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Volumn 24, Issue 3, 1999, Pages 371-382

Maitotoxin induces calpain but not caspase-3 activation and necrotic cell death in primary septo-hippocampal cultures

Author keywords

Apoptosis; Calpain; Caspases; Maitotoxin; Necrosis

Indexed keywords

CALCIUM CHANNEL; CALPAIN; CASPASE 3; MAITOTOXIN;

EID: 0032965137     PISSN: 03643190     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1020933616351     Document Type: Article
Times cited : (58)

References (72)
  • 1
    • 0024466037 scopus 로고
    • The calpains
    • Melloni, E., and Pontremoli, S. 1989. The calpains. TINS 12:438-444.
    • (1989) TINS , vol.12 , pp. 438-444
    • Melloni, E.1    Pontremoli, S.2
  • 2
    • 0022462405 scopus 로고
    • Proteolysis of the calcium-dependent protease inhibitor by myocardial calcium-dependent protease
    • Mellgren, R.L., Mericle, M.T., and Lane, R.D. 1986. Proteolysis of the calcium-dependent protease inhibitor by myocardial calcium-dependent protease. Arch. Biochem. Biophys. 246(1):233-9.
    • (1986) Arch. Biochem. Biophys. , vol.246 , Issue.1 , pp. 233-239
    • Mellgren, R.L.1    Mericle, M.T.2    Lane, R.D.3
  • 3
    • 0028088153 scopus 로고
    • Calpain: New perspectives in molecular diversity and physiological-pathological involvement
    • Saido, T.C., Sorimachi, H., and Suzuki, K. 1994. Calpain: new perspectives in molecular diversity and physiological-pathological involvement. FASEB J. 8:814-822.
    • (1994) FASEB J. , vol.8 , pp. 814-822
    • Saido, T.C.1    Sorimachi, H.2    Suzuki, K.3
  • 4
    • 0029360698 scopus 로고
    • Calpain: Novel family members, activation and physiological function
    • Suzuki, K., Sorimachi. H., Yoshizawa, T., Kinbara, K., and Ishiura, S. 1995. Calpain: novel family members, activation and physiological function. Biol. Chem. 376:523-529.
    • (1995) Biol. Chem. , vol.376 , pp. 523-529
    • Suzuki, K.1    Sorimachi, H.2    Yoshizawa, T.3    Kinbara, K.4    Ishiura, S.5
  • 6
    • 0023000721 scopus 로고
    • Distribution of calpains I and II in rat brain
    • Hamakubo, T., Kannagi, R., Murachi, T., Matus, A. 1986. Distribution of calpains I and II in rat brain. J. Neurosci. 6(11):3103-11.
    • (1986) J. Neurosci. , vol.6 , Issue.11 , pp. 3103-3111
    • Hamakubo, T.1    Kannagi, R.2    Murachi, T.3    Matus, A.4
  • 7
    • 0025285178 scopus 로고
    • Distribution of calcium-activated protease calpain in the rat brain
    • Perlmutter, L.S., Gall, C., Baudry, M., and Lynch, G. 1990. Distribution of calcium-activated protease calpain in the rat brain. J. Comp. Neurol. 296:269-276.
    • (1990) J. Comp. Neurol. , vol.296 , pp. 269-276
    • Perlmutter, L.S.1    Gall, C.2    Baudry, M.3    Lynch, G.4
  • 8
    • 0029896181 scopus 로고    scopus 로고
    • Role of calpain in spinal cord injury: Increased calpain immunoreactivity in rat spinal cord after impact trauma
    • Li, Z., Hogan, E.L., and Banik, N.L. 1996. Role of calpain in spinal cord injury: increased calpain immunoreactivity in rat spinal cord after impact trauma. Neurochemical Res. 21(4):441-8.
    • (1996) Neurochemical Res. , vol.21 , Issue.4 , pp. 441-448
    • Li, Z.1    Hogan, E.L.2    Banik, N.L.3
  • 9
    • 0024407571 scopus 로고
    • Calmodulin-binding proteins as calpain substrates
    • Wang, K.K.W., Villalobo, A., and Roufogalis, B.D. 1989. Calmodulin-binding proteins as calpain substrates. Biochem. J. 262: 693-706.
    • (1989) Biochem. J. , vol.262 , pp. 693-706
    • Wang, K.K.W.1    Villalobo, A.2    Roufogalis, B.D.3
  • 10
    • 0030951668 scopus 로고    scopus 로고
    • Mechanisms of calpain proteolysis following traumatic brain injury: Implications for pathology and therapy; implications for pathology and therapy: a review and update
    • Kampfl, A., Posmantur, R.M., Zhao, X., Schmutzhard, E., Clifton, G.L., and Hayes, R.L. 1997. Mechanisms of calpain proteolysis following traumatic brain injury: implications for pathology and therapy; implications for pathology and therapy: a review and update. J. Neurotrauma 14:121-134.
    • (1997) J. Neurotrauma , vol.14 , pp. 121-134
    • Kampfl, A.1    Posmantur, R.M.2    Zhao, X.3    Schmutzhard, E.4    Clifton, G.L.5    Hayes, R.L.6
  • 11
    • 0029854806 scopus 로고    scopus 로고
    • Non-erythroid α-spectrin breakdown by calpain and interleukin 1β-converting-enzyme-like protease(s) in apoptotic cells: Contributory roles of both protease families in neuronal apoptosis
    • Yuen, P., Gilbertsen, R.B., and Wang, K.K.W. 1996. Non-erythroid α-spectrin breakdown by calpain and interleukin 1β-converting-enzyme-like protease(s) in apoptotic cells: contributory roles of both protease families in neuronal apoptosis. Biochem. J. 319:683-690.
    • (1996) Biochem. J. , vol.319 , pp. 683-690
    • Yuen, P.1    Gilbertsen, R.B.2    Wang, K.K.W.3
  • 12
    • 0001454672 scopus 로고    scopus 로고
    • The calpain hypothesis of neurodegeneration: Evidence for a common cytotoxic pathway
    • Bartus, R.T. 1997. The calpain hypothesis of neurodegeneration: Evidence for a common cytotoxic pathway. Neuroscientist 3:314-327.
    • (1997) Neuroscientist , vol.3 , pp. 314-327
    • Bartus, R.T.1
  • 13
    • 0030893206 scopus 로고    scopus 로고
    • Effects of ICE-like proteases and calpain inhibitors on neuronal apoptosis
    • Nath, R., McGinnis, K.J., Nadimpalli, R., Stafford, D., and Wang, K.K.W. 1996. Effects of ICE-like proteases and calpain inhibitors on neuronal apoptosis. Neuroreport 8:249-255.
    • (1996) Neuroreport , vol.8 , pp. 249-255
    • Nath, R.1    McGinnis, K.J.2    Nadimpalli, R.3    Stafford, D.4    Wang, K.K.W.5
  • 17
    • 0032101643 scopus 로고    scopus 로고
    • Temporal relationships between de Novo protein synthesis, calpain and caspase-3 (CPP32) protease activation, and DNA fragmentation during apoptosis in septo-hippocampal cultures
    • In press
    • Pike, B.R., Zhao, X., Newcomb, J.K., Wang, K.K.W., Posmantur, R.M., and Hayes, R.L. 1998. Temporal relationships between De Novo protein synthesis, calpain and caspase-3 (CPP32) protease activation, and DNA fragmentation during apoptosis in septo-hippocampal cultures. J. Neurosci. Res., In press.
    • (1998) J. Neurosci. Res.
    • Pike, B.R.1    Zhao, X.2    Newcomb, J.K.3    Wang, K.K.W.4    Posmantur, R.M.5    Hayes, R.L.6
  • 18
    • 0028874795 scopus 로고
    • Apoptosis induced by protein kinase-C inhibition in a neuroblastoma cell line
    • Behrens, M.M., Marinez, J.L., Moratilla, C., and Renart, J. 1995. Apoptosis induced by protein kinase-C inhibition in a neuroblastoma cell line. Cell Growth Diff. 6:1375-1380.
    • (1995) Cell Growth Diff. , vol.6 , pp. 1375-1380
    • Behrens, M.M.1    Marinez, J.L.2    Moratilla, C.3    Renart, J.4
  • 19
    • 0030893610 scopus 로고    scopus 로고
    • Role of calpain-and interleukin-1β converting enzyme-like proteases in the β-amyloid-induced death of rat hippocampal neurons in culture
    • Jordan, J., Galindo, M.F., and Miller, R.J. 1997. Role of calpain-and interleukin-1β converting enzyme-like proteases in the β-amyloid-induced death of rat hippocampal neurons in culture. J. Neurochem. 68:1612-1621.
    • (1997) J. Neurochem. , vol.68 , pp. 1612-1621
    • Jordan, J.1    Galindo, M.F.2    Miller, R.J.3
  • 20
    • 0030804678 scopus 로고    scopus 로고
    • The role of CED-3-related cysteine proteases in apoptosis of cerebellar granule
    • Eldadah, B.A., Yakovlev, A.G., and Faden, A.I. 1997. The role of CED-3-related cysteine proteases in apoptosis of cerebellar granule. J. Neurosci. 17(16):6105-6113.
    • (1997) J. Neurosci. , vol.17 , Issue.16 , pp. 6105-6113
    • Eldadah, B.A.1    Yakovlev, A.G.2    Faden, A.I.3
  • 21
    • 0029995766 scopus 로고    scopus 로고
    • A license to kill
    • Fraser, A., and Evan, G. 1996. A license to kill. Cell 85(6):781-4.
    • (1996) Cell , vol.85 , Issue.6 , pp. 781-784
    • Fraser, A.1    Evan, G.2
  • 22
    • 0027449187 scopus 로고
    • Induction of apoptosis in fibroblasts by IL-1 beta-converting enzyme, a mammalian homolog of the C. elegans cell death gene ced-3
    • Miura, M., Zhu, H., Rotello, R., Hartwieg, E.A., and Yuan, J. 1993. Induction of apoptosis in fibroblasts by IL-1 beta-converting enzyme, a mammalian homolog of the C. elegans cell death gene ced-3. Cell 75(4):653-60.
    • (1993) Cell , vol.75 , Issue.4 , pp. 653-660
    • Miura, M.1    Zhu, H.2    Rotello, R.3    Hartwieg, E.A.4    Yuan, J.5
  • 24
    • 0030931876 scopus 로고    scopus 로고
    • Caspases: The executioners of apoptosis
    • Cohen, G.M. 1997. Caspases: the executioners of apoptosis. Biochem. J. 326:1-16.
    • (1997) Biochem. J. , vol.326 , pp. 1-16
    • Cohen, G.M.1
  • 26
    • 0029854806 scopus 로고    scopus 로고
    • Non-erythroid alpha-spectrin breakdown by calpain and interleukin 1 beta-converting-enzyme-like protease(s) in apoptotic cells: Contributory roles of both protease families in neuronal apoptosis
    • Nath, R., Raser, K.J., Stafford, D., Hajimohammadreza, I., Posner, A., Allen, H., Talanian, R.V., Yuen, P., Gilbertsen, R.B., and Wang, K.K. 1996. Non-erythroid alpha-spectrin breakdown by calpain and interleukin 1 beta-converting-enzyme-like protease(s) in apoptotic cells: contributory roles of both protease families in neuronal apoptosis. Biochemical J. 319 (Pt 3):683-90.
    • (1996) Biochemical J. , vol.319 , Issue.3 PT , pp. 683-690
    • Nath, R.1    Raser, K.J.2    Stafford, D.3    Hajimohammadreza, I.4    Posner, A.5    Allen, H.6    Talanian, R.V.7    Yuen, P.8    Gilbertsen, R.B.9    Wang, K.K.10
  • 27
    • 0031814454 scopus 로고    scopus 로고
    • Evidence for activation of caspase-3-like protease in excitotoxins and hipoxia/hypoglycemia-injured cerebrocortical neurons
    • In press
    • Nath, R., Robert, A., Mcginnis, K.M., and Wang, K.K.W. 1998. Evidence for activation of caspase-3-like protease in excitotoxins and hipoxia/hypoglycemia-injured cerebrocortical neurons. J. Neurochem., In press.
    • (1998) J. Neurochem.
    • Nath, R.1    Robert, A.2    Mcginnis, K.M.3    Wang, K.K.W.4
  • 28
    • 0027276494 scopus 로고
    • The protein kinase inhibitor staurosporine induces morphological changes typical of apoptosis in MOLT-4 cells without concomitant DNA fragmentation
    • Falcieri, E., Marrtelli, A.M., Bareggi, R., Cataldi, A., and Cocco, L. 1993. The protein kinase inhibitor staurosporine induces morphological changes typical of apoptosis in MOLT-4 cells without concomitant DNA fragmentation. Biochem. Biophys. Res. Comm. 193:19-25.
    • (1993) Biochem. Biophys. Res. Comm. , vol.193 , pp. 19-25
    • Falcieri, E.1    Marrtelli, A.M.2    Bareggi, R.3    Cataldi, A.4    Cocco, L.5
  • 30
    • 0030586363 scopus 로고    scopus 로고
    • Hajimohammadreza I. Maitotoxin induces calpain activation in SH-SY5Y neuroblastoma cells and cerebrocortical cultures
    • Wang, K.K.W., Nath, R., and Raser, K.J. 1996. Hajimohammadreza I. Maitotoxin induces calpain activation in SH-SY5Y neuroblastoma cells and cerebrocortical cultures. Arch. Biochem. Biophys. 331(2):208-14.
    • (1996) Arch. Biochem. Biophys. , vol.331 , Issue.2 , pp. 208-214
    • Wang, K.K.W.1    Nath, R.2    Raser, K.J.3
  • 31
    • 0025358492 scopus 로고
    • Maitotoxin: A unique pharmacological tool for research on calcium-dependent mechanisms
    • Gusovsky, F., and Daly, J.W. 1990. Maitotoxin: a unique pharmacological tool for research on calcium-dependent mechanisms. Biochem. Pharmacol. 39(11):1633-9.
    • (1990) Biochem. Pharmacol. , vol.39 , Issue.11 , pp. 1633-1639
    • Gusovsky, F.1    Daly, J.W.2
  • 32
    • 0026556348 scopus 로고
    • Maitotoxin effects are blocked by SK&F 96365, an inhibitor of receptor-mediated calcium entry
    • Soergel, D.G., Yasumoto, T., Daly, J.W., and Gusovsky, F. 1992. Maitotoxin effects are blocked by SK&F 96365, an inhibitor of receptor-mediated calcium entry. Mol. Pharmacol. 41:487-493.
    • (1992) Mol. Pharmacol. , vol.41 , pp. 487-493
    • Soergel, D.G.1    Yasumoto, T.2    Daly, J.W.3    Gusovsky, F.4
  • 33
    • 0026729258 scopus 로고
    • Maitotoxin-induced intracellular calcium rise in PC12 cells: Involvement of dihydropyridine-sensitive and omega-conotoxin-sensitive calcium channels and phosphoinositide breakdown
    • Meucci, O., Grimaldi, M., Scorziello, A., Govoni, S., Bergamaschi, S., Yasumoto, T., and Schettini, G. 1992. Maitotoxin-induced intracellular calcium rise in PC12 cells: involvement of dihydropyridine-sensitive and omega-conotoxin-sensitive calcium channels and phosphoinositide breakdown. J. Neurochem. 59:679-688.
    • (1992) J. Neurochem. , vol.59 , pp. 679-688
    • Meucci, O.1    Grimaldi, M.2    Scorziello, A.3    Govoni, S.4    Bergamaschi, S.5    Yasumoto, T.6    Schettini, G.7
  • 34
    • 0028132844 scopus 로고
    • Maitotoxin activates cation channels distinct from the receptor-activated non-selective cation channels of HL-60 cells
    • Musgrave, I.F., Seifert, R., and Schultz, G. 1994. Maitotoxin activates cation channels distinct from the receptor-activated non-selective cation channels of HL-60 cells. Biochem. J. 301:437-441.
    • (1994) Biochem. J. , vol.301 , pp. 437-441
    • Musgrave, I.F.1    Seifert, R.2    Schultz, G.3
  • 35
    • 0029589516 scopus 로고
    • Ultrastructure of excitotoxic neuronal death in murine cortical culture
    • Regan, R.F., Panter, S.S., Witz, A., Tilly, J.L., and Giffard, R.G. 1995. Ultrastructure of excitotoxic neuronal death in murine cortical culture. Brain Res. 705(1-2):188-98.
    • (1995) Brain Res. , vol.705 , Issue.1-2 , pp. 188-198
    • Regan, R.F.1    Panter, S.S.2    Witz, A.3    Tilly, J.L.4    Giffard, R.G.5
  • 36
    • 0028282502 scopus 로고
    • Immunolocalization of calpain I-mediated spectrin degradation to vulnerable neurons in the ischemic gerbil brain
    • Roberts-Lewis, J.M., Savage, M.J., Marcy, V.R., Pinsker, L.R., and Siman, R. 1994. Immunolocalization of calpain I-mediated spectrin degradation to vulnerable neurons in the ischemic gerbil brain. J. Neurosci. 14(6):3934-44.
    • (1994) J. Neurosci. , vol.14 , Issue.6 , pp. 3934-3944
    • Roberts-Lewis, J.M.1    Savage, M.J.2    Marcy, V.R.3    Pinsker, L.R.4    Siman, R.5
  • 37
    • 0344284697 scopus 로고    scopus 로고
    • An overview of calpain
    • In press
    • Wang, K.K.W. 1998. An overview of calpain. Bio-reguladores, In press.
    • (1998) Bio-reguladores
    • Wang, K.K.W.1
  • 38
    • 0030070664 scopus 로고    scopus 로고
    • Calpain inhibitors protect against depolarization induced neurofilament protein loss of septo-hippocampal neurons in culture
    • Kampfl, A., Zhao, X., Whitson, J.S., Posmantur, R., Dixon, C.E., Yang, K., Clifton, G.L., and Hayes, R.L. 1996. Calpain inhibitors protect against depolarization induced neurofilament protein loss of septo-hippocampal neurons in culture. Eur. J. Neurosci. 8:344-352.
    • (1996) Eur. J. Neurosci. , vol.8 , pp. 344-352
    • Kampfl, A.1    Zhao, X.2    Whitson, J.S.3    Posmantur, R.4    Dixon, C.E.5    Yang, K.6    Clifton, G.L.7    Hayes, R.L.8
  • 40
    • 0023851503 scopus 로고
    • Inhibitors of protein synthesis and RNA synthesis prevent neuronal death caused by nerve growth factor deprivation
    • Martin, D.P., Schmidt, R.E., DiStefano, P.S., Lowry, O.H., Carter, J.G., and Johnson, E.M. 1988. Inhibitors of protein synthesis and RNA synthesis prevent neuronal death caused by nerve growth factor deprivation. J. Cell. Biol. 106:829-844.
    • (1988) J. Cell. Biol. , vol.106 , pp. 829-844
    • Martin, D.P.1    Schmidt, R.E.2    DiStefano, P.S.3    Lowry, O.H.4    Carter, J.G.5    Johnson, E.M.6
  • 41
    • 0021925444 scopus 로고
    • An improved method to determine cell viability by simultaneous staining with fluorescein diacetate-propidium iodide
    • Jones, K.H., and Senft, A.J. 1985. An improved method to determine cell viability by simultaneous staining with fluorescein diacetate-propidium iodide. J. Histochem. Cytochem 33:77-79.
    • (1985) J. Histochem. Cytochem , vol.33 , pp. 77-79
    • Jones, K.H.1    Senft, A.J.2
  • 42
    • 0028323164 scopus 로고
    • A selective procedure for DNA extraction from apoptotic cells applicable for gel electrophoresis and flow cytometry
    • Gong, J., Traganos, F., and Darzynkiewicz, Z. 1994. A selective procedure for DNA extraction from apoptotic cells applicable for gel electrophoresis and flow cytometry. Analyt. Biochem. 218(2): 314-319.
    • (1994) Analyt. Biochem. , vol.218 , Issue.2 , pp. 314-319
    • Gong, J.1    Traganos, F.2    Darzynkiewicz, Z.3
  • 43
    • 0023880781 scopus 로고    scopus 로고
    • Histopathological studies of experimental marine toxin poisoning. II. the acute effects of maitotoxin on the stomach, heart and lymphoid tissues in mice and rats
    • 1988.
    • Terao, K., Ito, E., Sakamaki, Y., Igarashi, K., Yokoyama, A., and Yasumoto, T. 1998. Histopathological studies of experimental marine toxin poisoning. II. The acute effects of maitotoxin on the stomach, heart and lymphoid tissues in mice and rats. Toxicon 26(4):395-402, 1988.
    • (1998) Toxicon , vol.26 , Issue.4 , pp. 395-402
    • Terao, K.1    Ito, E.2    Sakamaki, Y.3    Igarashi, K.4    Yokoyama, A.5    Yasumoto, T.6
  • 45
    • 0023472120 scopus 로고
    • Maitotoxin stimulates phosphoinositide breakdown in neuroblastoma hybrid NCB-20 cells
    • Gusovsky, F., Yasumoto, T., and Daly, J.W. 1987. Maitotoxin stimulates phosphoinositide breakdown in neuroblastoma hybrid NCB-20 cells. Cell. Mol. Neurobiol. 7(3):317-22.
    • (1987) Cell. Mol. Neurobiol. , vol.7 , Issue.3 , pp. 317-322
    • Gusovsky, F.1    Yasumoto, T.2    Daly, J.W.3
  • 46
    • 0022549919 scopus 로고
    • Maitotoxin stimulates the formation of inositol phosphates in rat aortic myocytes
    • Berta, P., Sladeczek, F., Derancourt, J., Durand, M., Travo, P., and Haiech, J. 1986. Maitotoxin stimulates the formation of inositol phosphates in rat aortic myocytes. FEBS Lett. 197(1-2):349-52.
    • (1986) FEBS Lett. , vol.197 , Issue.1-2 , pp. 349-352
    • Berta, P.1    Sladeczek, F.2    Derancourt, J.3    Durand, M.4    Travo, P.5    Haiech, J.6
  • 47
    • 0025021676 scopus 로고
    • Maitotoxin: Effects on calcium channels, phosphoinositide breakdown, and arachidonate release in pheochromocytoma PC12 cells
    • Choi, O.H., Padgett, W.L., Nishizawa, Y., Gusovsky, F., Yasumoto, T., and Daly, J.W. 1990. Maitotoxin: effects on calcium channels, phosphoinositide breakdown, and arachidonate release in pheochromocytoma PC12 cells. Mol. Pharmacol. 37(2):222-30.
    • (1990) Mol. Pharmacol. , vol.37 , Issue.2 , pp. 222-230
    • Choi, O.H.1    Padgett, W.L.2    Nishizawa, Y.3    Gusovsky, F.4    Yasumoto, T.5    Daly, J.W.6
  • 48
    • 0032007328 scopus 로고    scopus 로고
    • Modification of ion homestasis by lipid peroxidation-roles in neuronal degeneration and adaptive plasticity
    • Mattson, M.P. 1998. Modification of ion homestasis by lipid peroxidation-roles in neuronal degeneration and adaptive plasticity. TINS 21(2):53-57.
    • (1998) TINS , vol.21 , Issue.2 , pp. 53-57
    • Mattson, M.P.1
  • 49
    • 0031062295 scopus 로고    scopus 로고
    • Calpain activation and not oxidative damage mediates L-2-chloropropionic acid-induced cerebellar granule cell necrosis
    • Widdowson, P.S., Gyte, A., Upton, R., Foster, J., Coutts, C.T., and Wyatt, I. 1997. Calpain activation and not oxidative damage mediates L-2-chloropropionic acid-induced cerebellar granule cell necrosis. Tox. Appl. Pharmacol. 142(2):248-55.
    • (1997) Tox. Appl. Pharmacol. , vol.142 , Issue.2 , pp. 248-255
    • Widdowson, P.S.1    Gyte, A.2    Upton, R.3    Foster, J.4    Coutts, C.T.5    Wyatt, I.6
  • 50
    • 0030872701 scopus 로고    scopus 로고
    • Immunohistochemical study of calpain-mediated breakdown products to alpha-spectrin following controlled cortical impact injury in the rat
    • Newcomb, J.K., Kampfl, A., Posmantur, R.M., Zhao, X., Pike, B.R., Liu, S.J., Clifton, G.L., and Hayes, R.L. 1997. Immunohistochemical study of calpain-mediated breakdown products to alpha-spectrin following controlled cortical impact injury in the rat. J. Neurotrauma 14(6):369-83.
    • (1997) J. Neurotrauma , vol.14 , Issue.6 , pp. 369-383
    • Newcomb, J.K.1    Kampfl, A.2    Posmantur, R.M.3    Zhao, X.4    Pike, B.R.5    Liu, S.J.6    Clifton, G.L.7    Hayes, R.L.8
  • 51
    • 10544238107 scopus 로고    scopus 로고
    • Protease involvement in fodrin cleavage and phosphatidylserine exposure in apoptosis
    • Vanags, D.M., Porn-Ares, M.I., Coppola, S., Burgess, D.H., and Orrenius, S. 1996. Protease involvement in fodrin cleavage and phosphatidylserine exposure in apoptosis. J. Biol. Chem. 271: 31075-31081.
    • (1996) J. Biol. Chem. , vol.271 , pp. 31075-31081
    • Vanags, D.M.1    Porn-Ares, M.I.2    Coppola, S.3    Burgess, D.H.4    Orrenius, S.5
  • 52
    • 0031037897 scopus 로고    scopus 로고
    • The release of cytochrome c from mitochondria: A primary site for Bcl-2 regulation of apoptosis
    • Kluck, R.M., Bossy-Wetzel, E., Green, D.R., and Newmeyer, D.D. 1997. The release of cytochrome c from mitochondria: a primary site for Bcl-2 regulation of apoptosis. Science 275:1132-1136.
    • (1997) Science , vol.275 , pp. 1132-1136
    • Kluck, R.M.1    Bossy-Wetzel, E.2    Green, D.R.3    Newmeyer, D.D.4
  • 53
    • 0024746304 scopus 로고
    • Maitotoxin-induced liver cell death involving loss of cell ATP following influx of calcium
    • Kutty, R.K., Singh, Y., Santostasi, and G., Krishna, G. 1989. Maitotoxin-induced liver cell death involving loss of cell ATP following influx of calcium. Tox. Appl. Pharmacol. 101(1):1-10.
    • (1989) Tox. Appl. Pharmacol. , vol.101 , Issue.1 , pp. 1-10
    • Kutty, R.K.1    Singh, Y.2    Santostasi3    Krishna, G.4
  • 54
    • 0025070340 scopus 로고
    • Maitotoxin-induced myocardial cell injury: Calcium accumulation followed by ATP depletion precedes cell death
    • Santostasi, G., Kutty, R.K., Bartorelli, A.L., Yasumoto, T., and Krishna, G. 1990. Maitotoxin-induced myocardial cell injury: calcium accumulation followed by ATP depletion precedes cell death. Tox. Appl. Pharmacol. 102(1):164-73.
    • (1990) Tox. Appl. Pharmacol. , vol.102 , Issue.1 , pp. 164-173
    • Santostasi, G.1    Kutty, R.K.2    Bartorelli, A.L.3    Yasumoto, T.4    Krishna, G.5
  • 55
    • 0024495862 scopus 로고
    • Increased vulnerability of the mildly traumatized brain to cerebral ischemia: The use of controlled secondary ischemia as a research tool to identify common or different mechanisms contributing to mechanical and ischemic brain injury
    • Jenkins, L.W., Moszynski, K., Lyeth B.G., Lewelt, W., DeWitt, D.S., Allen, A., Dixon, C.E., Povlishock, J.T., Majewski, T.J., Clifton, G.L., Young, H.F., Becker, D.P., and Hayes, R.L. 1989. Increased vulnerability of the mildly traumatized brain to cerebral ischemia: the use of controlled secondary ischemia as a research tool to identify common or different mechanisms contributing to mechanical and ischemic brain injury. Brain Injury 477:211-224.
    • (1989) Brain Injury , vol.477 , pp. 211-224
    • Jenkins, L.W.1    Moszynski, K.2    Lyeth, B.G.3    Lewelt, W.4    DeWitt, D.S.5    Allen, A.6    Dixon, C.E.7    Povlishock, J.T.8    Majewski, T.J.9    Clifton, G.L.10    Young, H.F.11    Becker, D.P.12    Hayes, R.L.13
  • 56
    • 0025002707 scopus 로고
    • Prolonged memory impairment in the absence of hippocampal cell death following traumatic brain injury in the rat
    • Lyeth, B.G., Jenkins, L.W., Hamm, R.J., Dixon, C.E., Phillips, L.L., Clifton, G.L., Young, H.F., and Hayes, R.L. 1990. Prolonged memory impairment in the absence of hippocampal cell death following traumatic brain injury in the rat. Brain Res. 526(2):249-58.
    • (1990) Brain Res. , vol.526 , Issue.2 , pp. 249-258
    • Lyeth, B.G.1    Jenkins, L.W.2    Hamm, R.J.3    Dixon, C.E.4    Phillips, L.L.5    Clifton, G.L.6    Young, H.F.7    Hayes, R.L.8
  • 57
    • 0031029107 scopus 로고    scopus 로고
    • Protection with lubeluzole against delayed ischemic brain damage in rats. a quantitative histopathologic study
    • Haseldonckx, M., Van Reempts, J., Van de Ven, M., Wouters, L., and Borgers, M. 1997. Protection with lubeluzole against delayed ischemic brain damage in rats. A quantitative histopathologic study. Stroke 28(2):428-32.
    • (1997) Stroke , vol.28 , Issue.2 , pp. 428-432
    • Haseldonckx, M.1    Van Reempts, J.2    Van De Ven, M.3    Wouters, L.4    Borgers, M.5
  • 59
    • 0030906889 scopus 로고    scopus 로고
    • Lesioning of deep prepiriform cortex protects against ischemic neuronal necrosis by attenuating extracellular glutamate concentrations
    • Kawaguchi, K., Huerbin, M., and Simon, R.P. 1997. Lesioning of deep prepiriform cortex protects against ischemic neuronal necrosis by attenuating extracellular glutamate concentrations. J. Neurochem. 69(1):412-7.
    • (1997) J. Neurochem. , vol.69 , Issue.1 , pp. 412-417
    • Kawaguchi, K.1    Huerbin, M.2    Simon, R.P.3
  • 60
    • 0024508256 scopus 로고
    • Experimental fluid percussion brain injury: Vascular disruption and neuronal and glial alterations
    • Cortez, S.C., McIntosh, T.K., and Noble, L.J. 1989. Experimental fluid percussion brain injury: vascular disruption and neuronal and glial alterations. Brain Res. 482(2):271-82.
    • (1989) Brain Res. , vol.482 , Issue.2 , pp. 271-282
    • Cortez, S.C.1    McIntosh, T.K.2    Noble, L.J.3
  • 62
    • 0030580454 scopus 로고    scopus 로고
    • Apoptotic morphology of dentate gyrus granule cells following experimental cortical impact injury in rats: Possible role in spatial memory deficits
    • Colicos, M.A., and Dash, P.K. 1996. Apoptotic morphology of dentate gyrus granule cells following experimental cortical impact injury in rats: possible role in spatial memory deficits. Brain Res. 739:120-131.
    • (1996) Brain Res. , vol.739 , pp. 120-131
    • Colicos, M.A.1    Dash, P.K.2
  • 63
    • 0029960060 scopus 로고    scopus 로고
    • Experimental brain injury induces differential expression of tumor necrosis factor-alpha mRNA in the CNS
    • Fan, L., Young, P.R., Barone, F.C., Feuerstein, G.Z., Smith, D.H., and McIntosh, T.K. 1996. Experimental brain injury induces differential expression of tumor necrosis factor-alpha mRNA in the CNS. Mol. Brain Res. 36(2):287-91.
    • (1996) Mol. Brain Res. , vol.36 , Issue.2 , pp. 287-291
    • Fan, L.1    Young, P.R.2    Barone, F.C.3    Feuerstein, G.Z.4    Smith, D.H.5    McIntosh, T.K.6
  • 64
    • 0030298059 scopus 로고    scopus 로고
    • Global ischemia induces apoptosis-associated genes in hippocampus
    • Honkaniemi, J., Massa, S.M., Breckinridge, M., and Sharp, F.R. 1996. Global ischemia induces apoptosis-associated genes in hippocampus. Mol. Brain Res. 42:79-88.
    • (1996) Mol. Brain Res. , vol.42 , pp. 79-88
    • Honkaniemi, J.1    Massa, S.M.2    Breckinridge, M.3    Sharp, F.R.4
  • 65
    • 0027714833 scopus 로고
    • Global ischemia can cause DNA fragmentation indicative of apoptosis in rat brain
    • MacManus, J.P., Buchan, A.M., Hill, I.E., Rasquinha, I., and Preston, E. 1993. Global ischemia can cause DNA fragmentation indicative of apoptosis in rat brain. Neurosci. Lett. 164:89-92.
    • (1993) Neurosci. Lett. , vol.164 , pp. 89-92
    • MacManus, J.P.1    Buchan, A.M.2    Hill, I.E.3    Rasquinha, I.4    Preston, E.5
  • 66
    • 0028924890 scopus 로고
    • Delayed neuronal death in the CA1 pyramidal cell layer of the gerbil hippocampus following transient ischemia is apoptosis
    • Nitatori, T., Sato, N., Waguri, S., Karasawa, Y., Araki, H., Shibanai, K., Kominami, E., and Uchiyama, Y. 1995. Delayed neuronal death in the CA1 pyramidal cell layer of the gerbil hippocampus following transient ischemia is apoptosis. J. Neurosci. 15(2):1001-11.
    • (1995) J. Neurosci. , vol.15 , Issue.2 , pp. 1001-1011
    • Nitatori, T.1    Sato, N.2    Waguri, S.3    Karasawa, Y.4    Araki, H.5    Shibanai, K.6    Kominami, E.7    Uchiyama, Y.8
  • 67
    • 0011016979 scopus 로고    scopus 로고
    • Delayed apoptotic cell death following lateral fluid percussion brain injury in the rat: A long-term study
    • abstract
    • Conti, A.C., Raghupathi, R., Becher, O., Rink, A.D., Trojanowski, J.O., and McIntosh, T.K. 1996. Delayed apoptotic cell death following lateral fluid percussion brain injury in the rat: a long-term study. J. Neurotrauma 13(10):595 [abstract].
    • (1996) J. Neurotrauma , vol.13 , Issue.10 , pp. 595
    • Conti, A.C.1    Raghupathi, R.2    Becher, O.3    Rink, A.D.4    Trojanowski, J.O.5    McIntosh, T.K.6
  • 68
    • 0028860616 scopus 로고
    • Evidence of apoptotic cell death after experimental traumatic brain injury in the rat
    • Rink, A., Fung, K., Trojanowski, J.Q., Lee, V.M., Neugebauer, E., and McIntosh, T.K. 1995. Evidence of apoptotic cell death after experimental traumatic brain injury in the rat. Am. J. Pathol. 147:1575-1583.
    • (1995) Am. J. Pathol. , vol.147 , pp. 1575-1583
    • Rink, A.1    Fung, K.2    Trojanowski, J.Q.3    Lee, V.M.4    Neugebauer, E.5    McIntosh, T.K.6
  • 69
    • 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., and Faden, A.I. 1997. Activation of CPP32-like caspases contributes to neuronal apoptosis and neurological dysfunction after traumatic brain injury. J. Neurosci. 17(19):7415-7424.
    • (1997) J. Neurosci. , vol.17 , Issue.19 , 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
  • 70
    • 0027381394 scopus 로고
    • Calpain activity increases in hepatocytes following addition of ATP. Demonstration by a novel fluorescent approach
    • Rosser, B.G., Powers, S.P., and Gores, G.J. 1993. Calpain activity increases in hepatocytes following addition of ATP. Demonstration by a novel fluorescent approach. J. Biol. Chem. 268(31): 23593-600.
    • (1993) J. Biol. Chem. , vol.268 , Issue.31 , pp. 23593-23600
    • Rosser, B.G.1    Powers, S.P.2    Gores, G.J.3
  • 71
    • 0020332392 scopus 로고
    • Maitotoxin, a Ca2+ channel activator candidate
    • Takahashi, M., Ohizumi, Y., and Yasumoto, T. 1982. Maitotoxin, a Ca2+ channel activator candidate. J. Biol. Chem. 257(13):7287-89.
    • (1982) J. Biol. Chem. , vol.257 , Issue.13 , pp. 7287-7289
    • Takahashi, M.1    Ohizumi, Y.2    Yasumoto, T.3
  • 72
    • 0030879848 scopus 로고    scopus 로고
    • Caspase inhibition selectively reduces the apoptotic component of oxygen-glucose deprivation-induced cortical neuronal cell death
    • Gottron, F.J., Ying, H.S., and Choi, D.W. 1997. Caspase inhibition selectively reduces the apoptotic component of oxygen-glucose deprivation-induced cortical neuronal cell death. Mol. Cell. Neurosci. 9(3):159-69.
    • (1997) Mol. Cell. Neurosci. , vol.9 , Issue.3 , pp. 159-169
    • Gottron, F.J.1    Ying, H.S.2    Choi, D.W.3


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