Advertisement

In Vivo Detection of Free Radicals in Real Time by Low-Frequency Electron Paramagnetic Resonance Spectroscopy

  • Gerald M. Rosen
  • Sovitj Pou
  • Howard J. Halpern
Part of the Methods in Molecular Biology™ book series (MIMB, volume 108)

Abstract

During his studies on the properties of oxygen, Priestley (1) noted that this gas, an essential ingredient for life processes, appears to “burn out the candle of life too quickly.” More than two centuries would elapse, however, before this observation would be associated with Grubbé’s (2) accounts of redness and irritation on the hands of his workers testing X-ray tubes. By 1954, Gerschman et al. (3) suggested that free radicals were the common element linking the observed toxicity of oxygen to the harmful effects of ionizing radiation. The implication of this hypothesis seemed remote at that time. However, within a decade, the search for biologically generated free radicals would lead to the discovery of superoxide and an enzyme that attenuated cellular levels of this free radical (4,5). In the intervening years, free radicals have been recognized as common intermediates in cellular metabolism (6,7), found to play an essential role in host immune response (8) and demonstrated to regulate many essential physiologic functions (9).

Keywords

Free Radical Electron Paramagnetic Resonance Electron Paramagnetic Resonance Spectrum Electron Paramagnetic Resonance Signal Spin Trap 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

References

  1. 1.
    Gilbert, D. L. (1981) Perspective on the History of Oxygen and Life, in Oxygen and Living Processes. An Interdisciplinary Approach (Gilbert, D. L., ed.), Springer-Verlag, NY, pp 1–43.Google Scholar
  2. 2.
    Grubbé E. H. (1933) Priority in the therapeutic use of X-rays. Radiology 21, 156–162.Google Scholar
  3. 3.
    Gerschman, R., Gilbert, D. L., Nye, S. W., Dwyer, P., and Fenn, W. O. (1954) Oxygen poisoning and x-irradiation: a mechanism in common. Science 119, 623–626.PubMedCrossRefGoogle Scholar
  4. 4.
    McCord, J. M and Fridovich, I. (1968) The reduction of cytochrome c by milk xanthine oxidase. J Biol. Chem. 243, 5753–5760.PubMedGoogle Scholar
  5. 5.
    McCord, J. M. and Fridovich, I. (1969) Superoxide dismutase: an enzymic function for erythrocuprein (hemocuprem). J. Biol. Chem. 244, 6049–6055.PubMedGoogle Scholar
  6. 6.
    Fridovich, I. (1978) The biology of oxygen radicals. Science 201, 875–880PubMedCrossRefGoogle Scholar
  7. 7.
    Guengench, F. P. and Macdonald, T. L. (1984) Chemical mechanisms of catalysis by cytochrome P-450: a unified view. Acc. Chem. Res. 17, 9–16.CrossRefGoogle Scholar
  8. 8.
    Babior, B. M., Kipnes, R. S., and Curnutte, J. T. (1973) Biological defense mechanisms: the production by leukocytes of superoxide, a potential bactericidal agent. J. Clin. Invest. 52, 741–744PubMedCrossRefGoogle Scholar
  9. 9.
    Moncada, S. and Higgs, A. (1993) The L-arginine-nitric oxide pathway. N Engl J. Med. 329, 2002–2012.PubMedCrossRefGoogle Scholar
  10. 10.
    Janzen, E. G. and Blackburn, B. J. (1968) Detection and identification of shortlived free radicals by an electron spin resonance trapping technique. J. Am Chem Soc 90, 5909–5910CrossRefGoogle Scholar
  11. 11.
    Mackor, A., Wajer, Th. A. J. W., and de Boer, Th. J. (1967) C-Nitroso compounds Part III Alkoxy-alkyl-nitroxides as intermediates in the reaction of alkoxyl-radicals with nitroso compounds. Tetrahedron Lett. 385–390.Google Scholar
  12. 12.
    Iwamura, M. and Inamoto, N. (1970) Reactions of nitrones with free radicals. II Formation of nitroxides. Bull. Chem. Soc. Japan 43, 860–863CrossRefGoogle Scholar
  13. 13.
    Janzen, E. G. (1971) Spin trapping. Acct. Chem. Res 4, 31–40.CrossRefGoogle Scholar
  14. 14.
    Finkelstein, E., Rosen, G. M., and Rauckman, E. J. (1980) Spin trapping of superoxide and hydroxyl radical, practical aspects. Arch. Biochem. Biophys. 200, 1–16.PubMedCrossRefGoogle Scholar
  15. 15.
    Janzen, E. G. (1980) A critical review of spin trapping in biological systems, in Free Radicals in Biology, (Pryor, W. A., ed), vol 4, Academic Press, NY, pp 116–154Google Scholar
  16. 16.
    Halpern, H. J., Spencer, D. P, vanPolen, J., Bowman, M. K., Nelson, A. C., Dowey, E. M., and Teicher, B. A (1989) Imaging radio frequency electron-spinresonance spectrometer with high resolution and sensitivity for in vivo measurements. Rev. Sci. Instrum 60, 1040–1050CrossRefGoogle Scholar
  17. 17.
    Lai, C.-S. and Komarov, A. M. (1994) Spin trapping of nitric oxide produced in vivo in septic-shock in mice. FEBS Letts. 345, 120–124CrossRefGoogle Scholar
  18. 18.
    Halpern, H. J., Yu, C., Barth, E., Penc, M., and Rosen, G. M. (1995) In situ detection, by spin trapping of hydroxyl radical markers produced from ionizing radiation in the tumor of a living mouse. Proc. Natl Acad Sci USA 92, 796–800PubMedCrossRefGoogle Scholar
  19. 19.
    Jiang, J. J., Liu, K. J., Shi, X., and Swartz, H. M. (1995) Detection of short-lived free radicals by low-frequency electron paramagnetic resonance spin trapping in whole living animals. Arch. Biochem. Biophys. 319, 570–573.PubMedCrossRefGoogle Scholar
  20. 20.
    Poyer, J. L. and McCay, P. B. (1971) Reduced triphosphopyndine nucleotide oxidase-catalyzed alterations of membrane phospholipids. IV: dependence on Fe+3. J. Biol. Chem. 246, 263–269.PubMedGoogle Scholar
  21. 21.
    Gutteridge, J. M. C. (1987) A method for removal of trace iron contamination from biological buffers. FEBS Lett 214, 362–364.PubMedCrossRefGoogle Scholar
  22. 22.
    Buettner, G. R. (1988) In the absence of catalytic metals ascorbate does not autoxidize at pH 7: ascorbate as a test for catalytic metals. J. Biochem. Biophys Methods 16, 27–40PubMedCrossRefGoogle Scholar
  23. 23.
    Buettner, G. R., Oberley, L. W., and Leuthauser, S. W. H. C. (1978) The effect of iron on the distribution of superoxide and hydroxyl radicals as seen by spin trapping and on the superoxide dismutase assay. Photochem. Photobiol. 28, 693–695.PubMedCrossRefGoogle Scholar
  24. 24.
    Bottomley, P. A., and Andrew, E. R. (1978) RF filed penetration, phase shift, and power dissipation in biological tissues: implications for NMR imaging. Phys. Med. Biol 23, 630–643.PubMedCrossRefGoogle Scholar
  25. 25.
    Johnson, C. C. and Guy, A. W. (1972) Nonionizing electromagnetic wave effects in biological materials and systems. IEEE 60, 692–718.CrossRefGoogle Scholar
  26. 26.
    Roschmann, P. (1987) Radiofrequency penetration and absorption in the human body: limitations to high-field whole-body nuclear magnetic resonance imaging. Med. Phys 14, 922–928PubMedCrossRefGoogle Scholar
  27. 27.
    Halpern, H. J., Pou, S., Peric, M., Yu, C., Barth, E., and Rosen, G. M (1993) Detection and imaging of oxygen-centered free radicals with low-frequency electron paramagnetic resonance and signal-enhancing deuterium containing spin traps. J Am. Chem Soc. 115, 218–223CrossRefGoogle Scholar
  28. 28.
    Pou, S, Cohen, M. S., Britigan, B. E., and Rosen, G. M. (1989) Spin trapping and human neutrophils: Limits of detection of hydroxyl radica. J. Biol Chem. 264, 12299–12302.PubMedGoogle Scholar
  29. 29.
    Pou, S., Rosen, G. M., Wu, Y., and Keana, J. F. W. (1990) Synthesis of deuterium-and 15N-containing pyrroline 1-oxides: a spin trapping study. J Org. Chem 55, 4438–4443.CrossRefGoogle Scholar
  30. 30.
    Pou, S., Ramos, C. L., Gladwell, T., Renks, E., Centra, M., Young, D., Cohen, M. S, and Rosen, G. M. (1994) A kinetic approach to the selection of a sensitive spin trapping system for the detection of hydroxyl radical. Anal. Biochem. 217, 76–83PubMedCrossRefGoogle Scholar
  31. 31.
    Ramos, C. L., Pou, S., Britigan, B. E., Cohen, M. S., and Rosen, G. M. (1992) Spin trapping evidence for myeloperoxidase-dependent hydroxyl radical formation by human neutrophils and monocytes. J. Biol. Chem 267, 8307–8312PubMedGoogle Scholar

Copyright information

© Humana Press Inc., Totowa, NJ 1998

Authors and Affiliations

  • Gerald M. Rosen
    • 1
  • Sovitj Pou
    • 2
  • Howard J. Halpern
    • 2
  1. 1.Pharmaceutical Sciences Department, Pharmacology and Toxicology Program, School of PharmacyUniversity of Maryland at Baltimore
  2. 2.Department of Pharmacology and Toxicology, School of PharmacologyUniversity of Maryland at Baltimore

Personalised recommendations