메뉴 건너뛰기




Volumn 10, Issue 6, 2005, Pages 1243-1259

Upstream control of apoptosis by caspase-2 in serum-deprived primary neurons

Author keywords

Bax; Caspase 2; Checkpoint; Mitochondria; Neuronal apoptosis; Serum deprivation

Indexed keywords

CASPASE 2; CASPASE 3; CASPASE 9; CASPASE INHIBITOR; CYTOCHROME C; ENZYME INHIBITOR; PHOSPHATIDYLSERINE; PROTEIN BAX; SMALL INTERFERING RNA;

EID: 30944446002     PISSN: 13608185     EISSN: 1573675X     Source Type: Journal    
DOI: 10.1007/s10495-005-1681-x     Document Type: Article
Times cited : (33)

References (62)
  • 1
    • 0032845121 scopus 로고    scopus 로고
    • Ischemic cell death in brain neurons
    • Lipton P. Ischemic cell death in brain neurons. Physiol Rev 1999; 79: 1431-1568.
    • (1999) Physiol Rev , vol.79 , pp. 1431-1568
    • Lipton, P.1
  • 2
    • 0034641936 scopus 로고    scopus 로고
    • Apoptosis in the nervous system
    • Yuan J, Yankner B. Apoptosis in the nervous system. Nature 2000; 407: 802-809.
    • (2000) Nature , vol.407 , pp. 802-809
    • Yuan, J.1    Yankner, B.2
  • 3
    • 0034329742 scopus 로고    scopus 로고
    • Apoptosis in neurodegenerative disorders
    • Mattson MP. Apoptosis in neurodegenerative disorders. Nat Rev Mol Cell Biol 2000; 1: 120-129.
    • (2000) Nat Rev Mol Cell Biol , vol.1 , pp. 120-129
    • Mattson, M.P.1
  • 4
    • 0033971898 scopus 로고    scopus 로고
    • Mitochondria and neuronal survival
    • Nicholls DG, Budd SL. Mitochondria and neuronal survival. Physiol Rev 2000; 80: 315-360.
    • (2000) Physiol Rev , vol.80 , pp. 315-360
    • Nicholls, D.G.1    Budd, S.L.2
  • 5
    • 0141884305 scopus 로고    scopus 로고
    • Diversity in the mechanisms of neuronal cell death
    • Yuan J, Lipinski M, Degterev A. Diversity in the mechanisms of neuronal cell death. Neuron 2003; 40: 401-413.
    • (2003) Neuron , vol.40 , pp. 401-413
    • Yuan, J.1    Lipinski, M.2    Degterev, A.3
  • 6
    • 0034888540 scopus 로고    scopus 로고
    • Caspase inhibition: A potential therapeutic strategy in neurological diseases
    • Rideout HJ, Stefanis L. Caspase inhibition: A potential therapeutic strategy in neurological diseases. Histol Histopathol 2001; 16: 895-908.
    • (2001) Histol Histopathol , vol.16 , pp. 895-908
    • Rideout, H.J.1    Stefanis, L.2
  • 7
    • 0037186898 scopus 로고    scopus 로고
    • Apoptosis and age-related disorders: Role of caspase-dependent and caspase-independent pathways
    • Nicotera P. Apoptosis and age-related disorders: Role of caspase-dependent and caspase-independent pathways. Toxicol Letters 2002; 127: 189-195.
    • (2002) Toxicol Letters , vol.127 , pp. 189-195
    • Nicotera, P.1
  • 8
    • 0038464650 scopus 로고    scopus 로고
    • Calcium: Regulation of cell death: The calcium-apoptosis link
    • Orrenius S, Zhivotovsky B, Nicotera P. Calcium: Regulation of cell death: the calcium-apoptosis link. Nat Rev Mol Cell Biol 2003; 4: 552-565.
    • (2003) Nat Rev Mol Cell Biol , vol.4 , pp. 552-565
    • Orrenius, S.1    Zhivotovsky, B.2    Nicotera, P.3
  • 9
    • 0037458021 scopus 로고    scopus 로고
    • Caspase 3 activation is essential for neuroprotection in preconditioning
    • McLaughlin B, Hartnett KA, Erhardt JA, et al. Caspase 3 activation is essential for neuroprotection in preconditioning. Proc Natl Acad Sci USA 2003; 100: 715-720.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 715-720
    • McLaughlin, B.1    Hartnett, K.A.2    Erhardt, J.A.3
  • 10
    • 12944250987 scopus 로고    scopus 로고
    • Caspase-3: A vulnerability factor and final effector in apoptotic death of dopaminergic neurons in Parkinson's disease
    • Hartmann A, Hunot S, Michel PP, et al. Caspase-3: A vulnerability factor and final effector in apoptotic death of dopaminergic neurons in Parkinson's disease. Proc Natl Acad Sci USA 2000; 97: 2875-2880.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 2875-2880
    • Hartmann, A.1    Hunot, S.2    Michel, P.P.3
  • 11
    • 0034023082 scopus 로고    scopus 로고
    • Caspase activities and tumor necrosis factor receptor R1 (p55) level are elevated in the substantia nigra from parkinsonian brain
    • Mogi M, Togari A, Kondo T, et al. Caspase activities and tumor necrosis factor receptor R1 (p55) level are elevated in the substantia nigra from parkinsonian brain. J Neural Transm 2000; 107: 335-341.
    • (2000) J Neural Transm , vol.107 , pp. 335-341
    • Mogi, M.1    Togari, A.2    Kondo, T.3
  • 12
    • 0042837889 scopus 로고    scopus 로고
    • Caspase activation in the limbic cortex of subjects with early Alzheimer's disease
    • Gastard MC, Troncoso JC, Koliatsos VE. Caspase activation in the limbic cortex of subjects with early Alzheimer's disease. Ann Neurol 2003; 54, 393-398.
    • (2003) Ann Neurol , vol.54 , pp. 393-398
    • Gastard, M.C.1    Troncoso, J.C.2    Koliatsos, V.E.3
  • 13
    • 0033213973 scopus 로고    scopus 로고
    • Caspase and calpain substrates: Roles in synaptic plasticity and cell death
    • Chan SL, Mattson ML. Caspase and calpain substrates: roles in synaptic plasticity and cell death. J Neurosci Res 1999; 58: 167-190.
    • (1999) J Neurosci Res , vol.58 , pp. 167-190
    • Chan, S.L.1    Mattson, M.L.2
  • 14
    • 0030458720 scopus 로고    scopus 로고
    • Genetic and metabolic status of NGF-deprived sympathetic neurons saved by an inhibitor of ICE family proteases
    • Deshmukh M, Vasilakos J, Deckwerth TL, et al. Genetic and metabolic status of NGF-deprived sympathetic neurons saved by an inhibitor of ICE family proteases. J Cell Biol 1996; 135: 1341-1354.
    • (1996) J Cell Biol , vol.135 , pp. 1341-1354
    • Deshmukh, M.1    Vasilakos, J.2    Deckwerth, T.L.3
  • 15
    • 0037162833 scopus 로고    scopus 로고
    • Requirement for caspase-2 in stress-induced apoptosis before mitochondrial permeabilization
    • Lassus P, Opitz-Araya X, Lazebnik Y. Requirement for caspase-2 in stress-induced apoptosis before mitochondrial permeabilization. Science 2002; 297: 1352-1354.
    • (2002) Science , vol.297 , pp. 1352-1354
    • Lassus, P.1    Opitz-Araya, X.2    Lazebnik, Y.3
  • 16
    • 0037119491 scopus 로고    scopus 로고
    • Caspase-2 acts upstream of mitochondria to promote cytochrome c release during etoposide-induced apoptosis
    • Robertson JD, Enoksson M, Suomela M, et al. Caspase-2 acts upstream of mitochondria to promote cytochrome c release during etoposide-induced apoptosis. J Biol Chem 2002; 277: 29803-29809.
    • (2002) J Biol Chem , vol.277 , pp. 29803-29809
    • Robertson, J.D.1    Enoksson, M.2    Suomela, M.3
  • 17
    • 4344663051 scopus 로고    scopus 로고
    • Processed caspase-2 can induce mitochondria-mediated apoptosis independently of its enzymatic activity
    • Robertson JD, Gogvadze V, Kropotov A, et al. Processed caspase-2 can induce mitochondria-mediated apoptosis independently of its enzymatic activity. EMBO Rep 2004; 5: 643-648.
    • (2004) EMBO Rep , vol.5 , pp. 643-648
    • Robertson, J.D.1    Gogvadze, V.2    Kropotov, A.3
  • 19
    • 0031018396 scopus 로고    scopus 로고
    • Nedd2 is required for apoptosis after trophic factor withdrawal, but not superoxide dismutase (SOD1) downregulation in sympathetic neurons and PC12 cells
    • Troy CM, Stefanis L, Greene LA, et al. Nedd2 is required for apoptosis after trophic factor withdrawal, but not superoxide dismutase (SOD1) downregulation in sympathetic neurons and PC12 cells. J Neurosci 1997; 17: 1911-1918.
    • (1997) J Neurosci , vol.17 , pp. 1911-1918
    • Troy, C.M.1    Stefanis, L.2    Greene, L.A.3
  • 20
    • 0034652232 scopus 로고    scopus 로고
    • Caspase-2 mediates neuronal cell death induced by beta-amyloid
    • Troy CM, Rabacchi SA, Friedman WJ, et al. Caspase-2 mediates neuronal cell death induced by beta-amyloid. J Neurosci 2000; 20: 1386-1392.
    • (2000) J Neurosci , vol.20 , pp. 1386-1392
    • Troy, C.M.1    Rabacchi, S.A.2    Friedman, W.J.3
  • 21
    • 0032101642 scopus 로고    scopus 로고
    • Need for caspase-2 in apoptosis of growth-factor-deprived PC12 cells
    • Haviv R, Lindenboim L, Yuan J, Stein R. Need for caspase-2 in apoptosis of growth-factor-deprived PC12 cells. J Neurosci Res 1998; 52: 491-497.
    • (1998) J Neurosci Res , vol.52 , pp. 491-497
    • Haviv, R.1    Lindenboim, L.2    Yuan, J.3    Stein, R.4
  • 22
    • 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, et al. 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 1997; 69: 1425-1437.
    • (1997) J Neurochem , vol.69 , pp. 1425-1437
    • Stefanis, L.1    Troy, C.M.2    Qi, H.3
  • 23
    • 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 (CPP32)-like activity
    • Stefanis L, Troy CM, Qi H, et al. Caspase-2 (Nedd-2) processing and death of trophic factor-deprived PC12 cells and sympathetic neurons occur independently of caspase-3 (CPP32)-like activity. J Neurosci 1998; 18: 9204-9215.
    • (1998) J Neurosci , vol.18 , pp. 9204-9215
    • Stefanis, L.1    Troy, C.M.2    Qi, H.3
  • 24
    • 0035076483 scopus 로고    scopus 로고
    • Beta-Amyloid-induced neuronal apoptosis requires c-Jun N-terminal kinase activation
    • Troy CM, Rabacchi SA, Xu Z, et al. Beta-Amyloid-induced neuronal apoptosis requires c-Jun N-terminal kinase activation. J Neurochem 2001; 77: 157-164.
    • (2001) J Neurochem , vol.77 , pp. 157-164
    • Troy, C.M.1    Rabacchi, S.A.2    Xu, Z.3
  • 25
    • 0032080197 scopus 로고    scopus 로고
    • Defects in regulation of apoptosis in caspase-2-deficient mice
    • Bergeron L, Perez GI, Macdonald G, et al. Defects in regulation of apoptosis in caspase-2-deficient mice. Genes Dev 1998; 12: 1304-1314.
    • (1998) Genes Dev , vol.12 , pp. 1304-1314
    • Bergeron, L.1    Perez, G.I.2    Macdonald, G.3
  • 26
    • 11144357398 scopus 로고    scopus 로고
    • Specific caspase interactions and amplification are involved in selective neuronal vulnerability in Huntington's disease
    • Hermel E, Gafni J, Propp SS, et al. Specific caspase interactions and amplification are involved in selective neuronal vulnerability in Huntington's disease. Cell Death Differ 2004; 11: 424-438.
    • (2004) Cell Death Differ , vol.11 , pp. 424-438
    • Hermel, E.1    Gafni, J.2    Propp, S.S.3
  • 27
    • 0030881653 scopus 로고    scopus 로고
    • Activation of caspase-2 in apoptosis
    • Li H, Bergeron L, Cryns V, et al. Activation of caspase-2 in apoptosis. J Biol Chem 1997; 272: 21010-21017.
    • (1997) J Biol Chem , vol.272 , pp. 21010-21017
    • Li, H.1    Bergeron, L.2    Cryns, V.3
  • 28
    • 3343002907 scopus 로고    scopus 로고
    • Fixed- and real-time cytofluorometric technologies for dynamic analysis of apoptosis in primary cortical neurons
    • Lecoeur H, Chauvier D, Langonné A, et al. Fixed- and real-time cytofluorometric technologies for dynamic analysis of apoptosis in primary cortical neurons. Apoptosis 2004; 9: 157-169.
    • (2004) Apoptosis , vol.9 , pp. 157-169
    • Lecoeur, H.1    Chauvier, D.2    Langonné, A.3
  • 29
    • 0033521741 scopus 로고    scopus 로고
    • Molecular characterization of mitochondrial apoptosis-inducing factor
    • Susin SA, Lorenzo H, Zamzami N, et al. Molecular characterization of mitochondrial apoptosis-inducing factor. Nature 1999; 397: 441-446.
    • (1999) Nature , vol.397 , pp. 441-446
    • Susin, S.A.1    Lorenzo, H.2    Zamzami, N.3
  • 30
    • 0038118283 scopus 로고    scopus 로고
    • Brain-derived neurotrophic factor protection of cortical neurons from serum withdrawal-induced apoptosis is inhibited by cAMP
    • Poser S, Impey S, Xia Z, et al. Brain-derived neurotrophic factor protection of cortical neurons from serum withdrawal-induced apoptosis is inhibited by cAMP. J Neurosci 2003; 23: 4420-4427.
    • (2003) J Neurosci , vol.23 , pp. 4420-4427
    • Poser, S.1    Impey, S.2    Xia, Z.3
  • 31
    • 0041666539 scopus 로고    scopus 로고
    • Q-VD-OPh, a broad spectrum caspase inhibitor with potent antiapoptotic properties
    • Caserta TM, Smith AN, Gultice AD, et al. Q-VD-OPh, a broad spectrum caspase inhibitor with potent antiapoptotic properties. Apoptosis 2003; 8: 345-352.
    • (2003) Apoptosis , vol.8 , pp. 345-352
    • Caserta, T.M.1    Smith, A.N.2    Gultice, A.D.3
  • 32
    • 0029830345 scopus 로고    scopus 로고
    • Induction of CPP32-like activity in PC12 cells by withdrawal of trophic support. Dissociation from apoptosis
    • Stefanis L, Park DS, Yan CY, et al. Induction of CPP32-like activity in PC12 cells by withdrawal of trophic support. Dissociation from apoptosis. J Biol Chem 1996; 271: 30663-30671.
    • (1996) J Biol Chem , vol.271 , pp. 30663-30671
    • Stefanis, L.1    Park, D.S.2    Yan, C.Y.3
  • 33
    • 0034631832 scopus 로고    scopus 로고
    • Caspase inhibition extends the commitment to neuronal death beyond cytochrome c release to the point of mitochondrial depolarization
    • Deshmukh M, Kuida K, Johnson EM Jr. Caspase inhibition extends the commitment to neuronal death beyond cytochrome c release to the point of mitochondrial depolarization. J Cell Biol 2000; 150: 131-143.
    • (2000) J Cell Biol , vol.150 , pp. 131-143
    • Deshmukh, M.1    Kuida, K.2    Johnson Jr., E.M.3
  • 34
    • 0030245811 scopus 로고    scopus 로고
    • BAX is required for neuronal death after trophic factor deprivation and during development
    • Deckwerth TL, Elliott JL, Knudson CM, et al. BAX is required for neuronal death after trophic factor deprivation and during development. Neuron 1996; 17: 401-411.
    • (1996) Neuron , vol.17 , pp. 401-411
    • Deckwerth, T.L.1    Elliott, J.L.2    Knudson, C.M.3
  • 35
    • 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 EM. Evidence of a novel event during neuronal death: development of competence-to-die in response to cytoplasmic cytochrome c. Neuron 1998; 21: 695-705.
    • (1998) Neuron , vol.21 , pp. 695-705
    • Deshmukh, M.1    Johnson, E.M.2
  • 36
    • 0033198217 scopus 로고    scopus 로고
    • BAX translocation is a critical event in neuronal apoptosis: Regulation by neuroprotectants, BCL-2, and caspases
    • Putcha GV, Deshmukh M, Johnson EM. BAX translocation is a critical event in neuronal apoptosis: regulation by neuroprotectants, BCL-2, and caspases. J Neurosci 1999; 19: 7476-7485.
    • (1999) J Neurosci , vol.19 , pp. 7476-7485
    • Putcha, G.V.1    Deshmukh, M.2    Johnson, E.M.3
  • 37
    • 0037053298 scopus 로고    scopus 로고
    • The course of etoposide-induced apoptosis from damage to DNA and p53 activation to mitochondrial release of cytochrome c
    • Karpinich NO, Tafani M, Rothman RJ. The course of etoposide-induced apoptosis from damage to DNA and p53 activation to mitochondrial release of cytochrome c. J Biol Chem 2002; 277: 16547-1652.
    • (2002) J Biol Chem , vol.277 , pp. 16547-21652
    • Karpinich, N.O.1    Tafani, M.2    Rothman, R.J.3
  • 38
    • 0037147147 scopus 로고    scopus 로고
    • Regulation of intracellular pH mediates Bax activation in HeLa cells treated with staurosporine or tumor necrosis factor-alpha
    • Tafani M, Cohn JA, Karpinich NO, et al. Regulation of intracellular pH mediates Bax activation in HeLa cells treated with staurosporine or tumor necrosis factor-alpha. J Biol Chem 2002; 277: 49569-49576.
    • (2002) J Biol Chem , vol.277 , pp. 49569-49576
    • Tafani, M.1    Cohn, J.A.2    Karpinich, N.O.3
  • 39
    • 0037134495 scopus 로고    scopus 로고
    • Caspase-2 induces apoptosis by releasing proapoptotic proteins from mitochondria
    • Guo Y, Srinivasula SM, Druilhe A, et al. Caspase-2 induces apoptosis by releasing proapoptotic proteins from mitochondria. J Biol Chem 2002; 277: 13430-13437.
    • (2002) J Biol Chem , vol.277 , pp. 13430-13437
    • Guo, Y.1    Srinivasula, S.M.2    Druilhe, A.3
  • 40
    • 0032480260 scopus 로고    scopus 로고
    • Bax cleavage is mediated by calpain during drug-induced apoptosis
    • Wood DE, Thomas A, Devi LA, et al. Bax cleavage is mediated by calpain during drug-induced apoptosis. Oncogene 1998; 17: 1069-1078.
    • (1998) Oncogene , vol.17 , pp. 1069-1078
    • Wood, D.E.1    Thomas, A.2    Devi, L.A.3
  • 41
    • 0034967241 scopus 로고    scopus 로고
    • Cleavage of Bax is mediated by caspase-dependent or -independent calpain activation in dopaminergic neuronal cells: Protective role of Bcl-2
    • Choi WS, Lee EH, Chung CW, et al. Cleavage of Bax is mediated by caspase-dependent or -independent calpain activation in dopaminergic neuronal cells: protective role of Bcl-2. J Neurochem 2001; 77: 1531-1541.
    • (2001) J Neurochem , vol.77 , pp. 1531-1541
    • Choi, W.S.1    Lee, E.H.2    Chung, C.W.3
  • 42
    • 3042592579 scopus 로고    scopus 로고
    • Bcl-2-regulated apoptosis and cytochrome c release can occur independently of both caspase-2 and caspase-9
    • Marsden VS, Ekert PG, Van Delft M, et al. Bcl-2-regulated apoptosis and cytochrome c release can occur independently of both caspase-2 and caspase-9. J Cell Biol 2004, 165; 775-780.
    • (2004) J Cell Biol , vol.165 , pp. 775-780
    • Marsden, V.S.1    Ekert, P.G.2    Van Delft, M.3
  • 43
    • 0035879074 scopus 로고    scopus 로고
    • Death in the balance: Alternative participation of the caspase-2 and -9 pathways in neuronal death induced by nerve growth factor deprivation
    • Troy CM, Rabacchi SA, Hohl JB, et al. Death in the balance: alternative participation of the caspase-2 and -9 pathways in neuronal death induced by nerve growth factor deprivation. J Neurosci 2001; 21: 5007-5016.
    • (2001) J Neurosci , vol.21 , pp. 5007-5016
    • Troy, C.M.1    Rabacchi, S.A.2    Hohl, J.B.3
  • 44
    • 0035019143 scopus 로고    scopus 로고
    • Caspase-2 activation is redundant during seizure-induced neuronal death
    • Henshall DC, Skradski SL, Bonislawski DP, et al. Caspase-2 activation is redundant during seizure-induced neuronal death. J Neurochem 2001; 77: 886-895.
    • (2001) J Neurochem , vol.77 , pp. 886-895
    • Henshall, D.C.1    Skradski, S.L.2    Bonislawski, D.P.3
  • 45
    • 3042687605 scopus 로고    scopus 로고
    • Apaf-1 and caspase-9 accelerate apoptosis, but do not determine whether factor-deprived or drug-treated cells die
    • Ekert PG., Read SH, Silke J, et al. Apaf-1 and caspase-9 accelerate apoptosis, but do not determine whether factor-deprived or drug-treated cells die. J Cell Biol 2004; 165, 835-842.
    • (2004) J Cell Biol , vol.165 , pp. 835-842
    • Ekert, P.G.1    Read, S.H.2    Silke, J.3
  • 46
    • 2542478966 scopus 로고    scopus 로고
    • Caspase-dependent cytochrome c release and cell death in chick cardiomyocytes following simulated ischemia-reperfusion
    • Qin Y, Van den Hoek TL, Wojcik K, et al. Caspase-dependent cytochrome c release and cell death in chick cardiomyocytes following simulated ischemia-reperfusion. Am J Physiol Heart Circ Physiol 2004; 286: H2280-2286.
    • (2004) Am J Physiol Heart Circ Physiol , vol.286
    • Qin, Y.1    Van Den Hoek, T.L.2    Wojcik, K.3
  • 47
    • 0028168593 scopus 로고
    • Ich-1, an Ice/ced-3-related gene, encodes both positive and negative regulators of programmed cell death
    • Wang L, Miura M, Bergeron L, et al. Ich-1, an Ice/ced-3-related gene, encodes both positive and negative regulators of programmed cell death. Cell 1994; 78, 739-750.
    • (1994) Cell , vol.78 , pp. 739-750
    • Wang, L.1    Miura, M.2    Bergeron, L.3
  • 48
    • 0035803568 scopus 로고    scopus 로고
    • Apoptosis-associated release of Smac/DIABLO from mitochondria requires active caspases and is blocked by Bcl-2
    • Adrain C, Creagh EM, Martin SJ. Apoptosis-associated release of Smac/DIABLO from mitochondria requires active caspases and is blocked by Bcl-2. EMBO J 2001; 20: 6627-6636.
    • (2001) EMBO J , vol.20 , pp. 6627-6636
    • Adrain, C.1    Creagh, E.M.2    Martin, S.J.3
  • 49
    • 0035877605 scopus 로고    scopus 로고
    • Caspase-2-induced apoptosis is dependent on caspase-9, but its processing during UV-or tumor necrosis factor-dependent cell death requires caspase-3
    • Paroni G, Henderson C, Schneider C. Caspase-2-induced apoptosis is dependent on caspase-9, but its processing during UV-or tumor necrosis factor-dependent cell death requires caspase-3. J Biol Chem 2001; 276: 21907-21915.
    • (2001) J Biol Chem , vol.276 , pp. 21907-21915
    • Paroni, G.1    Henderson, C.2    Schneider, C.3
  • 50
    • 0347319036 scopus 로고    scopus 로고
    • Induction of apoptosis by enediyne antibiotic calicheamicin thetaII proceeds through a caspase-mediated mitochondrial amplification loop in an entirely Bax-dependent manner
    • Prokop A, Wrasidlo W, Lode H, et al. Induction of apoptosis by enediyne antibiotic calicheamicin thetaII proceeds through a caspase-mediated mitochondrial amplification loop in an entirely Bax-dependent manner. Oncogene 2003; 22: 9107-9120.
    • (2003) Oncogene , vol.22 , pp. 9107-9120
    • Prokop, A.1    Wrasidlo, W.2    Lode, H.3
  • 51
    • 0037177809 scopus 로고    scopus 로고
    • Caspase-2 can trigger cytochrome c release and apoptosis from the nucleus
    • Paroni G, Henderson C, Schneider C, et al. Caspase-2 can trigger cytochrome c release and apoptosis from the nucleus. J Biol Chem 2002; 277: 15147-15161.
    • (2002) J Biol Chem , vol.277 , pp. 15147-15161
    • Paroni, G.1    Henderson, C.2    Schneider, C.3
  • 52
    • 0032544397 scopus 로고    scopus 로고
    • Prodomain-dependent nuclear localization of the caspase-2 (Nedd2) precursor. A novel function for a caspase prodomain
    • Colussi PA, Harvey NL, Kumar S. Prodomain-dependent nuclear localization of the caspase-2 (Nedd2) precursor. A novel function for a caspase prodomain. J Biol Chem 1998; 273: 24535-24542.
    • (1998) J Biol Chem , vol.273 , pp. 24535-24542
    • Colussi, P.A.1    Harvey, N.L.2    Kumar, S.3
  • 53
    • 0033579810 scopus 로고    scopus 로고
    • Mitochondrial release of caspase-2 and -9 during the apoptotic process
    • Susin SA, Lorenzo H, Zamzami N, et al. Mitochondrial release of caspase-2 and -9 during the apoptotic process. J Exp Med 1999; 189: 381-394.
    • (1999) J Exp Med , vol.189 , pp. 381-394
    • Susin, S.A.1    Lorenzo, H.2    Zamzami, N.3
  • 54
    • 0036024020 scopus 로고    scopus 로고
    • Caspase-2 is not required for thymocyte or neuronal apoptosis even though cleavage of caspase-2 is dependent on both Apaf-1 and caspase-9
    • O'Reilly LA, Ekert P, Harvey N, et al. Caspase-2 is not required for thymocyte or neuronal apoptosis even though cleavage of caspase-2 is dependent on both Apaf-1 and caspase-9. Cell Death Differ 2002; 9: 832-841.
    • (2002) Cell Death Differ , vol.9 , pp. 832-841
    • O'Reilly, L.A.1    Ekert, P.2    Harvey, N.3
  • 55
    • 0034194338 scopus 로고    scopus 로고
    • Caspase-2 is localized at the Golgi complex and cleaves golgin-160 during apoptosis
    • Mancini M, Machamer CE, Roy S, et al. Caspase-2 is localized at the Golgi complex and cleaves golgin-160 during apoptosis. J Cell Biol 2000; 149: 603-612.
    • (2000) J Cell Biol , vol.149 , pp. 603-612
    • Mancini, M.1    Machamer, C.E.2    Roy, S.3
  • 56
    • 1642633791 scopus 로고    scopus 로고
    • ASC is a Bax adaptor and regulates the p53-Bax mitochondrial apoptosis pathway
    • Ohtsuka T, Ryu H, Minamishima YA, et al. ASC is a Bax adaptor and regulates the p53-Bax mitochondrial apoptosis pathway. Nat Cell Biol 2004; 6: 121-128.
    • (2004) Nat Cell Biol , vol.6 , pp. 121-128
    • Ohtsuka, T.1    Ryu, H.2    Minamishima, Y.A.3
  • 57
    • 0038136890 scopus 로고    scopus 로고
    • Role of prodomain in importin-mediated nuclear localization and activation of caspase-2
    • Baliga BC, Colussi PA, Read SH, et al. Role of prodomain in importin-mediated nuclear localization and activation of caspase-2. J Biol Chem 2003; 278: 4899-4905.
    • (2003) J Biol Chem , vol.278 , pp. 4899-4905
    • Baliga, B.C.1    Colussi, P.A.2    Read, S.H.3
  • 58
    • 0034193138 scopus 로고    scopus 로고
    • Cleavage of Bax enhances its cell death function
    • Wood DE, Newcomb EW. Cleavage of Bax enhances its cell death function. Exp Cell Res 2000; 256: 375-382.
    • (2000) Exp Cell Res , vol.256 , pp. 375-382
    • Wood, D.E.1    Newcomb, E.W.2
  • 59
    • 0141481980 scopus 로고    scopus 로고
    • Cleavage of Bax to p18 Bax accelerates stress-induced apoptosis, and a cathepsin-like protease may rapidly degrade p18 Bax
    • Cao X, Deng X, May WS. Cleavage of Bax to p18 Bax accelerates stress-induced apoptosis, and a cathepsin-like protease may rapidly degrade p18 Bax. Blood 2003; 102: 2605-2614.
    • (2003) Blood , vol.102 , pp. 2605-2614
    • Cao, X.1    Deng, X.2    May, W.S.3
  • 60
    • 0037386258 scopus 로고    scopus 로고
    • Cytoprotective membrane-permeable peptides designed from the Bax-binding domain of Ku70
    • Sawada M, Hayes P, Matsuyama S. Cytoprotective membrane-permeable peptides designed from the Bax-binding domain of Ku70. Nat Cell Biol 2003; 5: 352-357.
    • (2003) Nat Cell Biol , vol.5 , pp. 352-357
    • Sawada, M.1    Hayes, P.2    Matsuyama, S.3
  • 61
    • 0038485614 scopus 로고    scopus 로고
    • Humanin peptide suppresses apoptosis by interfering with Bax activation
    • Guo B, Zhai D, Cabezas E, et al. Humanin peptide suppresses apoptosis by interfering with Bax activation. Nature 2003; 423: 456-461.
    • (2003) Nature , vol.423 , pp. 456-461
    • Guo, B.1    Zhai, D.2    Cabezas, E.3
  • 62
    • 1642633791 scopus 로고    scopus 로고
    • ASC is a Bax adaptor and regulates the p53-Bax mitochondrial apoptosis pathway
    • Ohtsuka T, Ryu H, Minamishima YA, et al. ASC is a Bax adaptor and regulates the p53-Bax mitochondrial apoptosis pathway. Nat Cell Biol 2004; 6, 121-128.
    • (2004) Nat Cell Biol , vol.6 , pp. 121-128
    • Ohtsuka, T.1    Ryu, H.2    Minamishima, Y.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.