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Volumn 1606, Issue 1-3, 2003, Pages 137-146

Rhodamine 123 as a probe of mitochondrial membrane potential: Evaluation of proton flux through F0 during ATP synthesis

Author keywords

ATP synthase; Membrane potential; Mitochondria; Proton transport; Rhodamine 123

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; CARBONYL CYANIDE 4 (TRIFLUOROMETHOXY)PHENYLHYDRAZONE; DICYCLOHEXYLCARBODIIMIDE; OLIGOMYCIN; PROTON; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; RHODAMINE 123; SUCCINIC ACID;

EID: 0142042958     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0005-2728(03)00110-5     Document Type: Article
Times cited : (461)

References (42)
  • 1
    • 0024148694 scopus 로고
    • Mitochondrial membrane potential in living cells
    • Chen L.B. Mitochondrial membrane potential in living cells. Annu. Rev. Cell Biol. 4:1988;155-181.
    • (1988) Annu. Rev. Cell Biol. , vol.4 , pp. 155-181
    • Chen, L.B.1
  • 2
    • 0025267390 scopus 로고
    • Potential-sensitive molecular probes in membranes of bioenergetic relevance
    • Smith J.C. Potential-sensitive molecular probes in membranes of bioenergetic relevance. Biochim. Biophys. Acta. 1016:1990;1-28.
    • (1990) Biochim. Biophys. Acta , vol.1016 , pp. 1-28
    • Smith, J.C.1
  • 3
    • 0035229641 scopus 로고    scopus 로고
    • Assessment of mitochondrial membrane potential in situ using single potentiometric dyes and a novel fluorescence resonance energy transfer technique
    • Dykens J.A., Stout A.K. Assessment of mitochondrial membrane potential in situ using single potentiometric dyes and a novel fluorescence resonance energy transfer technique. Methods Cell Biol. 65:2001;285-309.
    • (2001) Methods Cell Biol. , vol.65 , pp. 285-309
    • Dykens, J.A.1    Stout, A.K.2
  • 4
    • 0021207554 scopus 로고
    • Membrane potential and surface potential in mitochondria: Uptake and binding of lipophilic cations
    • Rottenberg H. Membrane potential and surface potential in mitochondria: uptake and binding of lipophilic cations. J. Membr. Biol. 81:1984;127-138.
    • (1984) J. Membr. Biol. , vol.81 , pp. 127-138
    • Rottenberg, H.1
  • 5
    • 0022556745 scopus 로고
    • Methods for the determination of membrane potential in bioenergetic systems
    • Jackson J.B., Nicholls D.G. Methods for the determination of membrane potential in bioenergetic systems. Methods Enzymol. 127:1986;557-577.
    • (1986) Methods Enzymol. , vol.127 , pp. 557-577
    • Jackson, J.B.1    Nicholls, D.G.2
  • 6
    • 0019325159 scopus 로고
    • Safranine as membrane potential probe in rat liver mitochondria
    • Zanotti A., Azzone G.F. Safranine as membrane potential probe in rat liver mitochondria. Arch. Biochem. Biophys. 201:1980;255-265.
    • (1980) Arch. Biochem. Biophys. , vol.201 , pp. 255-265
    • Zanotti, A.1    Azzone, G.F.2
  • 8
    • 0019480519 scopus 로고
    • Monitoring of relative mitochondrial membrane potential in living cells by fluorescence microscopy
    • Johnson L.V., Walsh M.L., Bockus B.J., Chen L.B. Monitoring of relative mitochondrial membrane potential in living cells by fluorescence microscopy. J. Cell Biol. 88:1981;526-535.
    • (1981) J. Cell Biol. , vol.88 , pp. 526-535
    • Johnson, L.V.1    Walsh, M.L.2    Bockus, B.J.3    Chen, L.B.4
  • 9
    • 0022438530 scopus 로고
    • Mitochondrial analysis in living cells: The use of rhodamine 123 and flow cytometry
    • Ronot X., Benel L., Adolphe M., Mounolou J.C. Mitochondrial analysis in living cells: the use of rhodamine 123 and flow cytometry. Biol. Cell. 57:1986;1-7.
    • (1986) Biol. Cell , vol.57 , pp. 1-7
    • Ronot, X.1    Benel, L.2    Adolphe, M.3    Mounolou, J.C.4
  • 10
    • 0022492812 scopus 로고
    • Rhodamine 123 as a probe of transmembrane potential in isolated rat liver mitochondria: Spectral and metabolic properties
    • Emaus R.K., Grunwald R., Lemasters J.J. Rhodamine 123 as a probe of transmembrane potential in isolated rat liver mitochondria: spectral and metabolic properties. Biochim. Biophys. Acta. 850:1986;436-448.
    • (1986) Biochim. Biophys. Acta , vol.850 , pp. 436-448
    • Emaus, R.K.1    Grunwald, R.2    Lemasters, J.J.3
  • 11
    • 0345120940 scopus 로고    scopus 로고
    • Measurement of mitochondrial membrane potential using fluorescent rhodamine derivatives
    • Scaduto R.C. Jr., Grotyohann L.W. Measurement of mitochondrial membrane potential using fluorescent rhodamine derivatives. Biophys. J. 76:1999;469-477.
    • (1999) Biophys. J. , vol.76 , pp. 469-477
    • Scaduto R.C., Jr.1    Grotyohann, L.W.2
  • 14
    • 0025238864 scopus 로고
    • Analysis of the control of respiration rate, phosphorylation rate, proton leak rate and protonmotive force in isolated mitochondria using the "top-down" approach of metabolic control theory
    • Hafner R.P., Brown G.C., Brand M.D. Analysis of the control of respiration rate, phosphorylation rate, proton leak rate and protonmotive force in isolated mitochondria using the "top-down" approach of metabolic control theory. Eur. J. Biochem. 188:1990;313-319.
    • (1990) Eur. J. Biochem. , vol.188 , pp. 313-319
    • Hafner, R.P.1    Brown, G.C.2    Brand, M.D.3
  • 15
    • 0026580059 scopus 로고
    • Influx and efflux kinetics of cationic dye binding to respiring mitochondria
    • Bunting J.R. Influx and efflux kinetics of cationic dye binding to respiring mitochondria. Biophys. Chem. 42:1992;163-175.
    • (1992) Biophys. Chem. , vol.42 , pp. 163-175
    • Bunting, J.R.1
  • 16
    • 0018404130 scopus 로고
    • Stabilization of mitochondrial functions with digitonin
    • Kun E., Kirsten E., Piper W.N. Stabilization of mitochondrial functions with digitonin. Methods Enzymol. 55:1979;115-118.
    • (1979) Methods Enzymol. , vol.55 , pp. 115-118
    • Kun, E.1    Kirsten, E.2    Piper, W.N.3
  • 17
    • 29744466425 scopus 로고
    • Determination of serum proteins by means of the biuret reaction
    • Gornall A.G., Bardawill C.J., David M.M. Determination of serum proteins by means of the biuret reaction. J. Biol. Chem. 177:1949;751-766.
    • (1949) J. Biol. Chem. , vol.177 , pp. 751-766
    • Gornall, A.G.1    Bardawill, C.J.2    David, M.M.3
  • 18
    • 0020363762 scopus 로고
    • Effects of niridazole and 5-nitroimidazoles on heart mitochondrial respiration
    • Aicardi G., Solaini G. Effects of niridazole and 5-nitroimidazoles on heart mitochondrial respiration. Biochem. Pharmacol. 31:1982;3703-3705.
    • (1982) Biochem. Pharmacol. , vol.31 , pp. 3703-3705
    • Aicardi, G.1    Solaini, G.2
  • 20
    • 0020558033 scopus 로고
    • Inhibition of an oligomycin-sensitive ATPase by cationic dyes, some of which are atypical uncouplers of intact mitochondria
    • Mai M.S., Allison W.S. Inhibition of an oligomycin-sensitive ATPase by cationic dyes, some of which are atypical uncouplers of intact mitochondria. Arch. Biochem. Biophys. 221:1983;467-476.
    • (1983) Arch. Biochem. Biophys. , vol.221 , pp. 467-476
    • Mai, M.S.1    Allison, W.S.2
  • 22
    • 0023227833 scopus 로고
    • Basis for the selective cytotoxicity of rhodamine 123
    • Modica-Napolitano J.S., Aprille J.R. Basis for the selective cytotoxicity of rhodamine 123. Cancer Res. 47:1987;4361-4365.
    • (1987) Cancer Res. , vol.47 , pp. 4361-4365
    • Modica-Napolitano, J.S.1    Aprille, J.R.2
  • 23
    • 0030592172 scopus 로고    scopus 로고
    • The permeability transition pore. Control points of a cyclosporin A-sensitive mitochondrial channel involved in cell death
    • Bernardi P. The permeability transition pore. Control points of a cyclosporin A-sensitive mitochondrial channel involved in cell death. Biochim. Biophys. Acta. 1275:1996;5-9.
    • (1996) Biochim. Biophys. Acta , vol.1275 , pp. 5-9
    • Bernardi, P.1
  • 24
    • 0024360271 scopus 로고
    • Cyclosporin A is a potent inhibitor of the inner membrane permeability transition in liver mitochondria
    • Broekemeier K.M., Dempsey M.E., Pfeiffer D.R. Cyclosporin A is a potent inhibitor of the inner membrane permeability transition in liver mitochondria. J. Biol. Chem. 264:1989;7826-7830.
    • (1989) J. Biol. Chem. , vol.264 , pp. 7826-7830
    • Broekemeier, K.M.1    Dempsey, M.E.2    Pfeiffer, D.R.3
  • 25
    • 0018370836 scopus 로고
    • Respiratory control and oxidative phosphorylation measurements in mitochondria
    • Van Dam K., Wiechmann A.H. Respiratory control and oxidative phosphorylation measurements in mitochondria. Methods Enzymol. 55:1979;225-229.
    • (1979) Methods Enzymol. , vol.55 , pp. 225-229
    • Van Dam, K.1    Wiechmann, A.H.2
  • 27
    • 0021707105 scopus 로고
    • An investigation on the effect of oligomycin on state-4 respiration in isolated rat-liver mitochondria
    • Masini A., Ceccarelli-Stanzani D., Moscatello U. An investigation on the effect of oligomycin on state-4 respiration in isolated rat-liver mitochondria. Biochim. Biophys. Acta. 767:1984;130-137.
    • (1984) Biochim. Biophys. Acta , vol.767 , pp. 130-137
    • Masini, A.1    Ceccarelli-Stanzani, D.2    Moscatello, U.3
  • 28
    • 0014470420 scopus 로고
    • Estimation of membrane potential pH difference across the cristae membrane of rat liver mitochondria
    • Mitchell P., Moyle J. Estimation of membrane potential pH difference across the cristae membrane of rat liver mitochondria. Eur. J. Biochem. 7:1969;471-484.
    • (1969) Eur. J. Biochem. , vol.7 , pp. 471-484
    • Mitchell, P.1    Moyle, J.2
  • 29
    • 0018371450 scopus 로고
    • Inhibitors of the ATP synthethase system
    • Linnett P.E., Beechey R.B. Inhibitors of the ATP synthethase system. Methods Enzymol. 55:1979;472-518.
    • (1979) Methods Enzymol. , vol.55 , pp. 472-518
    • Linnett, P.E.1    Beechey, R.B.2
  • 31
    • 0015874366 scopus 로고
    • The binding of aurovertin to mitochondria and its effect on mitochondrial respiration
    • Bertina R.M., Schrier P.I., Slater E.C. The binding of aurovertin to mitochondria and its effect on mitochondrial respiration. Biochim. Biophys. Acta. 305:1973;503-518.
    • (1973) Biochim. Biophys. Acta , vol.305 , pp. 503-518
    • Bertina, R.M.1    Schrier, P.I.2    Slater, E.C.3
  • 32
    • 0021825076 scopus 로고
    • Mechanism of inhibition of mitochondrial adenosine triphosphatase by dicyclohexylcarbodimide and oligomycin: Relationship to ATP synthesis
    • Penefsky H.S. Mechanism of inhibition of mitochondrial adenosine triphosphatase by dicyclohexylcarbodimide and oligomycin: relationship to ATP synthesis. Proc. Natl. Acad. Sci. U. S. A. 82:1985;1589-1593.
    • (1985) Proc. Natl. Acad. Sci. U. S. A. , vol.82 , pp. 1589-1593
    • Penefsky, H.S.1
  • 33
    • 0024759595 scopus 로고
    • Fluorescent cationic probes of mitochondria: Metrics and mechanism of interaction
    • Bunting J.R., Phan T.V., Kamali E., Dowben R.M. Fluorescent cationic probes of mitochondria: metrics and mechanism of interaction. Biophys. J. 56:1989;979-993.
    • (1989) Biophys. J. , vol.56 , pp. 979-993
    • Bunting, J.R.1    Phan, T.V.2    Kamali, E.3    Dowben, R.M.4
  • 34
    • 0033927209 scopus 로고    scopus 로고
    • Quantitation of mitochondrial transmembrane potential in cells and in isolated mitochondria
    • Zamzami N., Metivier D., Kroemer G. Quantitation of mitochondrial transmembrane potential in cells and in isolated mitochondria. Methods Enzymol. 322:2000;208-213.
    • (2000) Methods Enzymol. , vol.322 , pp. 208-213
    • Zamzami, N.1    Metivier, D.2    Kroemer, G.3
  • 35
    • 0028345801 scopus 로고
    • A fast kinetic method for assessing mitochondrial membrane potential in isolated hepatocytes with rhodamine 123 and flow cytometry
    • Juan G., Cavazzoni M., Saez G.T., O'Connor J.E. A fast kinetic method for assessing mitochondrial membrane potential in isolated hepatocytes with rhodamine 123 and flow cytometry. Cytometry. 15:1994;335-342.
    • (1994) Cytometry , vol.15 , pp. 335-342
    • Juan, G.1    Cavazzoni, M.2    Saez, G.T.3    O'Connor, J.E.4
  • 36
    • 0018864653 scopus 로고
    • Energy transduction in intact synaptosomes: Influence of plasma-membrane depolarization on the respiration and membrane potential of internal mitochondria determined in situ
    • Scott I.D., Nicholls D.G. Energy transduction in intact synaptosomes: influence of plasma-membrane depolarization on the respiration and membrane potential of internal mitochondria determined in situ. Biochem. J. 186:1980;21-33.
    • (1980) Biochem. J. , vol.186 , pp. 21-33
    • Scott, I.D.1    Nicholls, D.G.2
  • 38
    • 0032504575 scopus 로고
    • Mitochondria as regulators of apoptosis: Doubt no more
    • Susin S., Zamzami N., Kroemer G. Mitochondria as regulators of apoptosis: doubt no more. Biochim. Biophys. Acta. 1366:1988;151-165.
    • (1988) Biochim. Biophys. Acta , vol.1366 , pp. 151-165
    • Susin, S.1    Zamzami, N.2    Kroemer, G.3
  • 39
    • 0033776271 scopus 로고    scopus 로고
    • Changes in intramitochondrial cytosolic pH: Early events that modulate caspase activation during apoptosis
    • Matsuyama S., Llopis J., Deveraux Q.L., Tsien R.Y., Reed J.C. Changes in intramitochondrial cytosolic pH: early events that modulate caspase activation during apoptosis. Nat. Cell Biol. 2:2000;318-325.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 318-325
    • Matsuyama, S.1    Llopis, J.2    Deveraux, Q.L.3    Tsien, R.Y.4    Reed, J.C.5
  • 40
    • 0034635388 scopus 로고    scopus 로고
    • Catalytic activities of mitochondrial ATP synthase in patients with mitochondrial DNA T8993G mutation in the ATPase 6 gene encoding subunit a
    • Baracca A., Barogi S., Carelli V., Lenaz G., Solaini G. Catalytic activities of mitochondrial ATP synthase in patients with mitochondrial DNA T8993G mutation in the ATPase 6 gene encoding subunit a. J. Biol. Chem. 275:2000;4177-4182.
    • (2000) J. Biol. Chem. , vol.275 , pp. 4177-4182
    • Baracca, A.1    Barogi, S.2    Carelli, V.3    Lenaz, G.4    Solaini, G.5
  • 41
    • 0028175787 scopus 로고
    • MtDNA and nuclear mutations affecting oxidative phosphorylation: Correlating severity of clinical defect with extent of bioenergetic compromise
    • Robinson B.H. MtDNA and nuclear mutations affecting oxidative phosphorylation: correlating severity of clinical defect with extent of bioenergetic compromise. J. Bioenerg. Biomembr. 26:1994;311-316.
    • (1994) J. Bioenerg. Biomembr. , vol.26 , pp. 311-316
    • Robinson, B.H.1
  • 42
    • 0027936218 scopus 로고
    • Cytoplasmic transfer of the mtDNA nt 8993 T→G (ATP6) point mutation associated with Leigh syndrome into mtDNA-less cells demonstrates cosegregation with a decrease in state III respiration and ADP/O ratio
    • Trounce I., Neill S., Wallace D.C. Cytoplasmic transfer of the mtDNA nt 8993 T→G (ATP6) point mutation associated with Leigh syndrome into mtDNA-less cells demonstrates cosegregation with a decrease in state III respiration and ADP/O ratio. Proc. Natl. Acad. Sci. U. S. A. 91:1994;8334-8338.
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 8334-8338
    • Trounce, I.1    Neill, S.2    Wallace, D.C.3


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