In vivo detection of intrinsic reactive oxygen species using acyl-protected hydroxylamine in puromycin nephrosis

References

• Ricardo SD, Bertram JF, Ryan GB. Reactive oxygen species in puromycin aminonucleoside nephrosis: in vitro studies. Kidney Int 1994; 45: 1057–1069
   PubMed Web of Science ®Google Scholar
• Gwinner W, Landmesser U, Brandes RP, Kubat B, Plasger J, Eberhard O, Koch KM, Olbricht CJ. Reactive oxygen species and antioxidant defense in puromycin aminonucleoside glomerulopathy. J Am Soc Nephrol 1997; 8: 1722–1731
   PubMed Web of Science ®Google Scholar
• Ricardo SD, Bertram JF, Ryan GB. Antioxidants protect podocyte foot processes in puromycin aminonucleoside-treated rats. J Am Soc Nephrol 1994; 4: 1974–1986
   PubMed Web of Science ®Google Scholar
• Diamond JR, Bonventre JV, Karnovsky MJ. A role for oxygen free radicals in aminonucleoside nephrosis. Kidney Int 1986; 29: 478–483
   PubMed Web of Science ®Google Scholar
• Nosaka K, Takahashi T, Nishi T, Imaki H, Suzuki T, Suzuki K, Kurokawa K, Endou H. An adenosine deaminase inhibitor prevents puromycin aminonucleoside nephrotoxicity. Free Radic Biol Med 1997; 22: 597–605
   PubMed Web of Science ®Google Scholar
• Pedraza-Chaverri J, Granados-Silvestre MD, Medina-Campos ON, Hernandez-Pando R. Effect of the in vivo catalase inhibition on aminonucleoside nephrosis. Free Radic Biol Med 1999; 27: 245–253
   PubMed Web of Science ®Google Scholar
• Ueda A, Nagase S, Yokoyama H, Tada M, Ohya H, Kamada H, Hirayama A, Koyama A. Identification by an EPR technique of decreased mitochondrial reducing activity in puromycin aminonucleoside-induced nephrosis. Free Radic Biol Med 2002; 33: 1082–1088
   PubMed Web of Science ®Google Scholar
• Halliwell B, Gutteridge JMC. The chemistry of free radicals and related ‘reactive species’. Free radicals in biology and medicine3rd ed., B Halliwell, JMC Gutteridge. Oxford University Press, London 1999; 36–104
   Google Scholar
• Kasparova S, Brezova V, Valko M, Horecky J, Mlynarik V, Liptaj T, Vancova O, Ulicna O, Dobrota D. Study of the oxidative stress in a rat model of chronic brain hypoperfusion. Neurochem Int 2005; 46: 601–611
   PubMed Web of Science ®Google Scholar
• Kozlov AV, Szalay L, Umar F, Fink B, Kropik K, Nohl H, Redl H, Bahrami S. Epr analysis reveals three tissues responding to endotoxin by increased formation of reactive oxygen and nitrogen species. Free Radic Biol Med 2003; 34: 1555–1562
   PubMed Web of Science ®Google Scholar
• Kleschyov AL, Mollnau H, Oelze M, Meinertz T, Huang Y, Harrison DG, Munzel T. Spin trapping of vascular nitric oxide using colloid Fe(II)-diethyldithiocarbamate. Biochem Biophys Res Commun 2000; 275: 672–677
   PubMed Web of Science ®Google Scholar
• Itoh O, Aoyama M, Yokoyama H, Obara H, Ohya-Nishiguchi H, Kamada H. Sensitive ESR determination of intracellular oxidative stress by using acyl-protected hydrxylamine as new spin reagents. Chem Lett 2000; 304–305
   Web of Science ®Google Scholar
• Yokoyama H, Ogata T, Tsuchihashi N, Hiramatsu M, Mori N. A spatiotemporal study on the distribution of intraperitoneally injected nitroxide radical in the rat head using an in vivo ESR imaging system. Magn Reson Imaging 1992; 10: 21–27
   Google Scholar
• Hirata H, Iwai H, Ono M. Analysis of a flexible surface-coil-type resonator for magnetic resonance measurements. Rev Sci Instrum 1995; 66: 4529–4534
   Web of Science ®Google Scholar
• Lin Y, Yokoyama H, Ishida S, Tsuchihashi N, Ogata T. In vivo electron spin resonance analysis of nitroxide radicals injected into a rat by a flexible surface-coil-type resonator as an endoscope- or a stethoscope-like device. Magn Reson Mater Phys Biol Med 1997; 5: 99–103
   Google Scholar
• Tada M, Yokoyama H, Toyoda Y, Ohya H, Itoh T, Ogata T. Surface-coil-type resonators for in vivo temporal ESR measurements in different organs of nitroxide-treated rats. Appl Magn Reson 2000; 18: 575–582
   Web of Science ®Google Scholar
• Aoyagi K, Akiyama K, Tomida C, Gotoh M, Hirayama A, Takemura K, Ueda A, Nagase S, Koyama A, Narita M. Imaging of hydroperoxides in a rat glomerulus stimulated by puromycin aminonucleoside. Kidney Int Suppl 1999; 71: S153–S155
   Google Scholar
• Dikalov S, Skatchkov M, Bassenge E. Quantification of peroxinitrite, superoxide, and peroxyl radicals by a new spin trap hydroxylamine 1-hydroxyl-2,2,6,6-tetramethyl-4-oxo-piperidine. Biochem Biophys Res Commun 1997; 230: 54–57
   PubMed Web of Science ®Google Scholar
• Boulden BM, Widder JD, Allen JC, Smith DA, Al-Baldawi RN, Harrison DG, Dikalov SI, Jo H, Dudley SC, Jr. Early determinants of H2O2-induced endothelial dysfunction. Free Radic Biol Med 2006; 41: 810–817
   PubMed Web of Science ®Google Scholar
• Hirayama A, Yoh K, Nagase S, Ueda A, Itoh K, Morito N, Hirayama K, Takahashi S, Yamamoto M, Koyama A. EPR imaging of reducing activity in Nrf2 transcriptional factor-deficient mice. Free Radic Biol Med 2003; 34: 1236–1242
   PubMed Web of Science ®Google Scholar
• Hirayama A, Nagase S, Ueda A, Oteki T, Takada K, Obara M, Inoue M, Yoh K, Hirayama K, Koyama A. In vivo imaging of oxidative stress in ischemia-reperfusion renal injury using electron paramagnetic resonance. Am J Physiol Renal Physiol 2005; 288: 597–603
   Web of Science ®Google Scholar
• Oteki T, Nagase S, Yokoyama H, Ohya H, Akatsuka T, Tada M, Ueda A, Hirayama A, Koyama A. Evaluation of adriamycin nephropathy by an in vivo electron paramagnetic resonance. Biochem Biophys Res Commun 2005; 332: 326–331
   PubMed Web of Science ®Google Scholar
• Quintanilha AT, Packer L. Surface localization of sites of reduction of nitoxide spin-labeled molecules in mitochondria. Proc Natl Acad Sci USA 1977; 74: 570–574
   PubMed Web of Science ®Google Scholar
• Chen K, Morse PD, Swartz HM. Kinetics of enzyme-mediated reduction of lipid soluble nitroxide spin labels by living cells. Biochim Biophys Acta 1988; 943: 477–484
   PubMed Web of Science ®Google Scholar
• Rosen GM, Rauckman EJ. Formation and reduction of a nitroxide radicals by liver microsomes. Biochem Pharmacol 1977; 26: 675–678
   PubMed Web of Science ®Google Scholar
• Iannone A, Bini A, Swartz HM, Tomasi A, Vannini V. Metabolism in rat liver microsomes of the nitroxide spin probe tempol. Biochem Pharmacol 1989; 38: 2581–2586
   PubMed Web of Science ®Google Scholar
• Couet WR, Brasch RC, Sosnovsky G, Tozer TN. Factors affecting nitroxide reduction in ascorbate solution and tissue homogenates. Magn Reson Imaging 1986; 3: 83–88
   Google Scholar
• Iannone A, Tomasi A, Vannini V, Swartz HM. Metabolism of nitroxide spin labels in subcellular fraction of rat liver II. Reduction in the cytosol. Biochim Biophys Acta 1990; 1034: 290–293
   PubMed Web of Science ®Google Scholar
• Yokoyama H, Itoh O, Aoyama M, Obara H, Ohya H, Kamada H. In vivo EPR imaging by using an acyl-protected hydroxylamine to analyze intracerebral oxidative stress in rats after epileptic seizures. Magn Reson Imaging 2000; 18: 875–879
   PubMed Web of Science ®Google Scholar