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Volumn 71, Issue 2, 1999, Pages 225-237

CPP32/CASPASE-3-like proteases in hypoxia-induced apoptosis in developing brain neurons

Author keywords

Apoptosis; Caspase inhibitors; Caspase 3 induction; Cultured brain neurons; Hypoxia reoxygenation; Neurogenesis; PARP cleavage

Indexed keywords

CASPASE 3; CASPASE INHIBITOR; PROTEINASE;

EID: 0032694633     PISSN: 0169328X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0169-328X(99)00190-4     Document Type: Article
Times cited : (35)

References (61)
  • 1
    • 0031044652 scopus 로고    scopus 로고
    • Mammalian cell death proteases: A family of highly conserved aspartate specific cysteine proteases
    • Alnemri E.S. Mammalian cell death proteases: a family of highly conserved aspartate specific cysteine proteases. J. Cell. Biochem. 64:1997;33-42.
    • (1997) J. Cell. Biochem. , vol.64 , pp. 33-42
    • Alnemri, E.S.1
  • 3
    • 0032536753 scopus 로고    scopus 로고
    • Hypoxia/reoxygenation induces apoptosis through biphasic induction of protein synthesis in central neurons
    • Bossenmeyer C., Chihab R., Muller S., Schroeder H., Daval J.L. Hypoxia/reoxygenation induces apoptosis through biphasic induction of protein synthesis in central neurons. Brain Res. 787:1998;107-116.
    • (1998) Brain Res. , vol.787 , pp. 107-116
    • Bossenmeyer, C.1    Chihab, R.2    Muller, S.3    Schroeder, H.4    Daval, J.L.5
  • 4
    • 0001971438 scopus 로고    scopus 로고
    • Differential expression of specific proteins associated with apoptosis (Bax) or cell survival (Bcl-2, HSP70, HSP105) after short- And long-lasting hypoxia in cultured central neurons
    • Bossenmeyer C., Chihab R., Muller S., Vert P., Daval J.L. Differential expression of specific proteins associated with apoptosis (Bax) or cell survival (Bcl-2, HSP70, HSP105) after short- and long-lasting hypoxia in cultured central neurons. Pediatr. Res. 41:1997;41A.
    • (1997) Pediatr. Res. , vol.41
    • Bossenmeyer, C.1    Chihab, R.2    Muller, S.3    Vert, P.4    Daval, J.L.5
  • 5
    • 0032905937 scopus 로고    scopus 로고
    • Transient hypoxia may lead to neuronal proliferation in the developing mammalian brain: From apoptosis to cell cycle completion
    • Bossenmeyer-Pourié C., Chihab R., Schroeder H., Daval J.L. Transient hypoxia may lead to neuronal proliferation in the developing mammalian brain: from apoptosis to cell cycle completion. Neuroscience. 91:1999;221-231.
    • (1999) Neuroscience , vol.91 , pp. 221-231
    • Bossenmeyer-Pourié, C.1    Chihab, R.2    Schroeder, H.3    Daval, J.L.4
  • 6
    • 0032527816 scopus 로고    scopus 로고
    • Prevention from hypoxia-induced apoptosis by preconditioning: A mechanistic approach in cultured neurons from fetal rat forebrain
    • Bossenmeyer-Pourié C., Daval J.L. Prevention from hypoxia-induced apoptosis by preconditioning: a mechanistic approach in cultured neurons from fetal rat forebrain. Mol. Brain Res. 58:1998;237-239.
    • (1998) Mol. Brain Res. , vol.58 , pp. 237-239
    • Bossenmeyer-Pourié, C.1    Daval, J.L.2
  • 8
    • 0032124903 scopus 로고    scopus 로고
    • Induction of caspase-3-like protease may mediate delayed neuronal death in the hippocampus after transient cerebral ischemia
    • Chen J., Nagayama T., Jin K., Stetler R.A., Zhu R.L., Graham S.H., Simon R.P. Induction of caspase-3-like protease may mediate delayed neuronal death in the hippocampus after transient cerebral ischemia. J. Neurosci. 18:1998;4914-4928.
    • (1998) J. Neurosci. , vol.18 , pp. 4914-4928
    • Chen, J.1    Nagayama, T.2    Jin, K.3    Stetler, R.A.4    Zhu, R.L.5    Graham, S.H.6    Simon, R.P.7
  • 10
    • 0031845126 scopus 로고    scopus 로고
    • Lack of correlation between the effects of transient exposure to glutamate and those of hypoxia/reoxygenation in immature neurons in vitro
    • Chihab R., Bossenmeyer C., Oillet J., Daval J.L. Lack of correlation between the effects of transient exposure to glutamate and those of hypoxia/reoxygenation in immature neurons in vitro. J. Neurochem. 71:1998;1177-1186.
    • (1998) J. Neurochem. , vol.71 , pp. 1177-1186
    • Chihab, R.1    Bossenmeyer, C.2    Oillet, J.3    Daval, J.L.4
  • 11
    • 0032506659 scopus 로고    scopus 로고
    • Sequential activation of activator protein-1-related transcription factors and JNK protein kinases may contribute to apoptotic death induced by transient hypoxia in developing brain neurons
    • Chihab R., Ferry C., Koziel V., Monin P., Daval J.L. Sequential activation of activator protein-1-related transcription factors and JNK protein kinases may contribute to apoptotic death induced by transient hypoxia in developing brain neurons. Mol. Brain Res. 63:1998;105-120.
    • (1998) Mol. Brain Res. , vol.63 , pp. 105-120
    • Chihab, R.1    Ferry, C.2    Koziel, V.3    Monin, P.4    Daval, J.L.5
  • 13
    • 0030931876 scopus 로고    scopus 로고
    • Caspases: The executioners of apoptosis
    • Cohen G.M. Caspases: the executioners of apoptosis. Biochem. J. 326:1996;1-16.
    • (1996) Biochem. J. , vol.326 , pp. 1-16
    • Cohen, G.M.1
  • 14
    • 0029099845 scopus 로고
    • Activation of the apoptotic protease CPP32 by cytotoxic T-cell-derived granzyme B
    • Darmon A.J., Ehrman N., Caputo A., Fujinaga J., Bleackley R.C. Activation of the apoptotic protease CPP32 by cytotoxic T-cell-derived granzyme B. Nature. 377:1995;446-448.
    • (1995) Nature , vol.377 , pp. 446-448
    • Darmon, A.J.1    Ehrman, N.2    Caputo, A.3    Fujinaga, J.4    Bleackley, R.C.5
  • 16
    • 0028857607 scopus 로고
    • A simple method for evaluation of superoxide radical production in neural cells under various culture conditions: Application to hypoxia
    • Daval J.L., Ghersi-Egea J.F., Oillet J., Koziel V. A simple method for evaluation of superoxide radical production in neural cells under various culture conditions: application to hypoxia. J. Cereb. Blood Flow Metab. 15:1995;71-77.
    • (1995) J. Cereb. Blood Flow Metab. , vol.15 , pp. 71-77
    • Daval, J.L.1    Ghersi-Egea, J.F.2    Oillet, J.3    Koziel, V.4
  • 17
    • 0030462766 scopus 로고    scopus 로고
    • Apoptosis in perinatal hypoxic-ischaemic cerebral damage
    • Edwards A.D., Mehmet H. Apoptosis in perinatal hypoxic-ischaemic cerebral damage. Neuropathol. Appl. Neurobiol. 22:1996;494-498.
    • (1996) Neuropathol. Appl. Neurobiol. , vol.22 , pp. 494-498
    • Edwards, A.D.1    Mehmet, H.2
  • 19
    • 0029978182 scopus 로고    scopus 로고
    • Sequential activation of ICE-like and CPP32-like proteases during Fas-mediated apoptosis
    • Enari M., Talanian R.V., Wong W.W., Nagata S. Sequential activation of ICE-like and CPP32-like proteases during Fas-mediated apoptosis. Nature. 380:1996;723-726.
    • (1996) Nature , vol.380 , pp. 723-726
    • Enari, M.1    Talanian, R.V.2    Wong, W.W.3    Nagata, S.4
  • 21
    • 0002028043 scopus 로고    scopus 로고
    • Detection of apoptotic or necrotic death in neuronal cells by morphological, biochemical, and molecular analysis.
    • in: J. Poirier (Ed.), Apoptosis Techniques and Protocols, Humana Press, Totowa
    • M. Gschwind, G. Huber, Detection of apoptotic or necrotic death in neuronal cells by morphological, biochemical, and molecular analysis. in: J. Poirier (Ed.), Apoptosis Techniques and Protocols, Neuromethods, Vol. 29, Humana Press, Totowa, 1997, pp. 13-31.
    • (1997) Neuromethods , vol.29 , pp. 13-31
    • Gschwind, M.1    Huber, G.2
  • 23
    • 0030024840 scopus 로고    scopus 로고
    • Protease activity of in vitro transcribed and translated Caenorhabditis elegans cell death gene (ced-3) product
    • Hugunin M., Quintal L.J., Mankovich J.A., Ghayur T. Protease activity of in vitro transcribed and translated Caenorhabditis elegans cell death gene (ced-3) product. J. Biol. Chem. 271:1996;3517-3522.
    • (1996) J. Biol. Chem. , vol.271 , pp. 3517-3522
    • Hugunin, M.1    Quintal, L.J.2    Mankovich, J.A.3    Ghayur, T.4
  • 24
    • 0032476668 scopus 로고    scopus 로고
    • HSP70 exerts its anti-apoptotic function downstream of caspase-3-like proteases
    • Jäättelä M., Wissing D., Kokholm K., Kallunki T., Egeblad M. HSP70 exerts its anti-apoptotic function downstream of caspase-3-like proteases. EMBO J. 17:1998;6124-6134.
    • (1998) EMBO J. , vol.17 , pp. 6124-6134
    • Jäättelä, M.1    Wissing, D.2    Kokholm, K.3    Kallunki, T.4    Egeblad, M.5
  • 26
    • 0028803791 scopus 로고
    • Regional alterations of ATP and heat-shock protein-72 mRNA following hypoxia-ischemia in neonatal rat brain
    • Kobayashi S., Welsh F.A. Regional alterations of ATP and heat-shock protein-72 mRNA following hypoxia-ischemia in neonatal rat brain. J. Cereb. Blood Flow Metab. 15:1995;1047-1056.
    • (1995) J. Cereb. Blood Flow Metab. , vol.15 , pp. 1047-1056
    • Kobayashi, S.1    Welsh, F.A.2
  • 27
    • 0030031514 scopus 로고    scopus 로고
    • Cyclin D1 is an essential mediator of apoptotic neuronal cell death
    • Kranenburg O., van der Eb A.J., Zantema A. Cyclin D1 is an essential mediator of apoptotic neuronal cell death. EMBO J. 15:1996;46-54.
    • (1996) EMBO J. , vol.15 , pp. 46-54
    • Kranenburg, O.1    Van Der Eb, A.J.2    Zantema, A.3
  • 29
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 30
    • 0030715323 scopus 로고    scopus 로고
    • Ctochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade
    • Li P., Nijhawan D., Budihardjo I., Srinivasula S.M., Ahmad M., Alnemri E.S., Wang X. Ctochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade. Cell. 91:1997;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
  • 31
    • 0030013054 scopus 로고    scopus 로고
    • Purification and characterisation of an interleukin-1β-converting enzyme family protease that activates cysteine protease P32 (CPP32)
    • Liu X., Kim C.N., Pohl J., Wang X. Purification and characterisation of an interleukin-1β-converting enzyme family protease that activates cysteine protease P32 (CPP32). J. Biol. Chem. 271:1996;13371-13376.
    • (1996) J. Biol. Chem. , vol.271 , pp. 13371-13376
    • Liu, X.1    Kim, C.N.2    Pohl, J.3    Wang, X.4
  • 33
    • 0031906033 scopus 로고    scopus 로고
    • Apoptosis of central and peripheral neurons can be prevented with cyclin-dependent kinase/mitogen-activated protein kinase inhibitors
    • Maas J.W. Jr., Horstmann S., Borasio G.D., Anneser J.M.H., Shooter E.M., Kahle P.J. Apoptosis of central and peripheral neurons can be prevented with cyclin-dependent kinase/mitogen-activated protein kinase inhibitors. J. Neurochem. 70:1998;1401-1410.
    • (1998) J. Neurochem. , vol.70 , pp. 1401-1410
    • Maas J.W., Jr.1    Horstmann, S.2    Borasio, G.D.3    Anneser, J.M.H.4    Shooter, E.M.5    Kahle, P.J.6
  • 34
    • 0030897988 scopus 로고    scopus 로고
    • Substrate and inhibitor specificity of interleukin-1-β-converting enzyme and related caspases
    • Margolin N., Raybuck S.A., Wilson K.P., Chen W., Fox T., Gu Y., Livingston D.J. Substrate and inhibitor specificity of interleukin-1-β-converting enzyme and related caspases. J. Biol. Chem. 272:1997;7223-7228.
    • (1997) J. Biol. Chem. , vol.272 , pp. 7223-7228
    • Margolin, N.1    Raybuck, S.A.2    Wilson, K.P.3    Chen, W.4    Fox, T.5    Gu, Y.6    Livingston, D.J.7
  • 35
    • 0030273773 scopus 로고    scopus 로고
    • ICE-like proteases execute the neuronal death program
    • Martinou J.C., Sadoul R. ICE-like proteases execute the neuronal death program. Curr. Opin. Neurobiol. 6:1996;609-614.
    • (1996) Curr. Opin. Neurobiol. , vol.6 , pp. 609-614
    • Martinou, J.C.1    Sadoul, R.2
  • 37
    • 0031589219 scopus 로고    scopus 로고
    • Bcl-2 relieves the trans-repressive function of the glucocorticoid receptor and inhibits the activation of CPP32-like cysteine proteases
    • Miyashita T., U M., Inoue T., Reed J.C., Yamada M. Bcl-2 relieves the trans-repressive function of the glucocorticoid receptor and inhibits the activation of CPP32-like cysteine proteases. Biochem. Biophys. Res. Commun. 233:1997;781-787.
    • (1997) Biochem. Biophys. Res. Commun. , vol.233 , pp. 781-787
    • Miyashita, T.1    U., M.2    Inoue, T.3    Reed, J.C.4    Yamada, M.5
  • 38
    • 0028787189 scopus 로고
    • Bcl-2 protects neural cells from cyanide/aglycemia-induced lipid oxidation, mitochondrial injury, and loss of viability
    • Myers K.M., Fiskum G., Liu Y., Simmens S.J., Bredesen D.E., Murphy A.N. Bcl-2 protects neural cells from cyanide/aglycemia-induced lipid oxidation, mitochondrial injury, and loss of viability. J. Neurochem. 65:1995;2432-2440.
    • (1995) J. Neurochem. , vol.65 , pp. 2432-2440
    • Myers, K.M.1    Fiskum, G.2    Liu, Y.3    Simmens, S.J.4    Bredesen, D.E.5    Murphy, A.N.6
  • 40
    • 0031814454 scopus 로고    scopus 로고
    • Evidence for activation of caspase-3-like protease in excitotoxin- And hypoxia/hypoglycemia-injured neurons
    • Nath R., Probert A. Jr., McGinnis K.M., Wang K.K.W. Evidence for activation of caspase-3-like protease in excitotoxin- and hypoxia/hypoglycemia-injured neurons. J. Neurochem. 71:1998;186-195.
    • (1998) J. Neurochem. , vol.71 , pp. 186-195
    • Nath, R.1    Probert A., Jr.2    McGinnis, K.M.3    Wang, K.K.W.4
  • 41
    • 0029670265 scopus 로고    scopus 로고
    • ICE/CED3-like proteases as therapeutic targets for the control of inappropriate apoptosis
    • Nicholson D.W. ICE/CED3-like proteases as therapeutic targets for the control of inappropriate apoptosis. Nat. Biotechnol. 14:1996;297-301.
    • (1996) Nat. Biotechnol. , vol.14 , pp. 297-301
    • Nicholson, D.W.1
  • 44
    • 0028231413 scopus 로고
    • The heat-shock/stress response in focal cerebral ischemia
    • Nowak T.S., Jacewicz M. The heat-shock/stress response in focal cerebral ischemia. Brain Pathol. 4:1994;67-76.
    • (1994) Brain Pathol. , vol.4 , pp. 67-76
    • Nowak, T.S.1    Jacewicz, M.2
  • 45
    • 0031775603 scopus 로고    scopus 로고
    • Caspases mediate 6-hydroxydopamine-induced apoptosis but not necrosis in PC12 cells
    • Ochu E.E., Rothwell N.J., Waters C.M. Caspases mediate 6-hydroxydopamine-induced apoptosis but not necrosis in PC12 cells. J. Neurochem. 70:1998;2637-2640.
    • (1998) J. Neurochem. , vol.70 , pp. 2637-2640
    • Ochu, E.E.1    Rothwell, N.J.2    Waters, C.M.3
  • 46
    • 0026058318 scopus 로고
    • Cell death during development of the nervous system
    • Oppenheim R.W. Cell death during development of the nervous system. Annu. Rev. Neurosci. 14:1991;453-501.
    • (1991) Annu. Rev. Neurosci. , vol.14 , pp. 453-501
    • Oppenheim, R.W.1
  • 47
    • 0031016498 scopus 로고    scopus 로고
    • G1/S cell cycle blockers and inhibitors of cyclin-dependent kinases suppress camptothecin-induced neuronal apoptosis
    • Park D.S., Morris E.J., Greene L.A., Geller H.M. G1/S cell cycle blockers and inhibitors of cyclin-dependent kinases suppress camptothecin-induced neuronal apoptosis. J. Neurosci. 17:1997;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
  • 49
    • 0029954311 scopus 로고    scopus 로고
    • Potassium deprivation-induced apoptosis of cerebellar granule neurons: A sequential requirement for new mRNA and protein synthesis, ICE-like protease activity, and reactive oxygen species
    • Schulz J.B., Weller M., Klockgether T. Potassium deprivation-induced apoptosis of cerebellar granule neurons: a sequential requirement for new mRNA and protein synthesis, ICE-like protease activity, and reactive oxygen species. J. Neurosci. 16:1996;4696-4706.
    • (1996) J. Neurosci. , vol.16 , pp. 4696-4706
    • Schulz, J.B.1    Weller, M.2    Klockgether, T.3
  • 50
    • 0025328443 scopus 로고
    • Chronic hypoxia in neuronal cell culture: Metabolic consequences
    • Sher P.K. Chronic hypoxia in neuronal cell culture: metabolic consequences. Brain Dev. 12:1990;293-300.
    • (1990) Brain Dev. , vol.12 , pp. 293-300
    • Sher, P.K.1
  • 53
    • 0032528139 scopus 로고    scopus 로고
    • Roles of Bcl-2 and caspases in hypoxia-induced neuronal cell death: A possible neuroprotective mechanism of peptide growth factors
    • Tamatani M., Ogawa S., Tohyama M. Roles of Bcl-2 and caspases in hypoxia-induced neuronal cell death: a possible neuroprotective mechanism of peptide growth factors. Mol. Brain Res. 58:1998;27-39.
    • (1998) Mol. Brain Res. , vol.58 , pp. 27-39
    • Tamatani, M.1    Ogawa, S.2    Tohyama, M.3
  • 54
    • 0030939043 scopus 로고    scopus 로고
    • Apoptosis in cerebellar granule neurones: Involvement of interleukin-1β converting enzyme-like proteases
    • Taylor J., Gatchalian L., Keen G., Rubin L.L. Apoptosis in cerebellar granule neurones: involvement of interleukin-1β converting enzyme-like proteases. J. Neurochem. 68:1997;1598-1605.
    • (1997) J. Neurochem. , vol.68 , pp. 1598-1605
    • Taylor, J.1    Gatchalian, L.2    Keen, G.3    Rubin, L.L.4
  • 55
    • 0028943734 scopus 로고
    • Apoptosis in the pathogenesis and treatment of disease
    • Thompson C.B. Apoptosis in the pathogenesis and treatment of disease. Science. 267:1995;1456-1462.
    • (1995) Science , vol.267 , pp. 1456-1462
    • Thompson, C.B.1
  • 56
    • 0029890689 scopus 로고    scopus 로고
    • The contrasting roles of ICE family proteases and interleukin-1β in apoptosis induced by trophic factor withdrawal and by copper/zinc superoxide dismutase down-regulation
    • Troy C.M., Stefanis L., Prochiantz A., Greene L.A., Shelanski M.L. The contrasting roles of ICE family proteases and interleukin-1β in apoptosis induced by trophic factor withdrawal and by copper/zinc superoxide dismutase down-regulation. Proc. Natl. Acad. Sci. U.S.A. 93:1996;5635-5640.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 5635-5640
    • Troy, C.M.1    Stefanis, L.2    Prochiantz, A.3    Greene, L.A.4    Shelanski, M.L.5
  • 57
    • 0029871920 scopus 로고    scopus 로고
    • Cleavage of sterol regulatory element binding proteins (SREBPs) by CPP32 during apoptosis
    • Wang X., Zelenski N.G., Yang J., Sakai J., Brown M.S., Goldstein J.L. Cleavage of sterol regulatory element binding proteins (SREBPs) by CPP32 during apoptosis. EMBO J. 15:1996;1012-1020.
    • (1996) EMBO J. , vol.15 , pp. 1012-1020
    • Wang, X.1    Zelenski, N.G.2    Yang, J.3    Sakai, J.4    Brown, M.S.5    Goldstein, J.L.6
  • 60
    • 0030804272 scopus 로고    scopus 로고
    • Activation of CPP32-like caspases contributes to neuronal apoptosis and neurological dysfunction after traumatic brain injury
    • Yakovlev A.G., Knoblach S.M., Fan L., Fox G.B., Goodnight R., Faden A.I. Activation of CPP32-like caspases contributes to neuronal apoptosis and neurological dysfunction after traumatic brain injury. J. Neurosci. 17:1997;7415-7424.
    • (1997) J. Neurosci. , vol.17 , pp. 7415-7424
    • Yakovlev, A.G.1    Knoblach, S.M.2    Fan, L.3    Fox, G.B.4    Goodnight, R.5    Faden, A.I.6
  • 61
    • 0027525104 scopus 로고
    • The C. elegans cell death gene ced-3 encodes a protein similar to mammalian interleukin-1 beta-converting enzyme
    • Yuan J., Shaham S., Ledoux S., Ellis H.M., Horvitz H.R. The C. elegans cell death gene ced-3 encodes a protein similar to mammalian interleukin-1 beta-converting enzyme. Cell. 75:1993;641-652.
    • (1993) Cell , vol.75 , pp. 641-652
    • Yuan, J.1    Shaham, S.2    Ledoux, S.3    Ellis, H.M.4    Horvitz, H.R.5


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