Abstract
Cellular redox environment is a critical determinant of stress-induced cellular responses and the progression of disease (1). Under normal (nonstress) conditions, the cell maintains a strong reducing environment that favors reductive over highly compartmentalized oxidative biochemistry. Exposure of cellular macromolecules to reactive oxygen (ROS) and reactive nitrogen species (RNS) is tightly controlled. Environmental stress can shift the redox balance away from reductive biochemistry however, promoting transition metal activation, and nonprogrammed oxidative and/or nitrosative reactions. Metalcatalyzed oxidative and nitrosative stress have been implicated in the etiology of numerous clinical disorders including inflammation, ischemia-reperfusion injury, rheumatoid arthritis, and aging (1).
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Schafer, F. Q. and Beuttner, G. R. (2001) Redox state of the cell as viewed through the glutathione disulfide/glutathione couple. Free Radical Bio. Med. 30, 1191–1212.
Hall, D. M., Buettner, G. R., Matthis, R. D., and Gisolfi, C. V. (1994) Hyperthermia stimulates nitric oxide formation: electron paramagnetic resonance detection of ·NO-heme in blood. J. Appl. Physiol. 77(2), 548–553.
Buettner, G. R., Scott, B. D., Kerber, R. E., and Mugge, A. (1991) Free radicals from plastic syringes. Free Radical Biol. Med. 11, 69–70.
Kregel, K. C., Wall, P. T., and Gisolfi, C. V. (1988) Peripheral vascular responses to hyperthermia in the rat. J. Appl. Physiol. 64(6), 2582–2588.
Westenberger, U., Thanner, S., Ruf, H. H., Gersonde, K., Sutter G., and Trentz, O. (1990) Formation of free radicals and nitric oxide derivative of hemoglobin in rats during endotoxin shock. Free Radical Res. Commun. 11, 167–178.
Chamulitrat, W., Skrepnik, N. V., and Spitzer, J. J. (1996) Nitrosyl complex formation during endotoxin-induced injury in the rat small intestine. Shock 5(1), 59–65.
Kozlov, A. V., Yegorov, D. U., Vladimirov, Y. A., and Azizova, O. A. (1992) Intracellular free iron in liver tissue and liver homogenate. Free Rad. Biol. Med. 13, 9–16.
Hall, D. M., Oberley, T. D., Moseley, P. M., Buettner, G. R., Oberley, L. W., Weindruch, R. H., and Kregel, K. C. (2000) Caloric restriction improves thermo-tolerance and reduces hyperthermia-induced cellular damage in old rats. FASEB J. (In Press.)
Lancaster, J. R., Jr. and Hibbs, J. B., Jr. (1990) EPR demonstration of iron-nitrosyl complex formation by cytotoxic activated macrophages. Proc. Natl. Acad. Sci. USA 87, 1223–1227.
Stamler, J. S., Singel, D. J., and Loscalzo, J. (1992) Biochemistry of ·NO and its redox activated forms. Science 258, 1898.
Henry, Y., Lepoivre, M., Drapier, J., Ducrocq, C., Boucher, J., and Guissani, A. (1993) EPR characterization of molecular targets for ·NO in mammalian cells and organelles. FASEB J. 7(12), 1124–1134.
Henry, Y., Ducrocq, C., Drapier, J.-C., Servant, D., Pellat, C., and Guissani, A. (1991) Nitric oxide, a biological effector. EPR detection of nitrosyl-iron-protein complexes in whole cells. Eur. Biophys. J. 20(1), 1–15.
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© 2002 Humana Press Inc.
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Hall, D.M., Buettner, G.R. (2002). In Vivo Detection of Transition Metals and Nitrosyl-Heme Complexes Using Ex Vivo Electron Paramagnetic Resonance Spectroscopy. In: Armstrong, D. (eds) Oxidants and Antioxidants. Methods in Molecular Biology™, vol 196. Humana Press. https://doi.org/10.1385/1-59259-274-0:211
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DOI: https://doi.org/10.1385/1-59259-274-0:211
Publisher Name: Humana Press
Print ISBN: 978-0-89603-851-6
Online ISBN: 978-1-59259-274-6
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