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Journal of the Optical Society of America B

Journal of the Optical Society of America B


  • Vol. 17, Iss. 6 — Jun. 1, 2000
  • pp: 1058–1067

Accumulated photon-echo spectroscopy for stained tissue samples

K. Uchikawa, M. Sakamoto, A. Koreeda, and S. Saikan  »View Author Affiliations

JOSA B, Vol. 17, Issue 6, pp. 1058-1067 (2000)

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We performed phase relaxation-time measurements of the accumulated photon echo for normal and cancerous tissue samples of human liver, that were stained with several kinds of dye. Each dye interacted selectively with a specific kind of biomolecule in the tissues, for example, DNA, proteins, or lipids. The cancerous tissues showed a tendency to have shorter relaxation times than the normal tissues had. The difference of relaxation time observed between the normal and the cancerous tissues depended on the dyes that were used for staining, and the difference became most clear when the tissues were stained with a cyanine dye derivative, i.e., YO-PRO3 Iodide, which has a high selectivity for DNA. We performed the relaxation-time mapping of the accumulated photon echo (photon-echo imaging) for a liver tissue sample stained by YO-PRO3 Iodide. The photon-echo imaging was successful in showing a region of a highly differentiated hepatocellular carcinoma in the tissue sample, while fluorescence-intensity mapping could not identify the cancerous region in the same tissue sample. These results indicated a possibility that the reduction of accumulated photon-echo relaxation time observed in the cancerous tissues was caused by a change of microscopic dynamics of DNA.

© 2000 Optical Society of America

OCIS Codes
(170.6930) Medical optics and biotechnology : Tissue
(260.2510) Physical optics : Fluorescence
(270.1670) Quantum optics : Coherent optical effects
(300.6420) Spectroscopy : Spectroscopy, nonlinear
(300.6500) Spectroscopy : Spectroscopy, time-resolved

K. Uchikawa, M. Sakamoto, A. Koreeda, and S. Saikan, "Accumulated photon-echo spectroscopy for stained tissue samples," J. Opt. Soc. Am. B 17, 1058-1067 (2000)

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  1. R. Damadian, “Tumor detection by nuclear magnetic resonance,” Science 171, 1151–1153 (1971). [CrossRef] [PubMed]
  2. D. P. Hollis, L. A. Saryan, J. C. Eggleston, and H. P. Morris, “Nuclear magnetic resonance studies of cancer. VI. Relationship among spin-lattice relaxation times, growth rate, and water content of Morris hepatomas,” J. Natl. Cancer Inst. 54, 1469–1472 (1975). [PubMed]
  3. R. Cooke and R. Wien, “Nuclear magnetic resonance studies of intracellular water protons,” Ann. (N.Y.) Acad. Sci. 204, 197–209 (1973). [CrossRef]
  4. S. H. Koenig, “The dynamics of water–protein interactions,” ACS Symp. Ser. 127, 157–176 (1980). [CrossRef]
  5. G. N. Ling, M. M. Ochsenfeld, C. L. Walton, and T. J. Bersinger, “Experimental confirmation from model studies of a key prediction of the polarized multilayer theory of cell water,” Physiol. Chem. Phys. 10, 87–88 (1978).
  6. W. Bovee, P. Huisman, and J. Schmidt, “Tumor detection and nuclear magnetic resonance,” J. Natl. Cancer Inst. 52, 595 (1974). [PubMed]
  7. B. T. Beall, B. B. Asch, D. C. Chang, D. Medina, and C. R. Hazelwood, “Distinction of normal, preneoplastic, and neoplastic mouse mammary primary cell cultures by water nuclear magnetic resonance relaxation times,” J. Natl. Cancer Inst. 64, 335–338 (1980). [PubMed]
  8. A. Furusawa, T. Suga, and K. Uchikawa, “Photon-echo spectroscopy on biological systems. I. Application to tissues,” J. Opt. Soc. Am. B 11, 1456–1461 (1994). [CrossRef]
  9. K. Uchikawa and M. Okada, “Accumulated photon echo spectroscopy on a human stomach cancer,” Laser Phys. 5, 687–692 (1995).
  10. K. Uchikawa, H. Ohsawa, T. Suga, and S. Saikan, “Fluorescence detection of femtosecond accumulated photon echo,” Opt. Lett. 16, 13–14 (1991). [CrossRef] [PubMed]
  11. R. Damadian, K. Zanec, D. Hor, and T. Dimaio, “Human tumors detected by nuclear magnetic resonance,” Proc. Natl. Acad. Sci. USA 71, 1471–1473 (1974). [CrossRef] [PubMed]
  12. K. Uchikawa and M. Sakamoto, “Accumulated photon-echo imaging for tissue samples,” J. Opt. Soc. Am. B 14, 689–696 (1997). [CrossRef]
  13. W. H. Hesselink and D. A. Wiersma, “Picosecond photon echoes stimulated from an accumulated grating,” Phys. Rev. Lett. 43, 1991–1994 (1979). [CrossRef]
  14. W. H. Hesselink and D. A. Wiersma, “Photon echoes stimulated from an accumulated grating: theory of generation and detection,” J. Chem. Phys. 75, 4192–4197 (1981). [CrossRef]
  15. S. Saikan, K. Uchikawa, and H. Ohsawa, “Phase-modulation technique for accumulated photon echo,” Opt. Lett. 16, 10–12 (1991). [CrossRef] [PubMed]
  16. H. Zewail, T. E. Orlowski, K. E. Jones, and D. E. Godar, “Spontaneously detected photon echoes in excited molecular ensembles: a probe pulse laser technique for the detection of optical coherence of inhomogeneously broadened electronic transitions,” Chem. Phys. Lett. 48, 256–261 (1977). [CrossRef]
  17. J. H. Fourkas, W. L. Wilson, G. Wackerle, A. E. Frost, and M. D. Fayer, “Picosecond time-scale phase-related optical pulses: measurement of sodium optical coherence decay by observation of incoherent fluorescence,” J. Opt. Soc. Am. B 6, 1905–1910 (1989). [CrossRef]
  18. S. Mukamel and R. F. Loring, “Nonlinear response function for time-domain and frequency-domain four-wave mixing,” J. Opt. Soc. Am. B 3, 595–606 (1986). [CrossRef]
  19. M. Berg, C. A. Walsh, L. R. Narasimhan, K. A. Littau, and M. D. Fayer, “Dynamics in low temperature glasses: theory and experiments on optical dephasing spectral diffusion, and hydrogen tunneling,” J. Chem. Phys. 88, 1564–1587 (1988). [CrossRef]
  20. M. D. Levenson, Introduction to Nonlinear Laser Spectroscopy (Academic, New York, 1982).
  21. C. Carlsson, A. Larsson, M. Jonsson, B. Albinsson, and B. Norden, “Optical and photophysical properties of the oxazole yellow DNA probes YO and YOYO,” J. Phys. Chem. 98, 10313–10321 (1994). [CrossRef]
  22. E. S. Mansfield, M. Vainer, S. Enad, D. L. Barker, D. Harris, E. Rappaport, and P. Fortina, “Sensitivity, reproducibility, and accuracy in short tandem repeat genotyping using capillary array electrophoresis,” Genome Res. 6, 893–903 (1996). [CrossRef] [PubMed]
  23. N. J. Abernethy, W. Chin, H. Lyons, and J. B. Hay, “A dual laser analysis of the migration of XRITC-labeled, FITC-labeled, and double-labeled lymphocytes in sheep,” Cytometry 6, 407–413 (1985). [CrossRef] [PubMed]
  24. G. S. Elemer and T. S. Edgington, “Microfilament reorganization is associated with functional activation of αMβ2 on monocytic cells,” J. Biol. Chem. 269, 3159–3166 (1994). [PubMed]
  25. I. D. Johnson, H. C. Kang, and R. P. Haugland, “Fluorescence membrane probes incorporating dipyrrometheneboron difluoride fluorophores,” Anal. Biochem. 198, 228–237 (1991). [CrossRef] [PubMed]
  26. M. Sakamoto, Y. Ino, A. Ochiai, Y. Kanai, S. Akimoto, and S. Hirohashi, “Formation of focal adhesion and spreading of polarized human colon cancer cells association with tyrosine phosphorylation of paxillin in response to phorbol ester,” Lab. Invest. 74, 199–208 (1996). [PubMed]
  27. S. Hakomori and R. Kannagi, “Glycosphingolipids as tumor-associated and differentiation markers,” J. Natl. Cancer Inst. 71, 231–251 (1983). [PubMed]
  28. P. W. Anderson, B. I. Halperin, and C. W. Varma, “Anomalous low-temperature thermal properties of glasses and spin glasses,” Philos. Mag. 25, 1–9 (1972). [CrossRef]
  29. D. T. Leeson, D. A. Wiersma, K. Fritsch, and J. Friedrich, “The energy landscape of myoglobin: an optical study,” J. Phys. Chem. B 101, 6331–6340 (1997). [CrossRef]
  30. S. Saikan, J. W-I. Lin, and H. Nemoto, “Non-Markovian relaxation observed in photon echoes of iron-free myoglobin,” Phys. Rev. B 46, 11125–11128 (1992). [CrossRef]
  31. B. Albert, D. Bray, J. Lewis, M. Raff, K. Roberts, and J. D. Watson, Molecular Biology of The Cell, 2nd ed. (Garland, New York, 1989).

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