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Volumn 19, Issue 15, 1999, Pages 6235-6247

Caspase-dependent and -independent death of camptothecin-treated embryonic cortical neurons

Author keywords

Apoptosis; Cell cycle; Cytochrome c; DNA damage; Mitochondria; Transmembrane potential

Indexed keywords

CAMPTOTHECIN; CASPASE; CASPASE INHIBITOR; CYTOCHROME C; FLAVOPIRIDOL; OLOMOUCINE;

EID: 0033178444     PISSN: 02706474     EISSN: None     Source Type: Journal    
DOI: 10.1523/jneurosci.19-15-06235.1999     Document Type: Article
Times cited : (198)

References (48)
  • 1
    • 0027270211 scopus 로고
    • Characterization of the cellular reduction of 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT): Subcellular localization, substrate dependence, and involvement of mitochondrial electron transport in MTT reduction
    • Berridge MV, Tan AS (1993) Characterization of the cellular reduction of 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT): subcellular localization, substrate dependence, and involvement of mitochondrial electron transport in MTT reduction. Arch Biochem Biophys 303:474-482.
    • (1993) Arch Biochem Biophys , vol.303 , pp. 474-482
    • Berridge, M.V.1    Tan, A.S.2
  • 2
    • 0032472329 scopus 로고    scopus 로고
    • Mitochondrial cytochrome c release in apoptosis occurs upstream of DEVD-specific caspase activation and independently of mitochondrial transmembrane depolarization
    • Bossy-Wetzel E, Newmeyer DD, Green DR (1998) Mitochondrial cytochrome c release in apoptosis occurs upstream of DEVD-specific caspase activation and independently of mitochondrial transmembrane depolarization. EMBO J 17:39-47.
    • (1998) EMBO J , vol.17 , pp. 39-47
    • Bossy-Wetzel, E.1    Newmeyer, D.D.2    Green, D.R.3
  • 3
    • 0017184389 scopus 로고
    • A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein dye-binding
    • Bradford MM (1976) A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein dye-binding. Anal Biochem 72:248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 4
    • 0032192529 scopus 로고    scopus 로고
    • Evidence of a novel event during neuronal death: Development of competence-to-die in response to cytoplasmic cytochrome c
    • Deshmukh M, Johnson Jr EM (1998) Evidence of a novel event during neuronal death: development of competence-to-die in response to cytoplasmic cytochrome c. Neuron 21:695-705.
    • (1998) Neuron , vol.21 , pp. 695-705
    • Deshmukh, M.1    Johnson E.M., Jr.2
  • 5
    • 0030458720 scopus 로고    scopus 로고
    • Genetic and metabolic status of NGF-deprived sympathetic neurons saved by an inhibitor of the ICE family
    • Deshmukh M, Vasilakos J, Deckwerth TL, Lampe PA, Shivers BD, Johnson Jr EM (1996) Genetic and metabolic status of NGF-deprived sympathetic neurons saved by an inhibitor of the ICE family. J Cell Biol 135:1341-1354.
    • (1996) J Cell Biol , vol.135 , pp. 1341-1354
    • Deshmukh, M.1    Vasilakos, J.2    Deckwerth, T.L.3    Lampe, P.A.4    Shivers, B.D.5    Johnson E.M., Jr.6
  • 6
    • 0019121308 scopus 로고
    • Effect of striatal cells on in vitro maturation of mesencephalic dopaminergic neurones grown in serum-free conditions
    • Di Porzio U, Daguet MC, Glowinski J, Prochiantz A (1980) Effect of striatal cells on in vitro maturation of mesencephalic dopaminergic neurones grown in serum-free conditions. Nature 288:370-373.
    • (1980) Nature , vol.288 , pp. 370-373
    • Di Porzio, U.1    Daguet, M.C.2    Glowinski, J.3    Prochiantz, A.4
  • 7
    • 0030915587 scopus 로고    scopus 로고
    • Intracellular ATP levels determine cell death fate by apoptosis or necrosis
    • Eguchi Y, Shimizu S, Tsujimoto Y (1997) Intracellular ATP levels determine cell death fate by apoptosis or necrosis. Cancer Res 57:1835-1840.
    • (1997) Cancer Res , vol.57 , pp. 1835-1840
    • Eguchi, Y.1    Shimizu, S.2    Tsujimoto, Y.3
  • 8
    • 0029972440 scopus 로고    scopus 로고
    • Cell cycle blockers mimosine, ciclopirox and deferoxamine prevent the death of PC12 cells and postmitotic sympathetic neurons after removal of trophic support
    • Farinelli SE, Greene LA (1996) Cell cycle blockers mimosine, ciclopirox and deferoxamine prevent the death of PC12 cells and postmitotic sympathetic neurons after removal of trophic support. J Neurosci 16:1150-1162.
    • (1996) J Neurosci , vol.16 , pp. 1150-1162
    • Farinelli, S.E.1    Greene, L.A.2
  • 9
    • 0032528153 scopus 로고    scopus 로고
    • Neuroprotective actions of dipyridamole on cultured CNS neurons
    • Farinelli SE, Greene LA, Friedman WJ (1998) Neuroprotective actions of dipyridamole on cultured CNS neurons. J Neurosci 18:5112-5123.
    • (1998) J Neurosci , vol.18 , pp. 5112-5123
    • Farinelli, S.E.1    Greene, L.A.2    Friedman, W.J.3
  • 10
    • 0029995766 scopus 로고    scopus 로고
    • A license to kill
    • Fraser A, Evan G (1996) A license to kill. Cell 85:781-784.
    • (1996) Cell , vol.85 , pp. 781-784
    • Fraser, A.1    Evan, G.2
  • 12
    • 0031975026 scopus 로고    scopus 로고
    • Response of postmitotic neurons to X-irradiation: Implications for the role of DNA damage in neuronal apoptosis
    • Gobbel GT, Bellinzona M, Vogt AR, Gupta N, Fike JR, Chan PH (1998) Response of postmitotic neurons to X-irradiation: implications for the role of DNA damage in neuronal apoptosis. J Neurosci 18:147-155.
    • (1998) J Neurosci , vol.18 , pp. 147-155
    • Gobbel, G.T.1    Bellinzona, M.2    Vogt, A.R.3    Gupta, N.4    Fike, J.R.5    Chan, P.H.6
  • 13
    • 0032544268 scopus 로고    scopus 로고
    • Apoptotic pathways: The roads to ruin
    • Green DR (1998) Apoptotic pathways: the roads to ruin. Cell 94:695-698.
    • (1998) Cell , vol.94 , pp. 695-698
    • Green, D.R.1
  • 14
    • 0032404536 scopus 로고    scopus 로고
    • The central executioners of apoptosis: Caspases or mitochondria?
    • Green DR, Kroemer G (1998) The central executioners of apoptosis: caspases or mitochondria? Trends Cell Biol 8:267-271.
    • (1998) Trends Cell Biol , vol.8 , pp. 267-271
    • Green, D.R.1    Kroemer, G.2
  • 15
    • 0032575752 scopus 로고    scopus 로고
    • Mitochondria and apoptosis
    • Green DR, Reed JC (1998) Mitochondria and apoptosis. Science 281:1309-1312.
    • (1998) Science , vol.281 , pp. 1309-1312
    • Green, D.R.1    Reed, J.C.2
  • 16
    • 0031921562 scopus 로고    scopus 로고
    • Commitment and effector phases of the physiological cell death pathway elucidated with respect to Bcl-2, caspase, and cyclin-dependent kinase activities
    • Harvey KJ, Blomquist JF, Ucker DS (1998) Commitment and effector phases of the physiological cell death pathway elucidated with respect to Bcl-2, caspase, and cyclin-dependent kinase activities. Mol Cell Biol 18:2912-2922.
    • (1998) Mol Cell Biol , vol.18 , pp. 2912-2922
    • Harvey, K.J.1    Blomquist, J.F.2    Ucker, D.S.3
  • 17
    • 17544394927 scopus 로고
    • β-Amyloid inhibition of MTT reduction is not mimicked by inhibitors of mitochondrial respiration
    • Hawtin SR, Dobbins AC, Vipula JT, Shearman MS (1995) β-Amyloid inhibition of MTT reduction is not mimicked by inhibitors of mitochondrial respiration. Biochem Soc Trans 23:56S.
    • (1995) Biochem Soc Trans , vol.23
    • Hawtin, S.R.1    Dobbins, A.C.2    Vipula, J.T.3    Shearman, M.S.4
  • 18
    • 0030698810 scopus 로고    scopus 로고
    • The apoptosis-necrosis paradox. Apoptogenic proteases activated after mitochondrial permeability transition determine the mode of cell death
    • Hirsch T, Marchetti P, Susin SA, Dallaporta B, Zamzami N, Marzo I, Geuskens M, Kroemer G (1997) The apoptosis-necrosis paradox. Apoptogenic proteases activated after mitochondrial permeability transition determine the mode of cell death. Oncogene 15:1573-1582.
    • (1997) Oncogene , vol.15 , pp. 1573-1582
    • Hirsch, T.1    Marchetti, P.2    Susin, S.A.3    Dallaporta, B.4    Zamzami, N.5    Marzo, I.6    Geuskens, M.7    Kroemer, G.8
  • 19
    • 0033560927 scopus 로고    scopus 로고
    • Contribution of p53-dependent caspase activation to neuronal cell death declines with neuronal maturation
    • Johnson MD, Kinoshita Y, Xiang H, Ghatan S, Morrison RS (1999) Contribution of p53-dependent caspase activation to neuronal cell death declines with neuronal maturation. J Neurosci 19:2996-3006.
    • (1999) J Neurosci , vol.19 , pp. 2996-3006
    • Johnson, M.D.1    Kinoshita, Y.2    Xiang, H.3    Ghatan, S.4    Morrison, R.S.5
  • 20
    • 0029811838 scopus 로고    scopus 로고
    • Loss of function of cytochrome c in Jurkat cells undergoing Fas-mediated apoptosis
    • Krippner A, Matsuno-Yagi A, Gottlieb RA, Babior BM (1996) Loss of function of cytochrome c in Jurkat cells undergoing Fas-mediated apoptosis. J Biol Chem 271:21629-21636.
    • (1996) J Biol Chem , vol.271 , pp. 21629-21636
    • Krippner, A.1    Matsuno-Yagi, A.2    Gottlieb, R.A.3    Babior, B.M.4
  • 22
    • 0030900980 scopus 로고    scopus 로고
    • Intracellular adenosine triphosphate (ATP) concentration: A switch in the decision between apoptosis and necrosis
    • Leist M, Single B, Castoldi AF, Kuhnle S, Nicotera P (1997) Intracellular adenosine triphosphate (ATP) concentration: a switch in the decision between apoptosis and necrosis. J Exp Med 185:1481-1486.
    • (1997) J Exp Med , vol.185 , pp. 1481-1486
    • Leist, M.1    Single, B.2    Castoldi, A.F.3    Kuhnle, S.4    Nicotera, P.5
  • 23
    • 0030715323 scopus 로고    scopus 로고
    • Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade
    • Li P, Nijhawan D, Budihardjo I, Srinivasula SM, Ahmad M, Alnemri ES, Wang X (1997) Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade. Cell 91:479-489.
    • (1997) Cell , vol.91 , pp. 479-489
    • Li, P.1    Nijhawan, D.2    Budihardjo, I.3    Srinivasula, S.M.4    Ahmad, M.5    Alnemri, E.S.6    Wang, X.7
  • 24
    • 0030581151 scopus 로고    scopus 로고
    • Induction of apoptotic program in cell-free extracts: Requirement for dATP and cytochrome c
    • Liu X, Kim CN, Pohl J, Wang X (1996) Induction of apoptotic program in cell-free extracts: requirement for dATP and cytochrome c. Cell 86:147-157.
    • (1996) Cell , vol.86 , pp. 147-157
    • Liu, X.1    Kim, C.N.2    Pohl, J.3    Wang, X.4
  • 25
    • 0030852948 scopus 로고    scopus 로고
    • Mechanism of cellular 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) reduction
    • Liu Y, Peterson DA, Kimura H, Schubert D (1997) Mechanism of cellular 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) reduction. J Neurochem 69:581-593.
    • (1997) J Neurochem , vol.69 , pp. 581-593
    • Liu, Y.1    Peterson, D.A.2    Kimura, H.3    Schubert, D.4
  • 27
    • 0021902977 scopus 로고
    • The structure, function and evolution of cytochromes
    • Mathews FS (1985) The structure, function and evolution of cytochromes. Prog Biophys Mol Biol 45:1-56.
    • (1985) Prog Biophys Mol Biol , vol.45 , pp. 1-56
    • Mathews, F.S.1
  • 28
    • 0031033274 scopus 로고    scopus 로고
    • Inhibition of Ced3/ICE-related proteases does not prevent cell death induced by oncogenes, DNA damage, or the bcl-2 homologue Bak
    • McCarthy NJ, Whyte MKB, Gilbert CS, Evan GI (1997) Inhibition of Ced3/ICE-related proteases does not prevent cell death induced by oncogenes, DNA damage, or the bcl-2 homologue Bak. J Cell Biol 136:215-227.
    • (1997) J Cell Biol , vol.136 , pp. 215-227
    • McCarthy, N.J.1    Whyte, M.K.B.2    Gilbert, C.S.3    Evan, G.I.4
  • 29
    • 0030797727 scopus 로고    scopus 로고
    • Bax deletion further orders the cell death pathway in cerebellar granule cells and suggests a caspase-independent pathway to cell death
    • Miller TM, Moulder KL, Knudson CM, Creedon DJ, Deshmukh M, Korsmeyer SJ, Johnson Jr EM (1997) Bax deletion further orders the cell death pathway in cerebellar granule cells and suggests a caspase-independent pathway to cell death. J Cell Biol 139:205-217.
    • (1997) J Cell Biol , vol.139 , pp. 205-217
    • Miller, T.M.1    Moulder, K.L.2    Knudson, C.M.3    Creedon, D.J.4    Deshmukh, M.5    Korsmeyer, S.J.6    Johnson E.M., Jr.7
  • 30
    • 0029738086 scopus 로고    scopus 로고
    • Induction of neuronal apoptosis by camptothecin, an inhibitor of DNA topoisomerase-I: Evidence for cell cycle-independent toxicity
    • Morris EJ, Geller HM (1996) Induction of neuronal apoptosis by camptothecin, an inhibitor of DNA topoisomerase-I: evidence for cell cycle-independent toxicity. J Cell Biol 134:757-770.
    • (1996) J Cell Biol , vol.134 , pp. 757-770
    • Morris, E.J.1    Geller, H.M.2
  • 31
    • 0032555934 scopus 로고    scopus 로고
    • Blocking cytochrome c activity within intact neurons inhibits apoptosis
    • Neame SJ, Rubin LL, Philpott KL (1998) Blocking cytochrome c activity within intact neurons inhibits apoptosis. J Cell Biol 142:1583-1593.
    • (1998) J Cell Biol , vol.142 , pp. 1583-1593
    • Neame, S.J.1    Rubin, L.L.2    Philpott, K.L.3
  • 32
    • 0029838165 scopus 로고    scopus 로고
    • Inhibitors of cyclin-dependent kinases promote survival of post-mitotic neuronally differentiated cells and sympathetic neurons
    • Park DS, Farinelli SE, Greene LA (1996) Inhibitors of cyclin-dependent kinases promote survival of post-mitotic neuronally differentiated cells and sympathetic neurons. J Biol Chem 271:21898-21905.
    • (1996) J Biol Chem , vol.271 , pp. 21898-21905
    • Park, D.S.1    Farinelli, S.E.2    Greene, L.A.3
  • 33
    • 0031016498 scopus 로고    scopus 로고
    • G1/S cell cycle blockers and inhibitors of cyclin-dependent kinases suppress camptothecin-induced apoptosis
    • Park DS, Morris EJ, Greene LA, Geller HM (1997) G1/S cell cycle blockers and inhibitors of cyclin-dependent kinases suppress camptothecin-induced apoptosis. J Neurosci 17:1256-1270.
    • (1997) J Neurosci , vol.17 , pp. 1256-1270
    • Park, D.S.1    Morris, E.J.2    Greene, L.A.3    Geller, H.M.4
  • 36
    • 0025939423 scopus 로고
    • Multiple agents rescue PC12 cells from serum-free cell death by translation- and transcription-independent mechanisms
    • Rukenstein A, Rydel RE, Greene LA (1991) Multiple agents rescue PC12 cells from serum-free cell death by translation- and transcription-independent mechanisms. J Neurosci 11:2552-2563.
    • (1991) J Neurosci , vol.11 , pp. 2552-2563
    • Rukenstein, A.1    Rydel, R.E.2    Greene, L.A.3
  • 37
    • 0030702084 scopus 로고    scopus 로고
    • Caspases: Intracellular signaling by proteolysis
    • Salvesen GS, Dixit VM (1997) Caspases: intracellular signaling by proteolysis. Cell 91:443-446.
    • (1997) Cell , vol.91 , pp. 443-446
    • Salvesen, G.S.1    Dixit, V.M.2
  • 39
    • 0030984171 scopus 로고    scopus 로고
    • Inhibitors of trypsin-like serine proteases inhibit processing of the caspase Nedd-2 and protect PC12 cells and sympathetic neurons from death evoked by withdrawal of trophic support
    • Stefanis L, Troy CM, Qi H, Greene LA (1997) Inhibitors of trypsin-like serine proteases inhibit processing of the caspase Nedd-2 and protect PC12 cells and sympathetic neurons from death evoked by withdrawal of trophic support. J Neurochem 69:1425-1437.
    • (1997) J Neurochem , vol.69 , pp. 1425-1437
    • Stefanis, L.1    Troy, C.M.2    Qi, H.3    Greene, L.A.4
  • 40
    • 0032533317 scopus 로고    scopus 로고
    • Caspase-2 (Nedd-2) processing and death of trophic factor-deprived PC12 cells and sympathetic neurons occur independently of caspase-3-like activity
    • Stefanis L, Troy CM, Qi H, Shelanski ML, Greene LA (1998) Caspase-2 (Nedd-2) processing and death of trophic factor-deprived PC12 cells and sympathetic neurons occur independently of caspase-3-like activity. J Neurosci 18:9204-9215.
    • (1998) J Neurosci , vol.18 , pp. 9204-9215
    • Stefanis, L.1    Troy, C.M.2    Qi, H.3    Shelanski, M.L.4    Greene, L.A.5
  • 42
    • 0030785790 scopus 로고    scopus 로고
    • The central executioner of apoptosis: Multiple connections between protease activation and mitochondria in Fas/APO-1/CD95- and ceramide-induced apoptosis
    • Susin SA, Zamzami N, Castedo M, Daugas E, Wang H, Geley S, Fassy F, Reed JC, Kroemer G (1997) The central executioner of apoptosis: multiple connections between protease activation and mitochondria in Fas/APO-1/CD95- and ceramide-induced apoptosis. J Exp Med 186:25-37.
    • (1997) J Exp Med , vol.186 , pp. 25-37
    • Susin, S.A.1    Zamzami, N.2    Castedo, M.3    Daugas, E.4    Wang, H.5    Geley, S.6    Fassy, F.7    Reed, J.C.8    Kroemer, G.9
  • 43
    • 0031018396 scopus 로고    scopus 로고
    • Nedd2 is required for apoptosis after trophic factor withdrawal, but not superoxide dismutase (SOD1) down-regulation, in sympathetic neurons and PC12 cells
    • Troy CM, Stefanis L, Greene LA, Shelanski ML (1997) Nedd2 is required for apoptosis after trophic factor withdrawal, but not Superoxide dismutase (SOD1) down-regulation, in sympathetic neurons and PC12 cells. J Neurosci 17:1911-1918.
    • (1997) J Neurosci , vol.17 , pp. 1911-1918
    • Troy, C.M.1    Stefanis, L.2    Greene, L.A.3    Shelanski, M.L.4
  • 46
    • 0029906828 scopus 로고    scopus 로고
    • Bax-induced cell death may not require interleukin 1β-converting enzyme-like proteases
    • Xiang J, Chao DT, Korsmeyer SJ (1996) Bax-induced cell death may not require interleukin 1β-converting enzyme-like proteases. Proc Natl Acad Sci USA 93:14559-14563.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 14559-14563
    • Xiang, J.1    Chao, D.T.2    Korsmeyer, S.J.3
  • 47
    • 0029880987 scopus 로고    scopus 로고
    • The caenorhabditis elegans cell-death protein CED-3 is a cysteine protease with substrate specificities similar to those of human CPP32 protease
    • Xue D, Shaham S, Horvitz HR (1996) The Caenorhabditis elegans cell-death protein CED-3 is a cysteine protease with substrate specificities similar to those of human CPP32 protease. Genes Dev 10:1073-1083.
    • (1996) Genes Dev , vol.10 , pp. 1073-1083
    • Xue, D.1    Shaham, S.2    Horvitz, H.R.3
  • 48
    • 0030745646 scopus 로고    scopus 로고
    • Apaf-1, a human protein homologous to C. elegans CED-4: Participates in cytochrome c-dependent activation of caspase-3
    • Zhou H, Henzel WJ, Liu X, Lutschg A, Wang X (1997) Apaf-1, a human protein homologous to C. elegans CED-4: participates in cytochrome c-dependent activation of caspase-3. Cell 90:405-413.
    • (1997) Cell , vol.90 , pp. 405-413
    • Zhou, H.1    Henzel, W.J.2    Liu, X.3    Lutschg, A.4    Wang, X.5


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