메뉴 건너뛰기




Volumn 19, Issue 4, 1999, Pages 356-365

Ischemic delayed neuronal death: Role of the cysteine proteases calpain and cathepsins

Author keywords

Brain ischemia; Calpain; Cathepsin; Delayed neuronal death

Indexed keywords

CALCIUM ION; CALPAIN; CATHEPSIN; CYSTEINE PROTEINASE;

EID: 0033398499     PISSN: 09196544     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1440-1789.1999.00259.x     Document Type: Review
Times cited : (11)

References (82)
  • 1
    • 0020051129 scopus 로고
    • Delayed neuronal death in the gerbil hippocampus following ischemia
    • Kirino T. Delayed neuronal death in the gerbil hippocampus following ischemia. Brain Res 1982; 239: 57-69.
    • (1982) Brain Res , vol.239 , pp. 57-69
    • Kirino, T.1
  • 2
    • 0020067965 scopus 로고
    • Temporal profile of neuronal damage in a model of transient brain ischemia
    • Pulsinelli WA, Brierly JB, Plum F. Temporal profile of neuronal damage in a model of transient brain ischemia. Ann Neurol 1982; 11: 491-498.
    • (1982) Ann Neurol , vol.11 , pp. 491-498
    • Pulsinelli, W.A.1    Brierly, J.B.2    Plum, F.3
  • 3
    • 0022871903 scopus 로고
    • Human amnesia and the medical temporal region: Enduring memory impairment following a bilateral lesion limited to field CA1 of the hippocampus
    • Zola-Morgan S, Squire LR, Amaral DG. Human amnesia and the medical temporal region: Enduring memory impairment following a bilateral lesion limited to field CA1 of the hippocampus. J Neurosci 1986; 6: 2950-2967.
    • (1986) J Neurosci , vol.6 , pp. 2950-2967
    • Zola-Morgan, S.1    Squire, L.R.2    Amaral, D.G.3
  • 4
    • 0023390566 scopus 로고
    • Delayed hippocampal damage in humans following cardiorespiratory arrest
    • Petito CK, Feldmann E, Pulsinelli WA, Plum F. Delayed hippocampal damage in humans following cardiorespiratory arrest. Neurology 1987; 37: 1281-1286.
    • (1987) Neurology , vol.37 , pp. 1281-1286
    • Petito, C.K.1    Feldmann, E.2    Pulsinelli, W.A.3    Plum, F.4
  • 5
    • 0023153653 scopus 로고
    • Calcium accumulation and neuronal damage in the rat hippocampus following cerebral ischemia
    • Deshpande JK, Siesjö BK, Wieloch T. Calcium accumulation and neuronal damage in the rat hippocampus following cerebral ischemia. J Cereb Blood Flow Metab 1987; 7: 89-95.
    • (1987) J Cereb Blood Flow Metab , vol.7 , pp. 89-95
    • Deshpande, J.K.1    Siesjö, B.K.2    Wieloch, T.3
  • 6
    • 0028924890 scopus 로고
    • Delayed neuronal death in the CA1 pyramidal cell layer of the gerbil hippocampus following cerebral ischemia is apoptosis
    • Nitatori T, Sato N, Waguri S et al. Delayed neuronal death in the CA1 pyramidal cell layer of the gerbil hippocampus following cerebral ischemia is apoptosis. J Neurosci 1995; 15: 1001-1011.
    • (1995) J Neurosci , vol.15 , pp. 1001-1011
    • Nitatori, T.1    Sato, N.2    Waguri, S.3
  • 7
    • 0030852994 scopus 로고    scopus 로고
    • Granule cell apoptosis and protein expression in hippocampal dentate gyrus after forebrain ischemia in the rat
    • Li Y, Chopp M, Powers C. Granule cell apoptosis and protein expression in hippocampal dentate gyrus after forebrain ischemia in the rat. J Neurol Sci 1997; 150: 93-102.
    • (1997) J Neurol Sci , vol.150 , pp. 93-102
    • Li, Y.1    Chopp, M.2    Powers, C.3
  • 8
    • 0031953601 scopus 로고    scopus 로고
    • Calcium in ischemic cell death
    • Kristián T, Siesjö BK. Calcium in ischemic cell death. Stroke 1998; 29: 705-718.
    • (1998) Stroke , vol.29 , pp. 705-718
    • Kristián, T.1    Siesjö, B.K.2
  • 9
    • 0023748168 scopus 로고
    • Accumulation of calcium and loss of potassium in the hippocampus following transient cerebral ischemia: A proton microprobe study
    • Martins E, Yanase H, Sakai K et al. Accumulation of calcium and loss of potassium in the hippocampus following transient cerebral ischemia: a proton microprobe study. J Cereb Blood Flow Metab 1988; 8: 531-538.
    • (1988) J Cereb Blood Flow Metab , vol.8 , pp. 531-538
    • Martins, E.1    Yanase, H.2    Sakai, K.3
  • 10
    • 0028178088 scopus 로고
    • 2+ and energy levels during in vitro ischemia in the gerbil hippocampal slice
    • 2+ and energy levels during in vitro ischemia in the gerbil hippocampal slice. J Neurochem 1994; 62: 626-634.
    • (1994) J Neurochem , vol.62 , pp. 626-634
    • Mitani, A.1    Takeyasu, S.2    Yanase, H.3
  • 11
    • 0027336413 scopus 로고
    • 2+ influx in the pathogenesis of delayed neuronal death after brief forebrain ischemia in gerbils
    • 2+ influx in the pathogenesis of delayed neuronal death after brief forebrain ischemia in gerbils. Brain Res 1993; 613: 181-192.
    • (1993) Brain Res , vol.613 , pp. 181-192
    • Nakamura, K.1    Hatakeyama, T.2    Furuta, S.3
  • 12
    • 0032966890 scopus 로고    scopus 로고
    • Continuing postischemic neuronal death in CA1: Influence of ischemia duration and cytoprotective doses of NBQX and SNX-111 in rats
    • Colbourne F, Li H, Buchan AM et al. Continuing postischemic neuronal death in CA1: influence of ischemia duration and cytoprotective doses of NBQX and SNX-111 in rats. Stroke 1999; 30: 662-668.
    • (1999) Stroke , vol.30 , pp. 662-668
    • Colbourne, F.1    Li, H.2    Buchan, A.M.3
  • 14
    • 0028670209 scopus 로고
    • 2+ mobilization induced by hypoxia-hypoglycemia in the monkey hippocampal slices
    • 2+ mobilization induced by hypoxia-hypoglycemia in the monkey hippocampal slices. Biochem Biophys Res Commun 1994; 205: 1843-1849.
    • (1994) Biochem Biophys Res Commun , vol.205 , pp. 1843-1849
    • Yamashima, T.1    Takita, M.2    Akaike, S.3
  • 15
    • 0033023077 scopus 로고    scopus 로고
    • Involvement of glial NO synthase/NO in neuronal apoptosis in the brain
    • Nomura Y. Involvement of glial NO synthase/NO in neuronal apoptosis in the brain. Neuropathology 1999; 19: 1-9.
    • (1999) Neuropathology , vol.19 , pp. 1-9
    • Nomura, Y.1
  • 16
    • 0029784671 scopus 로고    scopus 로고
    • 2 and calpain responses prior to delayed neuronal death in monkeys
    • 2 and calpain responses prior to delayed neuronal death in monkeys. Eur J Neurosci 1996; 8: 1932-1944.
    • (1996) Eur J Neurosci , vol.8 , pp. 1932-1944
    • Yamashima, T.1    Saido, T.C.2    Takita, M.3
  • 17
    • 0031817004 scopus 로고    scopus 로고
    • Inhibition of ischemic hippocampal neuronal death in primates with cathepsin B inhibitor CA-074: A novel strategy for neuroprotection based on 'calpain-cathepsin hypothesis'
    • Yamashima T, Kohda Y, Tsuchiya K et al. Inhibition of ischemic hippocampal neuronal death in primates with cathepsin B inhibitor CA-074: a novel strategy for neuroprotection based on 'calpain-cathepsin hypothesis'. Eur J Neurosci 1998; 10: 1723-1733.
    • (1998) Eur J Neurosci , vol.10 , pp. 1723-1733
    • Yamashima, T.1    Kohda, Y.2    Tsuchiya, K.3
  • 18
    • 0032976738 scopus 로고    scopus 로고
    • Postictal blockade of ischemic hippocampal neuronal death in primates using selective cathepsin inhibitors
    • Tsuchiya K, Kohda Y, Yoshida M et al. Postictal blockade of ischemic hippocampal neuronal death in primates using selective cathepsin inhibitors. Exp Neurol 1999; 155: 187-194.
    • (1999) Exp Neurol , vol.155 , pp. 187-194
    • Tsuchiya, K.1    Kohda, Y.2    Yoshida, M.3
  • 19
    • 0031452173 scopus 로고    scopus 로고
    • Structure and physiological function of calpains
    • Sorimachi H, Ishiura S, Suzuki K. Structure and physiological function of calpains. Biochem J 1997; 328: 721-732.
    • (1997) Biochem J , vol.328 , pp. 721-732
    • Sorimachi, H.1    Ishiura, S.2    Suzuki, K.3
  • 20
    • 0025831476 scopus 로고
    • Calcium-activated neutral protease (calpain) system: Structure, function, and regulation
    • Croall DE, Demartino GN. Calcium-activated neutral protease (calpain) system: structure, function, and regulation. Physiol Rev 1991; 81: 813-847.
    • (1991) Physiol Rev , vol.81 , pp. 813-847
    • Croall, D.E.1    Demartino, G.N.2
  • 21
    • 0030970119 scopus 로고    scopus 로고
    • Emerging roles for cysteine proteases in human biology
    • Chapman HA, Riese RJ, Shi GP. Emerging roles for cysteine proteases in human biology. Annu Rev Physiol 1997; 59: 63-88.
    • (1997) Annu Rev Physiol , vol.59 , pp. 63-88
    • Chapman, H.A.1    Riese, R.J.2    Shi, G.P.3
  • 22
    • 0030320775 scopus 로고    scopus 로고
    • Tumor progression and angiogenesis: Cathepsin & Co
    • Keppler D, Sameni M, Moin K et al. Tumor progression and angiogenesis: cathepsin & Co. Biochem Cell Biol 1996; 74: 799-810.
    • (1996) Biochem Cell Biol , vol.74 , pp. 799-810
    • Keppler, D.1    Sameni, M.2    Moin, K.3
  • 23
    • 0031969695 scopus 로고    scopus 로고
    • Calpain inhibitors, but not caspase inhibitors, prevent actin proteolysis and DNA fragmentation during apoptosis
    • Villa PG, Henzel WJ, Sensenbrenner M et al. Calpain inhibitors, but not caspase inhibitors, prevent actin proteolysis and DNA fragmentation during apoptosis. J Cell Sci 1998; 111: 713-722.
    • (1998) J Cell Sci , vol.111 , pp. 713-722
    • Villa, P.G.1    Henzel, W.J.2    Sensenbrenner, M.3
  • 24
    • 0028282502 scopus 로고
    • Immunolocalization of calpain I-mediated spectrin degradation to vulnerable neurons of the ischemic gerbil brain
    • Roberts-Lewis JM, Savage MJ, Marcy VR et al. Immunolocalization of calpain I-mediated spectrin degradation to vulnerable neurons of the ischemic gerbil brain. J Neurosci 1994; 14: 3934-3944.
    • (1994) J Neurosci , vol.14 , pp. 3934-3944
    • Roberts-Lewis, J.M.1    Savage, M.J.2    Marcy, V.R.3
  • 25
    • 0032479912 scopus 로고    scopus 로고
    • Regional calpain and caspase-3 proteolysis of α-spectrin after traumatic brain injury
    • Pike BR, Zhao X, Newcomb JK et al. Regional calpain and caspase-3 proteolysis of α-spectrin after traumatic brain injury. Neuroreport 1998; 9: 2437-2442.
    • (1998) Neuroreport , vol.9 , pp. 2437-2442
    • Pike, B.R.1    Zhao, X.2    Newcomb, J.K.3
  • 26
    • 0031790060 scopus 로고    scopus 로고
    • Immunoblot analyses of the relative contributions of cysteine and aspartic proteases to neurofilament breakdown products following experimental brain injury in rats
    • Posmantur RM, Zhao X, Kampfl A et al. Immunoblot analyses of the relative contributions of cysteine and aspartic proteases to neurofilament breakdown products following experimental brain injury in rats. Neurochem Res 1998; 23: 1265-1276.
    • (1998) Neurochem Res , vol.23 , pp. 1265-1276
    • Posmantur, R.M.1    Zhao, X.2    Kampfl, A.3
  • 27
    • 17344365975 scopus 로고    scopus 로고
    • Tau cleavage and dephosphorylation in cerebellar granule neurons undergoing apoptosis
    • Canu N, Dus L, Barbato C et al. Tau cleavage and dephosphorylation in cerebellar granule neurons undergoing apoptosis. J Neurosci 1998; 18: 7061-7074.
    • (1998) J Neurosci , vol.18 , pp. 7061-7074
    • Canu, N.1    Dus, L.2    Barbato, C.3
  • 28
    • 0027990307 scopus 로고
    • The calpain cleavage sites in the epidermal growth factor receptor kinase domain
    • Gregoriou M, Willis AC, Pearson MA et al. The calpain cleavage sites in the epidermal growth factor receptor kinase domain. Eur J Biochem 1994; 223: 455-464.
    • (1994) Eur J Biochem , vol.223 , pp. 455-464
    • Gregoriou, M.1    Willis, A.C.2    Pearson, M.A.3
  • 29
    • 0027441185 scopus 로고
    • Specific cleavage of transcription factors by the thiol protease, m-calpain
    • Watt F, Molloy PL. Specific cleavage of transcription factors by the thiol protease, m-calpain. Nucl Acid Res 1993; 21: 5092-5100.
    • (1993) Nucl Acid Res , vol.21 , pp. 5092-5100
    • Watt, F.1    Molloy, P.L.2
  • 30
    • 0029133838 scopus 로고
    • Eukaryotic initiation factor 4E degradation during brain ischemia
    • Neumar RW, DeGracia DJ, White BC et al. Eukaryotic initiation factor 4E degradation during brain ischemia. J Neurochem 1995; 65: 1391-1394.
    • (1995) J Neurochem , vol.65 , pp. 1391-1394
    • Neumar, R.W.1    DeGracia, D.J.2    White, B.C.3
  • 31
    • 0001541499 scopus 로고    scopus 로고
    • Regulation of cyclin Dl by calpain protease
    • Choi YH, Lee SJ, Nguyen P et al. Regulation of cyclin Dl by calpain protease. J Biol Chem 1997; 272: 28479-28484.
    • (1997) J Biol Chem , vol.272 , pp. 28479-28484
    • Choi, Y.H.1    Lee, S.J.2    Nguyen, P.3
  • 32
    • 0031014946 scopus 로고    scopus 로고
    • Proteolytic cleavage of human p53 by calpain: A potential regulator of protein stability
    • Kubbutat MH, Vousden KH. Proteolytic cleavage of human p53 by calpain: a potential regulator of protein stability. Mol Cell Biol 1997; 17: 460-468.
    • (1997) Mol Cell Biol , vol.17 , pp. 460-468
    • Kubbutat, M.H.1    Vousden, K.H.2
  • 33
    • 0031902117 scopus 로고    scopus 로고
    • The involvement of calpain-dependent proteolysis of the tumor suppressor NF2 (merlin) in schwannomas and meningiomas
    • Kimura Y, Koga H, Araki N et al. The involvement of calpain-dependent proteolysis of the tumor suppressor NF2 (merlin) in schwannomas and meningiomas. Nat Med 1998; 4: 915-922.
    • (1998) Nat Med , vol.4 , pp. 915-922
    • Kimura, Y.1    Koga, H.2    Araki, N.3
  • 34
    • 0030571563 scopus 로고    scopus 로고
    • Cleavage of caldesmon and calponin by calpain: Substrate recognition is not dependent on calmodulin binding domains
    • Croall DE, Chacko S, Wang Z. Cleavage of caldesmon and calponin by calpain: substrate recognition is not dependent on calmodulin binding domains. Biochim Biophys Acta 1996; 1298: 276-284.
    • (1996) Biochim Biophys Acta , vol.1298 , pp. 276-284
    • Croall, D.E.1    Chacko, S.2    Wang, Z.3
  • 35
    • 0041018181 scopus 로고    scopus 로고
    • Cleavage of the calpain inhibitor, calpastatin, during apoptosis
    • Porn-Ares MI, Samali A, Orrenius S. Cleavage of the calpain inhibitor, calpastatin, during apoptosis. Cell Death Differ 1998; 5: 1028-1033.
    • (1998) Cell Death Differ , vol.5 , pp. 1028-1033
    • Porn-Ares, M.I.1    Samali, A.2    Orrenius, S.3
  • 36
    • 0030960334 scopus 로고    scopus 로고
    • Mechanisms of suppression of inducible nitric-oxide synthase (iNOS) expression in interferon (IFN)-gamma-stimulated RAW 264.7 cells by dexamethasone. Evidence for glucocorticoid-induced degradation of iNOS protein by calpain as a key step in post-transcriptional regulation
    • Walker G, Pfeilschifter J, Kunz D. Mechanisms of suppression of inducible nitric-oxide synthase (iNOS) expression in interferon (IFN)-gamma-stimulated RAW 264.7 cells by dexamethasone. Evidence for glucocorticoid-induced degradation of iNOS protein by calpain as a key step in post-transcriptional regulation. J Biol Chem 1997; 272: 16679-16687.
    • (1997) J Biol Chem , vol.272 , pp. 16679-16687
    • Walker, G.1    Pfeilschifter, J.2    Kunz, D.3
  • 37
    • 0030466065 scopus 로고    scopus 로고
    • The calpain cascade, μ-calpain activates m-calpain
    • Tompa P, Baki A, Schad E et al. The calpain cascade, μ-calpain activates m-calpain. J Biol Chem 1996; 271: 33161-33164.
    • (1996) J Biol Chem , vol.271 , pp. 33161-33164
    • Tompa, P.1    Baki, A.2    Schad, E.3
  • 38
    • 0028104428 scopus 로고
    • Selective nuclear transport of mu-calpain
    • Mellgren RL, Lu Q. Selective nuclear transport of mu-calpain. Biochem Biophys Res Commun 1994; 204: 544-550.
    • (1994) Biochem Biophys Res Commun , vol.204 , pp. 544-550
    • Mellgren, R.L.1    Lu, Q.2
  • 39
    • 0000976935 scopus 로고    scopus 로고
    • Participation of intracellular cysteine proteinases, in particular cathepsin B, in degradation of collagen in periosteal tissue explants
    • Creemers LB, Hoeben KA, Jansen DC et al. Participation of intracellular cysteine proteinases, in particular cathepsin B, in degradation of collagen in periosteal tissue explants. Matrix Biol 1998; 16: 575-584.
    • (1998) Matrix Biol , vol.16 , pp. 575-584
    • Creemers, L.B.1    Hoeben, K.A.2    Jansen, D.C.3
  • 40
    • 0025834586 scopus 로고
    • Latent fibronectin-degrading serine proteinase activity in N-terminal heparin-binding domain of human plasma fibronectin
    • Lambert Vidmar S, Lottspeich F et al. Latent fibronectin-degrading serine proteinase activity in N-terminal heparin-binding domain of human plasma fibronectin. Eur J Biochem 1991; 201: 71-77.
    • (1991) Eur J Biochem , vol.201 , pp. 71-77
    • Lambert Vidmar, S.1    Lottspeich, F.2
  • 41
    • 0022638636 scopus 로고
    • Acidic lipids enhance cathepsin D cleavage of the myelin basic protein
    • Williams KR, Williams ND, Konigsberg W et al. Acidic lipids enhance cathepsin D cleavage of the myelin basic protein. J Neurosci Res 1986; 15: 137-145.
    • (1986) J Neurosci Res , vol.15 , pp. 137-145
    • Williams, K.R.1    Williams, N.D.2    Konigsberg, W.3
  • 42
    • 0023179385 scopus 로고
    • The breakdown of the individual neurofilament proteins by cathepsin D
    • Banay-Schwartz M, Dahl D, Hui KS, Lajtha A. The breakdown of the individual neurofilament proteins by cathepsin D. Neurochem Res 1987; 12: 361-367.
    • (1987) Neurochem Res , vol.12 , pp. 361-367
    • Banay-Schwartz, M.1    Dahl, D.2    Hui, K.S.3    Lajtha, A.4
  • 43
    • 0026072245 scopus 로고
    • Proteolysis of microtubule-associated protein 2 and tubulin by cathepsin D
    • Johnson GV, Litersky JM, Whitaker JN. Proteolysis of microtubule-associated protein 2 and tubulin by cathepsin D. J Neurochem 1991; 57: 1577-1583.
    • (1991) J Neurochem , vol.57 , pp. 1577-1583
    • Johnson, G.V.1    Litersky, J.M.2    Whitaker, J.N.3
  • 44
    • 0029804989 scopus 로고    scopus 로고
    • Degradation of Alzheimer's β-amyloid protein by human cathepsin D
    • McDermott JR, Gibson AM. Degradation of Alzheimer's β-amyloid protein by human cathepsin D. Neuroreport 1996; 7: 2163-2166.
    • (1996) Neuroreport , vol.7 , pp. 2163-2166
    • McDermott, J.R.1    Gibson, A.M.2
  • 45
    • 0027260790 scopus 로고
    • Conversion of proendothelin-1 into endothelin-1 by asparylproteases
    • Savage P, Shetty SS, Martin LL et al. Conversion of proendothelin-1 into endothelin-1 by asparylproteases. Int J Pept Protein Res 1993; 42: 227-232.
    • (1993) Int J Pept Protein Res , vol.42 , pp. 227-232
    • Savage, P.1    Shetty, S.S.2    Martin, L.L.3
  • 46
    • 0032969486 scopus 로고    scopus 로고
    • Prorenin processing by cathepsin B in vitro and in transfected cells
    • Jutras I, Reudelhuber TL. Prorenin processing by cathepsin B in vitro and in transfected cells. FEBS Lett 1999; 443: 48-52.
    • (1999) FEBS Lett , vol.443 , pp. 48-52
    • Jutras, I.1    Reudelhuber, T.L.2
  • 47
    • 0030764160 scopus 로고    scopus 로고
    • Identification and characterization of cathepsin B as the cellular MARCKS cleaving enzyme
    • Spizz G, Blackshear PJ. Identification and characterization of cathepsin B as the cellular MARCKS cleaving enzyme. J Biol Chem 1997; 272: 23833-23842.
    • (1997) J Biol Chem , vol.272 , pp. 23833-23842
    • Spizz, G.1    Blackshear, P.J.2
  • 48
    • 0031793017 scopus 로고    scopus 로고
    • Atractyloside-induced release of cathepsin B, a protease with caspase-processing activity
    • Vancompernolle K, Van Herreweghe F, Pynaert G et al. Atractyloside-induced release of cathepsin B, a protease with caspase-processing activity. FEBS Lett 1998; 438: 150-158.
    • (1998) FEBS Lett , vol.438 , pp. 150-158
    • Vancompernolle, K.1    Van Herreweghe, F.2    Pynaert, G.3
  • 49
    • 17744417425 scopus 로고    scopus 로고
    • Activation of caspase-3-like protease by digitonin-treated lysosomes
    • Ishisaka R, Utsumi T, Yabuki M et al. Activation of caspase-3-like protease by digitonin-treated lysosomes. FEBS Lett 1998; 435: 233-236.
    • (1998) FEBS Lett , vol.435 , pp. 233-236
    • Ishisaka, R.1    Utsumi, T.2    Yabuki, M.3
  • 50
    • 0032529621 scopus 로고    scopus 로고
    • Caspase-mediated fragmentation of calpain inhibitor protein calpastatin during apoptosis
    • Wang KK, Postmantur R, Nadimpalli R et al. Caspase-mediated fragmentation of calpain inhibitor protein calpastatin during apoptosis. Arch Biochem Biophys 1998; 356: 187-196.
    • (1998) Arch Biochem Biophys , vol.356 , pp. 187-196
    • Wang, K.K.1    Postmantur, R.2    Nadimpalli, R.3
  • 51
    • 0026542341 scopus 로고
    • Autolytic transition of μ-calpain upon activation as resolved by antibodies distinguishing between the pre- and post-autolysis forms
    • Saido TC, Nagao S, Shiramine M et al. Autolytic transition of μ-calpain upon activation as resolved by antibodies distinguishing between the pre- and post-autolysis forms. J Biochem 1992; 111: 81-86.
    • (1992) J Biochem , vol.111 , pp. 81-86
    • Saido, T.C.1    Nagao, S.2    Shiramine, M.3
  • 53
    • 0022742338 scopus 로고
    • Purification and tissue distribution of cathepsin L
    • Bando Y, Kominami E, Katunuma N. Purification and tissue distribution of cathepsin L. Biochem Tokyo 1986; 100: 35-42.
    • (1986) Biochem Tokyo , vol.100 , pp. 35-42
    • Bando, Y.1    Kominami, E.2    Katunuma, N.3
  • 54
    • 0030581677 scopus 로고    scopus 로고
    • Dynamic changes of cathepsin B and L expression in the monkey hippocampus after transient ischemia
    • Kohda Y, Yamashima T, Sakuda K et al. Dynamic changes of cathepsin B and L expression in the monkey hippocampus after transient ischemia. Biochem Biophys Res Commun 1996; 228: 616-622.
    • (1996) Biochem Biophys Res Commun , vol.228 , pp. 616-622
    • Kohda, Y.1    Yamashima, T.2    Sakuda, K.3
  • 55
    • 0028201739 scopus 로고
    • Evidence of nuclear DNA fragmentation following hypoxia-ischemia in the infant rat brain, and transient forebrain ischemia in the adult gerbil
    • Ferrer I, Tortoise A, Macaya A et al. Evidence of nuclear DNA fragmentation following hypoxia-ischemia in the infant rat brain, and transient forebrain ischemia in the adult gerbil. Brain Pathol 1994; 4: 115-122.
    • (1994) Brain Pathol , vol.4 , pp. 115-122
    • Ferrer, I.1    Tortoise, A.2    Macaya, A.3
  • 56
    • 0030044858 scopus 로고    scopus 로고
    • Apoptotic features of selective neuronal death in ischemia, epilepsy and gp120 toxicity
    • Charriaut-Marlangue C, Aggoun-Zouaoui D, Represa A et al. Apoptotic features of selective neuronal death in ischemia, epilepsy and gp120 toxicity. Trends Neurosci 1996; 19: 109-114.
    • (1996) Trends Neurosci , vol.19 , pp. 109-114
    • Charriaut-Marlangue, C.1    Aggoun-Zouaoui, D.2    Represa, A.3
  • 57
    • 0032575750 scopus 로고    scopus 로고
    • Caspases: Enemies within
    • Thornberry NA, Lazebnik Y. Caspases: enemies within. Science 1998; 281: 1312-1316.
    • (1998) Science , vol.281 , pp. 1312-1316
    • Thornberry, N.A.1    Lazebnik, Y.2
  • 58
    • 0030931876 scopus 로고    scopus 로고
    • Caspases: The executioners of apoptosis
    • Cohen GM. Caspases: the executioners of apoptosis. Biochem J 1997; 326: 1-16.
    • (1997) Biochem J , vol.326 , pp. 1-16
    • Cohen, G.M.1
  • 59
    • 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 et al. Induction of caspase-3-like protease may mediate delayed neuronal death in the hippocampus after transient cerebral ischemia. J Neurosci 1998; 18: 4914-4928.
    • (1998) J Neurosci , vol.18 , pp. 4914-4928
    • Chen, J.1    Nagayama, T.2    Jin, K.3
  • 60
    • 0031915562 scopus 로고    scopus 로고
    • Transient global forebrain ischemia induces a prolonged expression of the caspase-3 mRNA in rat hippocampal CA1 pyramidal neurons
    • Ni B, Wu X, Su X et al. Transient global forebrain ischemia induces a prolonged expression of the caspase-3 mRNA in rat hippocampal CA1 pyramidal neurons. J Cereb Blood Flow Metab 1998; 18: 248-256.
    • (1998) J Cereb Blood Flow Metab , vol.18 , pp. 248-256
    • Ni, B.1    Wu, X.2    Su, X.3
  • 61
    • 0031841171 scopus 로고    scopus 로고
    • A caspase inhibitor blocks ischemia-induced delayed neuronal death in the gerbil
    • Himi T, Ishizaki Y, Murota S. A caspase inhibitor blocks ischemia-induced delayed neuronal death in the gerbil. Eur J Neurosci 1998; 10: 777-781.
    • (1998) Eur J Neurosci , vol.10 , pp. 777-781
    • Himi, T.1    Ishizaki, Y.2    Murota, S.3
  • 62
    • 0032101643 scopus 로고    scopus 로고
    • Temporal relationship between de novo protein synthesis, calpain and caspase-3-like protease activation, and DNA fragmentation during apoptosis in septo-hippocampal cultures
    • Pike BR, Zhao X, Newcomb JK et al. Temporal relationship between de novo protein synthesis, calpain and caspase-3-like protease activation, and DNA fragmentation during apoptosis in septo-hippocampal cultures. J Neurosci Res 1998; 52: 505-520.
    • (1998) J Neurosci Res , vol.52 , pp. 505-520
    • Pike, B.R.1    Zhao, X.2    Newcomb, J.K.3
  • 63
    • 17444395181 scopus 로고    scopus 로고
    • Calpain activation is upstream of caspases in radiation-induced apoptosis
    • Waterhouse NJ, Finucane DM, Green DR et al. Calpain activation is upstream of caspases in radiation-induced apoptosis. Cell Death Differ 1998; 12: 1051-1061.
    • (1998) Cell Death Differ , vol.12 , pp. 1051-1061
    • Waterhouse, N.J.1    Finucane, D.M.2    Green, D.R.3
  • 64
    • 0032575752 scopus 로고    scopus 로고
    • Mitochondria and apoptosis
    • Green DR, Reed JC. Mitochondria and apoptosis. Science 1998; 281: 1309-1312.
    • (1998) Science , vol.281 , pp. 1309-1312
    • Green, D.R.1    Reed, J.C.2
  • 65
    • 0031892723 scopus 로고    scopus 로고
    • Mitochondrial permeability transition in apoptosis and necrosis
    • Hirsch T, Susin SA, Marzo I et al. Mitochondrial permeability transition in apoptosis and necrosis. Cell Biol Toxicol 1998; 14: 141-145.
    • (1998) Cell Biol Toxicol , vol.14 , pp. 141-145
    • Hirsch, T.1    Susin, S.A.2    Marzo, I.3
  • 66
    • 17444373424 scopus 로고    scopus 로고
    • Cytochrome c is released from mitochondria into the cytosol after cerebral anoxia or ischemia
    • Perez-Pinzon MA, Xu GP, Born J et al. Cytochrome c is released from mitochondria into the cytosol after cerebral anoxia or ischemia. J Cereb Blood Flow Metab 1999; 19: 39-43.
    • (1999) J Cereb Blood Flow Metab , vol.19 , pp. 39-43
    • Perez-Pinzon, M.A.1    Xu, G.P.2    Born, J.3
  • 67
    • 0033007651 scopus 로고    scopus 로고
    • Differences in the activation of the mitochondrial permeability transition among brain regions in the rat correlate with selective vulnerability
    • Friberg H, Connern C, Halestrap AP et al. Differences in the activation of the mitochondrial permeability transition among brain regions in the rat correlate with selective vulnerability. J Neurochem 1999; 72: 2488-2497.
    • (1999) J Neurochem , vol.72 , pp. 2488-2497
    • Friberg, H.1    Connern, C.2    Halestrap, A.P.3
  • 68
    • 0030951890 scopus 로고    scopus 로고
    • Amelioration by cyclosporin A of brain damage following 5-10 min of ischemia in rats subjected to preischemic hyperglycemia
    • Li PA, Uchino H, Elmer E et al. Amelioration by cyclosporin A of brain damage following 5-10 min of ischemia in rats subjected to preischemic hyperglycemia. Brain Res 1997; 753: 133-140.
    • (1997) Brain Res , vol.753 , pp. 133-140
    • Li, P.A.1    Uchino, H.2    Elmer, E.3
  • 69
    • 9844225599 scopus 로고    scopus 로고
    • Calcium-activated proteolysis as a therapeutic target in cerebrovascular disease
    • Lee KS, Yanamoto H, Fergus A et al. Calcium-activated proteolysis as a therapeutic target in cerebrovascular disease. Ann N Y Acad Sci 1997; 825: 95-103.
    • (1997) Ann N Y Acad Sci , vol.825 , pp. 95-103
    • Lee, K.S.1    Yanamoto, H.2    Fergus, A.3
  • 70
    • 0025826867 scopus 로고
    • Inhibition of proteolysis protects hippocampal neurons from ischemia
    • Lee KS, Frank S, Vanderklish P et al. Inhibition of proteolysis protects hippocampal neurons from ischemia. Proc Natl Acad Sci USA 1991; 88: 7233-7237.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 7233-7237
    • Lee, K.S.1    Frank, S.2    Vanderklish, P.3
  • 71
    • 0031841171 scopus 로고    scopus 로고
    • A caspase inhibitor blocks ischemia-induced delayed neuronal death in the gerbil
    • Himi T, Ishizaki Y, Murota S. A caspase inhibitor blocks ischemia-induced delayed neuronal death in the gerbil. Eur J Neurosci 1998; 10: 777-781.
    • (1998) Eur J Neurosci , vol.10 , pp. 777-781
    • Himi, T.1    Ishizaki, Y.2    Murota, S.3
  • 72
    • 0028817389 scopus 로고
    • Diazepam, given postischemia, protects selectively vulnerable neurons in the rat hippocampus and striatum
    • Schwartz RD, Yu X, Katzman MR et al. Diazepam, given postischemia, protects selectively vulnerable neurons in the rat hippocampus and striatum. J Neurosci 1995; 15: 529-539.
    • (1995) J Neurosci , vol.15 , pp. 529-539
    • Schwartz, R.D.1    Yu, X.2    Katzman, M.R.3
  • 73
    • 0031558633 scopus 로고    scopus 로고
    • Protective effect of a low dose of colchicine on the delayed cell death of hippocampal CAl neurons following transient forebrain ischemia
    • Kimura M, Saji M. Protective effect of a low dose of colchicine on the delayed cell death of hippocampal CAl neurons following transient forebrain ischemia. Brain Res 1997; 774: 229-233.
    • (1997) Brain Res , vol.774 , pp. 229-233
    • Kimura, M.1    Saji, M.2
  • 74
    • 0029918506 scopus 로고    scopus 로고
    • Neuroprotective effect of FK506, an immunosuppressant, on transient global ischemia in gerbil
    • Tokime T, Nozaki K, Kikuchi H. Neuroprotective effect of FK506, an immunosuppressant, on transient global ischemia in gerbil. Neurosci Lett 1996; 206: 81-84.
    • (1996) Neurosci Lett , vol.206 , pp. 81-84
    • Tokime, T.1    Nozaki, K.2    Kikuchi, H.3
  • 75
    • 0026795993 scopus 로고
    • Acidic fibroblast growth factor prevents death of hippocampal CA1 pyramidal cells following ischemia
    • Sasaki K, Oomura Y, Suzuki K et al. Acidic fibroblast growth factor prevents death of hippocampal CA1 pyramidal cells following ischemia. Neurochem Int 1992; 21: 397-402.
    • (1992) Neurochem Int , vol.21 , pp. 397-402
    • Sasaki, K.1    Oomura, Y.2    Suzuki, K.3
  • 76
    • 0000135127 scopus 로고    scopus 로고
    • Protection of hippocampal neurons from ischemia-induced delayed neuronal death by hepatocyte growth factor: A novel neurotrophic factor
    • Miyazata T, Matsumoto K, Ohmichi H et al. Protection of hippocampal neurons from ischemia-induced delayed neuronal death by hepatocyte growth factor: a novel neurotrophic factor. J Cereb Blood Flow Metab 1998; 18: 345-348.
    • (1998) J Cereb Blood Flow Metab , vol.18 , pp. 345-348
    • Miyazata, T.1    Matsumoto, K.2    Ohmichi, H.3
  • 77
    • 0032541386 scopus 로고    scopus 로고
    • Interleukin 3 prevents delayed neuronal death in the hippocampal CA1 field
    • Wen TC, Takaka J, Peng H et al. Interleukin 3 prevents delayed neuronal death in the hippocampal CA1 field. J Exp Med 1998; 188: 635-649.
    • (1998) J Exp Med , vol.188 , pp. 635-649
    • Wen, T.C.1    Takaka, J.2    Peng, H.3
  • 78
    • 0033083559 scopus 로고    scopus 로고
    • Neuronal cell death: A demise with different shapes
    • Nicotera P, Leist M, Manzo L. Neuronal cell death: a demise with different shapes. Trends Pharmacol Sci 1999; 20: 46-51.
    • (1999) Trends Pharmacol Sci , vol.20 , pp. 46-51
    • Nicotera, P.1    Leist, M.2    Manzo, L.3
  • 79
    • 0032125488 scopus 로고    scopus 로고
    • Neurodegeneration in excitotoxicity, global cerebral ischemia, and target deprivation: A perspective on the contributions of apoptosis and necrosis
    • Martin LJ, Al-Abdula NA, Brambrink AM et al. Neurodegeneration in excitotoxicity, global cerebral ischemia, and target deprivation: a perspective on the contributions of apoptosis and necrosis. Brain Res Bull 1998; 46: 281-309.
    • (1998) Brain Res Bull , vol.46 , pp. 281-309
    • Martin, L.J.1    Al-Abdula, N.A.2    Brambrink, A.M.3
  • 80
    • 0029891535 scopus 로고    scopus 로고
    • Retardation of chemical-induced necrotic death by bcl-2 and ICE inhibitors: Possible involvement of common mediators in apoptotic and necrotic signal transductions
    • Shimizu S, Eguchi Y, Kamiike W et al. Retardation of chemical-induced necrotic death by bcl-2 and ICE inhibitors: possible involvement of common mediators in apoptotic and necrotic signal transductions. Oncogens 1996; 12: 2045-2050.
    • (1996) Oncogens , vol.12 , pp. 2045-2050
    • Shimizu, S.1    Eguchi, Y.2    Kamiike, W.3
  • 81
    • 0031214063 scopus 로고    scopus 로고
    • Amyloid β-protein induces necrotic cell death mediated by ICE cascade in PC12 cells
    • Suzuki A. Amyloid β-protein induces necrotic cell death mediated by ICE cascade in PC12 cells. Exp Cell Res 1997; 234: 507-511.
    • (1997) Exp Cell Res , vol.234 , pp. 507-511
    • Suzuki, A.1
  • 82
    • 0032569838 scopus 로고    scopus 로고
    • Regulation of reactive oxygen species-induced apoptosis and necrosis by caspase 3-like proteases
    • Higuchi M, Honda T, Proske RJ et al. Regulation of reactive oxygen species-induced apoptosis and necrosis by caspase 3-like proteases. Oncogene 1998; 26: 2753-2760.
    • (1998) Oncogene , vol.26 , pp. 2753-2760
    • Higuchi, M.1    Honda, T.2    Proske, R.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.