Does the cellular labile iron pool participate in the oxidation of 2′,7′-dichlorodihydrofluorescein?

References

• Cathcart R, Schwiers E, Ames BN. Detection of picomole levels of hydroperoxides using a fluorescent dichlorofluorescein assay. Anal Biochem 1983; 134: 111–116
   PubMed Web of Science ®Google Scholar
• Crow JP. Dichlorodihydrofluorescein and dihydrorhodamine 123 are sensitive indicators of peroxynitrite in vitro: Implications for intracellular measurement of reactive nitrogen and oxygen species. Nitric Oxide 1997; 1: 145–157
   PubMed Web of Science ®Google Scholar
• Hempel SL, Buettner GR, O'Malley YQ, Wessels DA, Flaherty DM. Dihydrofluorescein diacetate is superior for detecting intracellular oxidants: Comparison with 2′,7′-dichlorodihydrofluorescein diacetate, 5(and 6)-carboxy-2′,7′-dichlorodihydrofluorescein diacetate, and dihydrorhodamine 123. Free Radic Biol Med 1999; 27: 146–159
   PubMed Web of Science ®Google Scholar
• Keller A, Mohamed A, Drose S, Brandt U, Fleming I, Brandes RP. Analysis of dichlorodihydrofluorescein and dihydrocalcein as probes for the detection of intracellular reactive oxygen species. Free Radic Res 2004; 38: 1257–1267
   PubMed Web of Science ®Google Scholar
• Bartosz G. Limitations and pitfalls of the use of spectroscopic probes for the detection of reactive oxygen species. Clin Chim Acta 2006; 368: 53–76
   PubMed Web of Science ®Google Scholar
• Kooy NW, Royall JA, Ischiropoulos H. Oxidation of 2′,7′-dichlorofluorescin by peroxynitrite. Free Radic Res 1997; 27: 245–254
   PubMed Web of Science ®Google Scholar
• Glebska J, Koppenol WH. Peroxynitrite-mediated oxidation of dichlorodihydrofluorescein and dihydrorhodamine. Free Radic Biol Med 2003; 35: 676–682
   PubMed Web of Science ®Google Scholar
• Burkitt MJ, Wardman P. Cytochrome c is a potent catalyst of dichlorofluorescin oxidation: Implications for the role of reactive oxygen species in apoptosis. Biochem Biophys Res Commun 2001; 23: 329–333
   Google Scholar
• Lawrence A, Jones CM, Wardman P, Burkitt MJ. Evidence for the role of a peroxidase compound I-type intermediate in the oxidation of glutathione, NADH, ascorbate, and dichlorofluorescin by cytochrome c/H2O2. Implications for oxidative stress during apoptosis. J Biol Chem 2003; 278: 29410–29419
   PubMedGoogle Scholar
• Kooy NW, Royall JA. Agonist-induced peroxynitrite production from endothelial cells. Arch Biochem Biophys 1994; 310: 352–359
   PubMed Web of Science ®Google Scholar
• Jakubowski W, Bartosz G. 2,7-Dichlorofluorescin oxidation and reactive oxygen species: What does it measure?. Cell Biol Int 2000; 24: 757–760
   PubMed Web of Science ®Google Scholar
• Cabantchik ZI, Kakhlon O, Epsztejn S, Zanninelli G, Breuer W. Intracellular and extracellular labile iron pools. Adv Exp Med Biol 2002; 509: 55–75
   PubMedGoogle Scholar
• Kakhlon O, Cabantchik ZI. The labile iron pool: Characterization, measurement, and participation in cellular processes. Free Radic Biol Med 2002; 33: 1037–1046
   PubMed Web of Science ®Google Scholar
• Kruszewski M. Labile iron pool: The main determinant of cellular response to oxidative stress. Mutat Res 2003; 531: 81–92
   PubMed Web of Science ®Google Scholar
• Petrat F, de Groot H, Rauen U. Determination of the chelatable iron pool of single intact cells by laser scanning microscopy. Arch Biochem Biophys 2000; 376: 74–81
   PubMed Web of Science ®Google Scholar
• Petrat F, de Groot H, Sustmann R, Rauen U. The chelatable iron pool in living cells: A methodically defined quantity. Biol Chem 2002; 383: 489–502
   PubMed Web of Science ®Google Scholar
• Buss JL, Neuzil J, Gellert N, Weber C, Ponka P. Pyridoxal isonicotinoyl hydrazone analogs induce apoptosis in hematopoietic cells due to their iron-chelating properties. Biochem Pharmacol 2003; 65: 161–172
   Google Scholar
• Buss JL, Neuzil J, Ponka P. Oxidative stress mediates toxicity of pyridoxal isonicotinoyl hydrazone analogs. Arch Biochem Biophys 2004; 421: 1–9
   PubMed Web of Science ®Google Scholar
• Hermes-Lima M, Santos NC, Yan J, Andrews M, Schulman HM, Ponka P. EPR spin trapping and 2-deoxyribose degradation studies of the effect of pyridoxal isonicotinoyl hydrazone (PIH) on √OH formation by the Fenton reaction. Biochim Biophys Acta 1999; 1426: 475–482
   PubMed Web of Science ®Google Scholar
• Mosmann T. Rapid colorimetric assay for cellular growth and survival: Application to proliferation and cytotoxicity assays. J Immunol Methods 1983; 65: 55–63
   PubMed Web of Science ®Google Scholar
• Urbanski NK, Beresewicz A. Generation of √OH initiated by interaction of Fe2+ and Cu+ with dioxygen; comparison with the Fenton chemistry. Acta Biochim Pol 2000; 47: 951–962
   PubMed Web of Science ®Google Scholar
• Qian SY, Buettner GR. Iron and dioxygen chemistry is an important route to initiation of biological free radical oxidations: An electron paramagnetic resonance spin trapping study. Free Radic Biol Med 1999; 26: 1447–1456
   PubMed Web of Science ®Google Scholar
• Jakubowski W, Bartosz G. Estimation of oxidative stress in Saccharomyces cerevisae with fluorescent probes. Int J Biochem Cell Biol 1997; 29: 1297–1301
   PubMed Web of Science ®Google Scholar
• Kim YM, Lim JM, Kim BC, Han S. Cu,Zn-superoxide dismutase is an intracellular catalyst for the H2O2-dependent oxidation of dichlorodihydrofluorescein. Mol Cells 2006; 21: 161–165
   PubMed Web of Science ®Google Scholar
• Sankarapandi S, Zweier JL. Bicarbonate is required for the peroxidase function of Cu, Zn-superoxide dismutase at physiological pH. J Biol Chem 1999; 274: 1226–1232
   PubMed Web of Science ®Google Scholar
• Zhang H, Joseph J, Gurney M, Becker D, Kalyanaraman B. Bicarbonate enhances peroxidase activity of Cu, Zn-superoxide dismutase. Role of carbonate anion radical and scavenging of carbonate anion radical by metalloporphyrin antioxidant enzyme mimetics. J Biol Chem 2002; 277: 1013–1020
   PubMed Web of Science ®Google Scholar
• Lipinski P, Drapier JC, Oliveira L, Retmanska H, Sochanowicz B, Kruszewski M. Intracellular iron status as a hallmark of mammalian cell susceptibility to oxidative stress: A study of L5178Y mouse lymphoma cell lines differentially sensitive to H2O2. Blood 2000; 95: 2960–2966
   PubMed Web of Science ®Google Scholar
• Epsztejn S, Kakhlon O, Glickstein H, Breuer W, Cabantchik I. Fluorescence analysis of the labile iron pool of mammalian cells. Anal Biochem 1997; 248: 31–40
   PubMed Web of Science ®Google Scholar
• Wrona M, Patel K, Wardman P. Reactivity of 2′,7′-dichlorodihydrofluorescein and dihydrorhodamine 123 and their oxidized forms toward carbonate, nitrogen dioxide, and hydroxyl radicals. Free Radic Biol Med 2005; 38: 262–270
   PubMed Web of Science ®Google Scholar
• Dubois J-E, Fakhrayan H, Doucet J-P, El Hage Chahine J-M. Kinetic and thermodynamic study of complex formation between iron(II) and pyridoxal isonicotinoylhydrazone and other synthetic chelating agents. Inorg Chem 1992; 31: 853–859
   Web of Science ®Google Scholar
• Gackowski D, Kruszewski M, Bartlomiejczyk T, Jawien A, Ciecierski M, Olinski R. The level of 8-oxo-7,8-dihydro-2′-deoxyguanosine is positively correlated with the size of the labile iron pool in human lymphocytes. J Biol Inorg Chem 2002; 7: 548–550
   PubMedGoogle Scholar
• Kruszewski M. The role of labile iron pool in cardiovascular diseases. Acta Biochim Pol 2004; 51: 471–480
   PubMed Web of Science ®Google Scholar