메뉴 건너뛰기




Volumn 542, Issue , 2014, Pages 243-262

Methods to monitor ROS production by fluorescence microscopy and fluorometry

Author keywords

Cytosol; Hydrogen peroxide; Mitochondria; Reactive oxygen species; Respiratory chain; Superoxide anion

Indexed keywords

CATALASE; COPPER ZINC SUPEROXIDE DISMUTASE; FLUORESCENT DYE; REACTIVE OXYGEN METABOLITE; SULFORHODAMINE B; SUPEROXIDE DISMUTASE; AMPLEX RED REAGENT; ETHIDIUM; FLUORENE DERIVATIVE; HYDROETHIDINE; MITOSOX RED; ORGANOPHOSPHORUS COMPOUND; OXAZINE DERIVATIVE; PHENANTHRIDINE DERIVATIVE; PROTEIN;

EID: 84901425119     PISSN: 00766879     EISSN: 15577988     Source Type: Book Series    
DOI: 10.1016/B978-0-12-416618-9.00013-3     Document Type: Chapter
Times cited : (246)

References (39)
  • 1
    • 62549102431 scopus 로고    scopus 로고
    • Reactive oxygen species: Destroyers or messengers?
    • G. Bartosz Reactive oxygen species: Destroyers or messengers? Biochemical Pharmacology 77 8 2009 1303 1315
    • (2009) Biochemical Pharmacology , vol.77 , Issue.8 , pp. 1303-1315
    • Bartosz, G.1
  • 2
    • 77952541558 scopus 로고    scopus 로고
    • The sites and topology of mitochondrial superoxide production
    • M.D. Brand The sites and topology of mitochondrial superoxide production Experimental Gerontology 45 2010 466 472
    • (2010) Experimental Gerontology , vol.45 , pp. 466-472
    • Brand, M.D.1
  • 3
    • 84856556021 scopus 로고    scopus 로고
    • There is no evidence that mitochondria are the main source of reactive oxygen species in mammalian cells
    • G.C. Brown, and V. Borutaite There is no evidence that mitochondria are the main source of reactive oxygen species in mammalian cells Mitochondrion 12 1 2011 1 4
    • (2011) Mitochondrion , vol.12 , Issue.1 , pp. 1-4
    • Brown, G.C.1    Borutaite, V.2
  • 5
    • 0033796250 scopus 로고    scopus 로고
    • Mitochondrial free radical generation, oxidative stress, and aging
    • E. Cadenas, and K.J. Davies Mitochondrial free radical generation, oxidative stress, and aging Free Radical Biology & Medicine 29 2000 222 230
    • (2000) Free Radical Biology & Medicine , vol.29 , pp. 222-230
    • Cadenas, E.1    Davies, K.J.2
  • 6
    • 34047219789 scopus 로고    scopus 로고
    • Measurement of reactive oxygen species in cardiovascular studies
    • S. Dikalov, K.K. Griendling, and D.G. Harrison Measurement of reactive oxygen species in cardiovascular studies Hypertension 49 4 2007 717 727
    • (2007) Hypertension , vol.49 , Issue.4 , pp. 717-727
    • Dikalov, S.1    Griendling, K.K.2    Harrison, D.G.3
  • 7
    • 84891778532 scopus 로고    scopus 로고
    • Methods for detection of mitochondrial and cellular reactive oxygen species
    • 10.1089/ars.2012.4886
    • S. Dikalov, and D.G. Harrison Methods for detection of mitochondrial and cellular reactive oxygen species Antioxidants & Redox Signaling 20 2014 372 382 10.1089/ars.2012.4886
    • (2014) Antioxidants & Redox Signaling , vol.20 , pp. 372-382
    • Dikalov, S.1    Harrison, D.G.2
  • 8
    • 0036086130 scopus 로고    scopus 로고
    • Free radicals in the physiological control of cell function
    • W. Dröge Free radicals in the physiological control of cell function Physiological Reviews 82 1 2002 47 95
    • (2002) Physiological Reviews , vol.82 , Issue.1 , pp. 47-95
    • Dröge, W.1
  • 11
    • 2942572700 scopus 로고    scopus 로고
    • Measuring reactive species and oxidative damage in vivo and in cell culture: How should you do it and what do the results mean?
    • B. Halliwell, and M. Whiteman Measuring reactive species and oxidative damage in vivo and in cell culture: How should you do it and what do the results mean? British Journal of Pharmacology 142 2 2004 231 255
    • (2004) British Journal of Pharmacology , vol.142 , Issue.2 , pp. 231-255
    • Halliwell, B.1    Whiteman, M.2
  • 12
    • 79958718704 scopus 로고    scopus 로고
    • Mitochondrial superoxide anion (O(2)(-)) inducible "mev-1" animal models for aging research
    • T. Ishii, M. Miyazawa, P.S. Hartman, and N. Ishii Mitochondrial superoxide anion (O(2)(-)) inducible "mev-1" animal models for aging research BMB Reports 44 5 2011 298 305
    • (2011) BMB Reports , vol.44 , Issue.5 , pp. 298-305
    • Ishii, T.1    Miyazawa, M.2    Hartman, P.S.3    Ishii, N.4
  • 13
    • 11244279161 scopus 로고    scopus 로고
    • A mutation in the SDHC gene of complex II increases oxidative stress, resulting in apoptosis and tumorigenesis
    • T. Ishii, K. Yasuda, A. Akatsuka, O. Hino, P.S. Hartman, and N. Ishii A mutation in the SDHC gene of complex II increases oxidative stress, resulting in apoptosis and tumorigenesis Cancer Research 65 1 2005 203 209
    • (2005) Cancer Research , vol.65 , Issue.1 , pp. 203-209
    • Ishii, T.1    Yasuda, K.2    Akatsuka, A.3    Hino, O.4    Hartman, P.S.5    Ishii, N.6
  • 15
    • 0020586897 scopus 로고
    • Effect of electron transfer inhibitors on superoxide generation in the cytochrome bc1 site of the mitochondrial respiratory chain
    • PubMed PMID: 6301880
    • M. Ksenzenko, A.A. Konstantinov, G.B. Khomutov, A.N. Tikhonov, and E.K. Ruuge Effect of electron transfer inhibitors on superoxide generation in the cytochrome bc1 site of the mitochondrial respiratory chain FEBS Letters 155 1 1983 19 24 PubMed PMID: 6301880
    • (1983) FEBS Letters , vol.155 , Issue.1 , pp. 19-24
    • Ksenzenko, M.1    Konstantinov, A.A.2    Khomutov, G.B.3    Tikhonov, A.N.4    Ruuge, E.K.5
  • 16
    • 44949185670 scopus 로고    scopus 로고
    • Analysis of mitochondrial function in situ in permeabilized muscle fibers, tissues and cells
    • A.V. Kuznetsov, V. Veksler, F.N. Gellerich, V. Saks, R. Margreiter, and W.S. Kunz Analysis of mitochondrial function in situ in permeabilized muscle fibers, tissues and cells Nature Protocols 3 6 2008 965 976
    • (2008) Nature Protocols , vol.3 , Issue.6 , pp. 965-976
    • Kuznetsov, A.V.1    Veksler, V.2    Gellerich, F.N.3    Saks, V.4    Margreiter, R.5    Kunz, W.S.6
  • 18
    • 63449133530 scopus 로고    scopus 로고
    • Chapter 23 Quantification of superoxide production by mouse brain and skeletal muscle mitochondria
    • D. Malinska, A.P. Kudin, G. Debska-Vielhaber, S. Vielhaber, and W.S. Kunz Chapter 23 Quantification of superoxide production by mouse brain and skeletal muscle mitochondria Methods in Enzymology 456 2009 419 437
    • (2009) Methods in Enzymology , vol.456 , pp. 419-437
    • Malinska, D.1    Kudin, A.P.2    Debska-Vielhaber, G.3    Vielhaber, S.4    Kunz, W.S.5
  • 19
    • 84875755955 scopus 로고    scopus 로고
    • Rapid and specific measurements of superoxide using fluorescence spectroscopy
    • R.R. Nazarewicz, A. Bikineyeva, and S.I. Dikalov Rapid and specific measurements of superoxide using fluorescence spectroscopy Journal of Biomolecular Screening 18 4 2013 498 503
    • (2013) Journal of Biomolecular Screening , vol.18 , Issue.4 , pp. 498-503
    • Nazarewicz, R.R.1    Bikineyeva, A.2    Dikalov, S.I.3
  • 20
    • 0034643340 scopus 로고    scopus 로고
    • Normalizing mitochondrial superoxide production blocks three pathways of hyperglycaemic damage
    • T. Nishikawa, D. Edelstein, X.L. Du, S. Yamagishi, T. Matsumura, and Y. Kaneda et al. Normalizing mitochondrial superoxide production blocks three pathways of hyperglycaemic damage Nature 404 2000 787 790
    • (2000) Nature , vol.404 , pp. 787-790
    • Nishikawa, T.1    Edelstein, D.2    Du, X.L.3    Yamagishi, S.4    Matsumura, T.5    Kaneda, Y.6
  • 23
    • 44949142269 scopus 로고    scopus 로고
    • The selective detection of mitochondrial superoxide by live cell imaging
    • K.M. Robinson, M.S. Janes, and J.S. Beckman The selective detection of mitochondrial superoxide by live cell imaging Nature Protocols 3 2008 941 947
    • (2008) Nature Protocols , vol.3 , pp. 941-947
    • Robinson, K.M.1    Janes, M.S.2    Beckman, J.S.3
  • 26
    • 0037160091 scopus 로고    scopus 로고
    • Topology of superoxide production from different sites in the mitochondrial electron transport chain
    • J. St-Pierre, J.A. Buckingham, S.J. Roebuck, and M.D. Brand Topology of superoxide production from different sites in the mitochondrial electron transport chain The Journal of Biological Chemistry 277 2002 44784 44790
    • (2002) The Journal of Biological Chemistry , vol.277 , pp. 44784-44790
    • St-Pierre, J.1    Buckingham, J.A.2    Roebuck, S.J.3    Brand, M.D.4
  • 27
    • 33845999916 scopus 로고    scopus 로고
    • Dihydrolipoyl dehydrogenase as a source of reactive oxygen species inhibited by caloric restriction and involved in Saccharomyces cerevisiae aging
    • E.B. Tahara, M.H. Barros, G.A. Oliveira, L.E. Netto, and A.J. Kowaltowski Dihydrolipoyl dehydrogenase as a source of reactive oxygen species inhibited by caloric restriction and involved in Saccharomyces cerevisiae aging The FASEB Journal 21 2007 274 283
    • (2007) The FASEB Journal , vol.21 , pp. 274-283
    • Tahara, E.B.1    Barros, M.H.2    Oliveira, G.A.3    Netto, L.E.4    Kowaltowski, A.J.5
  • 28
    • 34347230544 scopus 로고    scopus 로고
    • Sulforhodamine B colorimetric assay for cytotoxicity screening
    • V. Vichai, and K. Kirtikara Sulforhodamine B colorimetric assay for cytotoxicity screening Nature Protocols 3 2006 1112 1116
    • (2006) Nature Protocols , vol.3 , pp. 1112-1116
    • Vichai, V.1    Kirtikara, K.2
  • 29
    • 0034740585 scopus 로고    scopus 로고
    • DeltaPsi(m)-dependent and -independent production of reactive oxygen species by rat brain mitochondria
    • T.V. Votyakova, and I.J. Reynolds DeltaPsi(m)-dependent and -independent production of reactive oxygen species by rat brain mitochondria Journal of Neurochemistry 79 2 2001 266 277
    • (2001) Journal of Neurochemistry , vol.79 , Issue.2 , pp. 266-277
    • Votyakova, T.V.1    Reynolds, I.J.2
  • 30
    • 5344234747 scopus 로고    scopus 로고
    • Detection of hydrogen peroxide with Amplex Red: Interference by NADH and reduced glutathione auto-oxidation
    • T.V. Votyakova, and I.J. Reynolds Detection of hydrogen peroxide with Amplex Red: Interference by NADH and reduced glutathione auto-oxidation Archives of Biochemistry and Biophysics 431 2004 138 144
    • (2004) Archives of Biochemistry and Biophysics , vol.431 , pp. 138-144
    • Votyakova, T.V.1    Reynolds, I.J.2
  • 31
    • 34548126843 scopus 로고    scopus 로고
    • Fluorescent and luminescent probes for measurement of oxidative and nitrosative species in cells and tissues: Progress, pitfalls and prospects
    • P. Wardman Fluorescent and luminescent probes for measurement of oxidative and nitrosative species in cells and tissues: Progress, pitfalls and prospects Free Radical Biology & Medicine 43 2007 995 1022
    • (2007) Free Radical Biology & Medicine , vol.43 , pp. 995-1022
    • Wardman, P.1
  • 32
    • 84890114880 scopus 로고    scopus 로고
    • The challenges of using fluorescent probes to detect and quantify specific reactive oxygen species in living cells
    • C.C. Winterbourn The challenges of using fluorescent probes to detect and quantify specific reactive oxygen species in living cells Biochimica et Biophysica Acta 1840 2014 730 738
    • (2014) Biochimica et Biophysica Acta , vol.1840 , pp. 730-738
    • Winterbourn, C.C.1
  • 33
    • 0348150715 scopus 로고    scopus 로고
    • Architecture of succinate dehydrogenase and reactive oxygen species generation
    • V. Yankovskaya, R. Horsefield, S. Törnroth, C. Luna-Chavez, H. Miyoshi, and C. Léger et al. Architecture of succinate dehydrogenase and reactive oxygen species generation Science 299 5607 2003 700 704
    • (2003) Science , vol.299 , Issue.5607 , pp. 700-704
    • Yankovskaya, V.1    Horsefield, R.2    Törnroth, S.3    Luna-Chavez, C.4    Miyoshi, H.5    Léger, C.6
  • 34
    • 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
    • H. Zhao, S. Kalivendi, H. Zhang, J. Joseph, K. Nithipatikom, and J. Vásquez-Vivar et al. Superoxide reacts with hydroethidine but forms a fluorescent product that is distinctly different from ethidium: Potential implications in intracellular fluorescence detection of superoxide Free Radical Biology & Medicine 34 2003 1359 1368
    • (2003) Free Radical Biology & Medicine , vol.34 , pp. 1359-1368
    • Zhao, H.1    Kalivendi, S.2    Zhang, H.3    Joseph, J.4    Nithipatikom, K.5    Vásquez-Vivar, J.6
  • 35
    • 0031573401 scopus 로고    scopus 로고
    • A stable nonfluorescent derivative of resorufin for the fluorometric determination of trace hydrogen peroxide: Applications in detecting the activity of phagocyte NADPH oxidase and other oxidases
    • M. Zhou, Z. Diwu, N. Panchuk-Voloshina, and R.P. Haugland A stable nonfluorescent derivative of resorufin for the fluorometric determination of trace hydrogen peroxide: Applications in detecting the activity of phagocyte NADPH oxidase and other oxidases Analytical Biochemistry 253 2 1997 162 168
    • (1997) Analytical Biochemistry , vol.253 , Issue.2 , pp. 162-168
    • Zhou, M.1    Diwu, Z.2    Panchuk-Voloshina, N.3    Haugland, R.P.4
  • 36
    • 58149168842 scopus 로고    scopus 로고
    • HPLC study of oxidation products of hydroethidine in chemical and biological systems: Ramifications in superoxide measurements
    • J. Zielonka, M. Hardy, and B. Kalyanaraman HPLC study of oxidation products of hydroethidine in chemical and biological systems: Ramifications in superoxide measurements Free Radical Biology & Medicine 46 2009 329 338
    • (2009) Free Radical Biology & Medicine , vol.46 , pp. 329-338
    • Zielonka, J.1    Hardy, M.2    Kalyanaraman, B.3
  • 37
    • 77950515980 scopus 로고    scopus 로고
    • Hydroethidine- and MitoSOX-derived red fluorescence is not a reliable indicator of intracellular superoxide formation: Another inconvenient truth
    • J. Zielonka, and B. Kalyanaraman Hydroethidine- and MitoSOX-derived red fluorescence is not a reliable indicator of intracellular superoxide formation: Another inconvenient truth Free Radical Biology & Medicine 48 8 2010 983 1001
    • (2010) Free Radical Biology & Medicine , vol.48 , Issue.8 , pp. 983-1001
    • Zielonka, J.1    Kalyanaraman, B.2
  • 38
    • 39149083084 scopus 로고    scopus 로고
    • Cytochrome c-mediated oxidation of hydroethidine and mito-hydroethidine in mitochondria: Identification of homo- and heterodimers
    • J. Zielonka, S. Srinivasan, M. Hardy, O. Ouari, M. Lopez, and J. Vasquez-Vivar et al. Cytochrome c-mediated oxidation of hydroethidine and mito-hydroethidine in mitochondria: Identification of homo- and heterodimers Free Radical Biology & Medicine 44 2008 835 846
    • (2008) Free Radical Biology & Medicine , vol.44 , pp. 835-846
    • Zielonka, J.1    Srinivasan, S.2    Hardy, M.3    Ouari, O.4    Lopez, M.5    Vasquez-Vivar, J.6
  • 39
    • 38149142769 scopus 로고    scopus 로고
    • Detection of 2-hydroxyethidium in cellular systems: A unique marker product of superoxide and hydroethidine
    • J. Zielonka, J. Vasquez-Vivar, and B. Kalyanaraman Detection of 2-hydroxyethidium in cellular systems: A unique marker product of superoxide and hydroethidine Nature Protocols 3 2008 8 21
    • (2008) Nature Protocols , vol.3 , pp. 8-21
    • Zielonka, J.1    Vasquez-Vivar, J.2    Kalyanaraman, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.