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Volumn 94, Issue 4, 1999, Pages 1213-1218

Reduction of post-traumatic brain injury and free radical production by inhibition of the caspase-1 cascade

Author keywords

Apoptosis; Caspase inhibition; Caspase 1; DNA fragmentation; Interleukin 1 converting enzyme; TUNEL

Indexed keywords

CASPASE; CASPASE INHIBITOR; DNA FRAGMENT; FREE RADICAL; INTERLEUKIN 1BETA CONVERTING ENZYME;

EID: 0032708427     PISSN: 03064522     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0306-4522(99)00345-0     Document Type: Article
Times cited : (93)

References (53)
  • 4
    • 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., Dash P.K. Apoptotic morphology of dentate gyrus granule cells following experimental cortical impact injury in rats: possible role in spatial memory deficits. Brain Res. 739:1996;120-131.
    • (1996) Brain Res. , vol.739 , pp. 120-131
    • Colicos, M.A.1    Dash, P.K.2
  • 5
    • 0032146787 scopus 로고    scopus 로고
    • Experimental brain injury induces regionally distinct apoptosis during the acute and delayed post-traumatic period
    • Conti A.C., Raghupathi R., Trojanowski J.Q., McIntosh T.K. Experimental brain injury induces regionally distinct apoptosis during the acute and delayed post-traumatic period. J. Neurosci. 18:1998;5663-5672.
    • (1998) J. Neurosci. , vol.18 , pp. 5663-5672
    • Conti, A.C.1    Raghupathi, R.2    Trojanowski, J.Q.3    McIntosh, T.K.4
  • 7
    • 0027979691 scopus 로고
    • Post-traumatic brain hypothermia reduces histopathological damage following concussive brain injury in the rat
    • Dietrich W.D., Alonso O., Busto R., Globus M.Y., Ginsberg M.D. Post-traumatic brain hypothermia reduces histopathological damage following concussive brain injury in the rat. Acta neuropath., Berlin. 87:1994;250-258.
    • (1994) Acta Neuropath., Berlin , vol.87 , pp. 250-258
    • Dietrich, W.D.1    Alonso, O.2    Busto, R.3    Globus, M.Y.4    Ginsberg, M.D.5
  • 8
    • 0031888955 scopus 로고    scopus 로고
    • A caspase-activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD
    • Enari M., Sakahira H., Yokoyama K., Okawa K., Iwamatsu A., Nagata S. A caspase-activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD. Nature. 391:1998;43-50.
    • (1998) Nature , vol.391 , pp. 43-50
    • Enari, M.1    Sakahira, H.2    Yokoyama, K.3    Okawa, K.4    Iwamatsu, A.5    Nagata, S.6
  • 9
    • 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
  • 12
    • 8044252166 scopus 로고    scopus 로고
    • Expression of a dominant negative mutant of ICE in transgenic mice prevents neuronal cell death induced by trophic factor withdrawal and ischemic brain injury
    • Friedlander R.M., Gagliardini V., Hara H., Fink K.B., Li W., MacDonald G., Fishman M.C., Greenberg A.H., Moskowitz M.A., Yuan J. Expression of a dominant negative mutant of ICE in transgenic mice prevents neuronal cell death induced by trophic factor withdrawal and ischemic brain injury. J. exp. Med. 185:1997;933-940.
    • (1997) J. Exp. Med. , vol.185 , pp. 933-940
    • Friedlander, R.M.1    Gagliardini, V.2    Hara, H.3    Fink, K.B.4    Li, W.5    MacDonald, G.6    Fishman, M.C.7    Greenberg, A.H.8    Moskowitz, M.A.9    Yuan, J.10
  • 13
    • 0029788702 scopus 로고    scopus 로고
    • Functional role of interleukin-1β (IL-1β) in converting enzyme-mediated apoptosis
    • Friedlander R.M., Gagliardini V., Rotello R.J., Yuan J. Functional role of interleukin-1β (IL-1β) in converting enzyme-mediated apoptosis. J. exp. Med. 184:1996;717-724.
    • (1996) J. Exp. Med. , vol.184 , pp. 717-724
    • Friedlander, R.M.1    Gagliardini, V.2    Rotello, R.J.3    Yuan, J.4
  • 15
    • 0031730617 scopus 로고    scopus 로고
    • ICE, neuronal apoptosis and neurodegeneration
    • Friedlander R.M., Yuan J. ICE, neuronal apoptosis and neurodegeneration. Cell Death Diff. 5:1998;823-831.
    • (1998) Cell Death Diff. , vol.5 , pp. 823-831
    • Friedlander, R.M.1    Yuan, J.2
  • 16
    • 0026648674 scopus 로고
    • Identification of programmed cell death in situ via specific labeling of nuclear DNA fragmentation
    • Gavrieli Y., Sherman Y., Ben-Sasson S.A. Identification of programmed cell death in situ via specific labeling of nuclear DNA fragmentation. J. Cell Biol. 199:1992;493-501.
    • (1992) J. Cell Biol. , vol.199 , pp. 493-501
    • Gavrieli, Y.1    Sherman, Y.2    Ben-Sasson, S.A.3
  • 17
    • 0029130550 scopus 로고
    • Glutamate release and free radical production following brain injury: Effects of posttraumatic hypothermia
    • Globus M.Y., Alonso O., Dietrich W.D., Busto R., Ginsberg M.D. Glutamate release and free radical production following brain injury: effects of posttraumatic hypothermia. J. Neurochem. 65:1995;1704-1711.
    • (1995) J. Neurochem. , vol.65 , pp. 1704-1711
    • Globus, M.Y.1    Alonso, O.2    Dietrich, W.D.3    Busto, R.4    Ginsberg, M.D.5
  • 18
    • 0028893492 scopus 로고
    • Superoxide dismutase delays neuronal apoptosis: A role for reactive oxygen species in programmed neuronal death
    • Greenlund L.J.S., Deckwerth T.L., Johnson E.M. Jr. Superoxide dismutase delays neuronal apoptosis: a role for reactive oxygen species in programmed neuronal death. Neuron. 14:1995;303-315.
    • (1995) Neuron , vol.14 , pp. 303-315
    • Greenlund, L.J.S.1    Deckwerth, T.L.2    Johnson E.M., Jr.3
  • 22
    • 0030756576 scopus 로고    scopus 로고
    • Caspases: A treatment target for neurodegenerative diseases?
    • Holtzman D.M., Deshmukh M. Caspases: a treatment target for neurodegenerative diseases? Nat. Med. 3:1997;954-955.
    • (1997) Nat. Med. , vol.3 , pp. 954-955
    • Holtzman, D.M.1    Deshmukh, M.2
  • 24
    • 0028920863 scopus 로고
    • Altered cytokine export and apoptosis in mice dificient in interleukin-1β converting enzyme
    • Kuida K., Lippke J.A., Ku G., Harding M.W., Livingston D.J., Su M.S., Flavell R.A. Altered cytokine export and apoptosis in mice dificient in interleukin-1β converting enzyme. Science. 267:1995;2000-2003.
    • (1995) Science , vol.267 , pp. 2000-2003
    • Kuida, K.1    Lippke, J.A.2    Ku, G.3    Harding, M.W.4    Livingston, D.J.5    Su, M.S.6    Flavell, R.A.7
  • 27
    • 0029773397 scopus 로고    scopus 로고
    • An ICE inhibitor, z-VAD-DCB attenuates ischaemic brain damage in the rat
    • Loddick S.A., MacKenzie A., Rothwell N.J. An ICE inhibitor, z-VAD-DCB attenuates ischaemic brain damage in the rat. NeuroReport. 7:1996;1465-1468.
    • (1996) NeuroReport , vol.7 , pp. 1465-1468
    • Loddick, S.A.1    MacKenzie, A.2    Rothwell, N.J.3
  • 29
    • 0029114963 scopus 로고
    • Tumor necrosis factor-induced apoptosis is mediated by a CrmA-sensitive cell death pathway
    • Miura M., Friedlander R.M., Yuan J. Tumor necrosis factor-induced apoptosis is mediated by a CrmA-sensitive cell death pathway. Proc. natn. Acad. Sci. U.S.A. 92:1995;8318-8322.
    • (1995) Proc. Natn. Acad. Sci. U.S.A. , vol.92 , pp. 8318-8322
    • Miura, M.1    Friedlander, R.M.2    Yuan, J.3
  • 30
    • 0027449187 scopus 로고
    • Induction of apoptosis in fibroblasts by IL-1β converting enzyme, a mammalian homolog of the C. elegans cell death gene ced-3
    • Miura M., Zhu H., Rotello R., Hartwieg E.A., Yuan J. Induction of apoptosis in fibroblasts by IL-1β converting enzyme, a mammalian homolog of the C. elegans cell death gene ced-3. Cell. 75:1993;653-660.
    • (1993) Cell , vol.75 , pp. 653-660
    • Miura, M.1    Zhu, H.2    Rotello, R.3    Hartwieg, E.A.4    Yuan, J.5
  • 32
    • 0031915545 scopus 로고    scopus 로고
    • Multiple pathways of neuronal death induced by DNA-damaging agents NGF deprivation and oxidative stress
    • Park D.S., Morris E.J., Troy C.M., Shelanski M.L., Geller H.M., Greene L.A. Multiple pathways of neuronal death induced by DNA-damaging agents NGF deprivation and oxidative stress. J. Neurosci. 18:1998;830-840.
    • (1998) J. Neurosci. , vol.18 , pp. 830-840
    • Park, D.S.1    Morris, E.J.2    Troy, C.M.3    Shelanski, M.L.4    Geller, H.M.5    Greene, L.A.6
  • 36
    • 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
  • 37
    • 0023930960 scopus 로고
    • Experimental closed head injury in rats: Mechanical, pathophysiologic, and neurologic properties
    • Shapira Y., Shomami E., Sidi A., Soffer D., Freeman S., Cotev S. Experimental closed head injury in rats: mechanical, pathophysiologic, and neurologic properties. Crit. Care Med. 16:1988;258-265.
    • (1988) Crit. Care Med. , vol.16 , pp. 258-265
    • Shapira, Y.1    Shomami, E.2    Sidi, A.3    Soffer, D.4    Freeman, S.5    Cotev, S.6
  • 38
    • 0029891535 scopus 로고    scopus 로고
    • Retardation of chemical hypoxia-induced necrotic cell death by Bcl-2 and ICE inhibitors: Possible involvement of common mediators in apoptotic and necrotic signal transductions
    • Shimizu S., Eguchi Y., Kamiike W., Waguri S., Uchiyama Y., Matsuda H., Tsujimoto Y. Retardation of chemical hypoxia-induced necrotic cell death by Bcl-2 and ICE inhibitors: possible involvement of common mediators in apoptotic and necrotic signal transductions. Oncogene. 12:1996;2045-2050.
    • (1996) Oncogene , vol.12 , pp. 2045-2050
    • Shimizu, S.1    Eguchi, Y.2    Kamiike, W.3    Waguri, S.4    Uchiyama, Y.5    Matsuda, H.6    Tsujimoto, Y.7
  • 39
    • 0031020222 scopus 로고    scopus 로고
    • Improvement of cognitive deficits and decreased cholinergic neuronal cell loss and apoptotic cell death following neurotrophin infusion after experimental traumatic brain injury
    • Sinson G., Perri B.R., Trojanowskj J.Q., Flamm E.S., McIntosh T.K. Improvement of cognitive deficits and decreased cholinergic neuronal cell loss and apoptotic cell death following neurotrophin infusion after experimental traumatic brain injury. J. Neurosurg. 86:1997;511-518.
    • (1997) J. Neurosurg. , vol.86 , pp. 511-518
    • Sinson, G.1    Perri, B.R.2    Trojanowskj, J.Q.3    Flamm, E.S.4    McIntosh, T.K.5
  • 40
    • 0030002801 scopus 로고    scopus 로고
    • Benzyloxycarbonyl-Val-Ala-Asp (OMe) fluoromethylketone (Z-VAD.FMK) inhibits apoptosis by blocking the processing of CPP32
    • Slee E.A., Zhu H., Chow S.C., MacFarlane M., Nicholson D.W., Cohen G.M. Benzyloxycarbonyl-Val-Ala-Asp (OMe) fluoromethylketone (Z-VAD.FMK) inhibits apoptosis by blocking the processing of CPP32. Biochem. J. 315:1996;21-24.
    • (1996) Biochem. J. , vol.315 , pp. 21-24
    • Slee, E.A.1    Zhu, H.2    Chow, S.C.3    MacFarlane, M.4    Nicholson, D.W.5    Cohen, G.M.6
  • 41
    • 0028990125 scopus 로고
    • Yama/CPP32β, a mammalian homolog of CED-3, is a crmA-inhibitable protease that cleaves the death substrate poly(ADP ribose) polymerase
    • Tewari M., Quan L.T., O'Rourke K., Desnoyers S., Zeng Z., Beidler D.R., Poirier G.G., Salvesen G.S., Dixit V.M. Yama/CPP32β, a mammalian homolog of CED-3, is a crmA-inhibitable protease that cleaves the death substrate poly(ADP ribose) polymerase. Cell. 81:1995;801-809.
    • (1995) Cell , vol.81 , pp. 801-809
    • Tewari, M.1    Quan, L.T.2    O'Rourke, K.3    Desnoyers, S.4    Zeng, Z.5    Beidler, D.R.6    Poirier, G.G.7    Salvesen, G.S.8    Dixit, V.M.9
  • 44
    • 0032575750 scopus 로고    scopus 로고
    • Caspases: Enemies within
    • Thornberry N.A., Lazebnik Y. Caspases: enemies within. Science. 281:1998;1312-1316.
    • (1998) Science , vol.281 , pp. 1312-1316
    • Thornberry, N.A.1    Lazebnik, Y.2
  • 45
    • 0027404648 scopus 로고
    • Microscale autoradiographic method for the qualitative and quantitative analysis of apoptotic DNA fragmentation
    • Tilly J.L., Hsueh A.J.W. Microscale autoradiographic method for the qualitative and quantitative analysis of apoptotic DNA fragmentation. J. cell. Physiol. 154:1993;519-526.
    • (1993) J. Cell. Physiol. , vol.154 , pp. 519-526
    • Tilly, J.L.1    Hsueh, A.J.W.2
  • 46
    • 0028928605 scopus 로고
    • Reduced and oxidized forms of glutathione and alpha-tocopherol in the cerebrospinal fluid of parkinsonian patients: Comparison between before and after L-DOPA treatment
    • Tohgi H., Abe T., Saheki M., Shamato F., Sasaki K., Takahashi S. Reduced and oxidized forms of glutathione and alpha-tocopherol in the cerebrospinal fluid of parkinsonian patients: comparison between before and after L-DOPA treatment. Neurosci. Lett. 184:1995;21-24.
    • (1995) Neurosci. Lett. , vol.184 , pp. 21-24
    • Tohgi, H.1    Abe, T.2    Saheki, M.3    Shamato, F.4    Sasaki, K.5    Takahashi, S.6
  • 47
    • 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. natn. Acad. Sci. U.S.A. 93:1996;5635-5640.
    • (1996) Proc. Natn. 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
  • 49
    • 0031416299 scopus 로고    scopus 로고
    • Amelioration of mitochondrial function by a novel antioxidant U-101033E following traumatic brain injury in rats
    • Xiong Y., Peterson P.L., Muizelaar J.P., Lee C.P. Amelioration of mitochondrial function by a novel antioxidant U-101033E following traumatic brain injury in rats. J. Neurotrauma. 14:1997;907-917.
    • (1997) J. Neurotrauma , vol.14 , pp. 907-917
    • Xiong, Y.1    Peterson, P.L.2    Muizelaar, J.P.3    Lee, C.P.4
  • 50
    • 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
  • 51
    • 0025255636 scopus 로고
    • The Caenorhabditis elegans genes ced-3 and ced-4 act cell autonomously to cause programmed cell death
    • Yuan J., Horvitz H.R. The Caenorhabditis elegans genes ced-3 and ced-4 act cell autonomously to cause programmed cell death. Devl Biol. 138:1990;33-41.
    • (1990) Devl Biol. , vol.138 , pp. 33-41
    • Yuan, J.1    Horvitz, H.R.2
  • 52
    • 0027525104 scopus 로고
    • The C. elegans cell death gene ced-3 encodes a protein similar to mammalian interleukin-1β-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-1β-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
  • 53
    • 0028025024 scopus 로고
    • Interleukin 1 is released by murine macrophages during apoptosis induced by Shigella flexneri
    • Zychlinsky A., Fitting C., Cavalillon J.M., Sansonetti P.J. Interleukin 1 is released by murine macrophages during apoptosis induced by Shigella flexneri. J. clin. Invest. 94:1994;1328-1332.
    • (1994) J. Clin. Invest. , vol.94 , pp. 1328-1332
    • Zychlinsky, A.1    Fitting, C.2    Cavalillon, J.M.3    Sansonetti, P.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.