메뉴 건너뛰기




Volumn 10, Issue 5, 2010, Pages 487-496

Bupivacaine uncouples the mitochondrial oxidative phosphorylation, inhibits respiratory chain complexes I and III and enhances ROS production: Results of a study on cell cultures

Author keywords

Complex I; Complex III; Local anesthetic; OXPHOS uncoupling; Reactive oxygen species; Respiratory chain inhibition

Indexed keywords

BUPIVACAINE; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); UBIQUINOL CYTOCHROME C REDUCTASE;

EID: 77955432346     PISSN: 15677249     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mito.2010.05.005     Document Type: Article
Times cited : (77)

References (62)
  • 1
    • 0017201717 scopus 로고
    • Safranine as a probe of the mitochondrial membrane potential
    • Akerman K.E., Wikström M.K. Safranine as a probe of the mitochondrial membrane potential. FEBS Lett. 1976, 68:191-197.
    • (1976) FEBS Lett. , vol.68 , pp. 191-197
    • Akerman, K.E.1    Wikström, M.K.2
  • 2
    • 0018729672 scopus 로고
    • Cardiac arrest following regional anesthesia with etidocaine and bupivacaine
    • Albright G.A. Cardiac arrest following regional anesthesia with etidocaine and bupivacaine. Anesthesiology 1979, 51:285-287.
    • (1979) Anesthesiology , vol.51 , pp. 285-287
    • Albright, G.A.1
  • 3
    • 0036024973 scopus 로고    scopus 로고
    • In vivo and in organello assessment of OXPHOS activities
    • Barrientos A. In vivo and in organello assessment of OXPHOS activities. Methods 2002, 26:307-316.
    • (2002) Methods , vol.26 , pp. 307-316
    • Barrientos, A.1
  • 4
    • 77049249588 scopus 로고
    • Respiratory enzymes in oxidative phosphorylation: III. The steady state
    • Chance B., Williams C.M. Respiratory enzymes in oxidative phosphorylation: III. The steady state. J. Biol. Chem. 1955, 217:405-427.
    • (1955) J. Biol. Chem. , vol.217 , pp. 405-427
    • Chance, B.1    Williams, C.M.2
  • 5
    • 27744491193 scopus 로고    scopus 로고
    • Emerging functions of mammalian mitochondrial fusion and fission
    • Chen H., Chan D.C. Emerging functions of mammalian mitochondrial fusion and fission. Hum. Mol. Genet. 2005, 14:283-289.
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 283-289
    • Chen, H.1    Chan, D.C.2
  • 6
    • 27844605495 scopus 로고    scopus 로고
    • Superoxide generation from mitochondrial NADH dehydrogenase induces self-inactivation with specific protein radical formation
    • Chen Y.R., Chen C.L., Zhang L., Green-Church K.B., Zweier J.L. Superoxide generation from mitochondrial NADH dehydrogenase induces self-inactivation with specific protein radical formation. J. Biol. Chem. 2005, 280:37339-37348.
    • (2005) J. Biol. Chem. , vol.280 , pp. 37339-37348
    • Chen, Y.R.1    Chen, C.L.2    Zhang, L.3    Green-Church, K.B.4    Zweier, J.L.5
  • 8
    • 66149107066 scopus 로고    scopus 로고
    • Control and regulation of mitochondrial energetics in an integrated model of cardiomyocyte function
    • Cortassa S., O'Rourke B., Winslow R.L., Aon M.A. Control and regulation of mitochondrial energetics in an integrated model of cardiomyocyte function. Biophys. J. 2009, 96:2466-2478.
    • (2009) Biophys. J. , vol.96 , pp. 2466-2478
    • Cortassa, S.1    O'Rourke, B.2    Winslow, R.L.3    Aon, M.A.4
  • 10
    • 0023568357 scopus 로고
    • Uncoupling effects of local anesthetics on rat liver mitochondria
    • Dabadie P., Bendriss P., Erny P., Mazat J.P. Uncoupling effects of local anesthetics on rat liver mitochondria. FEBS Lett. 1987, 226:77-82.
    • (1987) FEBS Lett. , vol.226 , pp. 77-82
    • Dabadie, P.1    Bendriss, P.2    Erny, P.3    Mazat, J.P.4
  • 11
    • 75849160168 scopus 로고    scopus 로고
    • Rotenone induces apoptosis in MCF-7 human breast cancer cell-mediated ROS through JNK and p38 signaling
    • Deng Y.T., Huang H.C., Lin J.K. Rotenone induces apoptosis in MCF-7 human breast cancer cell-mediated ROS through JNK and p38 signaling. Mol. Carcinogen. doi: 2009, 10.1002/mc.20583.
    • (2009) Mol. Carcinogen. doi:
    • Deng, Y.T.1    Huang, H.C.2    Lin, J.K.3
  • 12
    • 52049104467 scopus 로고    scopus 로고
    • The mechanism of mitochondrial superoxide production by the cytochrome bc1 complex
    • Dröse S., Brandt U. The mechanism of mitochondrial superoxide production by the cytochrome bc1 complex. J. Biol. Chem. 2008, 283:21649-21654.
    • (2008) J. Biol. Chem. , vol.283 , pp. 21649-21654
    • Dröse, S.1    Brandt, U.2
  • 13
    • 58149381936 scopus 로고    scopus 로고
    • Mitochondrial production of reactive oxygen species: role of complex I and quinone analogues
    • Fato R., Bergamini C., Leoni S., Lenaz G. Mitochondrial production of reactive oxygen species: role of complex I and quinone analogues. Biofactors 2008, 32(1-4):31-39.
    • (2008) Biofactors , vol.32 , Issue.1-4 , pp. 31-39
    • Fato, R.1    Bergamini, C.2    Leoni, S.3    Lenaz, G.4
  • 15
    • 0034008060 scopus 로고    scopus 로고
    • Levobupivacaine: a review of its pharmacology and use as a local anaesthetic
    • Foster R.H., Markham A. Levobupivacaine: a review of its pharmacology and use as a local anaesthetic. Drugs 2000, 59:551-579.
    • (2000) Drugs , vol.59 , pp. 551-579
    • Foster, R.H.1    Markham, A.2
  • 16
    • 0025028839 scopus 로고
    • Effect of local anaesthetics on mitochondrial membrane potential in living cells
    • Grouselle M., Tueux O., Dabadie P., Georgescaud D., Mazat J.P. Effect of local anaesthetics on mitochondrial membrane potential in living cells. Biochem. J. 1990, 271:269-272.
    • (1990) Biochem. J. , vol.271 , pp. 269-272
    • Grouselle, M.1    Tueux, O.2    Dabadie, P.3    Georgescaud, D.4    Mazat, J.P.5
  • 17
    • 0030826778 scopus 로고    scopus 로고
    • Cyclosporin A binding to mitochondrial cyclophilin inhibits the permeability transition pore and protects hearts from ischaemia/reperfusion injury
    • Halestrap A.P., Connern C.P., Griffiths E.J., Kerr P.M. Cyclosporin A binding to mitochondrial cyclophilin inhibits the permeability transition pore and protects hearts from ischaemia/reperfusion injury. Mol. Cell. Biochem. 1997, 174:167-172.
    • (1997) Mol. Cell. Biochem. , vol.174 , pp. 167-172
    • Halestrap, A.P.1    Connern, C.P.2    Griffiths, E.J.3    Kerr, P.M.4
  • 19
    • 0018337793 scopus 로고
    • Uncouplers of oxidative phosphorylation
    • Heytler P.G. Uncouplers of oxidative phosphorylation. Methods Enzymol. 1979, 55:462-542.
    • (1979) Methods Enzymol. , vol.55 , pp. 462-542
    • Heytler, P.G.1
  • 20
    • 50249148905 scopus 로고    scopus 로고
    • Cardiolipin, the heart of mitochondrial metabolism
    • Houtkooper R.H., Vaz F.M. Cardiolipin, the heart of mitochondrial metabolism. Cell Mol. Life Sci. 2008, 65:2493-2506.
    • (2008) Cell Mol. Life Sci. , vol.65 , pp. 2493-2506
    • Houtkooper, R.H.1    Vaz, F.M.2
  • 21
    • 0038730358 scopus 로고    scopus 로고
    • Protonmotive pathways and mechanisms in the cytochrome bc1 complex
    • Hunte C., Palsdottir H., Trumpower B.L. Protonmotive pathways and mechanisms in the cytochrome bc1 complex. FEBS Lett. 2003, 545:39-46.
    • (2003) FEBS Lett. , vol.545 , pp. 39-46
    • Hunte, C.1    Palsdottir, H.2    Trumpower, B.L.3
  • 22
    • 0037438730 scopus 로고    scopus 로고
    • Biological significance of phospholipid hydroperoxide glutathione peroxidase (PHGPx, GPx4) in mammalian cells
    • Imai H., Nakagawa Y. Biological significance of phospholipid hydroperoxide glutathione peroxidase (PHGPx, GPx4) in mammalian cells. Free Radical Biol. Med. 2003, 34:145-169.
    • (2003) Free Radical Biol. Med. , vol.34 , pp. 145-169
    • Imai, H.1    Nakagawa, Y.2
  • 24
    • 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. 1981, 88:526-535.
    • (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
  • 25
    • 33646948530 scopus 로고    scopus 로고
    • Parkinson's disease brain mitochondrial complex I has oxidatively damaged subunits and is functionally impaired and misassembled
    • Keeney P.M., Xie J., Capaldi R.A., Bennett J.P. Parkinson's disease brain mitochondrial complex I has oxidatively damaged subunits and is functionally impaired and misassembled. J. Neurosci. 2006, 26:5256-5264.
    • (2006) J. Neurosci. , vol.26 , pp. 5256-5264
    • Keeney, P.M.1    Xie, J.2    Capaldi, R.A.3    Bennett, J.P.4
  • 26
    • 33845977959 scopus 로고    scopus 로고
    • Mitochondrial membrane permeabilization in cell death
    • Kroemer G., Galluzzi L., Brenner C. Mitochondrial membrane permeabilization in cell death. Physiol. Rev. 2007, 87:99-163.
    • (2007) Physiol. Rev. , vol.87 , pp. 99-163
    • Kroemer, G.1    Galluzzi, L.2    Brenner, C.3
  • 27
    • 33646716659 scopus 로고    scopus 로고
    • The mechanism of superoxide production by NADH: ubiquinone oxidoreductase (complex I) from bovine heart mitochondria
    • Kussmaul L., Hirst J. The mechanism of superoxide production by NADH: ubiquinone oxidoreductase (complex I) from bovine heart mitochondria. Proc. Natl. Acad. Sci. USA 2006, 103:7607-7612.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 7607-7612
    • Kussmaul, L.1    Hirst, J.2
  • 28
    • 0032080644 scopus 로고    scopus 로고
    • Heterogeneity of intracellular pH and of mechanisms that regulate intracellular pH in populations of cultured cells
    • Lee A.H., Tannock I.F. Heterogeneity of intracellular pH and of mechanisms that regulate intracellular pH in populations of cultured cells. Cancer Res. 1998, 58:901-908.
    • (1998) Cancer Res. , vol.58 , pp. 901-908
    • Lee, A.H.1    Tannock, I.F.2
  • 29
    • 55249110797 scopus 로고    scopus 로고
    • Pharmacology, toxicology, and clinical use of new long acting local anesthetics, ropivacaine and levobupivacaine
    • Leone S., Di Cianni S., Casati A., Fanelli G. Pharmacology, toxicology, and clinical use of new long acting local anesthetics, ropivacaine and levobupivacaine. Acta Biomed. 2008, 79:92-105.
    • (2008) Acta Biomed. , vol.79 , pp. 92-105
    • Leone, S.1    Di Cianni, S.2    Casati, A.3    Fanelli, G.4
  • 30
    • 0032545445 scopus 로고    scopus 로고
    • Diphenyleneiodonium, an NAD(P)H oxidase inhibitor, also potently inhibits mitochondrial reactive oxygen species production
    • Li Y., Trush M.A. Diphenyleneiodonium, an NAD(P)H oxidase inhibitor, also potently inhibits mitochondrial reactive oxygen species production. Biochem. Biophys. Res. Commun. 1998, 253:295-299.
    • (1998) Biochem. Biophys. Res. Commun. , vol.253 , pp. 295-299
    • Li, Y.1    Trush, M.A.2
  • 31
    • 67650868959 scopus 로고    scopus 로고
    • Mitochondrial dynamics in mammalian health and disease
    • Liesa M., Palacín M., Zorzano A. Mitochondrial dynamics in mammalian health and disease. Physiol. Rev. 2009, 89:799-845.
    • (2009) Physiol. Rev. , vol.89 , pp. 799-845
    • Liesa, M.1    Palacín, M.2    Zorzano, A.3
  • 32
    • 42449139616 scopus 로고    scopus 로고
    • In vitro, inhibition of mitogen-activated protein kinase pathways protects against bupivacaine- and ropivacaine-induced neurotoxicity
    • Lirk P., Haller I., Colvin H.P., Lang L., Tomaselli B., Klimaschewski L., Gerner P. In vitro, inhibition of mitogen-activated protein kinase pathways protects against bupivacaine- and ropivacaine-induced neurotoxicity. Anesth. Analg. 2008, 106:1456-1464.
    • (2008) Anesth. Analg. , vol.106 , pp. 1456-1464
    • Lirk, P.1    Haller, I.2    Colvin, H.P.3    Lang, L.4    Tomaselli, B.5    Klimaschewski, L.6    Gerner, P.7
  • 33
    • 0023198741 scopus 로고
    • The matrix water space of mitochondria in situ in isolated hepatocytes
    • Lund P., Wiggins D. The matrix water space of mitochondria in situ in isolated hepatocytes. Biosci. Rep. 1987, 7:59-66.
    • (1987) Biosci. Rep. , vol.7 , pp. 59-66
    • Lund, P.1    Wiggins, D.2
  • 34
    • 0004064798 scopus 로고    scopus 로고
    • Academic Press Limited, London, San Diego
    • Nicholls D.G., Ferguson S.J. Bioenergetics 3 2002, Academic Press Limited, London, San Diego, pp. 10-20.
    • (2002) Bioenergetics 3 , pp. 10-20
    • Nicholls, D.G.1    Ferguson, S.J.2
  • 35
    • 18744378827 scopus 로고    scopus 로고
    • Effects of bupivacaine on mitochondrial energy metabolism in heart of rats following exposure to chronic hypoxia
    • Nouette-Gaulain K., Forestier F., Malgat M., Marthan R., Mazat J.P., Sztark F. Effects of bupivacaine on mitochondrial energy metabolism in heart of rats following exposure to chronic hypoxia. Anesthesiology 2002, 97:1507-1511.
    • (2002) Anesthesiology , vol.97 , pp. 1507-1511
    • Nouette-Gaulain, K.1    Forestier, F.2    Malgat, M.3    Marthan, R.4    Mazat, J.P.5    Sztark, F.6
  • 36
    • 58149385697 scopus 로고    scopus 로고
    • Functional role of coenzyme Q in the energy coupling of NADH-CoQ oxidoreductase (complex I): stabilization of the semiquinone state with the application of inside-positive membrane potential to proteoliposomes
    • Ohnishi T., Ohnishi S.T., Shinzawa-Ito K., Yoshikawa S. Functional role of coenzyme Q in the energy coupling of NADH-CoQ oxidoreductase (complex I): stabilization of the semiquinone state with the application of inside-positive membrane potential to proteoliposomes. Biofactors 2008, 32:13-22.
    • (2008) Biofactors , vol.32 , pp. 13-22
    • Ohnishi, T.1    Ohnishi, S.T.2    Shinzawa-Ito, K.3    Yoshikawa, S.4
  • 37
    • 34548306674 scopus 로고    scopus 로고
    • Bupivacaine, but not lidocaine, disrupts cardiolipin-containing small biomimetic unilamellar liposomes
    • Onyüksel H., Sethi V., Weinberg G.L., Dudeja P.K., Rubinstein I. Bupivacaine, but not lidocaine, disrupts cardiolipin-containing small biomimetic unilamellar liposomes. Chem. Biol. Interact. 2007, 169:154-159.
    • (2007) Chem. Biol. Interact. , vol.169 , pp. 154-159
    • Onyüksel, H.1    Sethi, V.2    Weinberg, G.L.3    Dudeja, P.K.4    Rubinstein, I.5
  • 40
    • 0037387920 scopus 로고    scopus 로고
    • Decreased complex III activity in mitochondria isolated from rat heart subjected to ischemia and reperfusion: role of reactive oxygen species and cardiolipin
    • Petrosillo G., Ruggiero F.M., Di Venosa N., Paradies G. Decreased complex III activity in mitochondria isolated from rat heart subjected to ischemia and reperfusion: role of reactive oxygen species and cardiolipin. FASEB J. 2003, 17:714-716.
    • (2003) FASEB J. , vol.17 , pp. 714-716
    • Petrosillo, G.1    Ruggiero, F.M.2    Di Venosa, N.3    Paradies, G.4
  • 41
    • 57449084690 scopus 로고    scopus 로고
    • Mitochondrial complex I dysfunction in rat heart with aging: critical role of reactive oxygen species and cardiolipin
    • Petrosillo G., Matera M., Moro N., Ruggiero F.M., Paradies G. Mitochondrial complex I dysfunction in rat heart with aging: critical role of reactive oxygen species and cardiolipin. Free Radical Biol. Med. 2009, 46:88-94.
    • (2009) Free Radical Biol. Med. , vol.46 , pp. 88-94
    • Petrosillo, G.1    Matera, M.2    Moro, N.3    Ruggiero, F.M.4    Paradies, G.5
  • 42
    • 33744987954 scopus 로고    scopus 로고
    • Control by cytochrome c oxidase of the cellular oxidative phosphorylation system depends on the mitochondrial energy state
    • Piccoli C., Scrima R., Boffoli D., Capitanio N. Control by cytochrome c oxidase of the cellular oxidative phosphorylation system depends on the mitochondrial energy state. Biochem. J. 2006, 396:573-583.
    • (2006) Biochem. J. , vol.396 , pp. 573-583
    • Piccoli, C.1    Scrima, R.2    Boffoli, D.3    Capitanio, N.4
  • 43
    • 0141839654 scopus 로고    scopus 로고
    • Hepatoma HepG2 cells as a model for in vitro studies on mitochondrial toxicity of antiviral drugs: which correlation with the patient?
    • Pinti M., Troiano L., Nasi M., Ferraresi R., Dobrucki J., Cossarizza A. Hepatoma HepG2 cells as a model for in vitro studies on mitochondrial toxicity of antiviral drugs: which correlation with the patient?. J. Biol. Reg. Homeos. Agents 2003, 17:166-171.
    • (2003) J. Biol. Reg. Homeos. Agents , vol.17 , pp. 166-171
    • Pinti, M.1    Troiano, L.2    Nasi, M.3    Ferraresi, R.4    Dobrucki, J.5    Cossarizza, A.6
  • 44
    • 0036233943 scopus 로고    scopus 로고
    • Effect of epidural epinephrine on the minimum local analgesic concentration of epidural bupivacaine in labor
    • Polley L.S., Columb M.O., Naughton N.N., Wagner D.S., van de Ven C.J. Effect of epidural epinephrine on the minimum local analgesic concentration of epidural bupivacaine in labor. Anesthesiology 2002, 96:1123-1128.
    • (2002) Anesthesiology , vol.96 , pp. 1123-1128
    • Polley, L.S.1    Columb, M.O.2    Naughton, N.N.3    Wagner, D.S.4    van de Ven, C.J.5
  • 45
    • 0029852328 scopus 로고    scopus 로고
    • Changes in membrane potential induced by local anesthetic bupivacaine on mitochondria within Ehrlich ascites tumor cells
    • Pulselli R., Arcuri E., Paggi M.G., Floridi A. Changes in membrane potential induced by local anesthetic bupivacaine on mitochondria within Ehrlich ascites tumor cells. Oncol. Res. 1996, 8:267-271.
    • (1996) Oncol. Res. , vol.8 , pp. 267-271
    • Pulselli, R.1    Arcuri, E.2    Paggi, M.G.3    Floridi, A.4
  • 46
    • 0026716379 scopus 로고
    • Is bupivacaine a decoupler, a protonophore or a proton-leak-inducer?
    • Schönfeld P., Sztark F., Slimani M., Dabadie P., Mazat J.P. Is bupivacaine a decoupler, a protonophore or a proton-leak-inducer?. FEBS Lett. 1992, 304:273-276.
    • (1992) FEBS Lett. , vol.304 , pp. 273-276
    • Schönfeld, P.1    Sztark, F.2    Slimani, M.3    Dabadie, P.4    Mazat, J.P.5
  • 47
    • 0026669466 scopus 로고
    • On the mechanism by which bupivacaine conducts protons across the membranes of mitochondria and liposomes
    • Sun X., Garlid K.D. On the mechanism by which bupivacaine conducts protons across the membranes of mitochondria and liposomes. J. Biol. Chem. 1992, 267:19147-19154.
    • (1992) J. Biol. Chem. , vol.267 , pp. 19147-19154
    • Sun, X.1    Garlid, K.D.2
  • 48
    • 0027979133 scopus 로고
    • Effects of bupivacaine on cellular oxygen consumption and adenine nucleotide metabolism
    • Sztark F., Tueux O., Erny P., Dabadie P., Mazat J.P. Effects of bupivacaine on cellular oxygen consumption and adenine nucleotide metabolism. Anesth. Analg. 1994, 78:335-339.
    • (1994) Anesth. Analg. , vol.78 , pp. 335-339
    • Sztark, F.1    Tueux, O.2    Erny, P.3    Dabadie, P.4    Mazat, J.P.5
  • 49
    • 0030780863 scopus 로고    scopus 로고
    • Effects of the local anesthetic bupivacaine on mitochondrial energy metabolism: change from uncoupling to decoupling depending on the respiration state
    • Sztark F., Ouhabi R., Dabadie P., Mazat J.P. Effects of the local anesthetic bupivacaine on mitochondrial energy metabolism: change from uncoupling to decoupling depending on the respiration state. Biochem. Mol. Biol. Int. 1997, 43:997-1003.
    • (1997) Biochem. Mol. Biol. Int. , vol.43 , pp. 997-1003
    • Sztark, F.1    Ouhabi, R.2    Dabadie, P.3    Mazat, J.P.4
  • 50
    • 0031956338 scopus 로고    scopus 로고
    • Comparison of the effects of bupivacaine and ropivacaine on heart cell mitochondrial bioenergetics
    • Sztark F., Malgat M., Dabadie P., Mazat J.P. Comparison of the effects of bupivacaine and ropivacaine on heart cell mitochondrial bioenergetics. Anesthesiology 1998, 88:1340-1349.
    • (1998) Anesthesiology , vol.88 , pp. 1340-1349
    • Sztark, F.1    Malgat, M.2    Dabadie, P.3    Mazat, J.P.4
  • 51
    • 0033853187 scopus 로고    scopus 로고
    • Absence of stereospecific effects of bupivacaine isomers on heart mitochondrial bioenergetics
    • Sztark F., Nouette-Gaulain K., Malgat M., Dabadie P., Mazat J.P. Absence of stereospecific effects of bupivacaine isomers on heart mitochondrial bioenergetics. Anesthesiology 2000, 93:456-462.
    • (2000) Anesthesiology , vol.93 , pp. 456-462
    • Sztark, F.1    Nouette-Gaulain, K.2    Malgat, M.3    Dabadie, P.4    Mazat, J.P.5
  • 52
    • 0037490142 scopus 로고    scopus 로고
    • Reversible glutathionylation of complex I increases mitochondrial superoxide formation
    • Taylor E.R., Hurrell F., Shannon R.J., Lin T.K., Hirst J., Murphy M.P. Reversible glutathionylation of complex I increases mitochondrial superoxide formation. J. Biol. Chem. 2003, 278:19603-19610.
    • (2003) J. Biol. Chem. , vol.278 , pp. 19603-19610
    • Taylor, E.R.1    Hurrell, F.2    Shannon, R.J.3    Lin, T.K.4    Hirst, J.5    Murphy, M.P.6
  • 53
    • 0025269924 scopus 로고
    • Effects of the local anesthetic bupivacaine on oxidative phosphorylation in mitochondria. Change from decoupling to uncoupling by formation of a leakage type ion pathway specific for H+ in cooperation with hydrophobic anions
    • Terada H., Shima O., Yoshida K., Shinohara Y. Effects of the local anesthetic bupivacaine on oxidative phosphorylation in mitochondria. Change from decoupling to uncoupling by formation of a leakage type ion pathway specific for H+ in cooperation with hydrophobic anions. J. Biol. Chem. 1990, 265:7837-7842.
    • (1990) J. Biol. Chem. , vol.265 , pp. 7837-7842
    • Terada, H.1    Shima, O.2    Yoshida, K.3    Shinohara, Y.4
  • 54
    • 0014875911 scopus 로고
    • Effects of uncouplers of oxidative phosphorylation on the specific conductance of bimolecular lipid membranes
    • Ting H.P., Wilson D.F., Chance B. Effects of uncouplers of oxidative phosphorylation on the specific conductance of bimolecular lipid membranes. Arch. Biochem. Biophys. 1970, 141:141-146.
    • (1970) Arch. Biochem. Biophys. , vol.141 , pp. 141-146
    • Ting, H.P.1    Wilson, D.F.2    Chance, B.3
  • 55
    • 0142150051 scopus 로고    scopus 로고
    • Mitochondrial formation of reactive oxygen species
    • Turrens J.F. Mitochondrial formation of reactive oxygen species. J. Physiol. 2003, 552:335-344.
    • (2003) J. Physiol. , vol.552 , pp. 335-344
    • Turrens, J.F.1
  • 56
    • 0038124701 scopus 로고    scopus 로고
    • Biochemical and microarray analyses of bupivacaine-induced apoptosis
    • Unami A., Shinohara Y., Ichikawa T., Baba Y. Biochemical and microarray analyses of bupivacaine-induced apoptosis. J. Toxicol. Sci. 2003, 28:77-94.
    • (2003) J. Toxicol. Sci. , vol.28 , pp. 77-94
    • Unami, A.1    Shinohara, Y.2    Ichikawa, T.3    Baba, Y.4
  • 57
    • 0025685645 scopus 로고
    • Slipping pumps or proton leaks in oxidative phosphorylation. The local anesthetic bupivacaine causes slip in cytochrome c oxidase of mitochondria
    • van Dam K., Shinohara Y., Unami A., Yoshida K., Terada H. Slipping pumps or proton leaks in oxidative phosphorylation. The local anesthetic bupivacaine causes slip in cytochrome c oxidase of mitochondria. FEBS Lett. 1990, 277:131-133.
    • (1990) FEBS Lett. , vol.277 , pp. 131-133
    • van Dam, K.1    Shinohara, Y.2    Unami, A.3    Yoshida, K.4    Terada, H.5
  • 58
    • 0033795824 scopus 로고    scopus 로고
    • In vivo control of respiration by cytochrome c oxidase in human cells
    • Villani G., Attardi G. In vivo control of respiration by cytochrome c oxidase in human cells. Free Radical Biol. Med. 2000, 29:202-210.
    • (2000) Free Radical Biol. Med. , vol.29 , pp. 202-210
    • Villani, G.1    Attardi, G.2
  • 59
    • 17144366976 scopus 로고    scopus 로고
    • Generation of superoxide-radical by the NADH:ubiquinone oxidoreductase of heart mitochondria
    • Vinogradov A.D., Grivennikova V.G. Generation of superoxide-radical by the NADH:ubiquinone oxidoreductase of heart mitochondria. Biochemistry (Mosc) 2005, 70:120-127.
    • (2005) Biochemistry (Mosc) , vol.70 , pp. 120-127
    • Vinogradov, A.D.1    Grivennikova, V.G.2
  • 62


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.