMed]
  20. D. DiDonato and D. L. Brasaemle, “Fixation Methods for the Study of Lipid Droplets by Immunofluorescence Microscopy,” J. Histochem. Cytochem. 51, 773–780 (2003).
    [Crossref] [PubMed]
  21. P. G. Heytler, “Uncoupling of Oxidative Phosphorylation by Carbonyl Cyanide Phenylhydrazones. I. Some Characteristics of m-CI-CCP Action on Mitochondria and Chloroplasts,” Biochemistry 2, 357–361 (1963).
    [Crossref] [PubMed]
  22. R. A. Goldsby and P. G. Heytler, “Uncoupling Of Oxidative Phosphorylation By Carbonyl Cyanide Phenylhydrazones. Ii. Effects Of Carbonyl Cyanide M-Chlorophenylhydrazone On Mitochondrial Respiration,” Biochemistry 2, 1142–1147 (1963).
    [Crossref] [PubMed]
  23. B. Z. Cavari and Y. Avi-Dor, “Effect of carbonyl cyanide m-chlorophenylhydrazone on respiration and respiration-dependent phosphorylation in Escherichia coli,” Biochem. J. 103, 601–608 (1967).
    [PubMed]
  24. W. Gao, Y. Pu, K. Q. Luo, and D. C. Chang, “Temporal relationship between cytochrome c release and mitochondrial swelling during UV-induced apoptosis in living HeLa cells,” J. Cell Sci. 114, 2855–2862 (2001).
    [PubMed]
  25. I. Agalidis, S. Othman, A. Boussac, F. Reiss-Husson, and A. Desbois, “Purification, redox and spectroscopic properties of the tetraheme cytochrome c isolated from Rubrivivax gelatinosus,” Eur. J. Biochem. 261, 325 (1999).
    [Crossref] [PubMed]
  26. T. J. Sick and M. A. Perez-Pinzon, “Optical methods for probing mitochondrial function in brain slices,” Methods 18, 104–108 (1999).
    [Crossref] [PubMed]
  27. A. J. Borgdorff and D. Choquet, “Regulation of AMPA receptor lateral movements,” Nature 417, 649–653. (2002).
    [Crossref] [PubMed]
  28. R. Bertrand, E. Solary, P. O’Connor, K. W. Kohn, and Y. Pommier, “Induction of a common pathway of apoptosis by staurosporine,” Exp. Cell Res. 211, 314–321 (1994).
    [Crossref] [PubMed]

2006 (5)

M. A. Van Dijk, A. L. Tchebotareva, M. Orrit, M. Lippitz, S. Berciaud, D. Lasne, L. Cognet, and B. Lounis, “Absorption and scattering microscopy of single metal nanoparticles,” Phys. Chem. Chem. Phys. 8, 3486 (2006).
[Crossref] [PubMed]

S. Berciaud, D. Lasne, G. A. Blab, L. Cognet, and B. Lounis, “Photothermal Heterodyne Imaging of Individual Metallic Nanoparticles: Theory versus Experiments,” Phys. Rev. B 73, 045424 (2006).
[Crossref]

G. A. Blab, L. Cognet, S. Berciaud, I. Alexandre, D. Husar, J. Remacle, and B. Lounis, “Optical readout of gold nanoparticle-based DNA microarrays without silver enhancement,” Biophys. J. 90 (2006).
[Crossref]

S. DiMauro, “Mitochondrial myopathies,” Curr Opin Rheumatol 18, 636–641 (2006).
[Crossref] [PubMed]

V. P. Zharov, V. Galitovskiy, C. S. Lyle, and T. C. Chambers, “Superhigh-sensitivity photothermal monitoring of individual cell response to antitumor drug,” J Biomed Opt 11, 064034 (2006).
[Crossref]

2005 (2)

P. L. Gourley, J. K. Hendricks, A. E. McDonald, R. G. Copeland, K. E. Barrett, C. R. Gourley, K. K. Singh, and R. K. Naviaux, “Mitochondrial correlation microscopy and nanolaser spectroscopy - new tools for biophotonic detection of cancer in single cells,” Technol. Cancer Res Treat 4, 585–592 (2005).
[PubMed]

J. R. Gledhill and J. E. Walker, “Inhibition in F1-ATPase from bovine heart mitochondria,” Biochem. J. 386, 591 (2005).
[Crossref]

2004 (1)

S. Berciaud, L. Cognet, G. A. Blab, and B. Lounis, “Photothermal Heterodyne Imaging of Individual Nonfluorescent Nanoclusters and Nanocrystals,” Phys Rev Lett 93, 257402 (2004).
[Crossref]

2003 (2)

D. J. Stephens and V. J. Allan, “Light microscopy techniques for live cell imaging,” Science 300, 82–86 (2003).
[Crossref] [PubMed]

D. DiDonato and D. L. Brasaemle, “Fixation Methods for the Study of Lipid Droplets by Immunofluorescence Microscopy,” J. Histochem. Cytochem. 51, 773–780 (2003).
[Crossref] [PubMed]

2002 (2)

A. J. Borgdorff and D. Choquet, “Regulation of AMPA receptor lateral movements,” Nature 417, 649–653. (2002).
[Crossref] [PubMed]

E. Tamaki, K. Sato, M. Tokeshi, K. Sato, M. Aihara, and T. Kitamori, “Single-cell analysis by a scanning thermal lens microscope with a microchip: direct monitoring of cytochrome c distribution during apoptosis process,” Anal Chem 74, 1560–1564 (2002).
[Crossref] [PubMed]

2001 (2)

J. F. Buckman, H. Hernandez, G. J. Kress, T. V. Votyakova, S. Pal, and I. J. Reynolds, “MitoTracker labeling in primary neuronal and astrocytic cultures: influence of mitochondrial membrane potential and oxidants,” J. Neurosci. Method. 104, 165 (2001).
[Crossref]

W. Gao, Y. Pu, K. Q. Luo, and D. C. Chang, “Temporal relationship between cytochrome c release and mitochondrial swelling during UV-induced apoptosis in living HeLa cells,” J. Cell Sci. 114, 2855–2862 (2001).
[PubMed]

2000 (2)

J. C. Goldstein, N. J. Waterhouse, P. Juin, G. I. Evan, and D. R. Green, “The coordinate release of cytochrome c during apoptosis is rapid, complete and kinetically invariant,” Nat Cell Biol 2, 156–162 (2000).
[Crossref] [PubMed]

L. A. Ligon and O. Steward, “Movement of mitochondria in the axons and dendrites of cultured hippocampal neurons,” J. Comp. Neurol. 427, 340–350 (2000).
[Crossref] [PubMed]

1999 (3)

L. Scorrano, V. Petronilli, R. Colonna, F. Di Lisa, and P. Bernardi, “Chloromethyltetramethylrosamine (Mitotracker Orange) induces the mitochondrial permeability transition and inhibits respiratory complex I. Implications for the mechanism of cytochrome c release,” J Biol. Chem 274, 24657–24663 (1999).
[Crossref] [PubMed]

I. Agalidis, S. Othman, A. Boussac, F. Reiss-Husson, and A. Desbois, “Purification, redox and spectroscopic properties of the tetraheme cytochrome c isolated from Rubrivivax gelatinosus,” Eur. J. Biochem. 261, 325 (1999).
[Crossref] [PubMed]

T. J. Sick and M. A. Perez-Pinzon, “Optical methods for probing mitochondrial function in brain slices,” Methods 18, 104–108 (1999).
[Crossref] [PubMed]

1997 (2)

R. M. Kluck, E. Bossy-Wetzel, D. R. Green, and D. D. Newmeyer, “The release of cytochrome c from mitochondria: a primary site for Bcl-2 regulation of apoptosis,” Science 275, 1132–1136 (1997).
[Crossref] [PubMed]

J. Yang, X. Liu, K. Bhalla, C. N. Kim, A. M. Ibrado, J. Cai, T. I. Peng, D. P. Jones, and X. Wang, “Prevention of apoptosis by Bcl-2: release of cytochrome c from mitochondria blocked,” Science 275, 1129–1132 (1997).
[Crossref] [PubMed]

1995 (1)

R. Rizzuto, M. Brini, P. Pizzo, M. Murgia, and T. Pozzan, “Chimeric green fluorescent protein as a tool for visualizing subcellular organelles in living cells,” Curr. Biol. 5, 635 (1995).
[Crossref] [PubMed]

1994 (1)

R. Bertrand, E. Solary, P. O’Connor, K. W. Kohn, and Y. Pommier, “Induction of a common pathway of apoptosis by staurosporine,” Exp. Cell Res. 211, 314–321 (1994).
[Crossref] [PubMed]

1991 (1)

A. E. Vercesi, C. F. Bernardes, M. E. Hoffmann, F. R. Gadelha, and R. Docampo, “Digitonin permeabilization does not affect mitochondrial function and allows the determination of the mitochondrial membrane potential of Trypanosoma cruzi in situ,” J Biol Chem 266, 14431–14434 (1991).
[PubMed]

1968 (1)

C. Hoppel and C. Cooper, “The action of digitonin on rat liver mitochondria. The effects on enzyme content,” Biochem. J. 107, 367–375 (1968).
[PubMed]

1967 (1)

B. Z. Cavari and Y. Avi-Dor, “Effect of carbonyl cyanide m-chlorophenylhydrazone on respiration and respiration-dependent phosphorylation in Escherichia coli,” Biochem. J. 103, 601–608 (1967).
[PubMed]

1963 (2)

P. G. Heytler, “Uncoupling of Oxidative Phosphorylation by Carbonyl Cyanide Phenylhydrazones. I. Some Characteristics of m-CI-CCP Action on Mitochondria and Chloroplasts,” Biochemistry 2, 357–361 (1963).
[Crossref] [PubMed]

R. A. Goldsby and P. G. Heytler, “Uncoupling Of Oxidative Phosphorylation By Carbonyl Cyanide Phenylhydrazones. Ii. Effects Of Carbonyl Cyanide M-Chlorophenylhydrazone On Mitochondrial Respiration,” Biochemistry 2, 1142–1147 (1963).
[Crossref] [PubMed]

Agalidis, I.

I. Agalidis, S. Othman, A. Boussac, F. Reiss-Husson, and A. Desbois, “Purification, redox and spectroscopic properties of the tetraheme cytochrome c isolated from Rubrivivax gelatinosus,” Eur. J. Biochem. 261, 325 (1999).
[Crossref] [PubMed]

Aihara, M.

E. Tamaki, K. Sato, M. Tokeshi, K. Sato, M. Aihara, and T. Kitamori, “Single-cell analysis by a scanning thermal lens microscope with a microchip: direct monitoring of cytochrome c distribution during apoptosis process,” Anal Chem 74, 1560–1564 (2002).
[Crossref] [PubMed]

Alexandre, I.

G. A. Blab, L. Cognet, S. Berciaud, I. Alexandre, D. Husar, J. Remacle, and B. Lounis, “Optical readout of gold nanoparticle-based DNA microarrays without silver enhancement,” Biophys. J. 90 (2006).
[Crossref]

Allan, V. J.

D. J. Stephens and V. J. Allan, “Light microscopy techniques for live cell imaging,” Science 300, 82–86 (2003).
[Crossref] [PubMed]

Avi-Dor, Y.

B. Z. Cavari and Y. Avi-Dor, “Effect of carbonyl cyanide m-chlorophenylhydrazone on respiration and respiration-dependent phosphorylation in Escherichia coli,” Biochem. J. 103, 601–608 (1967).
[PubMed]

Barrett, K. E.

P. L. Gourley, J. K. Hendricks, A. E. McDonald, R. G. Copeland, K. E. Barrett, C. R. Gourley, K. K. Singh, and R. K. Naviaux, “Mitochondrial correlation microscopy and nanolaser spectroscopy - new tools for biophotonic detection of cancer in single cells,” Technol. Cancer Res Treat 4, 585–592 (2005).
[PubMed]

Berciaud, S.

M. A. Van Dijk, A. L. Tchebotareva, M. Orrit, M. Lippitz, S. Berciaud, D. Lasne, L. Cognet, and B. Lounis, “Absorption and scattering microscopy of single metal nanoparticles,” Phys. Chem. Chem. Phys. 8, 3486 (2006).
[Crossref] [PubMed]

S. Berciaud, D. Lasne, G. A. Blab, L. Cognet, and B. Lounis, “Photothermal Heterodyne Imaging of Individual Metallic Nanoparticles: Theory versus Experiments,” Phys. Rev. B 73, 045424 (2006).
[Crossref]

G. A. Blab, L. Cognet, S. Berciaud, I. Alexandre, D. Husar, J. Remacle, and B. Lounis, “Optical readout of gold nanoparticle-based DNA microarrays without silver enhancement,” Biophys. J. 90 (2006).
[Crossref]

S. Berciaud, L. Cognet, G. A. Blab, and B. Lounis, “Photothermal Heterodyne Imaging of Individual Nonfluorescent Nanoclusters and Nanocrystals,” Phys Rev Lett 93, 257402 (2004).
[Crossref]

Bernardes, C. F.

A. E. Vercesi, C. F. Bernardes, M. E. Hoffmann, F. R. Gadelha, and R. Docampo, “Digitonin permeabilization does not affect mitochondrial function and allows the determination of the mitochondrial membrane potential of Trypanosoma cruzi in situ,” J Biol Chem 266, 14431–14434 (1991).
[PubMed]

Bernardi, P.

L. Scorrano, V. Petronilli, R. Colonna, F. Di Lisa, and P. Bernardi, “Chloromethyltetramethylrosamine (Mitotracker Orange) induces the mitochondrial permeability transition and inhibits respiratory complex I. Implications for the mechanism of cytochrome c release,” J Biol. Chem 274, 24657–24663 (1999).
[Crossref] [PubMed]

Bertrand, R.

R. Bertrand, E. Solary, P. O’Connor, K. W. Kohn, and Y. Pommier, “Induction of a common pathway of apoptosis by staurosporine,” Exp. Cell Res. 211, 314–321 (1994).
[Crossref] [PubMed]

Bhalla, K.

J. Yang, X. Liu, K. Bhalla, C. N. Kim, A. M. Ibrado, J. Cai, T. I. Peng, D. P. Jones, and X. Wang, “Prevention of apoptosis by Bcl-2: release of cytochrome c from mitochondria blocked,” Science 275, 1129–1132 (1997).
[Crossref] [PubMed]

Blab, G. A.

G. A. Blab, L. Cognet, S. Berciaud, I. Alexandre, D. Husar, J. Remacle, and B. Lounis, “Optical readout of gold nanoparticle-based DNA microarrays without silver enhancement,” Biophys. J. 90 (2006).
[Crossref]

S. Berciaud, D. Lasne, G. A. Blab, L. Cognet, and B. Lounis, “Photothermal Heterodyne Imaging of Individual Metallic Nanoparticles: Theory versus Experiments,” Phys. Rev. B 73, 045424 (2006).
[Crossref]

S. Berciaud, L. Cognet, G. A. Blab, and B. Lounis, “Photothermal Heterodyne Imaging of Individual Nonfluorescent Nanoclusters and Nanocrystals,” Phys Rev Lett 93, 257402 (2004).
[Crossref]

Borgdorff, A. J.

A. J. Borgdorff and D. Choquet, “Regulation of AMPA receptor lateral movements,” Nature 417, 649–653. (2002).
[Crossref] [PubMed]

Bossy-Wetzel, E.

R. M. Kluck, E. Bossy-Wetzel, D. R. Green, and D. D. Newmeyer, “The release of cytochrome c from mitochondria: a primary site for Bcl-2 regulation of apoptosis,” Science 275, 1132–1136 (1997).
[Crossref] [PubMed]

Boussac, A.

I. Agalidis, S. Othman, A. Boussac, F. Reiss-Husson, and A. Desbois, “Purification, redox and spectroscopic properties of the tetraheme cytochrome c isolated from Rubrivivax gelatinosus,” Eur. J. Biochem. 261, 325 (1999).
[Crossref] [PubMed]

Brasaemle, D. L.

D. DiDonato and D. L. Brasaemle, “Fixation Methods for the Study of Lipid Droplets by Immunofluorescence Microscopy,” J. Histochem. Cytochem. 51, 773–780 (2003).
[Crossref] [PubMed]

Brini, M.

R. Rizzuto, M. Brini, P. Pizzo, M. Murgia, and T. Pozzan, “Chimeric green fluorescent protein as a tool for visualizing subcellular organelles in living cells,” Curr. Biol. 5, 635 (1995).
[Crossref] [PubMed]

Buckman, J. F.

J. F. Buckman, H. Hernandez, G. J. Kress, T. V. Votyakova, S. Pal, and I. J. Reynolds, “MitoTracker labeling in primary neuronal and astrocytic cultures: influence of mitochondrial membrane potential and oxidants,” J. Neurosci. Method. 104, 165 (2001).
[Crossref]

Cai, J.

J. Yang, X. Liu, K. Bhalla, C. N. Kim, A. M. Ibrado, J. Cai, T. I. Peng, D. P. Jones, and X. Wang, “Prevention of apoptosis by Bcl-2: release of cytochrome c from mitochondria blocked,” Science 275, 1129–1132 (1997).
[Crossref] [PubMed]

Cavari, B. Z.

B. Z. Cavari and Y. Avi-Dor, “Effect of carbonyl cyanide m-chlorophenylhydrazone on respiration and respiration-dependent phosphorylation in Escherichia coli,” Biochem. J. 103, 601–608 (1967).
[PubMed]

Chambers, T. C.

V. P. Zharov, V. Galitovskiy, C. S. Lyle, and T. C. Chambers, “Superhigh-sensitivity photothermal monitoring of individual cell response to antitumor drug,” J Biomed Opt 11, 064034 (2006).
[Crossref]

Chang, D. C.

W. Gao, Y. Pu, K. Q. Luo, and D. C. Chang, “Temporal relationship between cytochrome c release and mitochondrial swelling during UV-induced apoptosis in living HeLa cells,” J. Cell Sci. 114, 2855–2862 (2001).
[PubMed]

Choquet, D.

A. J. Borgdorff and D. Choquet, “Regulation of AMPA receptor lateral movements,” Nature 417, 649–653. (2002).
[Crossref] [PubMed]

Cognet, L.

S. Berciaud, D. Lasne, G. A. Blab, L. Cognet, and B. Lounis, “Photothermal Heterodyne Imaging of Individual Metallic Nanoparticles: Theory versus Experiments,” Phys. Rev. B 73, 045424 (2006).
[Crossref]

G. A. Blab, L. Cognet, S. Berciaud, I. Alexandre, D. Husar, J. Remacle, and B. Lounis, “Optical readout of gold nanoparticle-based DNA microarrays without silver enhancement,” Biophys. J. 90 (2006).
[Crossref]

M. A. Van Dijk, A. L. Tchebotareva, M. Orrit, M. Lippitz, S. Berciaud, D. Lasne, L. Cognet, and B. Lounis, “Absorption and scattering microscopy of single metal nanoparticles,” Phys. Chem. Chem. Phys. 8, 3486 (2006).
[Crossref] [PubMed]

S. Berciaud, L. Cognet, G. A. Blab, and B. Lounis, “Photothermal Heterodyne Imaging of Individual Nonfluorescent Nanoclusters and Nanocrystals,” Phys Rev Lett 93, 257402 (2004).
[Crossref]

Colonna, R.

L. Scorrano, V. Petronilli, R. Colonna, F. Di Lisa, and P. Bernardi, “Chloromethyltetramethylrosamine (Mitotracker Orange) induces the mitochondrial permeability transition and inhibits respiratory complex I. Implications for the mechanism of cytochrome c release,” J Biol. Chem 274, 24657–24663 (1999).
[Crossref] [PubMed]

Cooper, C.

C. Hoppel and C. Cooper, “The action of digitonin on rat liver mitochondria. The effects on enzyme content,” Biochem. J. 107, 367–375 (1968).
[PubMed]

Copeland, R. G.

P. L. Gourley, J. K. Hendricks, A. E. McDonald, R. G. Copeland, K. E. Barrett, C. R. Gourley, K. K. Singh, and R. K. Naviaux, “Mitochondrial correlation microscopy and nanolaser spectroscopy - new tools for biophotonic detection of cancer in single cells,” Technol. Cancer Res Treat 4, 585–592 (2005).
[PubMed]

Desbois, A.

I. Agalidis, S. Othman, A. Boussac, F. Reiss-Husson, and A. Desbois, “Purification, redox and spectroscopic properties of the tetraheme cytochrome c isolated from Rubrivivax gelatinosus,” Eur. J. Biochem. 261, 325 (1999).
[Crossref] [PubMed]

DiDonato, D.

D. DiDonato and D. L. Brasaemle, “Fixation Methods for the Study of Lipid Droplets by Immunofluorescence Microscopy,” J. Histochem. Cytochem. 51, 773–780 (2003).
[Crossref] [PubMed]

Dijk, M. A. Van

M. A. Van Dijk, A. L. Tchebotareva, M. Orrit, M. Lippitz, S. Berciaud, D. Lasne, L. Cognet, and B. Lounis, “Absorption and scattering microscopy of single metal nanoparticles,” Phys. Chem. Chem. Phys. 8, 3486 (2006).
[Crossref] [PubMed]

DiMauro, S.

S. DiMauro, “Mitochondrial myopathies,” Curr Opin Rheumatol 18, 636–641 (2006).
[Crossref] [PubMed]

Docampo, R.

A. E. Vercesi, C. F. Bernardes, M. E. Hoffmann, F. R. Gadelha, and R. Docampo, “Digitonin permeabilization does not affect mitochondrial function and allows the determination of the mitochondrial membrane potential of Trypanosoma cruzi in situ,” J Biol Chem 266, 14431–14434 (1991).
[PubMed]

Evan, G. I.

J. C. Goldstein, N. J. Waterhouse, P. Juin, G. I. Evan, and D. R. Green, “The coordinate release of cytochrome c during apoptosis is rapid, complete and kinetically invariant,” Nat Cell Biol 2, 156–162 (2000).
[Crossref] [PubMed]

Gadelha, F. R.

A. E. Vercesi, C. F. Bernardes, M. E. Hoffmann, F. R. Gadelha, and R. Docampo, “Digitonin permeabilization does not affect mitochondrial function and allows the determination of the mitochondrial membrane potential of Trypanosoma cruzi in situ,” J Biol Chem 266, 14431–14434 (1991).
[PubMed]

Galitovskiy, V.

V. P. Zharov, V. Galitovskiy, C. S. Lyle, and T. C. Chambers, “Superhigh-sensitivity photothermal monitoring of individual cell response to antitumor drug,” J Biomed Opt 11, 064034 (2006).
[Crossref]

Gao, W.

W. Gao, Y. Pu, K. Q. Luo, and D. C. Chang, “Temporal relationship between cytochrome c release and mitochondrial swelling during UV-induced apoptosis in living HeLa cells,” J. Cell Sci. 114, 2855–2862 (2001).
[PubMed]

Gledhill, J. R.

J. R. Gledhill and J. E. Walker, “Inhibition in F1-ATPase from bovine heart mitochondria,” Biochem. J. 386, 591 (2005).
[Crossref]

Goldsby, R. A.

R. A. Goldsby and P. G. Heytler, “Uncoupling Of Oxidative Phosphorylation By Carbonyl Cyanide Phenylhydrazones. Ii. Effects Of Carbonyl Cyanide M-Chlorophenylhydrazone On Mitochondrial Respiration,” Biochemistry 2, 1142–1147 (1963).
[Crossref] [PubMed]

Goldstein, J. C.

J. C. Goldstein, N. J. Waterhouse, P. Juin, G. I. Evan, and D. R. Green, “The coordinate release of cytochrome c during apoptosis is rapid, complete and kinetically invariant,” Nat Cell Biol 2, 156–162 (2000).
[Crossref] [PubMed]

Gourley, C. R.

P. L. Gourley, J. K. Hendricks, A. E. McDonald, R. G. Copeland, K. E. Barrett, C. R. Gourley, K. K. Singh, and R. K. Naviaux, “Mitochondrial correlation microscopy and nanolaser spectroscopy - new tools for biophotonic detection of cancer in single cells,” Technol. Cancer Res Treat 4, 585–592 (2005).
[PubMed]

Gourley, P. L.

P. L. Gourley, J. K. Hendricks, A. E. McDonald, R. G. Copeland, K. E. Barrett, C. R. Gourley, K. K. Singh, and R. K. Naviaux, “Mitochondrial correlation microscopy and nanolaser spectroscopy - new tools for biophotonic detection of cancer in single cells,” Technol. Cancer Res Treat 4, 585–592 (2005).
[PubMed]

Green, D. R.

J. C. Goldstein, N. J. Waterhouse, P. Juin, G. I. Evan, and D. R. Green, “The coordinate release of cytochrome c during apoptosis is rapid, complete and kinetically invariant,” Nat Cell Biol 2, 156–162 (2000).
[Crossref] [PubMed]

R. M. Kluck, E. Bossy-Wetzel, D. R. Green, and D. D. Newmeyer, “The release of cytochrome c from mitochondria: a primary site for Bcl-2 regulation of apoptosis,” Science 275, 1132–1136 (1997).
[Crossref] [PubMed]

Hendricks, J. K.

P. L. Gourley, J. K. Hendricks, A. E. McDonald, R. G. Copeland, K. E. Barrett, C. R. Gourley, K. K. Singh, and R. K. Naviaux, “Mitochondrial correlation microscopy and nanolaser spectroscopy - new tools for biophotonic detection of cancer in single cells,” Technol. Cancer Res Treat 4, 585–592 (2005).
[PubMed]

Hernandez, H.

J. F. Buckman, H. Hernandez, G. J. Kress, T. V. Votyakova, S. Pal, and I. J. Reynolds, “MitoTracker labeling in primary neuronal and astrocytic cultures: influence of mitochondrial membrane potential and oxidants,” J. Neurosci. Method. 104, 165 (2001).
[Crossref]

Heytler, P. G.

R. A. Goldsby and P. G. Heytler, “Uncoupling Of Oxidative Phosphorylation By Carbonyl Cyanide Phenylhydrazones. Ii. Effects Of Carbonyl Cyanide M-Chlorophenylhydrazone On Mitochondrial Respiration,” Biochemistry 2, 1142–1147 (1963).
[Crossref] [PubMed]

P. G. Heytler, “Uncoupling of Oxidative Phosphorylation by Carbonyl Cyanide Phenylhydrazones. I. Some Characteristics of m-CI-CCP Action on Mitochondria and Chloroplasts,” Biochemistry 2, 357–361 (1963).
[Crossref] [PubMed]

Hoffmann, M. E.

A. E. Vercesi, C. F. Bernardes, M. E. Hoffmann, F. R. Gadelha, and R. Docampo, “Digitonin permeabilization does not affect mitochondrial function and allows the determination of the mitochondrial membrane potential of Trypanosoma cruzi in situ,” J Biol Chem 266, 14431–14434 (1991).
[PubMed]

Hoppel, C.

C. Hoppel and C. Cooper, “The action of digitonin on rat liver mitochondria. The effects on enzyme content,” Biochem. J. 107, 367–375 (1968).
[PubMed]

Husar, D.

G. A. Blab, L. Cognet, S. Berciaud, I. Alexandre, D. Husar, J. Remacle, and B. Lounis, “Optical readout of gold nanoparticle-based DNA microarrays without silver enhancement,” Biophys. J. 90 (2006).
[Crossref]

Ibrado, A. M.

J. Yang, X. Liu, K. Bhalla, C. N. Kim, A. M. Ibrado, J. Cai, T. I. Peng, D. P. Jones, and X. Wang, “Prevention of apoptosis by Bcl-2: release of cytochrome c from mitochondria blocked,” Science 275, 1129–1132 (1997).
[Crossref] [PubMed]

Jones, D. P.

J. Yang, X. Liu, K. Bhalla, C. N. Kim, A. M. Ibrado, J. Cai, T. I. Peng, D. P. Jones, and X. Wang, “Prevention of apoptosis by Bcl-2: release of cytochrome c from mitochondria blocked,” Science 275, 1129–1132 (1997).
[Crossref] [PubMed]

Juin, P.

J. C. Goldstein, N. J. Waterhouse, P. Juin, G. I. Evan, and D. R. Green, “The coordinate release of cytochrome c during apoptosis is rapid, complete and kinetically invariant,” Nat Cell Biol 2, 156–162 (2000).
[Crossref] [PubMed]

Kim, C. N.

J. Yang, X. Liu, K. Bhalla, C. N. Kim, A. M. Ibrado, J. Cai, T. I. Peng, D. P. Jones, and X. Wang, “Prevention of apoptosis by Bcl-2: release of cytochrome c from mitochondria blocked,” Science 275, 1129–1132 (1997).
[Crossref] [PubMed]

Kitamori, T.

E. Tamaki, K. Sato, M. Tokeshi, K. Sato, M. Aihara, and T. Kitamori, “Single-cell analysis by a scanning thermal lens microscope with a microchip: direct monitoring of cytochrome c distribution during apoptosis process,” Anal Chem 74, 1560–1564 (2002).
[Crossref] [PubMed]

Kluck, R. M.

R. M. Kluck, E. Bossy-Wetzel, D. R. Green, and D. D. Newmeyer, “The release of cytochrome c from mitochondria: a primary site for Bcl-2 regulation of apoptosis,” Science 275, 1132–1136 (1997).
[Crossref] [PubMed]

Kohn, K. W.

R. Bertrand, E. Solary, P. O’Connor, K. W. Kohn, and Y. Pommier, “Induction of a common pathway of apoptosis by staurosporine,” Exp. Cell Res. 211, 314–321 (1994).
[Crossref] [PubMed]

Kress, G. J.

J. F. Buckman, H. Hernandez, G. J. Kress, T. V. Votyakova, S. Pal, and I. J. Reynolds, “MitoTracker labeling in primary neuronal and astrocytic cultures: influence of mitochondrial membrane potential and oxidants,” J. Neurosci. Method. 104, 165 (2001).
[Crossref]

Lasne, D.

M. A. Van Dijk, A. L. Tchebotareva, M. Orrit, M. Lippitz, S. Berciaud, D. Lasne, L. Cognet, and B. Lounis, “Absorption and scattering microscopy of single metal nanoparticles,” Phys. Chem. Chem. Phys. 8, 3486 (2006).
[Crossref] [PubMed]

S. Berciaud, D. Lasne, G. A. Blab, L. Cognet, and B. Lounis, “Photothermal Heterodyne Imaging of Individual Metallic Nanoparticles: Theory versus Experiments,” Phys. Rev. B 73, 045424 (2006).
[Crossref]

Ligon, L. A.

L. A. Ligon and O. Steward, “Movement of mitochondria in the axons and dendrites of cultured hippocampal neurons,” J. Comp. Neurol. 427, 340–350 (2000).
[Crossref] [PubMed]

Lippitz, M.

M. A. Van Dijk, A. L. Tchebotareva, M. Orrit, M. Lippitz, S. Berciaud, D. Lasne, L. Cognet, and B. Lounis, “Absorption and scattering microscopy of single metal nanoparticles,” Phys. Chem. Chem. Phys. 8, 3486 (2006).
[Crossref] [PubMed]

Lisa, F. Di

L. Scorrano, V. Petronilli, R. Colonna, F. Di Lisa, and P. Bernardi, “Chloromethyltetramethylrosamine (Mitotracker Orange) induces the mitochondrial permeability transition and inhibits respiratory complex I. Implications for the mechanism of cytochrome c release,” J Biol. Chem 274, 24657–24663 (1999).
[Crossref] [PubMed]

Liu, X.

J. Yang, X. Liu, K. Bhalla, C. N. Kim, A. M. Ibrado, J. Cai, T. I. Peng, D. P. Jones, and X. Wang, “Prevention of apoptosis by Bcl-2: release of cytochrome c from mitochondria blocked,” Science 275, 1129–1132 (1997).
[Crossref] [PubMed]

Lounis, B.

M. A. Van Dijk, A. L. Tchebotareva, M. Orrit, M. Lippitz, S. Berciaud, D. Lasne, L. Cognet, and B. Lounis, “Absorption and scattering microscopy of single metal nanoparticles,” Phys. Chem. Chem. Phys. 8, 3486 (2006).
[Crossref] [PubMed]

S. Berciaud, D. Lasne, G. A. Blab, L. Cognet, and B. Lounis, “Photothermal Heterodyne Imaging of Individual Metallic Nanoparticles: Theory versus Experiments,” Phys. Rev. B 73, 045424 (2006).
[Crossref]

G. A. Blab, L. Cognet, S. Berciaud, I. Alexandre, D. Husar, J. Remacle, and B. Lounis, “Optical readout of gold nanoparticle-based DNA microarrays without silver enhancement,” Biophys. J. 90 (2006).
[Crossref]

S. Berciaud, L. Cognet, G. A. Blab, and B. Lounis, “Photothermal Heterodyne Imaging of Individual Nonfluorescent Nanoclusters and Nanocrystals,” Phys Rev Lett 93, 257402 (2004).
[Crossref]

Luo, K. Q.

W. Gao, Y. Pu, K. Q. Luo, and D. C. Chang, “Temporal relationship between cytochrome c release and mitochondrial swelling during UV-induced apoptosis in living HeLa cells,” J. Cell Sci. 114, 2855–2862 (2001).
[PubMed]

Lyle, C. S.

V. P. Zharov, V. Galitovskiy, C. S. Lyle, and T. C. Chambers, “Superhigh-sensitivity photothermal monitoring of individual cell response to antitumor drug,” J Biomed Opt 11, 064034 (2006).
[Crossref]

McDonald, A. E.

P. L. Gourley, J. K. Hendricks, A. E. McDonald, R. G. Copeland, K. E. Barrett, C. R. Gourley, K. K. Singh, and R. K. Naviaux, “Mitochondrial correlation microscopy and nanolaser spectroscopy - new tools for biophotonic detection of cancer in single cells,” Technol. Cancer Res Treat 4, 585–592 (2005).
[PubMed]

Murgia, M.

R. Rizzuto, M. Brini, P. Pizzo, M. Murgia, and T. Pozzan, “Chimeric green fluorescent protein as a tool for visualizing subcellular organelles in living cells,” Curr. Biol. 5, 635 (1995).
[Crossref] [PubMed]

Naviaux, R. K.

P. L. Gourley, J. K. Hendricks, A. E. McDonald, R. G. Copeland, K. E. Barrett, C. R. Gourley, K. K. Singh, and R. K. Naviaux, “Mitochondrial correlation microscopy and nanolaser spectroscopy - new tools for biophotonic detection of cancer in single cells,” Technol. Cancer Res Treat 4, 585–592 (2005).
[PubMed]

Newmeyer, D. D.

R. M. Kluck, E. Bossy-Wetzel, D. R. Green, and D. D. Newmeyer, “The release of cytochrome c from mitochondria: a primary site for Bcl-2 regulation of apoptosis,” Science 275, 1132–1136 (1997).
[Crossref] [PubMed]

O’Connor, P.

R. Bertrand, E. Solary, P. O’Connor, K. W. Kohn, and Y. Pommier, “Induction of a common pathway of apoptosis by staurosporine,” Exp. Cell Res. 211, 314–321 (1994).
[Crossref] [PubMed]

Orrit, M.

M. A. Van Dijk, A. L. Tchebotareva, M. Orrit, M. Lippitz, S. Berciaud, D. Lasne, L. Cognet, and B. Lounis, “Absorption and scattering microscopy of single metal nanoparticles,” Phys. Chem. Chem. Phys. 8, 3486 (2006).
[Crossref] [PubMed]

Othman, S.

I. Agalidis, S. Othman, A. Boussac, F. Reiss-Husson, and A. Desbois, “Purification, redox and spectroscopic properties of the tetraheme cytochrome c isolated from Rubrivivax gelatinosus,” Eur. J. Biochem. 261, 325 (1999).
[Crossref] [PubMed]

Pal, S.

J. F. Buckman, H. Hernandez, G. J. Kress, T. V. Votyakova, S. Pal, and I. J. Reynolds, “MitoTracker labeling in primary neuronal and astrocytic cultures: influence of mitochondrial membrane potential and oxidants,” J. Neurosci. Method. 104, 165 (2001).
[Crossref]

Peng, T. I.

J. Yang, X. Liu, K. Bhalla, C. N. Kim, A. M. Ibrado, J. Cai, T. I. Peng, D. P. Jones, and X. Wang, “Prevention of apoptosis by Bcl-2: release of cytochrome c from mitochondria blocked,” Science 275, 1129–1132 (1997).
[Crossref] [PubMed]

Perez-Pinzon, M. A.

T. J. Sick and M. A. Perez-Pinzon, “Optical methods for probing mitochondrial function in brain slices,” Methods 18, 104–108 (1999).
[Crossref] [PubMed]

Petronilli, V.

L. Scorrano, V. Petronilli, R. Colonna, F. Di Lisa, and P. Bernardi, “Chloromethyltetramethylrosamine (Mitotracker Orange) induces the mitochondrial permeability transition and inhibits respiratory complex I. Implications for the mechanism of cytochrome c release,” J Biol. Chem 274, 24657–24663 (1999).
[Crossref] [PubMed]

Pizzo, P.

R. Rizzuto, M. Brini, P. Pizzo, M. Murgia, and T. Pozzan, “Chimeric green fluorescent protein as a tool for visualizing subcellular organelles in living cells,” Curr. Biol. 5, 635 (1995).
[Crossref] [PubMed]

Pommier, Y.

R. Bertrand, E. Solary, P. O’Connor, K. W. Kohn, and Y. Pommier, “Induction of a common pathway of apoptosis by staurosporine,” Exp. Cell Res. 211, 314–321 (1994).
[Crossref] [PubMed]

Pozzan, T.

R. Rizzuto, M. Brini, P. Pizzo, M. Murgia, and T. Pozzan, “Chimeric green fluorescent protein as a tool for visualizing subcellular organelles in living cells,” Curr. Biol. 5, 635 (1995).
[Crossref] [PubMed]

Pu, Y.

W. Gao, Y. Pu, K. Q. Luo, and D. C. Chang, “Temporal relationship between cytochrome c release and mitochondrial swelling during UV-induced apoptosis in living HeLa cells,” J. Cell Sci. 114, 2855–2862 (2001).
[PubMed]

Reiss-Husson, F.

I. Agalidis, S. Othman, A. Boussac, F. Reiss-Husson, and A. Desbois, “Purification, redox and spectroscopic properties of the tetraheme cytochrome c isolated from Rubrivivax gelatinosus,” Eur. J. Biochem. 261, 325 (1999).
[Crossref] [PubMed]

Remacle, J.

G. A. Blab, L. Cognet, S. Berciaud, I. Alexandre, D. Husar, J. Remacle, and B. Lounis, “Optical readout of gold nanoparticle-based DNA microarrays without silver enhancement,” Biophys. J. 90 (2006).
[Crossref]

Reynolds, I. J.

J. F. Buckman, H. Hernandez, G. J. Kress, T. V. Votyakova, S. Pal, and I. J. Reynolds, “MitoTracker labeling in primary neuronal and astrocytic cultures: influence of mitochondrial membrane potential and oxidants,” J. Neurosci. Method. 104, 165 (2001).
[Crossref]

Rizzuto, R.

R. Rizzuto, M. Brini, P. Pizzo, M. Murgia, and T. Pozzan, “Chimeric green fluorescent protein as a tool for visualizing subcellular organelles in living cells,” Curr. Biol. 5, 635 (1995).
[Crossref] [PubMed]

Sato, K.

E. Tamaki, K. Sato, M. Tokeshi, K. Sato, M. Aihara, and T. Kitamori, “Single-cell analysis by a scanning thermal lens microscope with a microchip: direct monitoring of cytochrome c distribution during apoptosis process,” Anal Chem 74, 1560–1564 (2002).
[Crossref] [PubMed]

E. Tamaki, K. Sato, M. Tokeshi, K. Sato, M. Aihara, and T. Kitamori, “Single-cell analysis by a scanning thermal lens microscope with a microchip: direct monitoring of cytochrome c distribution during apoptosis process,” Anal Chem 74, 1560–1564 (2002).
[Crossref] [PubMed]

Scorrano, L.

L. Scorrano, V. Petronilli, R. Colonna, F. Di Lisa, and P. Bernardi, “Chloromethyltetramethylrosamine (Mitotracker Orange) induces the mitochondrial permeability transition and inhibits respiratory complex I. Implications for the mechanism of cytochrome c release,” J Biol. Chem 274, 24657–24663 (1999).
[Crossref] [PubMed]

Sick, T. J.

T. J. Sick and M. A. Perez-Pinzon, “Optical methods for probing mitochondrial function in brain slices,” Methods 18, 104–108 (1999).
[Crossref] [PubMed]

Singh, K. K.

P. L. Gourley, J. K. Hendricks, A. E. McDonald, R. G. Copeland, K. E. Barrett, C. R. Gourley, K. K. Singh, and R. K. Naviaux, “Mitochondrial correlation microscopy and nanolaser spectroscopy - new tools for biophotonic detection of cancer in single cells,” Technol. Cancer Res Treat 4, 585–592 (2005).
[PubMed]

Solary, E.

R. Bertrand, E. Solary, P. O’Connor, K. W. Kohn, and Y. Pommier, “Induction of a common pathway of apoptosis by staurosporine,” Exp. Cell Res. 211, 314–321 (1994).
[Crossref] [PubMed]

Stephens, D. J.

D. J. Stephens and V. J. Allan, “Light microscopy techniques for live cell imaging,” Science 300, 82–86 (2003).
[Crossref] [PubMed]

Steward, O.

L. A. Ligon and O. Steward, “Movement of mitochondria in the axons and dendrites of cultured hippocampal neurons,” J. Comp. Neurol. 427, 340–350 (2000).
[Crossref] [PubMed]

Tamaki, E.

E. Tamaki, K. Sato, M. Tokeshi, K. Sato, M. Aihara, and T. Kitamori, “Single-cell analysis by a scanning thermal lens microscope with a microchip: direct monitoring of cytochrome c distribution during apoptosis process,” Anal Chem 74, 1560–1564 (2002).
[Crossref] [PubMed]

Tchebotareva, A. L.

M. A. Van Dijk, A. L. Tchebotareva, M. Orrit, M. Lippitz, S. Berciaud, D. Lasne, L. Cognet, and B. Lounis, “Absorption and scattering microscopy of single metal nanoparticles,” Phys. Chem. Chem. Phys. 8, 3486 (2006).
[Crossref] [PubMed]

Tokeshi, M.

E. Tamaki, K. Sato, M. Tokeshi, K. Sato, M. Aihara, and T. Kitamori, “Single-cell analysis by a scanning thermal lens microscope with a microchip: direct monitoring of cytochrome c distribution during apoptosis process,” Anal Chem 74, 1560–1564 (2002).
[Crossref] [PubMed]

Vercesi, A. E.

A. E. Vercesi, C. F. Bernardes, M. E. Hoffmann, F. R. Gadelha, and R. Docampo, “Digitonin permeabilization does not affect mitochondrial function and allows the determination of the mitochondrial membrane potential of Trypanosoma cruzi in situ,” J Biol Chem 266, 14431–14434 (1991).
[PubMed]

Votyakova, T. V.

J. F. Buckman, H. Hernandez, G. J. Kress, T. V. Votyakova, S. Pal, and I. J. Reynolds, “MitoTracker labeling in primary neuronal and astrocytic cultures: influence of mitochondrial membrane potential and oxidants,” J. Neurosci. Method. 104, 165 (2001).
[Crossref]

Walker, J. E.

J. R. Gledhill and J. E. Walker, “Inhibition in F1-ATPase from bovine heart mitochondria,” Biochem. J. 386, 591 (2005).
[Crossref]

Wang, X.

J. Yang, X. Liu, K. Bhalla, C. N. Kim, A. M. Ibrado, J. Cai, T. I. Peng, D. P. Jones, and X. Wang, “Prevention of apoptosis by Bcl-2: release of cytochrome c from mitochondria blocked,” Science 275, 1129–1132 (1997).
[Crossref] [PubMed]

Waterhouse, N. J.

J. C. Goldstein, N. J. Waterhouse, P. Juin, G. I. Evan, and D. R. Green, “The coordinate release of cytochrome c during apoptosis is rapid, complete and kinetically invariant,” Nat Cell Biol 2, 156–162 (2000).
[Crossref] [PubMed]

Yang, J.

J. Yang, X. Liu, K. Bhalla, C. N. Kim, A. M. Ibrado, J. Cai, T. I. Peng, D. P. Jones, and X. Wang, “Prevention of apoptosis by Bcl-2: release of cytochrome c from mitochondria blocked,” Science 275, 1129–1132 (1997).
[Crossref] [PubMed]

Zharov, V. P.

V. P. Zharov, V. Galitovskiy, C. S. Lyle, and T. C. Chambers, “Superhigh-sensitivity photothermal monitoring of individual cell response to antitumor drug,” J Biomed Opt 11, 064034 (2006).
[Crossref]

Anal Chem (1)

E. Tamaki, K. Sato, M. Tokeshi, K. Sato, M. Aihara, and T. Kitamori, “Single-cell analysis by a scanning thermal lens microscope with a microchip: direct monitoring of cytochrome c distribution during apoptosis process,” Anal Chem 74, 1560–1564 (2002).
[Crossref] [PubMed]

Biochem. J. (3)

C. Hoppel and C. Cooper, “The action of digitonin on rat liver mitochondria. The effects on enzyme content,” Biochem. J. 107, 367–375 (1968).
[PubMed]

J. R. Gledhill and J. E. Walker, “Inhibition in F1-ATPase from bovine heart mitochondria,” Biochem. J. 386, 591 (2005).
[Crossref]

B. Z. Cavari and Y. Avi-Dor, “Effect of carbonyl cyanide m-chlorophenylhydrazone on respiration and respiration-dependent phosphorylation in Escherichia coli,” Biochem. J. 103, 601–608 (1967).
[PubMed]

Biochemistry (2)

P. G. Heytler, “Uncoupling of Oxidative Phosphorylation by Carbonyl Cyanide Phenylhydrazones. I. Some Characteristics of m-CI-CCP Action on Mitochondria and Chloroplasts,” Biochemistry 2, 357–361 (1963).
[Crossref] [PubMed]

R. A. Goldsby and P. G. Heytler, “Uncoupling Of Oxidative Phosphorylation By Carbonyl Cyanide Phenylhydrazones. Ii. Effects Of Carbonyl Cyanide M-Chlorophenylhydrazone On Mitochondrial Respiration,” Biochemistry 2, 1142–1147 (1963).
[Crossref] [PubMed]

Biophys. J. (1)

G. A. Blab, L. Cognet, S. Berciaud, I. Alexandre, D. Husar, J. Remacle, and B. Lounis, “Optical readout of gold nanoparticle-based DNA microarrays without silver enhancement,” Biophys. J. 90 (2006).
[Crossref]

Curr Opin Rheumatol (1)

S. DiMauro, “Mitochondrial myopathies,” Curr Opin Rheumatol 18, 636–641 (2006).
[Crossref] [PubMed]

Curr. Biol. (1)

R. Rizzuto, M. Brini, P. Pizzo, M. Murgia, and T. Pozzan, “Chimeric green fluorescent protein as a tool for visualizing subcellular organelles in living cells,” Curr. Biol. 5, 635 (1995).
[Crossref] [PubMed]

Eur. J. Biochem. (1)

I. Agalidis, S. Othman, A. Boussac, F. Reiss-Husson, and A. Desbois, “Purification, redox and spectroscopic properties of the tetraheme cytochrome c isolated from Rubrivivax gelatinosus,” Eur. J. Biochem. 261, 325 (1999).
[Crossref] [PubMed]

Exp. Cell Res. (1)

R. Bertrand, E. Solary, P. O’Connor, K. W. Kohn, and Y. Pommier, “Induction of a common pathway of apoptosis by staurosporine,” Exp. Cell Res. 211, 314–321 (1994).
[Crossref] [PubMed]

J Biol Chem (1)

A. E. Vercesi, C. F. Bernardes, M. E. Hoffmann, F. R. Gadelha, and R. Docampo, “Digitonin permeabilization does not affect mitochondrial function and allows the determination of the mitochondrial membrane potential of Trypanosoma cruzi in situ,” J Biol Chem 266, 14431–14434 (1991).
[PubMed]

J Biol. Chem (1)

L. Scorrano, V. Petronilli, R. Colonna, F. Di Lisa, and P. Bernardi, “Chloromethyltetramethylrosamine (Mitotracker Orange) induces the mitochondrial permeability transition and inhibits respiratory complex I. Implications for the mechanism of cytochrome c release,” J Biol. Chem 274, 24657–24663 (1999).
[Crossref] [PubMed]

J Biomed Opt (1)

V. P. Zharov, V. Galitovskiy, C. S. Lyle, and T. C. Chambers, “Superhigh-sensitivity photothermal monitoring of individual cell response to antitumor drug,” J Biomed Opt 11, 064034 (2006).
[Crossref]

J. Cell Sci. (1)

W. Gao, Y. Pu, K. Q. Luo, and D. C. Chang, “Temporal relationship between cytochrome c release and mitochondrial swelling during UV-induced apoptosis in living HeLa cells,” J. Cell Sci. 114, 2855–2862 (2001).
[PubMed]

J. Comp. Neurol. (1)

L. A. Ligon and O. Steward, “Movement of mitochondria in the axons and dendrites of cultured hippocampal neurons,” J. Comp. Neurol. 427, 340–350 (2000).
[Crossref] [PubMed]

J. Histochem. Cytochem. (1)

D. DiDonato and D. L. Brasaemle, “Fixation Methods for the Study of Lipid Droplets by Immunofluorescence Microscopy,” J. Histochem. Cytochem. 51, 773–780 (2003).
[Crossref] [PubMed]

J. Neurosci. Method. (1)

J. F. Buckman, H. Hernandez, G. J. Kress, T. V. Votyakova, S. Pal, and I. J. Reynolds, “MitoTracker labeling in primary neuronal and astrocytic cultures: influence of mitochondrial membrane potential and oxidants,” J. Neurosci. Method. 104, 165 (2001).
[Crossref]

Methods (1)

T. J. Sick and M. A. Perez-Pinzon, “Optical methods for probing mitochondrial function in brain slices,” Methods 18, 104–108 (1999).
[Crossref] [PubMed]

Nat Cell Biol (1)

J. C. Goldstein, N. J. Waterhouse, P. Juin, G. I. Evan, and D. R. Green, “The coordinate release of cytochrome c during apoptosis is rapid, complete and kinetically invariant,” Nat Cell Biol 2, 156–162 (2000).
[Crossref] [PubMed]

Nature (1)

A. J. Borgdorff and D. Choquet, “Regulation of AMPA receptor lateral movements,” Nature 417, 649–653. (2002).
[Crossref] [PubMed]

Phys Rev Lett (1)

S. Berciaud, L. Cognet, G. A. Blab, and B. Lounis, “Photothermal Heterodyne Imaging of Individual Nonfluorescent Nanoclusters and Nanocrystals,” Phys Rev Lett 93, 257402 (2004).
[Crossref]

Phys. Chem. Chem. Phys. (1)

M. A. Van Dijk, A. L. Tchebotareva, M. Orrit, M. Lippitz, S. Berciaud, D. Lasne, L. Cognet, and B. Lounis, “Absorption and scattering microscopy of single metal nanoparticles,” Phys. Chem. Chem. Phys. 8, 3486 (2006).
[Crossref] [PubMed]

Phys. Rev. B (1)

S. Berciaud, D. Lasne, G. A. Blab, L. Cognet, and B. Lounis, “Photothermal Heterodyne Imaging of Individual Metallic Nanoparticles: Theory versus Experiments,” Phys. Rev. B 73, 045424 (2006).
[Crossref]

Science (3)

D. J. Stephens and V. J. Allan, “Light microscopy techniques for live cell imaging,” Science 300, 82–86 (2003).
[Crossref] [PubMed]

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Figures (6)
Fig. 1.
Fig. 1. Experimental setup combining multi-imaging capabilities. LISNA uses the exciting beam which intensity is modulated with an acousto-optic modulator (AOM), the probe beam, the upper detector and the lock-in amplifier. For confocal fluorescence imaging, either the excitation or probe beam are used depending on the fluorophore to be excited and the fluorescence is filtered and detected by the avalanche photodiode (APD). For creating 2D images the sample is raster scanned by means of the piezo-scanner both for LISNA and confocal fluorescence imaging. White light is used to perform large field images of the sample that are recorded the CCD camera.

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Fig. 2.
Fig. 2. (a). Fluorescence (Mitotracker Deep Red) and (b) LISNA images of COS-7 cells. The scale bar represents 10 μm.

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Fig.3.
Fig.3. (a). Fluorescence (Mitotracker Deep Red) and (b) LISNA images of hippocampal neurons. The scale bar represents 2 μm.

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Fig. 4.
Fig. 4. LISNA images of COS-7 cells portions before (a) and after (b,c) 100 mM digitonin loading (The scale bar represents 10 μm).

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Fig. 5.
Fig. 5. Images of HeLa cells after apoptosis induction using staurosporin (The scale bar represents 10 μm). (a,c,e) Fluorescence images. Cytochrome c is fluorescently labeled and localized in mitochondria for most cells. But some cells (arrows) show very diffuse signal as cytochrome c is released into the cytosol during apoptosis. However, the LISNA signal (b,d,f) is very structured, even in those cells.

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Fig. 6.
Fig. 6. LISNA images of COS-7 cells portions before (a,b) and after (c,d) 1μM CCCP loading (The scale bar represents 10 μm).

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