메뉴 건너뛰기




Volumn 45, Issue 5, 2009, Pages 447-455

A comparison of Zn2+- and Ca2+-triggered depolarization of liver mitochondria reveals no evidence of Zn2+-induced permeability transition

Author keywords

Cyclosporine A; Intracellular calcium; Intracellular zinc; Mitochondrial transmembrane potential; Reactive oxygen species; Rhodamine 123

Indexed keywords

ADENOSINE DIPHOSPHATE; CALCEIN; CALCIUM ION; CYCLOSPORIN A; MAGNESIUM ION; RHODAMINE 123; ZINC ION; CALCIUM; CARRIER PROTEIN; CATION TRANSPORT PROTEIN; CYCLOSPORIN; ENZYME INHIBITOR; FLUORESCEIN DERIVATIVE; FLUORESCENT DYE; MITOCHONDRIAL PERMEABILITY TRANSITION PORE; RUTHENIUM RED; ZINC;

EID: 66949137119     PISSN: 01434160     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ceca.2009.03.002     Document Type: Article
Times cited : (27)

References (54)
  • 4
    • 0038637993 scopus 로고    scopus 로고
    • Zinc inhibition of cellular energy production: implications for mitochondria and neurodegeneration
    • Dineley K.E., Votyakova T.V., and Reynolds I.J. Zinc inhibition of cellular energy production: implications for mitochondria and neurodegeneration. Journal of Neurochemistry 85 (2003) 563-570
    • (2003) Journal of Neurochemistry , vol.85 , pp. 563-570
    • Dineley, K.E.1    Votyakova, T.V.2    Reynolds, I.J.3
  • 5
    • 9344254033 scopus 로고    scopus 로고
    • Nitrosative stress and potassium channel-mediated neuronal apoptosis: is zinc the link?
    • Pal S., He K., and Aizenman E. Nitrosative stress and potassium channel-mediated neuronal apoptosis: is zinc the link?. Pflugers Archiv-European Journal of Physiology 448 (2004) 296-303
    • (2004) Pflugers Archiv-European Journal of Physiology , vol.448 , pp. 296-303
    • Pal, S.1    He, K.2    Aizenman, E.3
  • 6
    • 1842536773 scopus 로고    scopus 로고
    • Rethinking the excitotoxic ionic milieu: the emerging role of Zn(2+) in ischemic neuronal injury
    • Sensi S.L., and Jeng J.M. Rethinking the excitotoxic ionic milieu: the emerging role of Zn(2+) in ischemic neuronal injury. Current Molecular Medicine 4 (2004) 87-111
    • (2004) Current Molecular Medicine , vol.4 , pp. 87-111
    • Sensi, S.L.1    Jeng, J.M.2
  • 7
    • 0343123179 scopus 로고
    • Inactivation of oxidative and phosphorylative systems in mitochondria by preincubation with phosphate and other ions
    • Hunter F.E., and Ford L. Inactivation of oxidative and phosphorylative systems in mitochondria by preincubation with phosphate and other ions. Journal of Biological Chemistry 216 (1955) 357-369
    • (1955) Journal of Biological Chemistry , vol.216 , pp. 357-369
    • Hunter, F.E.1    Ford, L.2
  • 10
    • 34548226964 scopus 로고    scopus 로고
    • Zinc irreversibly damages major enzymes of energy production and antioxidant defense prior to mitochondrial permeability transition
    • Gazaryan I.G., Krasinskaya I.P., Kristal B.S., and Brown A.M. Zinc irreversibly damages major enzymes of energy production and antioxidant defense prior to mitochondrial permeability transition. Journal of Biological Chemistry 282 (2007) 24373-24380
    • (2007) Journal of Biological Chemistry , vol.282 , pp. 24373-24380
    • Gazaryan, I.G.1    Krasinskaya, I.P.2    Kristal, B.S.3    Brown, A.M.4
  • 11
    • 0035861677 scopus 로고    scopus 로고
    • Zn(2+) induces permeability transition pore opening and release of pro-apoptotic peptides from neuronal mitochondria
    • Jiang D., Sullivan P.G., Sensi S.L., Steward O., and Weiss J.H. Zn(2+) induces permeability transition pore opening and release of pro-apoptotic peptides from neuronal mitochondria. Journal of Biological Chemistry 276 (2001) 47524-47529
    • (2001) Journal of Biological Chemistry , vol.276 , pp. 47524-47529
    • Jiang, D.1    Sullivan, P.G.2    Sensi, S.L.3    Steward, O.4    Weiss, J.H.5
  • 12
    • 34247549679 scopus 로고    scopus 로고
    • The mitochondrial permeability transition pore and its involvement in cell death and in disease pathogenesis
    • Rasola A., and Bernardi P. The mitochondrial permeability transition pore and its involvement in cell death and in disease pathogenesis. Apoptosis 12 (2007) 815-833
    • (2007) Apoptosis , vol.12 , pp. 815-833
    • Rasola, A.1    Bernardi, P.2
  • 13
    • 84900975500 scopus 로고    scopus 로고
    • Mitochondrial permeability transition in the CNS-composition, regulation, and pathophysiological relevance
    • Gibson G.E., and Diniel G. (Eds), Springer-Verlag, Heidelberg, Germany
    • Wieloch T., Mattiasson G., Hansson M.J., and Elmer E. Mitochondrial permeability transition in the CNS-composition, regulation, and pathophysiological relevance. In: Gibson G.E., and Diniel G. (Eds). Brain Energetics: Integration of Molecular and Cellular Processes vol. 5 (2007), Springer-Verlag, Heidelberg, Germany 667-702
    • (2007) Brain Energetics: Integration of Molecular and Cellular Processes , vol.5 , pp. 667-702
    • Wieloch, T.1    Mattiasson, G.2    Hansson, M.J.3    Elmer, E.4
  • 14
    • 0029116916 scopus 로고
    • The mitochondrial permeability transition
    • Zoratti M., and Szabo I. The mitochondrial permeability transition. Biochimica et Biophysica Acta 1241 (1995) 139-176
    • (1995) Biochimica et Biophysica Acta , vol.1241 , pp. 139-176
    • Zoratti, M.1    Szabo, I.2
  • 15
    • 85013719922 scopus 로고    scopus 로고
    • M.J. Devinney, L.M. Malaiyandi, O. Vergun, D.B. DeFranco, K.E. Dineley, Program 85.9. Zinc Does Not Cause Permeability Transition in Isolated Liver Mitochondria, Online, Society for Neuroscience, Atlanta, GA, 2006 (Abstract Viewer/Itinerary Planner).
    • M.J. Devinney, L.M. Malaiyandi, O. Vergun, D.B. DeFranco, K.E. Dineley, Program 85.9. Zinc Does Not Cause Permeability Transition in Isolated Liver Mitochondria, vol. Online, Society for Neuroscience, Atlanta, GA, 2006 (Abstract Viewer/Itinerary Planner).
  • 16
    • 23944497622 scopus 로고    scopus 로고
    • Distinct characteristics of Ca(2+)-induced depolarization of isolated brain and liver mitochondria
    • Vergun O., and Reynolds I.J. Distinct characteristics of Ca(2+)-induced depolarization of isolated brain and liver mitochondria. Biochimica et Biophysica Acta 1709 (2005) 127-137
    • (2005) Biochimica et Biophysica Acta , vol.1709 , pp. 127-137
    • Vergun, O.1    Reynolds, I.J.2
  • 17
    • 0034740585 scopus 로고    scopus 로고
    • DeltaPsi(m)-dependent and -independent production of reactive oxygen species by rat brain mitochondria
    • Votyakova T.V., and Reynolds I.J. DeltaPsi(m)-dependent and -independent production of reactive oxygen species by rat brain mitochondria. Journal of Neurochemistry 79 (2001) 266-277
    • (2001) Journal of Neurochemistry , vol.79 , pp. 266-277
    • Votyakova, T.V.1    Reynolds, I.J.2
  • 19
    • 20144370934 scopus 로고    scopus 로고
    • Direct visualization of mitochondrial zinc accumulation reveals uniporter-dependent and -independent transport mechanisms
    • Malaiyandi L.M., Vergun O., Dineley K.E., and Reynolds I.J. Direct visualization of mitochondrial zinc accumulation reveals uniporter-dependent and -independent transport mechanisms. Journal of Neurochemistry 93 (2005) 1242-1250
    • (2005) Journal of Neurochemistry , vol.93 , pp. 1242-1250
    • Malaiyandi, L.M.1    Vergun, O.2    Dineley, K.E.3    Reynolds, I.J.4
  • 20
    • 0033021780 scopus 로고    scopus 로고
    • Transient and long-lasting openings of the mitochondrial permeability transition pore can be monitored directly in intact cells by changes in mitochondrial calcein fluorescence
    • Petronilli V., Miotto G., Canton M., Brini M., Colonna R., Bernardi P., and Di Lisa F. Transient and long-lasting openings of the mitochondrial permeability transition pore can be monitored directly in intact cells by changes in mitochondrial calcein fluorescence. Biophysical Journal 76 (1999) 725-734
    • (1999) Biophysical Journal , vol.76 , pp. 725-734
    • Petronilli, V.1    Miotto, G.2    Canton, M.3    Brini, M.4    Colonna, R.5    Bernardi, P.6    Di Lisa, F.7
  • 21
    • 0018338308 scopus 로고
    • Preparation of synaptic and nonsynaptic mitochondria from mammalian brain
    • Lai J.C., and Clark J.B. Preparation of synaptic and nonsynaptic mitochondria from mammalian brain. Methods in Enzymology 55 (1979) 51-60
    • (1979) Methods in Enzymology , vol.55 , pp. 51-60
    • Lai, J.C.1    Clark, J.B.2
  • 22
    • 0037745119 scopus 로고    scopus 로고
    • Fluctuations in mitochondrial membrane potential caused by repetitive gating of the permeability transition pore.
    • Huser J., and Blatter L.A. Fluctuations in mitochondrial membrane potential caused by repetitive gating of the permeability transition pore. Biochemical Journal 343 Pt 2 (1999) 311-317
    • (1999) Biochemical Journal , vol.343 , Issue.PART 2 , pp. 311-317
    • Huser, J.1    Blatter, L.A.2
  • 23
    • 0038421272 scopus 로고    scopus 로고
    • Imaging the permeability pore transition in single mitochondria
    • Huser J., Rechenmacher C.E., and Blatter L.A. Imaging the permeability pore transition in single mitochondria. Biophysical Journal 74 (1998) 2129-2137
    • (1998) Biophysical Journal , vol.74 , pp. 2129-2137
    • Huser, J.1    Rechenmacher, C.E.2    Blatter, L.A.3
  • 25
    • 34547096752 scopus 로고    scopus 로고
    • Lithium desensitizes brain mitochondria to calcium, antagonizes permeability transition, and diminishes cytochrome C release
    • Shalbuyeva N., Brustovetsky T., and Brustovetsky N. Lithium desensitizes brain mitochondria to calcium, antagonizes permeability transition, and diminishes cytochrome C release. Journal of Biological Chemistry 282 (2007) 18057-18068
    • (2007) Journal of Biological Chemistry , vol.282 , pp. 18057-18068
    • Shalbuyeva, N.1    Brustovetsky, T.2    Brustovetsky, N.3
  • 26
    • 16344389388 scopus 로고    scopus 로고
    • Fluctuations in mitochondrial membrane potential in single isolated brain mitochondria: modulation by adenine nucleotides and Ca2+
    • Vergun O., and Reynolds I.J. Fluctuations in mitochondrial membrane potential in single isolated brain mitochondria: modulation by adenine nucleotides and Ca2+. Biophysical Journal 87 (2004) 3585-3593
    • (2004) Biophysical Journal , vol.87 , pp. 3585-3593
    • Vergun, O.1    Reynolds, I.J.2
  • 27
    • 0242290783 scopus 로고    scopus 로고
    • Spontaneous changes in mitochondrial membrane potential in single isolated brain mitochondria
    • Vergun O., Votyakova T.V., and Reynolds I.J. Spontaneous changes in mitochondrial membrane potential in single isolated brain mitochondria. Biophysical Journal 85 (2003) 3358-3366
    • (2003) Biophysical Journal , vol.85 , pp. 3358-3366
    • Vergun, O.1    Votyakova, T.V.2    Reynolds, I.J.3
  • 28
    • 0038143180 scopus 로고    scopus 로고
    • The relationship between free and total calcium concentrations in the matrix of liver and brain mitochondria
    • Chalmers S., and Nicholls D.G. The relationship between free and total calcium concentrations in the matrix of liver and brain mitochondria. Journal of Biological Chemistry 278 (2003) 19062-19070
    • (2003) Journal of Biological Chemistry , vol.278 , pp. 19062-19070
    • Chalmers, S.1    Nicholls, D.G.2
  • 29
  • 32
    • 0344069488 scopus 로고    scopus 로고
    • Zinc as an inducer of the membrane permeability transition in rat liver mitochondria
    • Wudarczyk J., Debska G., and Lenartowicz E. Zinc as an inducer of the membrane permeability transition in rat liver mitochondria. Archives of Biochemistry & Biophysics 363 (1999) 1-8
    • (1999) Archives of Biochemistry & Biophysics , vol.363 , pp. 1-8
    • Wudarczyk, J.1    Debska, G.2    Lenartowicz, E.3
  • 33
    • 13344259905 scopus 로고    scopus 로고
    • Zinc causes loss of membrane potential and elevates reactive oxygen species in rat brain mitochondria
    • Dineley K.E., Richards L.L., Votyakova T.V., and Reynolds I.J. Zinc causes loss of membrane potential and elevates reactive oxygen species in rat brain mitochondria. Mitochondrion 5 (2005) 55-65
    • (2005) Mitochondrion , vol.5 , pp. 55-65
    • Dineley, K.E.1    Richards, L.L.2    Votyakova, T.V.3    Reynolds, I.J.4
  • 34
    • 33845950074 scopus 로고    scopus 로고
    • The inhibition of mitochondrial complex I (NADH:ubiquinone oxidoreductase) by Zn2+
    • Sharpley M.S., and Hirst J. The inhibition of mitochondrial complex I (NADH:ubiquinone oxidoreductase) by Zn2+. Journal of Biological Chemistry 281 (2006) 34803-34809
    • (2006) Journal of Biological Chemistry , vol.281 , pp. 34803-34809
    • Sharpley, M.S.1    Hirst, J.2
  • 35
    • 0028808109 scopus 로고
    • Zinc ions inhibit the QP center of bovine heart mitochondrial bc1 complex by blocking a protonatable group
    • Link T.A., and von Jagow G. Zinc ions inhibit the QP center of bovine heart mitochondrial bc1 complex by blocking a protonatable group. Journal of Biological Chemistry 270 (1995) 25001-25006
    • (1995) Journal of Biological Chemistry , vol.270 , pp. 25001-25006
    • Link, T.A.1    von Jagow, G.2
  • 36
    • 33745607303 scopus 로고    scopus 로고
    • Inhibition of proton pumping by zinc ions during specific reaction steps in cytochrome c oxidase
    • Faxen K., Salomonsson L., Adelroth P., and Brzezinski P. Inhibition of proton pumping by zinc ions during specific reaction steps in cytochrome c oxidase. Biochimica et Biophysica Acta 1757 (2006) 388-394
    • (2006) Biochimica et Biophysica Acta , vol.1757 , pp. 388-394
    • Faxen, K.1    Salomonsson, L.2    Adelroth, P.3    Brzezinski, P.4
  • 39
    • 0032524880 scopus 로고    scopus 로고
    • Characterization of a plasma membrane zinc transporter in rat brain
    • Colvin R.A. Characterization of a plasma membrane zinc transporter in rat brain. Neuroscience Letters 247 (1998) 147-150
    • (1998) Neuroscience Letters , vol.247 , pp. 147-150
    • Colvin, R.A.1
  • 40
    • 0033597411 scopus 로고    scopus 로고
    • Nonproteolytic neuroprotection by human recombinant tissue plasminogen activator
    • Kim Y.H., Park J.H., Hong S.H., and Koh J.Y. Nonproteolytic neuroprotection by human recombinant tissue plasminogen activator. Science 284 (1999) 647-650
    • (1999) Science , vol.284 , pp. 647-650
    • Kim, Y.H.1    Park, J.H.2    Hong, S.H.3    Koh, J.Y.4
  • 41
    • 33751223540 scopus 로고    scopus 로고
    • Zinc-buffering capacity of a eukaryotic cell at physiological pZn
    • Krezel A., and Maret W. Zinc-buffering capacity of a eukaryotic cell at physiological pZn. Journal of Biological Inorganic Chemistry 11 (2006) 1049-1062
    • (2006) Journal of Biological Inorganic Chemistry , vol.11 , pp. 1049-1062
    • Krezel, A.1    Maret, W.2
  • 42
    • 0002639942 scopus 로고    scopus 로고
    • Measurement of intracellular free zinc concentrations accompanying zinc-induced neuronal death
    • Canzoniero L.M.T., Turetsky D.M., and Choi D.W. Measurement of intracellular free zinc concentrations accompanying zinc-induced neuronal death. Journal of Neuroscience 19 (1999) 1-6
    • (1999) Journal of Neuroscience , vol.19 , pp. 1-6
    • Canzoniero, L.M.T.1    Turetsky, D.M.2    Choi, D.W.3
  • 43
    • 0036765589 scopus 로고    scopus 로고
    • A reevaluation of neuronal zinc measurements: artifacts associated with high intracellular dye concentration
    • Dineley K.E., Malaiyandi L.M., and Reynolds I.J. A reevaluation of neuronal zinc measurements: artifacts associated with high intracellular dye concentration. Molecular Pharmacology 62 (2002) 618-627
    • (2002) Molecular Pharmacology , vol.62 , pp. 618-627
    • Dineley, K.E.1    Malaiyandi, L.M.2    Reynolds, I.J.3
  • 44
    • 0036774086 scopus 로고    scopus 로고
    • Elevated intracellular zinc and altered proton homeostasis in forebrain neurons
    • Dineley K.E., Brocard J.B., and Reynolds I.J. Elevated intracellular zinc and altered proton homeostasis in forebrain neurons. Neuroscience 114 (2002) 439-449
    • (2002) Neuroscience , vol.114 , pp. 439-449
    • Dineley, K.E.1    Brocard, J.B.2    Reynolds, I.J.3
  • 45
    • 0344820731 scopus 로고    scopus 로고
    • Mediation by membrane protein kinase C of zinc-induced oxidative neuronal injury in mouse cortical cultures
    • Noh K.M., Kim Y.H., and Koh J.Y. Mediation by membrane protein kinase C of zinc-induced oxidative neuronal injury in mouse cortical cultures. Journal of Neurochemistry 72 (1999) 1609-1616
    • (1999) Journal of Neurochemistry , vol.72 , pp. 1609-1616
    • Noh, K.M.1    Kim, Y.H.2    Koh, J.Y.3
  • 48
    • 0034535252 scopus 로고    scopus 로고
    • Quantitative biochemical and ultrastructural comparison of mitochondrial permeability transition in isolated brain and liver mitochondria: evidence for reduced sensitivity of brain mitochondria
    • Berman S.B., Watkins S.C., and Hastings T.G. Quantitative biochemical and ultrastructural comparison of mitochondrial permeability transition in isolated brain and liver mitochondria: evidence for reduced sensitivity of brain mitochondria. Experimental Neurology 164 (2000) 415-425
    • (2000) Experimental Neurology , vol.164 , pp. 415-425
    • Berman, S.B.1    Watkins, S.C.2    Hastings, T.G.3
  • 49
    • 0034668844 scopus 로고    scopus 로고
    • Limitations of cyclosporin A inhibition of the permeability transition in CNS mitochondria
    • Brustovetsky N., and Dubinsky J.M. Limitations of cyclosporin A inhibition of the permeability transition in CNS mitochondria. Journal of Neuroscience 20 (2000) 8229-8237
    • (2000) Journal of Neuroscience , vol.20 , pp. 8229-8237
    • Brustovetsky, N.1    Dubinsky, J.M.2
  • 50
    • 0033007651 scopus 로고    scopus 로고
    • Differences in the activation of the mitochondrial permeability transition among brain regions in the rat correlate with selective vulnerability
    • Friberg H., Connern C., Halestrap A.P., and Wieloch T. Differences in the activation of the mitochondrial permeability transition among brain regions in the rat correlate with selective vulnerability. Journal of Neurochemistry 72 (1999) 2488-2497
    • (1999) Journal of Neurochemistry , vol.72 , pp. 2488-2497
    • Friberg, H.1    Connern, C.2    Halestrap, A.P.3    Wieloch, T.4
  • 51
    • 0034663688 scopus 로고    scopus 로고
    • Crystallographic location of two Zn2+-binding sites in the avian cytochrome bc(1) complex
    • Berry E.A., Zhang Z., Bellamy H.D., and Huang L. Crystallographic location of two Zn2+-binding sites in the avian cytochrome bc(1) complex. Biochimica et Biophysica Acta 1459 (2000) 440-448
    • (2000) Biochimica et Biophysica Acta , vol.1459 , pp. 440-448
    • Berry, E.A.1    Zhang, Z.2    Bellamy, H.D.3    Huang, L.4
  • 52
    • 1642298968 scopus 로고    scopus 로고
    • Metallothionein can function as a chaperone for zinc uptake transport into prostate and liver mitochondria
    • Costello L.C., Guan Z., Franklin R.B., and Feng P. Metallothionein can function as a chaperone for zinc uptake transport into prostate and liver mitochondria. Journal of Inorganic Biochemistry 98 (2004) 664-666
    • (2004) Journal of Inorganic Biochemistry , vol.98 , pp. 664-666
    • Costello, L.C.1    Guan, Z.2    Franklin, R.B.3    Feng, P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.