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Volumn 218, Issue 2, 2009, Pages 203-212

Molecular participants in mitochondrial cell death channel formation during neuronal ischemia

Author keywords

Apoptosis; BCL 2; Brain ischemia; Ion channel; Mitochondria; Mitochondrial permeability transition; Programmed cell death; Synaptic transmission; VDAC

Indexed keywords

CALCIUM; CYTOCHROME C; ION CHANNEL; POTASSIUM; PROTEIN BAD; PROTEIN BCL 2; PROTEIN BCL XL; SODIUM; VOLTAGE DEPENDENT ANION CHANNEL; VOLTAGE DEPENDENT ANION CHANNEL 2; ZINC;

EID: 67649813198     PISSN: 00144886     EISSN: 10902430     Source Type: Journal    
DOI: 10.1016/j.expneurol.2009.03.025     Document Type: Review
Times cited : (45)

References (132)
  • 1
    • 33847328289 scopus 로고    scopus 로고
    • The Bcl-2 apoptotic switch in cancer development and therapy
    • Adams J.M., and Cory S. The Bcl-2 apoptotic switch in cancer development and therapy. Oncogene 26 (2007) 1324-1337
    • (2007) Oncogene , vol.26 , pp. 1324-1337
    • Adams, J.M.1    Cory, S.2
  • 2
    • 54049158483 scopus 로고    scopus 로고
    • Voltage-dependent anion channels (VDAC) in the plasma membrane play a critical role in apoptosis in differentiated hippocampal neurons but not in neural stem cells
    • Akanda N., Tofighi R., Brask J., Tamm C., Elinder F., and Ceccatelli S. Voltage-dependent anion channels (VDAC) in the plasma membrane play a critical role in apoptosis in differentiated hippocampal neurons but not in neural stem cells. Cell Cycle 7 (2008) 3225-3234
    • (2008) Cell Cycle , vol.7 , pp. 3225-3234
    • Akanda, N.1    Tofighi, R.2    Brask, J.3    Tamm, C.4    Elinder, F.5    Ceccatelli, S.6
  • 4
    • 0034650523 scopus 로고    scopus 로고
    • Bax oligomerization is required for channel-forming activity in liposomes and to trigger cytochrome c release from mitochondria
    • Antonsson B., Montessuit S., Lauper S., Eskes R., and Martinou J.C. Bax oligomerization is required for channel-forming activity in liposomes and to trigger cytochrome c release from mitochondria. Biochem. J. 345 Pt 2 (2000) 271-278
    • (2000) Biochem. J. , vol.345 , Issue.PART 2 , pp. 271-278
    • Antonsson, B.1    Montessuit, S.2    Lauper, S.3    Eskes, R.4    Martinou, J.C.5
  • 6
    • 34247895697 scopus 로고    scopus 로고
    • Voltage-dependent anion channels are dispensable for mitochondrial-dependent cell death. [see comment]
    • Baines C.P., Kaiser R.A., Sheiko T., Craigen W.J., and Molkentin J.D. Voltage-dependent anion channels are dispensable for mitochondrial-dependent cell death. [see comment]. Nat. Cell Biol. 9 (2007) 550-555
    • (2007) Nat. Cell Biol. , vol.9 , pp. 550-555
    • Baines, C.P.1    Kaiser, R.A.2    Sheiko, T.3    Craigen, W.J.4    Molkentin, J.D.5
  • 7
    • 0034739736 scopus 로고    scopus 로고
    • Mechanisms underlying hypoxia-induced neuronal apoptosis
    • Banasiak K.J., Xia Y., and Haddad G.G. Mechanisms underlying hypoxia-induced neuronal apoptosis. Prog. Neurobiol. 62 (2000) 215-249
    • (2000) Prog. Neurobiol. , vol.62 , pp. 215-249
    • Banasiak, K.J.1    Xia, Y.2    Haddad, G.G.3
  • 9
    • 0037147239 scopus 로고    scopus 로고
    • Bax-type apoptotic proteins porate pure lipid bilayers through a mechanism sensitive to intrinsic monolayer curvature
    • Basanez G., Sharpe J.C., Galanis J., Brandt T.B., Hardwick J.M., and Zimmerberg J. Bax-type apoptotic proteins porate pure lipid bilayers through a mechanism sensitive to intrinsic monolayer curvature. J. Biol. Chem. 277 (2002) 49360-49365
    • (2002) J. Biol. Chem. , vol.277 , pp. 49360-49365
    • Basanez, G.1    Sharpe, J.C.2    Galanis, J.3    Brandt, T.B.4    Hardwick, J.M.5    Zimmerberg, J.6
  • 10
    • 0026801183 scopus 로고
    • Modulation of the mitochondrial cyclosporin A-sensitive permeability transition pore by the proton electrochemical gradient. Evidence that the pore can be opened by membrane depolarization
    • Bernardi P. Modulation of the mitochondrial cyclosporin A-sensitive permeability transition pore by the proton electrochemical gradient. Evidence that the pore can be opened by membrane depolarization. J. Biol. Chem. 267 (1992) 8834-8839
    • (1992) J. Biol. Chem. , vol.267 , pp. 8834-8839
    • Bernardi, P.1
  • 11
    • 0032827410 scopus 로고    scopus 로고
    • Mitochondrial transport of cations: channels, exchangers, and permeability transition
    • Bernardi P. Mitochondrial transport of cations: channels, exchangers, and permeability transition. Physiol. Rev. 79 (1999) 1127-1155
    • (1999) Physiol. Rev. , vol.79 , pp. 1127-1155
    • Bernardi, P.1
  • 12
    • 0026687312 scopus 로고
    • Modulation of the mitochondrial permeability transition pore. Effect of protons and divalent cations
    • Bernardi P., Vassanelli S., Veronese P., Colonna R., Szabo I., and Zoratti M. Modulation of the mitochondrial permeability transition pore. Effect of protons and divalent cations. J. Biol. Chem. 267 (1992) 2934-2939
    • (1992) J. Biol. Chem. , vol.267 , pp. 2934-2939
    • Bernardi, P.1    Vassanelli, S.2    Veronese, P.3    Colonna, R.4    Szabo, I.5    Zoratti, M.6
  • 13
    • 0036093483 scopus 로고    scopus 로고
    • Persistent defect in transmitter release and synapsin phosphorylation in cerebral cortex after transient moderate ischemic injury. [see comment]
    • Bolay H., Gursoy-Ozdemir Y., Sara Y., Onur R., Can A., and Dalkara T. Persistent defect in transmitter release and synapsin phosphorylation in cerebral cortex after transient moderate ischemic injury. [see comment]. Stroke 33 (2002) 1369-1375
    • (2002) Stroke , vol.33 , pp. 1369-1375
    • Bolay, H.1    Gursoy-Ozdemir, Y.2    Sara, Y.3    Onur, R.4    Can, A.5    Dalkara, T.6
  • 17
    • 0036313059 scopus 로고    scopus 로고
    • Calcium-induced cytochrome c release from CNS mitochondria is associated with the permeability transition and rupture of the outer membrane
    • Brustovetsky N., Brustovetsky T., Jemmerson R., and Dubinsky J.M. Calcium-induced cytochrome c release from CNS mitochondria is associated with the permeability transition and rupture of the outer membrane. J. Neurochem. 80 (2002) 207-218
    • (2002) J. Neurochem. , vol.80 , pp. 207-218
    • Brustovetsky, N.1    Brustovetsky, T.2    Jemmerson, R.3    Dubinsky, J.M.4
  • 18
    • 0026074805 scopus 로고
    • Localization of the ATP/ADP translocator in the inner membrane and regulation of contact sites between mitochondrial envelope membranes by ADP. A study on freeze-fractured isolated liver mitochondria
    • Bucheler K., Adams V., and Brdiczka D. Localization of the ATP/ADP translocator in the inner membrane and regulation of contact sites between mitochondrial envelope membranes by ADP. A study on freeze-fractured isolated liver mitochondria. Biochim. Biophys. Acta 1056 (1991) 233-242
    • (1991) Biochim. Biophys. Acta , vol.1056 , pp. 233-242
    • Bucheler, K.1    Adams, V.2    Brdiczka, D.3
  • 19
    • 0030071252 scopus 로고    scopus 로고
    • A reevaluation of the role of mitochondria in neuronal Ca2+ homeostasis
    • Budd S.L., and Nicholls D.G. A reevaluation of the role of mitochondria in neuronal Ca2+ homeostasis. J. Neurochem. 66 (1996) 403-411
    • (1996) J. Neurochem. , vol.66 , pp. 403-411
    • Budd, S.L.1    Nicholls, D.G.2
  • 20
    • 0029827804 scopus 로고    scopus 로고
    • Mitochondria, calcium regulation, and acute glutamate excitotoxicity in cultured cerebellar granule cells
    • Budd S.L., and Nicholls D.G. Mitochondria, calcium regulation, and acute glutamate excitotoxicity in cultured cerebellar granule cells. J. Neurochem. 67 (1996) 2282-2291
    • (1996) J. Neurochem. , vol.67 , pp. 2282-2291
    • Budd, S.L.1    Nicholls, D.G.2
  • 21
    • 10844280686 scopus 로고    scopus 로고
    • Mitochondria and neuronal death/survival signaling pathways in cerebral ischemia
    • Chan P.H. Mitochondria and neuronal death/survival signaling pathways in cerebral ischemia. Neurochemical Research 29 (2004) 1943-1949
    • (2004) Neurochemical Research , vol.29 , pp. 1943-1949
    • Chan, P.H.1
  • 24
    • 0028642274 scopus 로고
    • Calcium and excitotoxic neuronal injury
    • Choi D.W. Calcium and excitotoxic neuronal injury. Ann. N. Y. Acad. Sci. 747 (1994) 162-171
    • (1994) Ann. N. Y. Acad. Sci. , vol.747 , pp. 162-171
    • Choi, D.W.1
  • 26
    • 0029685882 scopus 로고    scopus 로고
    • VDAC, a channel in the outer mitochondrial membrane
    • Colombini M., Blachly-Dyson E., and Forte M. VDAC, a channel in the outer mitochondrial membrane. Ion Channels 4 (1996) 169-202
    • (1996) Ion Channels , vol.4 , pp. 169-202
    • Colombini, M.1    Blachly-Dyson, E.2    Forte, M.3
  • 28
    • 0033565557 scopus 로고    scopus 로고
    • The mitochondrial permeability transition pore and its role in cell death
    • Crompton M. The mitochondrial permeability transition pore and its role in cell death. Biochem. J. 341 (1999) 233-249
    • (1999) Biochem. J. , vol.341 , pp. 233-249
    • Crompton, M.1
  • 29
    • 0032401567 scopus 로고    scopus 로고
    • Cyclophilin-D binds strongly to complexes of the voltage-dependent anion channel and the adenine nucleotide translocase to form the permeability transition pore
    • Crompton M., Virji S., and Ward J.M. Cyclophilin-D binds strongly to complexes of the voltage-dependent anion channel and the adenine nucleotide translocase to form the permeability transition pore. Eur. J. Biochem. 258 (1998) 729-735
    • (1998) Eur. J. Biochem. , vol.258 , pp. 729-735
    • Crompton, M.1    Virji, S.2    Ward, J.M.3
  • 32
    • 0035400014 scopus 로고    scopus 로고
    • Enhanced spontaneous transmitter release is the earliest consequence of neocortical hypoxia that can explain the disruption of normal circuit function
    • Fleidervish I.A., Gebhardt C., Astman N., Gutnick M.J., and Heinemann U. Enhanced spontaneous transmitter release is the earliest consequence of neocortical hypoxia that can explain the disruption of normal circuit function. J. Neurosci. 21 (2001) 4600-4608
    • (2001) J. Neurosci. , vol.21 , pp. 4600-4608
    • Fleidervish, I.A.1    Gebhardt, C.2    Astman, N.3    Gutnick, M.J.4    Heinemann, U.5
  • 33
    • 0032505124 scopus 로고    scopus 로고
    • Acceleration of apoptotic cell death after the cleavage of Bcl-XL protein by caspase-3-like proteases
    • Fujita N., Nagahashi A., Nagashima K., Rokudai S., and Tsuruo T. Acceleration of apoptotic cell death after the cleavage of Bcl-XL protein by caspase-3-like proteases. Oncogene 17 (1998) 1295-1304
    • (1998) Oncogene , vol.17 , pp. 1295-1304
    • Fujita, N.1    Nagahashi, A.2    Nagashima, K.3    Rokudai, S.4    Tsuruo, T.5
  • 34
    • 33751504957 scopus 로고    scopus 로고
    • Upgrading the BCL-2 network. [comment]
    • Galonek H.L., and Hardwick J.M. Upgrading the BCL-2 network. [comment]. Nat. Cell Biol. 8 (2006) 1317-1319
    • (2006) Nat. Cell Biol. , vol.8 , pp. 1317-1319
    • Galonek, H.L.1    Hardwick, J.M.2
  • 35
    • 33745763116 scopus 로고    scopus 로고
    • Cerebral preconditioning and ischaemic tolerance
    • Gidday J.M. Cerebral preconditioning and ischaemic tolerance. Nat. Rev. Neurosci. 7 (2006) 437-448
    • (2006) Nat. Rev. Neurosci. , vol.7 , pp. 437-448
    • Gidday, J.M.1
  • 36
    • 3442886811 scopus 로고    scopus 로고
    • The pathophysiology of mitochondrial cell death
    • Green D.R., and Kroemer G. The pathophysiology of mitochondrial cell death. Science 305 (2004) 626-629
    • (2004) Science , vol.305 , pp. 626-629
    • Green, D.R.1    Kroemer, G.2
  • 37
    • 0025292743 scopus 로고
    • Mechanisms by which mitochondria transport calcium
    • Gunter T.E., and Pfeiffer D.R. Mechanisms by which mitochondria transport calcium. Am. J. Physiol. 258 (1990) C755-C786
    • (1990) Am. J. Physiol. , vol.258
    • Gunter, T.E.1    Pfeiffer, D.R.2
  • 38
    • 0015517216 scopus 로고
    • States of activity and structure in mitochondrial membranes
    • Hackenbrock C.R. States of activity and structure in mitochondrial membranes. Ann. N. Y. Acad. Sci. 195 (1972) 492-505
    • (1972) Ann. N. Y. Acad. Sci. , vol.195 , pp. 492-505
    • Hackenbrock, C.R.1
  • 39
    • 0015144531 scopus 로고
    • Oxidative phosphorylation and ultrastructural transformation in mitochondria in the intact ascites tumor cell
    • Hackenbrock C.R., Rehn T.G., Weinbach E.C., and Lemasters J.J. Oxidative phosphorylation and ultrastructural transformation in mitochondria in the intact ascites tumor cell. J. Cell Biol. 51 (1971) 123-137
    • (1971) J. Cell Biol. , vol.51 , pp. 123-137
    • Hackenbrock, C.R.1    Rehn, T.G.2    Weinbach, E.C.3    Lemasters, J.J.4
  • 40
    • 15844404722 scopus 로고    scopus 로고
    • Biochemistry: a pore way to die. [comment]
    • Halestrap A. Biochemistry: a pore way to die. [comment]. Nature 434 (2005) 578-579
    • (2005) Nature , vol.434 , pp. 578-579
    • Halestrap, A.1
  • 41
    • 0034641918 scopus 로고    scopus 로고
    • The biochemistry of apoptosis. [see comment]
    • Hengartner M.O. The biochemistry of apoptosis. [see comment]. Nature 407 (2000) 770-776
    • (2000) Nature , vol.407 , pp. 770-776
    • Hengartner, M.O.1
  • 42
    • 40949143555 scopus 로고    scopus 로고
    • Bcl-xL inhibitor ABT-737 reveals a dual role for Bcl-xL in synaptic transmission
    • Hickman J.A., Hardwick J.M., Kaczmarek L.K., and Jonas E.A. Bcl-xL inhibitor ABT-737 reveals a dual role for Bcl-xL in synaptic transmission. J. Neurophysiol. 99 (2008) 1515-1522
    • (2008) J. Neurophysiol. , vol.99 , pp. 1515-1522
    • Hickman, J.A.1    Hardwick, J.M.2    Kaczmarek, L.K.3    Jonas, E.A.4
  • 43
    • 0032490646 scopus 로고    scopus 로고
    • Electrophysiological changes of CA3 neurons and dentate granule cells following transient forebrain ischemia
    • Howard E.M., Gao T.M., Pulsinelli W.A., and Xu Z.C. Electrophysiological changes of CA3 neurons and dentate granule cells following transient forebrain ischemia. Brain Res. 798 (1998) 109-118
    • (1998) Brain Res. , vol.798 , pp. 109-118
    • Howard, E.M.1    Gao, T.M.2    Pulsinelli, W.A.3    Xu, Z.C.4
  • 44
    • 0032562796 scopus 로고    scopus 로고
    • Bax in murine thymus is a soluble monomeric protein that displays differential detergent-induced conformations
    • Hsu Y.T., and Youle R.J. Bax in murine thymus is a soluble monomeric protein that displays differential detergent-induced conformations. J. Biol. Chem. 273 (1998) 10777-10783
    • (1998) J. Biol. Chem. , vol.273 , pp. 10777-10783
    • Hsu, Y.T.1    Youle, R.J.2
  • 45
    • 0021894480 scopus 로고
    • Nucleotide metabolism and cellular damage in myocardial ischemia
    • Jennings R.B., and Steenbergen Jr. C. Nucleotide metabolism and cellular damage in myocardial ischemia. Annu. Rev. Physiol. 47 (1985) 727-749
    • (1985) Annu. Rev. Physiol. , vol.47 , pp. 727-749
    • Jennings, R.B.1    Steenbergen Jr., C.2
  • 46
    • 10244246627 scopus 로고    scopus 로고
    • Regulation of synaptic transmission by mitochondrial ion channels
    • Jonas E. Regulation of synaptic transmission by mitochondrial ion channels. J. Bioenerg. Biomembr. 36 (2004) 357-361
    • (2004) J. Bioenerg. Biomembr. , vol.36 , pp. 357-361
    • Jonas, E.1
  • 47
    • 33749009587 scopus 로고    scopus 로고
    • BCL-xL regulates synaptic plasticity
    • Jonas E. BCL-xL regulates synaptic plasticity. Mol. Interv. 6 (2006) 208-222
    • (2006) Mol. Interv. , vol.6 , pp. 208-222
    • Jonas, E.1
  • 48
    • 0032698218 scopus 로고    scopus 로고
    • Prolonged activation of mitochondrial conductances during synaptic transmission
    • Jonas E.A., Buchanan J., and Kaczmarek L.K. Prolonged activation of mitochondrial conductances during synaptic transmission. Science 286 (1999) 1347-1350
    • (1999) Science , vol.286 , pp. 1347-1350
    • Jonas, E.A.1    Buchanan, J.2    Kaczmarek, L.K.3
  • 51
    • 24144493694 scopus 로고    scopus 로고
    • Actions of BAX on mitochondrial channel activity and on synaptic transmission
    • Jonas E.A., Hardwick J.M., and Kaczmarek L.K. Actions of BAX on mitochondrial channel activity and on synaptic transmission. Antioxid. Redox Signal. 7 (2005) 1092-1100
    • (2005) Antioxid. Redox Signal. , vol.7 , pp. 1092-1100
    • Jonas, E.A.1    Hardwick, J.M.2    Kaczmarek, L.K.3
  • 52
    • 14244251598 scopus 로고    scopus 로고
    • Exposure to hypoxia rapidly induces mitochondrial channel activity within a living synapse
    • Jonas E.A., Hickman J.A., Hardwick J.M., and Kaczmarek L.K. Exposure to hypoxia rapidly induces mitochondrial channel activity within a living synapse. J. Biol. Chem. 280 (2005) 4491-4497
    • (2005) J. Biol. Chem. , vol.280 , pp. 4491-4497
    • Jonas, E.A.1    Hickman, J.A.2    Hardwick, J.M.3    Kaczmarek, L.K.4
  • 53
    • 0037421190 scopus 로고    scopus 로고
    • Characterization of the signal that directs Bcl-x(L), but not Bcl-2, to the mitochondrial outer membrane
    • Kaufmann T., Schlipf S., Sanz J., Neubert K., Stein R., and Borner C. Characterization of the signal that directs Bcl-x(L), but not Bcl-2, to the mitochondrial outer membrane. J. Cell Biol. 160 (2003) 53-64
    • (2003) J. Cell Biol. , vol.160 , pp. 53-64
    • Kaufmann, T.1    Schlipf, S.2    Sanz, J.3    Neubert, K.4    Stein, R.5    Borner, C.6
  • 55
    • 0024433994 scopus 로고
    • Mitochondrial channel activity studied by patch-clamping mitoplasts
    • Kinnally K.W., Campo M.L., and Tedeschi H. Mitochondrial channel activity studied by patch-clamping mitoplasts. J. Bioenerg. Biomembr. 21 (1989) 497-506
    • (1989) J. Bioenerg. Biomembr. , vol.21 , pp. 497-506
    • Kinnally, K.W.1    Campo, M.L.2    Tedeschi, H.3
  • 57
  • 59
    • 1642540210 scopus 로고    scopus 로고
    • The mitochondrial calcium uniporter is a highly selective ion channel
    • Kirichok Y., Krapivinsky G., and Clapham D.E. The mitochondrial calcium uniporter is a highly selective ion channel. Nature 427 (2004) 360-364
    • (2004) Nature , vol.427 , pp. 360-364
    • Kirichok, Y.1    Krapivinsky, G.2    Clapham, D.E.3
  • 62
    • 0021111174 scopus 로고
    • Changes in freeze-fractured mitochondrial membranes correlated to their energetic state. Dynamic interactions of the boundary membranes
    • Knoll G., and Brdiczka D. Changes in freeze-fractured mitochondrial membranes correlated to their energetic state. Dynamic interactions of the boundary membranes. Biochim. Biophys. Acta 733 (1983) 102-110
    • (1983) Biochim. Biophys. Acta , vol.733 , pp. 102-110
    • Knoll, G.1    Brdiczka, D.2
  • 63
  • 64
    • 85047698632 scopus 로고    scopus 로고
    • Dynamics of expression of apoptosis-regulatory proteins Bid, Bcl-2, Bcl-X, Bax and Bak during development of murine nervous system
    • Krajewska M., Mai J.K., Zapata J.M., Ashwell K.W., Schendel S.L., Reed J.C., and Krajewski S. Dynamics of expression of apoptosis-regulatory proteins Bid, Bcl-2, Bcl-X, Bax and Bak during development of murine nervous system. Cell Death Differ. 9 (2002) 145-157
    • (2002) Cell Death Differ. , vol.9 , pp. 145-157
    • Krajewska, M.1    Mai, J.K.2    Zapata, J.M.3    Ashwell, K.W.4    Schendel, S.L.5    Reed, J.C.6    Krajewski, S.7
  • 65
    • 0034068601 scopus 로고    scopus 로고
    • Mitochondrial control of cell death
    • Kroemer G., and Reed J.C. Mitochondrial control of cell death. Nat. Med. 6 (2000) 513-519
    • (2000) Nat. Med. , vol.6 , pp. 513-519
    • Kroemer, G.1    Reed, J.C.2
  • 66
    • 0028172237 scopus 로고
    • Beta-NADH decreases the permeability of the mitochondrial outer membrane to ADP by a factor of 6
    • Lee A.C., Zizi M., and Colombini M. Beta-NADH decreases the permeability of the mitochondrial outer membrane to ADP by a factor of 6. J. Biol. Chem. 269 (1994) 30974-30980
    • (1994) J. Biol. Chem. , vol.269 , pp. 30974-30980
    • Lee, A.C.1    Zizi, M.2    Colombini, M.3
  • 67
    • 0033600277 scopus 로고    scopus 로고
    • The changing landscape of ischaemic brain injury mechanisms
    • Lee J.M., Zipfel G.J., and Choi D.W. The changing landscape of ischaemic brain injury mechanisms. Nature 399 (1999) A7-A14
    • (1999) Nature , vol.399
    • Lee, J.M.1    Zipfel, G.J.2    Choi, D.W.3
  • 68
    • 29344468832 scopus 로고    scopus 로고
    • Voltage-dependent anion channel. (VDAC) as mitochondrial governator-thinking outside the box
    • Lemasters J.J., and Holmuhamedov E. Voltage-dependent anion channel. (VDAC) as mitochondrial governator-thinking outside the box. Biochim. Biophys. Acta 1762 (2006) 181-190
    • (2006) Biochim. Biophys. Acta , vol.1762 , pp. 181-190
    • Lemasters, J.J.1    Holmuhamedov, E.2
  • 69
    • 0032555697 scopus 로고    scopus 로고
    • Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis
    • Li H., Zhu H., Xu C.J., and Yuan J. Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis. Cell 94 (1998) 491-501
    • (1998) Cell , vol.94 , pp. 491-501
    • Li, H.1    Zhu, H.2    Xu, C.J.3    Yuan, J.4
  • 70
    • 0034508217 scopus 로고    scopus 로고
    • The combined functions of proapoptotic Bcl-2 family members bak and bax are essential for normal development of multiple tissues
    • Lindsten T., et al. The combined functions of proapoptotic Bcl-2 family members bak and bax are essential for normal development of multiple tissues. Mol. Cell 6 (2000) 1389-1399
    • (2000) Mol. Cell , vol.6 , pp. 1389-1399
    • Lindsten, T.1
  • 71
    • 0032845121 scopus 로고    scopus 로고
    • Ischemic cell death in brain neurons
    • Lipton P. Ischemic cell death in brain neurons. Physiol. Rev. 79 (1999) 1431-1568
    • (1999) Physiol. Rev. , vol.79 , pp. 1431-1568
    • Lipton, P.1
  • 72
    • 0029024668 scopus 로고
    • Multiple conductance channel activity of wild-type and voltage-dependent anion-selective channel (VDAC)-less yeast mitochondria
    • Lohret T.A., and Kinnally K.W. Multiple conductance channel activity of wild-type and voltage-dependent anion-selective channel (VDAC)-less yeast mitochondria. Biophys. J. 68 (1995) 2299-2309
    • (1995) Biophys. J. , vol.68 , pp. 2299-2309
    • Lohret, T.A.1    Kinnally, K.W.2
  • 73
    • 0029981386 scopus 로고    scopus 로고
    • Activity of the mitochondrial multiple conductance channel is independent of the adenine nucleotide translocator
    • Lohret T.A., Murphy R.C., Drgon T., and Kinnally K.W. Activity of the mitochondrial multiple conductance channel is independent of the adenine nucleotide translocator. J. Biol. Chem. 271 (1996) 4846-4849
    • (1996) J. Biol. Chem. , vol.271 , pp. 4846-4849
    • Lohret, T.A.1    Murphy, R.C.2    Drgon, T.3    Kinnally, K.W.4
  • 74
    • 0032555716 scopus 로고    scopus 로고
    • Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors
    • Luo X., Budihardjo I., Zou H., Slaughter C., and Wang X. Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors. Cell 94 (1998) 481-490
    • (1998) Cell , vol.94 , pp. 481-490
    • Luo, X.1    Budihardjo, I.2    Zou, H.3    Slaughter, C.4    Wang, X.5
  • 75
    • 33846207499 scopus 로고    scopus 로고
    • NMR structural investigation of the mitochondrial outer membrane protein VDAC and its interaction with antiapoptotic Bcl-xL
    • Malia T.J., and Wagner G. NMR structural investigation of the mitochondrial outer membrane protein VDAC and its interaction with antiapoptotic Bcl-xL. Biochemistry 46 (2007) 514-525
    • (2007) Biochemistry , vol.46 , pp. 514-525
    • Malia, T.J.1    Wagner, G.2
  • 80
    • 36949083936 scopus 로고
    • Coupling of phosphorylation to electron and hydrogen transfer by a chemi-osmotic type of mechanism
    • Mitchell P. Coupling of phosphorylation to electron and hydrogen transfer by a chemi-osmotic type of mechanism. Nature 191 (1961) 144-148
    • (1961) Nature , vol.191 , pp. 144-148
    • Mitchell, P.1
  • 81
    • 0029949676 scopus 로고    scopus 로고
    • Attenuation of postischemic reperfusion injury is related to prevention of [Ca2+]m overload in rat hearts
    • Miyamae M., Camacho S.A., Weiner M.W., and Figueredo V.M. Attenuation of postischemic reperfusion injury is related to prevention of [Ca2+]m overload in rat hearts. Am. J. Physiol. 271 (1996) H2145-H2153
    • (1996) Am. J. Physiol. , vol.271
    • Miyamae, M.1    Camacho, S.A.2    Weiner, M.W.3    Figueredo, V.M.4
  • 83
    • 0025176934 scopus 로고
    • Electrophysiological characterization of contact sites in brain mitochondria. [erratum appears in J Biol Chem 1990 Jul 5;265(19):11405]
    • Moran O., Sandri G., Panfili E., Stuhmer W., and Sorgato M.C. Electrophysiological characterization of contact sites in brain mitochondria. [erratum appears in J Biol Chem 1990 Jul 5;265(19):11405]. J. Biol. Chem. 265 (1990) 908-913
    • (1990) J. Biol. Chem. , vol.265 , pp. 908-913
    • Moran, O.1    Sandri, G.2    Panfili, E.3    Stuhmer, W.4    Sorgato, M.C.5
  • 85
    • 15844407874 scopus 로고    scopus 로고
    • Cyclophilin D-dependent mitochondrial permeability transition regulates some necrotic but not apoptotic cell death. [see comment]
    • Nakagawa T., Shimizu S., Watanabe T., Yamaguchi O., Otsu K., Yamagata H., Inohara H., Kubo T., and Tsujimoto Y. Cyclophilin D-dependent mitochondrial permeability transition regulates some necrotic but not apoptotic cell death. [see comment]. Nature 434 (2005) 652-658
    • (2005) Nature , vol.434 , pp. 652-658
    • Nakagawa, T.1    Shimizu, S.2    Watanabe, T.3    Yamaguchi, O.4    Otsu, K.5    Yamagata, H.6    Inohara, H.7    Kubo, T.8    Tsujimoto, Y.9
  • 86
    • 1842430709 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and glutamate excitotoxicity studied in primary neuronal cultures
    • Nicholls D.G. Mitochondrial dysfunction and glutamate excitotoxicity studied in primary neuronal cultures. Curr. Mol. Med. 4 (2004) 149-177
    • (2004) Curr. Mol. Med. , vol.4 , pp. 149-177
    • Nicholls, D.G.1
  • 87
    • 10244257617 scopus 로고    scopus 로고
    • The integration of mitochondrial calcium transport and storage
    • Nicholls D.G., and Chalmers S. The integration of mitochondrial calcium transport and storage. J. Bioenerg. Biomembr. 36 (2004) 277-281
    • (2004) J. Bioenerg. Biomembr. , vol.36 , pp. 277-281
    • Nicholls, D.G.1    Chalmers, S.2
  • 88
    • 0035876476 scopus 로고    scopus 로고
    • Glutamate release and neuronal damage in ischemia
    • Nishizawa Y. Glutamate release and neuronal damage in ischemia. Life Sci. 69 (2001) 369-381
    • (2001) Life Sci. , vol.69 , pp. 369-381
    • Nishizawa, Y.1
  • 89
    • 0035869339 scopus 로고    scopus 로고
    • Delayed neurodegeneration in neonatal rat thalamus after hypoxia-ischemia is apoptosis
    • Northington F.J., Ferriero D.M., Flock D.L., and Martin L.J. Delayed neurodegeneration in neonatal rat thalamus after hypoxia-ischemia is apoptosis. J. Neurosci. 21 (2001) 1931-1938
    • (2001) J. Neurosci. , vol.21 , pp. 1931-1938
    • Northington, F.J.1    Ferriero, D.M.2    Flock, D.L.3    Martin, L.J.4
  • 90
    • 33947388409 scopus 로고    scopus 로고
    • Mitochondrial ion channels
    • O'Rourke B. Mitochondrial ion channels. Annu. Rev. Physiol. 69 (2007) 19-49
    • (2007) Annu. Rev. Physiol. , vol.69 , pp. 19-49
    • O'Rourke, B.1
  • 91
    • 20444486559 scopus 로고    scopus 로고
    • An inhibitor of Bcl-2 family proteins induces regression of solid tumours
    • Oltersdorf T., et al. An inhibitor of Bcl-2 family proteins induces regression of solid tumours. Nature 435 (2005) 677-681
    • (2005) Nature , vol.435 , pp. 677-681
    • Oltersdorf, T.1
  • 92
    • 0033503975 scopus 로고    scopus 로고
    • Survival- and death-promoting events after transient cerebral ischemia: phosphorylation of Akt, release of cytochrome C and Activation of caspase-like proteases
    • Ouyang Y.B., Tan Y., Comb M., Liu C.L., Martone M.E., Siesjo B.K., and Hu B.R. Survival- and death-promoting events after transient cerebral ischemia: phosphorylation of Akt, release of cytochrome C and Activation of caspase-like proteases. J. Cereb. Blood Flow Metab. 19 (1999) 1126-1135
    • (1999) J. Cereb. Blood Flow Metab. , vol.19 , pp. 1126-1135
    • Ouyang, Y.B.1    Tan, Y.2    Comb, M.3    Liu, C.L.4    Martone, M.E.5    Siesjo, B.K.6    Hu, B.R.7
  • 95
    • 0024787657 scopus 로고
    • The inner mitochondrial membrane contains ion-conducting channels similar to those found in bacteria
    • Petronilli V., Szabo I., and Zoratti M. The inner mitochondrial membrane contains ion-conducting channels similar to those found in bacteria. FEBS Lett. 259 (1989) 137-143
    • (1989) FEBS Lett. , vol.259 , pp. 137-143
    • Petronilli, V.1    Szabo, I.2    Zoratti, M.3
  • 96
    • 27844526600 scopus 로고    scopus 로고
    • Akt-dependent transformation: there is more to growth than just surviving
    • Plas D.R., and Thompson C.B. Akt-dependent transformation: there is more to growth than just surviving. Oncogene 24 (2005) 7435-7442
    • (2005) Oncogene , vol.24 , pp. 7435-7442
    • Plas, D.R.1    Thompson, C.B.2
  • 97
    • 0035853833 scopus 로고    scopus 로고
    • Akt and Bcl-xL promote growth factor-independent survival through distinct effects on mitochondrial physiology
    • Plas D.R., Talapatra S., Edinger A.L., Rathmell J.C., and Thompson C.B. Akt and Bcl-xL promote growth factor-independent survival through distinct effects on mitochondrial physiology. J. Biol. Chem. 276 (2001) 12041-12048
    • (2001) J. Biol. Chem. , vol.276 , pp. 12041-12048
    • Plas, D.R.1    Talapatra, S.2    Edinger, A.L.3    Rathmell, J.C.4    Thompson, C.B.5
  • 99
    • 4544298249 scopus 로고    scopus 로고
    • Mitochondrial mechanisms of neural cell apoptosis
    • Polster B.M., and Fiskum G. Mitochondrial mechanisms of neural cell apoptosis. J. Neurochem. 90 (2004) 1281-1289
    • (2004) J. Neurochem. , vol.90 , pp. 1281-1289
    • Polster, B.M.1    Fiskum, G.2
  • 100
    • 0035851110 scopus 로고    scopus 로고
    • BH3 death domain peptide induces cell type-selective mitochondrial outer membrane permeability
    • Polster B.M., Kinnally K.W., and Fiskum G. BH3 death domain peptide induces cell type-selective mitochondrial outer membrane permeability. J. Biol. Chem. 276 (2001) 37887-37894
    • (2001) J. Biol. Chem. , vol.276 , pp. 37887-37894
    • Polster, B.M.1    Kinnally, K.W.2    Fiskum, G.3
  • 101
    • 0242500310 scopus 로고    scopus 로고
    • Inhibition of Bax-induced cytochrome c release from neural cell and brain mitochondria by dibucaine and propranolol
    • Polster B.M., Basanez G., Young M., Suzuki M., and Fiskum G. Inhibition of Bax-induced cytochrome c release from neural cell and brain mitochondria by dibucaine and propranolol. J. Neurosci. 23 (2003) 2735-2743
    • (2003) J. Neurosci. , vol.23 , pp. 2735-2743
    • Polster, B.M.1    Basanez, G.2    Young, M.3    Suzuki, M.4    Fiskum, G.5
  • 102
    • 0033400517 scopus 로고    scopus 로고
    • Mitochondrial membrane potential and the permeability transition in excitotoxicity
    • Reynolds I.J. Mitochondrial membrane potential and the permeability transition in excitotoxicity. Ann. N. Y. Acad. Sci. 893 (1999) 33-41
    • (1999) Ann. N. Y. Acad. Sci. , vol.893 , pp. 33-41
    • Reynolds, I.J.1
  • 103
    • 0030947935 scopus 로고    scopus 로고
    • VDAC channels mediate and gate the flow of ATP: implications for the regulation of mitochondrial function
    • Rostovtseva T., and Colombini M. VDAC channels mediate and gate the flow of ATP: implications for the regulation of mitochondrial function. Biophys. J. 72 (1997) 1954-1962
    • (1997) Biophys. J. , vol.72 , pp. 1954-1962
    • Rostovtseva, T.1    Colombini, M.2
  • 105
    • 0037115740 scopus 로고    scopus 로고
    • Bax oligomerization in mitochondrial membranes requires tBid (caspase-8-cleaved Bid) and a mitochondrial protein
    • Roucou X., Montessuit S., Antonsson B., and Martinou J.C. Bax oligomerization in mitochondrial membranes requires tBid (caspase-8-cleaved Bid) and a mitochondrial protein. Biochem. J. 368 (2002) 915-921
    • (2002) Biochem. J. , vol.368 , pp. 915-921
    • Roucou, X.1    Montessuit, S.2    Antonsson, B.3    Martinou, J.C.4
  • 106
    • 0024059187 scopus 로고
    • Influence of Ca2+ on the isolation from rat brain mitochondria of a fraction enriched of boundary membrane contact sites
    • Sandri G., Siagri M., and Panfili E. Influence of Ca2+ on the isolation from rat brain mitochondria of a fraction enriched of boundary membrane contact sites. Cell Calcium 9 (1988) 159-165
    • (1988) Cell Calcium , vol.9 , pp. 159-165
    • Sandri, G.1    Siagri, M.2    Panfili, E.3
  • 107
    • 0034023864 scopus 로고    scopus 로고
    • Molecular mechanisms of calcium-dependent excitotoxicity
    • Sattler R., and Tymianski M. Molecular mechanisms of calcium-dependent excitotoxicity. J. Mol. Med. 78 (2000) 3-13
    • (2000) J. Mol. Med. , vol.78 , pp. 3-13
    • Sattler, R.1    Tymianski, M.2
  • 110
    • 0030995428 scopus 로고    scopus 로고
    • On the voltage dependence of the mitochondrial permeability transition pore. A critical appraisal
    • Scorrano L., Petronilli V., and Bernardi P. On the voltage dependence of the mitochondrial permeability transition pore. A critical appraisal. J. Biol. Chem. 272 (1997) 12295-12299
    • (1997) J. Biol. Chem. , vol.272 , pp. 12295-12299
    • Scorrano, L.1    Petronilli, V.2    Bernardi, P.3
  • 112
    • 0037199456 scopus 로고    scopus 로고
    • Peptides derived from BH3 domains of Bcl-2 family members: a comparative analysis of inhibition of Bcl-2, Bcl-x(L) and Bax oligomerization, induction of cytochrome c release, and activation of cell death
    • Shangary S., and Johnson D.E. Peptides derived from BH3 domains of Bcl-2 family members: a comparative analysis of inhibition of Bcl-2, Bcl-x(L) and Bax oligomerization, induction of cytochrome c release, and activation of cell death. Biochemistry 41 (2002) 9485-9495
    • (2002) Biochemistry , vol.41 , pp. 9485-9495
    • Shangary, S.1    Johnson, D.E.2
  • 113
    • 33745136102 scopus 로고    scopus 로고
    • The voltage-dependent anion channel (VDAC): function in intracellular signalling, cell life and cell death
    • Shoshan-Barmatz V., Israelson A., Brdiczka D., and Sheu S.S. The voltage-dependent anion channel (VDAC): function in intracellular signalling, cell life and cell death. Curr. Pharm. Des. 12 (2006) 2249-2270
    • (2006) Curr. Pharm. Des. , vol.12 , pp. 2249-2270
    • Shoshan-Barmatz, V.1    Israelson, A.2    Brdiczka, D.3    Sheu, S.S.4
  • 114
    • 0015489943 scopus 로고
    • Solution of the problem of energy coupling in terms of chemiosmotic theory
    • Skulachev V.P. Solution of the problem of energy coupling in terms of chemiosmotic theory. J. Bioenerg. 3 (1972) 25-38
    • (1972) J. Bioenerg. , vol.3 , pp. 25-38
    • Skulachev, V.P.1
  • 115
    • 0033570503 scopus 로고    scopus 로고
    • Mitochondrial release of cytochrome c corresponds to the selective vulnerability of hippocampal CA1 neurons in rats after transient global cerebral ischemia
    • Sugawara T., Fujimura M., Morita-Fujimura Y., Kawase M., and Chan P.H. Mitochondrial release of cytochrome c corresponds to the selective vulnerability of hippocampal CA1 neurons in rats after transient global cerebral ischemia. J. Neurosci. 19 (1999) RC39
    • (1999) J. Neurosci. , vol.19
    • Sugawara, T.1    Fujimura, M.2    Morita-Fujimura, Y.3    Kawase, M.4    Chan, P.H.5
  • 117
    • 0025905910 scopus 로고
    • The giant channel of the inner mitochondrial membrane is inhibited by cyclosporin A
    • Szabo I., and Zoratti M. The giant channel of the inner mitochondrial membrane is inhibited by cyclosporin A. J. Biol. Chem. 266 (1991) 3376-3379
    • (1991) J. Biol. Chem. , vol.266 , pp. 3376-3379
    • Szabo, I.1    Zoratti, M.2
  • 118
    • 0026550587 scopus 로고
    • The mitochondrial megachannel is the permeability transition pore
    • Szabo I., and Zoratti M. The mitochondrial megachannel is the permeability transition pore. J. Bioenerg. Biomembr. 24 (1992) 111-117
    • (1992) J. Bioenerg. Biomembr. , vol.24 , pp. 111-117
    • Szabo, I.1    Zoratti, M.2
  • 119
    • 0026703122 scopus 로고
    • Modulation of the mitochondrial megachannel by divalent cations and protons
    • Szabo I., Bernardi P., and Zoratti M. Modulation of the mitochondrial megachannel by divalent cations and protons. J. Biol. Chem. 267 (1992) 2940-2946
    • (1992) J. Biol. Chem. , vol.267 , pp. 2940-2946
    • Szabo, I.1    Bernardi, P.2    Zoratti, M.3
  • 121
    • 0023395489 scopus 로고
    • Channels in the mitochondrial outer membrane: evidence from patch clamp studies
    • Tedeschi H., and Kinnally K.W. Channels in the mitochondrial outer membrane: evidence from patch clamp studies. J. Bioenerg. Biomembr. 19 (1987) 321-327
    • (1987) J. Bioenerg. Biomembr. , vol.19 , pp. 321-327
    • Tedeschi, H.1    Kinnally, K.W.2
  • 122
  • 123
    • 0034036504 scopus 로고    scopus 로고
    • Glycolysis prevents anoxia-induced synaptic transmission damage in rat hippocampal slices
    • Tian G.F., and Baker A.J. Glycolysis prevents anoxia-induced synaptic transmission damage in rat hippocampal slices. J. Neurophysiol. 83 (2000) 1830-1839
    • (2000) J. Neurophysiol. , vol.83 , pp. 1830-1839
    • Tian, G.F.1    Baker, A.J.2
  • 124
    • 0034525413 scopus 로고    scopus 로고
    • VDAC regulation by the Bcl-2 family of proteins
    • Tsujimoto Y., and Shimizu S. VDAC regulation by the Bcl-2 family of proteins. Cell Death Differ. 7 (2000) 1174-1181
    • (2000) Cell Death Differ. , vol.7 , pp. 1174-1181
    • Tsujimoto, Y.1    Shimizu, S.2
  • 125
    • 0038445395 scopus 로고    scopus 로고
    • Apoptotic insults impair Na+, K+-ATPase activity as a mechanism of neuronal death mediated by concurrent ATP deficiency and oxidant stress
    • Wang X.Q., Xiao A.Y., Sheline C., Hyrc K., Yang A., Goldberg M.P., Choi D.W., and Yu S.P. Apoptotic insults impair Na+, K+-ATPase activity as a mechanism of neuronal death mediated by concurrent ATP deficiency and oxidant stress. J. Cell Sci. 116 (2003) 2099-2110
    • (2003) J. Cell Sci. , vol.116 , pp. 2099-2110
    • Wang, X.Q.1    Xiao, A.Y.2    Sheline, C.3    Hyrc, K.4    Yang, A.5    Goldberg, M.P.6    Choi, D.W.7    Yu, S.P.8
  • 127
    • 0034193138 scopus 로고    scopus 로고
    • Cleavage of Bax enhances its cell death function
    • Wood D.E., and Newcomb E.W. Cleavage of Bax enhances its cell death function. Exp. Cell Res. 256 (2000) 375-382
    • (2000) Exp. Cell Res. , vol.256 , pp. 375-382
    • Wood, D.E.1    Newcomb, E.W.2
  • 128
    • 0025772895 scopus 로고
    • Patch clamping VDAC in liposomes containing whole mitochondrial membranes
    • Wunder U.R., and Colombini M. Patch clamping VDAC in liposomes containing whole mitochondrial membranes. J. Membr. Biol. 123 (1991) 83-91
    • (1991) J. Membr. Biol. , vol.123 , pp. 83-91
    • Wunder, U.R.1    Colombini, M.2
  • 130
    • 37549048249 scopus 로고    scopus 로고
    • The BCL-2 protein family: opposing activities that mediate cell death
    • Youle R.J., and Strasser A. The BCL-2 protein family: opposing activities that mediate cell death. Nat. Rev. Mol. Cell Biol. 9 (2008) 47-59
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 47-59
    • Youle, R.J.1    Strasser, A.2
  • 131
    • 0030584088 scopus 로고    scopus 로고
    • Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not BCL-X(L) [see comment]
    • Zha J., Harada H., Yang E., Jockel J., and Korsmeyer S.J. Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not BCL-X(L) [see comment]. Cell 87 (1996) 619-628
    • (1996) Cell , vol.87 , pp. 619-628
    • Zha, J.1    Harada, H.2    Yang, E.3    Jockel, J.4    Korsmeyer, S.J.5
  • 132
    • 44449176302 scopus 로고    scopus 로고
    • Mohr J., Choi D., Grotta J., Weir B., and Wolf P. (Eds), Churchill Livingstone, Philadelphia
    • Zukin R.S. In: Mohr J., Choi D., Grotta J., Weir B., and Wolf P. (Eds). Stroke (2004), Churchill Livingstone, Philadelphia 829-854
    • (2004) Stroke , pp. 829-854
    • Zukin, R.S.1


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