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Volumn 44, Issue 5, 2008, Pages 835-846

Cytochrome c-mediated oxidation of hydroethidine and mito-hydroethidine in mitochondria: Identification of homo- and heterodimers

Author keywords

Cytochrome c; Dimerization; HPLC; Hydroethidine; Mitochondria; Superoxide

Indexed keywords

CYTOCHROME C; HETERODIMER; HYDROETHIDINE; SUPEROXIDE;

EID: 39149083084     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2007.11.013     Document Type: Article
Times cited : (95)

References (24)
  • 1
    • 0038368985 scopus 로고    scopus 로고
    • Superoxide reacts with hydroethidine but forms a fluorescent product that is distinctly different from ethidium: potential implications in intracellular fluorescence detection of superoxide
    • Zhao H., Kalivendi S., Zhang H., Joseph J., Nithipatikom K., Vasquez-Vivar J., and Kalyanaraman B. Superoxide reacts with hydroethidine but forms a fluorescent product that is distinctly different from ethidium: potential implications in intracellular fluorescence detection of superoxide. Free Radic. Biol. Med. 34 (2003) 1359-1368
    • (2003) Free Radic. Biol. Med. , vol.34 , pp. 1359-1368
    • Zhao, H.1    Kalivendi, S.2    Zhang, H.3    Joseph, J.4    Nithipatikom, K.5    Vasquez-Vivar, J.6    Kalyanaraman, B.7
  • 3
    • 33751438500 scopus 로고    scopus 로고
    • Pulse radiolysis and steady-state analyses of the reaction between hydroethidine and superoxide and other oxidants
    • Zielonka J., Sarna T., Roberts J.E., Wishart J.F., and Kalyanaraman B. Pulse radiolysis and steady-state analyses of the reaction between hydroethidine and superoxide and other oxidants. Arch. Biochem. Biophys. 456 (2006) 39-47
    • (2006) Arch. Biochem. Biophys. , vol.456 , pp. 39-47
    • Zielonka, J.1    Sarna, T.2    Roberts, J.E.3    Wishart, J.F.4    Kalyanaraman, B.5
  • 5
    • 4544363652 scopus 로고    scopus 로고
    • Detection of intracellular superoxide formation in endothelial cells and intact tissues using dihydroethidium and an HPLC-based assay
    • Fink B., Laude K., McCann L., Doughan A., Harrison D.G., and Dikalov S. Detection of intracellular superoxide formation in endothelial cells and intact tissues using dihydroethidium and an HPLC-based assay. Am. J. Physiol., Cell Physiol. 287 (2004) C895-C902
    • (2004) Am. J. Physiol., Cell Physiol. , vol.287
    • Fink, B.1    Laude, K.2    McCann, L.3    Doughan, A.4    Harrison, D.G.5    Dikalov, S.6
  • 6
    • 33748291680 scopus 로고    scopus 로고
    • The confounding effects of light, sonication, and Mn(III)TBAP on quantitation of superoxide using hydroethidine
    • Zielonka J., Vasquez-Vivar J., and Kalyanaraman B. The confounding effects of light, sonication, and Mn(III)TBAP on quantitation of superoxide using hydroethidine. Free Radic. Biol. Med. 41 (2006) 1050-1057
    • (2006) Free Radic. Biol. Med. , vol.41 , pp. 1050-1057
    • Zielonka, J.1    Vasquez-Vivar, J.2    Kalyanaraman, B.3
  • 7
    • 0032211437 scopus 로고    scopus 로고
    • Critical evaluation of the use of hydroethidine as a measure of superoxide anion radical
    • Benov L., Sztejnberg L., and Fridovich I. Critical evaluation of the use of hydroethidine as a measure of superoxide anion radical. Free Radic. Biol. Med. 25 (1998) 826-831
    • (1998) Free Radic. Biol. Med. , vol.25 , pp. 826-831
    • Benov, L.1    Sztejnberg, L.2    Fridovich, I.3
  • 8
    • 8444228495 scopus 로고    scopus 로고
    • The fluorescence detection of superoxide radical using hydroethidine could be complicated by the presence of heme proteins
    • Papapostolou I., Patsoukis N., and Georgiou C.D. The fluorescence detection of superoxide radical using hydroethidine could be complicated by the presence of heme proteins. Anal. Biochem. 332 (2004) 290-298
    • (2004) Anal. Biochem. , vol.332 , pp. 290-298
    • Papapostolou, I.1    Patsoukis, N.2    Georgiou, C.D.3
  • 10
    • 34247107954 scopus 로고    scopus 로고
    • Mitochondrial superoxide radicals mediate programmed cell death in Trypanosoma cruzi: cytoprotective action of mitochondrial iron superoxide dismutase overexpression
    • Piacenza L., Irigoin F., Alvarez M.N., Peluffo G., Taylor M.C., Kelly J.M., Wilkinson S.R., and Radi R. Mitochondrial superoxide radicals mediate programmed cell death in Trypanosoma cruzi: cytoprotective action of mitochondrial iron superoxide dismutase overexpression. Biochem. J. 403 (2007) 323-334
    • (2007) Biochem. J. , vol.403 , pp. 323-334
    • Piacenza, L.1    Irigoin, F.2    Alvarez, M.N.3    Peluffo, G.4    Taylor, M.C.5    Kelly, J.M.6    Wilkinson, S.R.7    Radi, R.8
  • 12
    • 0030939089 scopus 로고    scopus 로고
    • On the virtual existence of superoxide anions in mitochondria: thoughts regarding its role in pathophysiology
    • Forman H.J., and Azzi A. On the virtual existence of superoxide anions in mitochondria: thoughts regarding its role in pathophysiology. FASEB J. 11 (1997) 374-375
    • (1997) FASEB J. , vol.11 , pp. 374-375
    • Forman, H.J.1    Azzi, A.2
  • 13
    • 0023889649 scopus 로고
    • Multidimensional diffusion modes and collision frequencies of cytochrome c with its redox partners
    • Gupte S.S., and Hackenbrock C.R. Multidimensional diffusion modes and collision frequencies of cytochrome c with its redox partners. J. Biol. Chem. 263 (1988) 5241-5247
    • (1988) J. Biol. Chem. , vol.263 , pp. 5241-5247
    • Gupte, S.S.1    Hackenbrock, C.R.2
  • 14
    • 33644628456 scopus 로고    scopus 로고
    • Mechanistic similarities between oxidation of hydroethidine by Fremy's salt and superoxide: stopped-flow optical and EPR studies
    • Zielonka J., Zhao H., Xu Y., and Kalyanaraman B. Mechanistic similarities between oxidation of hydroethidine by Fremy's salt and superoxide: stopped-flow optical and EPR studies. Free Radic. Biol. Med. 39 (2005) 853-863
    • (2005) Free Radic. Biol. Med. , vol.39 , pp. 853-863
    • Zielonka, J.1    Zhao, H.2    Xu, Y.3    Kalyanaraman, B.4
  • 15
    • 0018908672 scopus 로고
    • Activation of aflatoxin B1 by a mono-oxygenase system localized in rat liver mitochondria
    • Niranjan B.G., and Avadhani N.G. Activation of aflatoxin B1 by a mono-oxygenase system localized in rat liver mitochondria. J. Biol. Chem. 255 (1980) 6575-6578
    • (1980) J. Biol. Chem. , vol.255 , pp. 6575-6578
    • Niranjan, B.G.1    Avadhani, N.G.2
  • 16
    • 0001497483 scopus 로고
    • The reversible removal of cytochrome c from mitochondria
    • Jacobs E.E., and Sanadi D.R. The reversible removal of cytochrome c from mitochondria. J. Biol. Chem. 235 (1960) 531-534
    • (1960) J. Biol. Chem. , vol.235 , pp. 531-534
    • Jacobs, E.E.1    Sanadi, D.R.2
  • 17
    • 0036119296 scopus 로고    scopus 로고
    • Mitochondrial superoxide anion production and release into intermembrane space
    • Han D., Antunes F., Daneri F., and Cadenas E. Mitochondrial superoxide anion production and release into intermembrane space. Methods Enzymol. 349 (2002) 271-280
    • (2002) Methods Enzymol. , vol.349 , pp. 271-280
    • Han, D.1    Antunes, F.2    Daneri, F.3    Cadenas, E.4
  • 18
    • 0035231595 scopus 로고    scopus 로고
    • Assaying mitochondrial respiratory complex activity in mitochondria isolated from human cells and tissues
    • Birch-Machin M.A., and Turnbull D.M. Assaying mitochondrial respiratory complex activity in mitochondria isolated from human cells and tissues. Methods Cell Biol. 65 (2001) 97-117
    • (2001) Methods Cell Biol. , vol.65 , pp. 97-117
    • Birch-Machin, M.A.1    Turnbull, D.M.2
  • 19
    • 0043032860 scopus 로고    scopus 로고
    • 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
    • Lawrence A., Jones C.M., Wardman P., and Burkitt M.J. 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. 278 (2003) 29410-29419
    • (2003) J. Biol. Chem. , vol.278 , pp. 29410-29419
    • Lawrence, A.1    Jones, C.M.2    Wardman, P.3    Burkitt, M.J.4
  • 21
    • 0030761155 scopus 로고    scopus 로고
    • Mitochondrial membrane potential and hydroethidine-monitored superoxide generation in cultured cerebellar granule cells
    • Budd S.L., Castilho R.F., and Nicholls D.G. Mitochondrial membrane potential and hydroethidine-monitored superoxide generation in cultured cerebellar granule cells. FEBS Lett. 415 (1997) 21-24
    • (1997) FEBS Lett. , vol.415 , pp. 21-24
    • Budd, S.L.1    Castilho, R.F.2    Nicholls, D.G.3
  • 22
    • 33847071146 scopus 로고    scopus 로고
    • Targeting antioxidants to mitochondria by conjugation to lipophilic cations
    • Murphy M.P., and Smith R.A.J. Targeting antioxidants to mitochondria by conjugation to lipophilic cations. Annu. Rev. Pharmacol. Toxicol. 47 (2007) 629-656
    • (2007) Annu. Rev. Pharmacol. Toxicol. , vol.47 , pp. 629-656
    • Murphy, M.P.1    Smith, R.A.J.2
  • 23
    • 0037428060 scopus 로고    scopus 로고
    • Oxidative stress-induced iron signaling is responsible for peroxide-dependent oxidation of dichlorodihydrofluorescein in endothelial cells: role of transferrin receptor-dependent iron uptake in apoptosis
    • Tampo Y., Kotamraju S., Chitambar C.R., Kalivendi S.V., Keszler A., Joseph J., and Kalyanaraman B. Oxidative stress-induced iron signaling is responsible for peroxide-dependent oxidation of dichlorodihydrofluorescein in endothelial cells: role of transferrin receptor-dependent iron uptake in apoptosis. Circ. Res. 92 (2003) 56-63
    • (2003) Circ. Res. , vol.92 , pp. 56-63
    • Tampo, Y.1    Kotamraju, S.2    Chitambar, C.R.3    Kalivendi, S.V.4    Keszler, A.5    Joseph, J.6    Kalyanaraman, B.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.