- About this Journal ·
- Abstracting and Indexing ·
- Aims and Scope ·
- Annual Issues ·
- Article Processing Charges ·
- Articles in Press ·
- Author Guidelines ·
- Bibliographic Information ·
- Citations to this Journal ·
- Contact Information ·
- Editorial Board ·
- Editorial Workflow ·
- Free eTOC Alerts ·
- Publication Ethics ·
- Reviewers Acknowledgment ·
- Submit a Manuscript ·
- Subscription Information ·
- Table of Contents
Oxidative Medicine and Cellular Longevity
Volume 2013 (2013), Article ID 323619, 11 pages
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.
- J. F. Turrens, “Mitochondrial formation of reactive oxygen species,” The Journal of Physiology, vol. 552, part 2, pp. 335–344, 2003.
- 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.
- 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.
- R. Carmel and D. W. Jacobsen, Eds., Homocysteine in Health and Disease, Cambridge University Press, Cambridge, UK, 2001.
- 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.
- 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.
- 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.
- R. P. Haugland, Ed., A Guide to Fluorescent Probes and Labeling Technologies, Molecular Probes, Eugene, Ore, USA, 10th edition, 2005.
- 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.
- 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.
- 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.
- 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.
- F. Helmchen and W. Denk, “Deep tissue two-photon microscopy,” Nature Methods, vol. 2, no. 12, pp. 932–940, 2005.
- 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.
- 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.
- H. M. Kim and B. R. Cho, “Two-photon fluorescent probes for metal ions,” Chemistry, vol. 6, no. 1, pp. 58–69, 2011.
- 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.
- 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.
- 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.
- 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.
- 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.
- B. L. Vallee and K. H. Falchuk, “The biochemical basis of zinc physiology,” Physiological Reviews, vol. 73, no. 1, pp. 79–118, 1993.
- 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.
- 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.
- 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.
- 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.
- 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.
- 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.
- 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.
- 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.
- 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.
- 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.
- 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.
- 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.
- 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.
- 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.
- 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.
- 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.
- T. Finkel and N. J. Holbrook, “Oxidants, oxidative stress and the biology of ageing,” Nature, vol. 408, no. 6809, pp. 239–247, 2000.
- E. R. Stadtman, “Protein oxidation and aging,” Free Radical Research, vol. 40, no. 12, pp. 1250–1258, 2006.
- 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.
- T. Finkel, M. Serrano, and M. A. Blasco, “The common biology of cancer and ageing,” Nature, vol. 448, no. 7155, pp. 767–774, 2007.
- 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.
- M. T. Lin and M. F. Beal, “Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases,” Nature, vol. 443, no. 7113, pp. 787–795, 2006.
- 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.
- 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.
- 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.
- 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.
- 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.
- 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.