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Oxidative Medicine and Cellular Longevity
Volume 2013 (2013), Article ID 323619, 11 pages
http://dx.doi.org/10.1155/2013/323619
Review Article

Mitochondrial-Targeted Two-Photon Fluorescent Probes for Zinc Ions, , and Thiols in Living Tissues

1Division of Energy Systems Research, Ajou University, Suwon 443-749, Republic of Korea
2Department of Chemistry, Korea University, 1-Anamdong, Seoul 136-701, Republic of Korea

Received 26 July 2012; Revised 26 October 2012; Accepted 28 December 2012

Academic Editor: Antonio Ascensao

Copyright © 2013 Hwan Myung Kim and Bong Rae Cho. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Linked References

  1. J. F. Turrens, “Mitochondrial formation of reactive oxygen species,” The Journal of Physiology, vol. 552, part 2, pp. 335–344, 2003. View at Publisher · View at Google Scholar · View at Scopus
  2. B. C. Dickinson and C. J. Chang, “Chemistry and biology of reactive oxygen species in signaling or stress responses,” Nature Chemical Biology, vol. 7, no. 8, pp. 504–511, 2011. View at Publisher · View at Google Scholar · View at Scopus
  3. Z. A. Wood, E. Schröder, J. Robin Harris, and L. B. Poole, “Structure, mechanism and regulation of peroxiredoxins,” Trends in Biochemical Sciences, vol. 28, no. 1, pp. 32–40, 2003. View at Publisher · View at Google Scholar · View at Scopus
  4. R. Carmel and D. W. Jacobsen, Eds., Homocysteine in Health and Disease, Cambridge University Press, Cambridge, UK, 2001.
  5. T. P. Dalton, H. G. Shertzer, and A. Puga, “Regulation of gene expression by reactive oxygen,” Annual Review of Pharmacology and Toxicology, vol. 39, pp. 67–101, 1999. View at Publisher · View at Google Scholar · View at Scopus
  6. M. Marí, A. Morales, A. Colell, C. García-Ruiz, and J. C. Fernández-Checa, “Mitochondrial glutathione, a key survival antioxidant,” Antioxidants & Redox Signaling, vol. 11, no. 11, pp. 2685–2700, 2009. View at Publisher · View at Google Scholar · View at Scopus
  7. S. L. Sensi, D. Ton-That, J. H. Weiss, A. Rothe, and K. R. Gee, “A new mitochondrial fluorescent zinc sensor,” Cell Calcium, vol. 34, no. 3, pp. 281–284, 2003. View at Publisher · View at Google Scholar · View at Scopus
  8. R. P. Haugland, Ed., A Guide to Fluorescent Probes and Labeling Technologies, Molecular Probes, Eugene, Ore, USA, 10th edition, 2005.
  9. B. C. Dickinson and C. J. Chang, “A targetable fluorescent probe for imaging hydrogen peroxide in the mitochondria of living cells,” Journal of the American Chemical Society, vol. 130, no. 30, pp. 9638–9639, 2008. View at Publisher · View at Google Scholar · View at Scopus
  10. N. Y. Baek, C. H. Heo, C. S. Lim, et al., “A highly sensitive two-photon fluorescent probe for mitochondrial zinc ions in living tissue,” Chemical Communications, vol. 48, no. 38, pp. 4546–4548, 2012. View at Publisher · View at Google Scholar
  11. G. Masanta, C. H. Heo, C. S. Lim, et al., “A mitochondria-localized two-photon fluorescent probe for ratiometric imaging of hydrogen peroxide in live tissue,” Chemical Communications, vol. 48, no. 29, pp. 3518–3520, 2012. View at Publisher · View at Google Scholar
  12. C. S. Lim, G. Masanta, H. J. Kim, J. H. Han, H. M. Kim, and B. R. Cho, “Ratiometric detection of mitochondrial thiols with a two-photon fluorescent probe,” Journal of the American Chemical Society, vol. 133, no. 29, pp. 11132–11135, 2011. View at Publisher · View at Google Scholar · View at Scopus
  13. F. Helmchen and W. Denk, “Deep tissue two-photon microscopy,” Nature Methods, vol. 2, no. 12, pp. 932–940, 2005. View at Publisher · View at Google Scholar · View at Scopus
  14. W. R. Zipfel, R. M. Williams, and W. W. Webb, “Nonlinear magic: multiphoton microscopy in the biosciences,” Nature Biotechnology, vol. 21, no. 11, pp. 1369–1377, 2003. View at Publisher · View at Google Scholar · View at Scopus
  15. H. M. Kim and B. R. Cho, “Two-photon probes for intracellular free metal ions, acidic vesicles, and lipid rafts in live tissues,” Accounts of Chemical Research, vol. 42, no. 7, pp. 863–872, 2009. View at Publisher · View at Google Scholar · View at Scopus
  16. H. M. Kim and B. R. Cho, “Two-photon fluorescent probes for metal ions,” Chemistry, vol. 6, no. 1, pp. 58–69, 2011. View at Publisher · View at Google Scholar · View at Scopus
  17. R. M. Williams, W. R. Zipfel, and W. W. Webb, “Multiphoton microscopy in biological research,” Current Opinion in Chemical Biology, vol. 5, no. 5, pp. 603–608, 2001. View at Publisher · View at Google Scholar · View at Scopus
  18. C. Xu, W. Zipfel, J. B. Shear, R. M. Williams, and W. W. Webb, “Multiphoton fluorescence excitation: new spectral windows for biological nonlinear microscopy,” Proceedings of the National Academy of Sciences of the United States of America, vol. 93, no. 20, pp. 10763–10768, 1996. View at Publisher · View at Google Scholar · View at Scopus
  19. G. Masanta, C. S. Lim, H. J. Kim, J. H. Han, H. M. Kim, and B. R. Cho, “A mitochondrial-targeted two-photon probe for zinc ion,” Journal of the American Chemical Society, vol. 133, no. 15, pp. 5698–5700, 2011. View at Publisher · View at Google Scholar · View at Scopus
  20. M. P. Murphy and R. A. J. Smith, “Targeting antioxidants to mitochondria by conjugation to lipophilic cations,” Annual Review of Pharmacology and Toxicology, vol. 47, pp. 629–656, 2007. View at Publisher · View at Google Scholar · View at Scopus
  21. L. F. Yousif, K. M. Stewart, and S. O. Kelley, “Targeting mitochondria with organelle-specific compounds: strategies and applications,” ChemBioChem, vol. 10, no. 12, pp. 1939–1950, 2009. View at Publisher · View at Google Scholar · View at Scopus
  22. B. L. Vallee and K. H. Falchuk, “The biochemical basis of zinc physiology,” Physiological Reviews, vol. 73, no. 1, pp. 79–118, 1993. View at Scopus
  23. J. M. Berg and Y. Shi, “The galvanization of biology: a growing appreciation for the roles of zinc,” Science, vol. 271, no. 5252, pp. 1081–1085, 1996. View at Scopus
  24. C. J. Frederickson, J. Y. Koh, and A. I. Bush, “The neurobiology of zinc in health and disease,” Nature Reviews Neuroscience, vol. 6, no. 6, pp. 449–462, 2005. View at Publisher · View at Google Scholar · View at Scopus
  25. S. Y. Assaf and S. H. Chung, “Release of endogenous Zn2+ from brain tissue during activity,” Nature, vol. 308, no. 5961, pp. 734–736, 1984. View at Scopus
  26. G. A. Howell, M. G. Welch, and C. J. Frederickson, “Stimulation-induced uptake and release of zinc in hippocampal slices,” Nature, vol. 308, no. 5961, pp. 736–738, 1984. View at Scopus
  27. S. L. Sensi, H. Z. Yin, and J. H. Weiss, “AMPA/kainate receptor-triggered Zn2+ entry into cortical neurons induces mitochondrial Zn2+ uptake and persistent mitochondrial dysfunction,” European Journal of Neuroscience, vol. 12, no. 10, pp. 3813–3818, 2000. View at Publisher · View at Google Scholar · View at Scopus
  28. S. L. Sensi, P. Paoletti, A. I. Bush, and I. Sekler, “Zinc in the physiology and pathology of the CNS,” Nature Reviews Neuroscience, vol. 10, no. 11, pp. 780–791, 2009. View at Publisher · View at Google Scholar · View at Scopus
  29. H. M. Kim, M. S. Seo, M. J. An et al., “Two-photon fluorescent probes for intracellular free zinc ions in living tissue,” Angewandte Chemie, vol. 47, no. 28, pp. 5167–5170, 2008. View at Publisher · View at Google Scholar · View at Scopus
  30. K. Komatsu, K. Kikuchi, H. Kojima, Y. Urano, and T. Nagano, “Selective zinc sensor molecules with various affinities for Zn2+, revealing dynamics and regional distribution of synaptically released Zn2+ in hippocampal slices,” Journal of the American Chemical Society, vol. 127, no. 29, pp. 10197–10204, 2005. View at Publisher · View at Google Scholar · View at Scopus
  31. A. P. de Silva, H. Q. N. Gunaratne, T. Gunnlaugsson et al., “Signaling recognition events with fluorescent sensors and switches,” Chemical Reviews, vol. 97, no. 5, pp. 1515–1566, 1997. View at Scopus
  32. E. U. Akkaya, M. E. Huston, and A. W. Czarnik, “Chelation-enhanced fluorescence of anthrylazamacrocycle conjugate probes in aqueous solution,” Journal of the American Chemical Society, vol. 112, no. 9, pp. 3590–3593, 1990. View at Scopus
  33. T. D. Rae, P. J. Schmidt, R. A. Pufahl, V. C. Culotta, and T. V. O'Halloran, “Undetectable intracellular free copper: the requirement of a copper chaperone for superoxide dismutase,” Science, vol. 284, no. 5415, pp. 805–808, 1999. View at Publisher · View at Google Scholar · View at Scopus
  34. K. Emmerson and K. Roehrig, “Epidermal growth factor (EGF) stimulation of ATP citrate lyase activity in isolated rat hepatocytes is age dependent,” Comparative Biochemistry and Physiology B, vol. 103, no. 3, pp. 663–667, 1992. View at Publisher · View at Google Scholar · View at Scopus
  35. S. L. Sensi, D. Ton-That, P. G. Sullivan et al., “Modulation of mitochondrial function by endogenous Zn2+ pools,” Proceedings of the National Academy of Sciences of the United States of America, vol. 100, no. 10, pp. 6157–6162, 2003. View at Publisher · View at Google Scholar · View at Scopus
  36. E. Aizenman, A. K. Stout, K. A. Hartnett, K. E. Dineley, B. McLaughlin, and I. J. Reynolds, “Induction of neuronal apoptosis by thiol oxidation: putative role of intracellular zinc release,” Journal of Neurochemistry, vol. 75, no. 5, pp. 1878–1888, 2000. View at Publisher · View at Google Scholar · View at Scopus
  37. T. Caporale, D. Ciavardelli, C. Di Ilio, P. Lanuti, D. Drago, and S. L. Sensi, “Ratiometric-pericam-mt, a novel tool to evaluate intramitochondrial zinc,” Experimental Neurology, vol. 218, no. 2, pp. 228–234, 2009. View at Publisher · View at Google Scholar · View at Scopus
  38. D. Harman, “The aging process,” Proceedings of the National Academy of Sciences of the United States of America, vol. 78, no. 11, pp. 7124–7128, 1981. View at Scopus
  39. T. Finkel and N. J. Holbrook, “Oxidants, oxidative stress and the biology of ageing,” Nature, vol. 408, no. 6809, pp. 239–247, 2000. View at Publisher · View at Google Scholar · View at Scopus
  40. E. R. Stadtman, “Protein oxidation and aging,” Free Radical Research, vol. 40, no. 12, pp. 1250–1258, 2006. View at Publisher · View at Google Scholar · View at Scopus
  41. E. A. Veal, A. M. Day, and B. A. Morgan, “Hydrogen peroxide sensing and signaling,” Molecular Cell, vol. 26, no. 1, pp. 1–14, 2007. View at Publisher · View at Google Scholar · View at Scopus
  42. T. Finkel, M. Serrano, and M. A. Blasco, “The common biology of cancer and ageing,” Nature, vol. 448, no. 7155, pp. 767–774, 2007. View at Publisher · View at Google Scholar · View at Scopus
  43. K. J. Barnham, C. L. Masters, and A. I. Bush, “Neurodegenerative diseases and oxidatives stress,” Nature Reviews Drug Discovery, vol. 3, no. 3, pp. 205–214, 2004. View at Scopus
  44. M. T. Lin and M. F. Beal, “Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases,” Nature, vol. 443, no. 7113, pp. 787–795, 2006. View at Publisher · View at Google Scholar · View at Scopus
  45. K. M. Geraghty, S. Chen, J. E. Harthill et al., “Regulation of multisite phosphorylation and 14-3-3 binding of AS160 in response to IGF-1, EGF, PMA and AICAR,” Biochemical Journal, vol. 407, no. 2, pp. 231–241, 2007. View at Publisher · View at Google Scholar · View at Scopus
  46. R. Kizek, J. Vacek, L. Trnková, and F. Jelen, “Cyclic voltammetric study of the redox system of glutathione using the disulfide bond reductant tris(2-carboxyethyl)phosphine,” Bioelectrochemistry, vol. 63, no. 1-2, pp. 19–24, 2004. View at Publisher · View at Google Scholar · View at Scopus
  47. M. Marí, A. Morales, A. Colell, C. García-Ruiz, and J. C. Fernández-Checa, “Mitochondrial glutathione, a key survival antioxidant,” Antioxidants and Redox Signaling, vol. 11, no. 11, pp. 2685–2700, 2009. View at Publisher · View at Google Scholar · View at Scopus
  48. F. Q. Schafer and G. R. Buettner, “Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple,” Free Radical Biology and Medicine, vol. 30, no. 11, pp. 1191–1212, 2001. View at Publisher · View at Google Scholar · View at Scopus
  49. B. Hultberg, A. Andersson, and A. Isaksson, “Lipoic acid increases glutathione production and enhances the effect of mercury in human cell lines,” Toxicology, vol. 175, no. 1–3, pp. 103–110, 2002. View at Publisher · View at Google Scholar · View at Scopus
  50. C. R. Yellaturu, M. Bhanoori, I. Neeli, and G. N. Rao, “N-Ethylmaleimide inhibits platelet-derived growth factor BB-stimulated Akt phosphorylation via activation of protein phosphatase 2A,” The Journal of Biological Chemistry, vol. 277, no. 42, pp. 40148–40155, 2002. View at Publisher · View at Google Scholar · View at Scopus