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Volumn 14, Issue 3, 1997, Pages 121-134

Mechanisms of calpain proteolysis following traumatic brain injury: Implications for pathology and therapy: A review and update

Author keywords

calpain; calpain inhibition; cell death; cytoskeleton; traumatic brain injury

Indexed keywords

AK 295; ALOXISTATIN ACID; CALCIUM; CALPAIN; CALPASTATIN; CYSTEINE PROTEINASE; CYSTEINE PROTEINASE INHIBITOR; LEUPEPTIN; MATRIX METALLOPROTEINASE; PROTEINASE; PROTEINASE INHIBITOR; UBIQUITIN; UNCLASSIFIED DRUG; [1 [(1 FORMYL 2 PHENYLETHYL)CARBAMOYL] 2 METHYLPROPYL]CARBAMIC ACID BENZYL ESTER;

EID: 0030951668     PISSN: 08977151     EISSN: None     Source Type: Journal    
DOI: 10.1089/neu.1997.14.121     Document Type: Review
Times cited : (183)

References (137)
  • 1
    • 0342592320 scopus 로고    scopus 로고
    • The ubiquitin-dependent proteolytic pathway in skeletal muscle: Its role in pathological states
    • ARGILES, J., and LOPEZ-SORIANO, J.L. (1996). The ubiquitin-dependent proteolytic pathway in skeletal muscle: its role in pathological states. Trends Pharmacol. Sci. 17, 222-226.
    • (1996) Trends Pharmacol. Sci. , vol.17 , pp. 222-226
    • Argiles, J.1    Lopez-Soriano, J.L.2
  • 2
    • 0023179385 scopus 로고
    • The breakdown of the individual neurofilament proteins by cathepsin D
    • BANAY-SCHWARTZ, M., DAHL, D., HUI, K.S., and LAJTHA, A. (1987). The breakdown of the individual neurofilament proteins by cathepsin D. D. Neurochem. Res. 12, 361-367.
    • (1987) D. Neurochem. Res. , vol.12 , pp. 361-367
    • Banay-Schwartz, M.1    Dahl, D.2    Hui, K.S.3    Lajtha, A.4
  • 3
    • 0020284468 scopus 로고
    • Degradation of cytoskeletal proteins in experimental spinal cord injury
    • BANIK N.L., HOGAN E.L., POWERS J.M., and WHETSTINE L. (1982). Degradation of cytoskeletal proteins in experimental spinal cord injury. Neurochem. Res. 7, 1465-1475.
    • (1982) Neurochem. Res. , vol.7 , pp. 1465-1475
    • Banik, N.L.1    Hogan, E.L.2    Powers, J.M.3    Whetstine, L.4
  • 4
    • 0028020515 scopus 로고
    • Calpain inhibitor AK295 protects neurons from focal brain ischemia. Effects of post occlusion intra-arterial administration
    • BARTUS, R.T., HAYWARD, N.L., ELLIOTT, P.J., et al. (1994). Calpain inhibitor AK295 protects neurons from focal brain ischemia. Effects of post occlusion intra-arterial administration. Stroke 25, 2265-2270.
    • (1994) Stroke , vol.25 , pp. 2265-2270
    • Bartus, R.T.1    Hayward, N.L.2    Elliott, P.J.3
  • 6
    • 0028850474 scopus 로고
    • Time related neuronal changes following middle cerebral artery occlusion: Implications for therapeutic intervention and the role of calpain
    • BARTUS, R.T., DEAN, R.L., CAVANAUGH, K., EVELETH, D., CARRIERO, D.L., and LYNCH, G. (1995b). Time related neuronal changes following middle cerebral artery occlusion: implications for therapeutic intervention and the role of calpain. J. Cereb. Blood Flow Metab. 15, 969-979.
    • (1995) J. Cereb. Blood Flow Metab. , vol.15 , pp. 969-979
    • Bartus, R.T.1    Dean, R.L.2    Cavanaugh, K.3    Eveleth, D.4    Carriero, D.L.5    Lynch, G.6
  • 8
    • 0029015969 scopus 로고
    • Delayed antagonism of calpain reduces excitotoxicity in cultured neurons
    • BRORSON, J.R., MARCUCILLI, C.J., and MILLER, R.J. (1995). Delayed antagonism of calpain reduces excitotoxicity in cultured neurons. Stroke 26, 1259-1267.
    • (1995) Stroke , vol.26 , pp. 1259-1267
    • Brorson, J.R.1    Marcucilli, C.J.2    Miller, R.J.3
  • 11
    • 0020855194 scopus 로고
    • The proteolytic digestion of ox neurofilament with trypsin and -chy-motrypsin
    • CHIN, T.K., EAGLES, P.A., and MAGGS, A. (1983). The proteolytic digestion of ox neurofilament with trypsin and -chy-motrypsin. Biochem. J. 215, 239-252.
    • (1983) Biochem. J. , vol.215 , pp. 239-252
    • Chin, T.K.1    Eagles, P.A.2    Maggs, A.3
  • 12
    • 0023870521 scopus 로고
    • Pharmacology of glutamate neurotoxicity in cortical cell culture: Attenuation of NMDA antagonists
    • CHOI, D.W. (1988). Pharmacology of glutamate neurotoxicity in cortical cell culture: attenuation of NMDA antagonists. J. Neurosci. 8, 185-196.
    • (1988) J. Neurosci. , vol.8 , pp. 185-196
    • Choi, D.W.1
  • 14
    • 0025612147 scopus 로고
    • Decreased protein kinase C activity during cerebral ischemia and after reperfusion in the adult rat
    • CRUMRINE, R.C., DUBYAK, G., and LAMANNA, J.C. (1990). Decreased protein kinase C activity during cerebral ischemia and after reperfusion in the adult rat. J. Neurochem. 55, 2001-2007.
    • (1990) J. Neurochem. , vol.55 , pp. 2001-2007
    • Crumrine, R.C.1    Dubyak, G.2    Lamanna, J.C.3
  • 15
    • 0028922688 scopus 로고
    • Spatial memory deficits, increased phosphorylation of the transcription factor CREB and induction of the AP-1 complex following experimental brain injury
    • DASH, P.K., MOORE, A.N., and DIXON, C.E. (1994). Spatial memory deficits, increased phosphorylation of the transcription factor CREB and induction of the AP-1 complex following experimental brain injury. J. Neurosci. 15, 2030-2039.
    • (1994) J. Neurosci. , vol.15 , pp. 2030-2039
    • Dash, P.K.1    Moore, A.N.2    Dixon, C.E.3
  • 16
    • 0025013459 scopus 로고
    • Development of hippocampal long term potentiation is reduced by recently introduced calpain inhibitors
    • DEL CERRO, S., LARSON, J., OLIVER, M.W., and LYNCH, G. (1990). Development of hippocampal long term potentiation is reduced by recently introduced calpain inhibitors. Brain Res. 530, 91-95.
    • (1990) Brain Res. , vol.530 , pp. 91-95
    • Del Cerro, S.1    Larson, J.2    Oliver, M.W.3    Lynch, G.4
  • 17
    • 0025848106 scopus 로고
    • The spectrin super-family
    • DHERMY, D. (1991). The spectrin super-family. Biol. Cell 71, 249-254.
    • (1991) Biol. Cell , vol.71 , pp. 249-254
    • Dhermy, D.1
  • 18
    • 0026073804 scopus 로고
    • Comparison of the autolyzed and unautolyzed forms of μ- and m-calpain from bovine skeletal muscle
    • EDMUNDS, T., NAGAINIS, P.A., SATHE, S.K., THOMPSON, V.F., and GOLL, D.E. (1991). Comparison of the autolyzed and unautolyzed forms of μ- and m-calpain from bovine skeletal muscle. Biochim. Biophys. Acta 1077, 197-208.
    • (1991) Biochim. Biophys. Acta , vol.1077 , pp. 197-208
    • Edmunds, T.1    Nagainis, P.A.2    Sathe, S.K.3    Thompson, V.F.4    Goll, D.E.5
  • 19
    • 0024365739 scopus 로고
    • The role of excitatory amino acids and NMDA receptors in traumatic brain injury
    • FADEN, A.I., DEMEDIUK, P., PANTER, S.S., and VINK, R. (1989). The role of excitatory amino acids and NMDA receptors in traumatic brain injury. Science 244, 798-800.
    • (1989) Science , vol.244 , pp. 798-800
    • Faden, A.I.1    Demediuk, P.2    Panter, S.S.3    Vink, R.4
  • 21
    • 0029995766 scopus 로고    scopus 로고
    • A license to kill
    • FRASER, A., and EVAN, G., (1996). A license to kill. Cell 85, 781-784.
    • (1996) Cell , vol.85 , pp. 781-784
    • Fraser, A.1    Evan, G.2
  • 22
    • 1842395128 scopus 로고
    • Identification of programed cell death in situ via specific labeling of nuclear DNA fragmentation
    • GAVRIELI, Y., SHERMAN, Y., and BEN-SASSON, S. (1992). Identification of programed cell death in situ via specific labeling of nuclear DNA fragmentation. J Cell Biol 127, 1717-1727.
    • (1992) J Cell Biol , vol.127 , pp. 1717-1727
    • Gavrieli, Y.1    Sherman, Y.2    Ben-Sasson, S.3
  • 23
    • 0028793887 scopus 로고
    • Axotomy induced axonal degeneration is mediated by calcium influx through ion-specific channels
    • GEORGE, E.B., GLASS, J.D., and GRIFFIN, J.W. (1995). Axotomy induced axonal degeneration is mediated by calcium influx through ion-specific channels. J. Neurosci. 15, 6445-6452.
    • (1995) J. Neurosci. , vol.15 , pp. 6445-6452
    • George, E.B.1    Glass, J.D.2    Griffin, J.W.3
  • 24
  • 25
    • 0028098023 scopus 로고
    • Diffuse axonal injury in craniocerebral trauma. A comparative histological and immunohistochemical study
    • GULTEKIN, S.H., and SMITH, T.W. (1994). Diffuse axonal injury in craniocerebral trauma. A comparative histological and immunohistochemical study. Arch Pathol Lab Med 118, 168-171.
    • (1994) Arch Pathol Lab Med , vol.118 , pp. 168-171
    • Gultekin, S.H.1    Smith, T.W.2
  • 26
    • 0023000721 scopus 로고
    • Distribution of calpains 1 and 2 in rat brain
    • HAMAKUBO, T., KANNAGI, R., MURACHI, T., and MATUS, A. (1986). Distribution of calpains 1 and 2 in rat brain. J. Neurosci. 6, 3103-3111.
    • (1986) J. Neurosci. , vol.6 , pp. 3103-3111
    • Hamakubo, T.1    Kannagi, R.2    Murachi, T.3    Matus, A.4
  • 27
    • 0027976921 scopus 로고
    • Calcium/calmodulin-dependent protein kinase II activity in focal ischemia with reperfusion in rats
    • HANSON, S.K., GROTTA, J.C., WAXHAM, M.N., ARONOWSKI, J., and OSTROW, J. (1994). Calcium/calmodulin-dependent protein kinase II activity in focal ischemia with reperfusion in rats. Stroke 25, 466-473.
    • (1994) Stroke , vol.25 , pp. 466-473
    • Hanson, S.K.1    Grotta, J.C.2    Waxham, M.N.3    Aronowski, J.4    Ostrow, J.5
  • 28
    • 0023792182 scopus 로고
    • The calmodulin binding site in alpha fodrin is near the calcium-dependent -protease-I cleavage site
    • HARRIS, A.S., CROALL, D.E., and MORROW, J.S. (1988). The calmodulin binding site in alpha fodrin is near the calcium-dependent -protease-I cleavage site. J. Biol. Chem. 263, 15754-15761.
    • (1988) J. Biol. Chem. , vol.263 , pp. 15754-15761
    • Harris, A.S.1    Croall, D.E.2    Morrow, J.S.3
  • 29
    • 0026518645 scopus 로고
    • Neurotransmitter-mediated mechanisms of traumatic brain injury
    • HAYES, R.L., JENKINS, L.K.W., and LYETH, B.G. (1992). Neurotransmitter-mediated mechanisms of traumatic brain injury. J. Neurotrauma 9, 173-187.
    • (1992) J. Neurotrauma , vol.9 , pp. 173-187
    • Hayes, R.L.1    Jenkins, L.K.W.2    Lyeth, B.G.3
  • 30
    • 0028902692 scopus 로고
    • Temporal response and effects of excitatory amino acid antagonism on microtubule associated protein 2 immunoreactivity following experimental brain injury in rats
    • HICKS, R., DOUGLAS, S.H., and McINTOSH, T.K. (1995). Temporal response and effects of excitatory amino acid antagonism on microtubule associated protein 2 immunoreactivity following experimental brain injury in rats. Brain Res. 678, 151-160.
    • (1995) Brain Res. , vol.678 , pp. 151-160
    • Hicks, R.1    Douglas, S.H.2    McIntosh, T.K.3
  • 31
    • 0025900722 scopus 로고
    • Degradation of transcription factors c-Jun and c-Fos, by calpain
    • HIRAI, S., KAWASAKI, H., YANIV, M., and SUZUKI, K. (1991). Degradation of transcription factors c-Jun and c-Fos, by calpain. FEBS Lett. 287, 57-61.
    • (1991) FEBS Lett. , vol.287 , pp. 57-61
    • Hirai, S.1    Kawasaki, H.2    Yaniv, M.3    Suzuki, K.4
  • 32
    • 0028132284 scopus 로고
    • Calcium activated proteolysis in rat neocortex induced by transient focal ischemia
    • HONG, S.C., LAZINO, G., GOTO, S., KANG, S.K., SCHOTTLER, F., KASSELL, N.F., and LEE, K.S. (1994b). Calcium activated proteolysis in rat neocortex induced by transient focal ischemia. Brain Res. 661, 43-50.
    • (1994) Brain Res. , vol.661 , pp. 43-50
    • Hong, S.C.1    Lazino, G.2    Goto, S.3    Kang, S.K.4    Schottler, F.5    Kassell, N.F.6    Lee, K.S.7
  • 33
    • 0028098014 scopus 로고
    • Neuroprotection with a calpain inhibitor in a model of focal cerebral ischemia
    • HONG, S.C., GOTO, Y., LANZINO, G., SOLEAU, S., KASSELL, N.F., and LEE, K.S. (1994a). Neuroprotection with a calpain inhibitor in a model of focal cerebral ischemia. Stroke 25, 663-669.
    • (1994) Stroke , vol.25 , pp. 663-669
    • Hong, S.C.1    Goto, Y.2    Lanzino, G.3    Soleau, S.4    Kassell, N.F.5    Lee, K.S.6
  • 34
    • 0025184647 scopus 로고
    • Suppressive effect of E-64 on ischemic degradation of cerebral proteins following occlusion of the middle cerebral artery in rats
    • INUZUKA, T., TAMURA, A., SHUZO, S., KIRINO, T., TOYOSHIMA, I., and MLYATAKE, Y. (1990a). Suppressive effect of E-64 on ischemic degradation of cerebral proteins following occlusion of the middle cerebral artery in rats. Brain Res. 526, 177-179.
    • (1990) Brain Res. , vol.526 , pp. 177-179
    • Inuzuka, T.1    Tamura, A.2    Shuzo, S.3    Kirino, T.4    Toyoshima, I.5    Mlyatake, Y.6
  • 35
    • 0025313518 scopus 로고
    • Changes in the concentrations of cerebral proteins following occlusion of the middle cerebral artery in rats
    • INUZUKA, T., TAMURA, A., SATO, S., KIRINO, T., TOYOSHIMA, I., and MIYATAKE, T. (1990b). Changes in the concentrations of cerebral proteins following occlusion of the middle cerebral artery in rats. Stroke 21, 917-922.
    • (1990) Stroke , vol.21 , pp. 917-922
    • Inuzuka, T.1    Tamura, A.2    Sato, S.3    Kirino, T.4    Toyoshima, I.5    Miyatake, T.6
  • 36
    • 0025731595 scopus 로고
    • Degradation of microtubule-associated protein 2 (MAP2) and brain spectrin by calpain: A comparative study
    • JOHNSON, G.V.W., LITERSKY, J.M., and JOPE, R.S. (1991). Degradation of microtubule-associated protein 2 (MAP2) and brain spectrin by calpain: a comparative study. J. Neurochem. 56, 1630-1638.
    • (1991) J. Neurochem. , vol.56 , pp. 1630-1638
    • Johnson, G.V.W.1    Litersky, J.M.2    Jope, R.S.3
  • 37
    • 0027509798 scopus 로고
    • Participation of cathepsin L on bone resorption
    • KAKEGAWA, H., NIKAWA, T., TAGAMI, K., KAMIOKA, H., et al. (1993). Participation of cathepsin L on bone resorption. FEBS Lett 321, 247-250.
    • (1993) FEBS Lett , vol.321 , pp. 247-250
    • Kakegawa, H.1    Nikawa, T.2    Tagami, K.3    Kamioka, H.4
  • 40
    • 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, S.J., POSMANTUR, R., DIXON, C.E., YANG, K., CLIFTON, G.L., and HAYES, R.L. (1996a). 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, S.J.3    Posmantur, R.4    Dixon, C.E.5    Yang, K.6    Clifton, G.L.7    Hayes, R.L.8
  • 42
    • 0029045236 scopus 로고
    • Calpain inhibitors reduce depolarization induced loss of tau protein in primary septo-hippocampal cultures
    • KAMPFL, A., WHITSON, S.J., ZHAO, X., POSMANTUR, R., CLIFTON, G.L., and HAYES, R.L. (1995). Calpain inhibitors reduce depolarization induced loss of tau protein in primary septo-hippocampal cultures. Neurosci. Lett. 194, 149-152.
    • (1995) Neurosci. Lett. , vol.194 , pp. 149-152
    • Kampfl, A.1    Whitson, S.J.2    Zhao, X.3    Posmantur, R.4    Clifton, G.L.5    Hayes, R.L.6
  • 43
    • 0027722010 scopus 로고
    • Lowthreshold calcium currents in dendrites of the adult rat hippocampus
    • KARST, H., JOELS, M., and WADMAN, W.J. (1993). Lowthreshold calcium currents in dendrites of the adult rat hippocampus. Neurosci. Lett. 164, 154-158.
    • (1993) Neurosci. Lett. , vol.164 , pp. 154-158
    • Karst, H.1    Joels, M.2    Wadman, W.J.3
  • 44
    • 0025774025 scopus 로고
    • Calcium-dependent glutamate release concomitant with massive potassium flux during cerebral ischemia in vivo
    • KATAYAMA, Y., KAWAMATA, T., TAMURA, T., HOVDA, D.A., BECKER, D.P., and TSUBOKAWA, T. (1991). Calcium-dependent glutamate release concomitant with massive potassium flux during cerebral ischemia in vivo. Brain Res. 558, 136-140.
    • (1991) Brain Res. , vol.558 , pp. 136-140
    • Katayama, Y.1    Kawamata, T.2    Tamura, T.3    Hovda, D.A.4    Becker, D.P.5    Tsubokawa, T.6
  • 45
    • 0025242563 scopus 로고
    • Massive increases in extracellular potassium and the indiscriminate release of glutamate following concussive brain injury
    • KATAYAMA, Y., BECKER, D.P., TAMURA, T., and HOVDA, D.A. (1990). Massive increases in extracellular potassium and the indiscriminate release of glutamate following concussive brain injury. J. Neurosurg. 73, 889-900.
    • (1990) J. Neurosurg. , vol.73 , pp. 889-900
    • Katayama, Y.1    Becker, D.P.2    Tamura, T.3    Hovda, D.A.4
  • 46
    • 0043151998 scopus 로고
    • Participation of lyposomal cathepsins in antigen processing and bone absorption
    • N. Katunuma, K. Suzuki, J. Travis, and H. Fritz (eds.). Scientific Press: Japan
    • KATUNUMA, N. (1994). Participation of lyposomal cathepsins in antigen processing and bone absorption, in Biological Functions of Proteases and Inhibitors. N. Katunuma, K. Suzuki, J. Travis, and H. Fritz (eds.). Scientific Press: Japan. pp. 3-22.
    • (1994) Biological Functions of Proteases and Inhibitors , pp. 3-22
    • Katunuma, N.1
  • 47
    • 0002204915 scopus 로고
    • Definition and incidence of apoptosis: An historical perspective of apoptosis
    • L.D. Tomei and F.O. Capo (eds.) Cold Spring Harbor Laboratory Press: Cold Spring Harbor, NY
    • KERR, J.F.R., and HARMON, B.V. (1991). Definition and incidence of apoptosis: an historical perspective of apoptosis, in The Molecular Basis of Cell Death. L.D. Tomei and F.O. Capo (eds.) Cold Spring Harbor Laboratory Press: Cold Spring Harbor, NY, p. 5.
    • (1991) The Molecular Basis of Cell Death , pp. 5
    • Kerr, J.F.R.1    Harmon, B.V.2
  • 48
    • 0024420534 scopus 로고
    • Microtubule-associated protein 2 as a sensitive marker for cerebral ischemic damage-immunohistochemical investigation of dendritic damage
    • KITAGAWA, K., MASTUMOTO, M., NINOBE, M., et al. (1989). Microtubule-associated protein 2 as a sensitive marker for cerebral ischemic damage-immunohistochemical investigation of dendritic damage. Neuroscience, 31, 401-411.
    • (1989) Neuroscience , vol.31 , pp. 401-411
    • Kitagawa, K.1    Mastumoto, M.2    Ninobe, M.3
  • 50
    • 0028102478 scopus 로고
    • Cleavage of poly (ADP-Ribosome) polymerase by a proteinase with properties like ICE
    • LAZENBIK, Y.A., KAUFMAN, S.H., DESNOYERS, POIRIER, G.G., and EARNSHAW, W.C. (1994). Cleavage of poly (ADP-Ribosome) polymerase by a proteinase with properties like ICE. Nature 371, 346-347.
    • (1994) Nature , vol.371 , pp. 346-347
    • Lazenbik, Y.A.1    Kaufman, S.H.2    Desnoyers3    Poirier, G.G.4    Earnshaw, W.C.5
  • 52
    • 0028812811 scopus 로고
    • The localization of mcalpain in myelin: Immunocytochemical evidence in different areas of rat brain and nerves
    • LI, Z., and BANIK, N.L. (1995). The localization of mcalpain in myelin: immunocytochemical evidence in different areas of rat brain and nerves. Brain Res. 697, 112-121.
    • (1995) Brain Res. , vol.697 , pp. 112-121
    • Li, Z.1    Banik, N.L.2
  • 53
    • 0027371221 scopus 로고
    • The neuronal cytoskeleton and its role in axonal and dendritic plasticity
    • LUDIN, P., and MATUS, A. (1993). The neuronal cytoskeleton and its role in axonal and dendritic plasticity. Hippocampus 3, 61-71.
    • (1993) Hippocampus , vol.3 , pp. 61-71
    • Ludin, P.1    Matus, A.2
  • 57
    • 0028087618 scopus 로고
    • Microtubule associated protein 2 as an early indicator of ischemia induced neurodegeneration in the gerbil forebrain
    • MATESIC, D.F., and LIN, R.C.S. (1994). Microtubule associated protein 2 as an early indicator of ischemia induced neurodegeneration in the gerbil forebrain. J. Neurochem. 63, 1012-1020.
    • (1994) J. Neurochem. , vol.63 , pp. 1012-1020
    • Matesic, D.F.1    Lin, R.C.S.2
  • 58
    • 0027161614 scopus 로고
    • Participation of cathepsin B in processing of antigen presentation to MHC class II
    • MATSUNAGA, Y., SAIBARA, T., TAGAMI, K., KAMIOKA, H. et al. (1993). Participation of cathepsin B in processing of antigen presentation to MHC class II. FEBS Lett 324, 325-330.
    • (1993) FEBS Lett , vol.324 , pp. 325-330
    • Matsunaga, Y.1    Saibara, T.2    Tagami, K.3    Kamioka, H.4
  • 59
    • 0027377278 scopus 로고
    • Novel pharmacological therapies in the treatment of experimental brain injury. A review
    • McINTOSH, T.K. (1993). Novel pharmacological therapies in the treatment of experimental brain injury. A review. J. Neurotrauma 10, 215-261.
    • (1993) J. Neurotrauma , vol.10 , pp. 215-261
    • McIntosh, T.K.1
  • 60
    • 0030014359 scopus 로고    scopus 로고
    • Therapeutic approaches for the prevention of secondary brain injury
    • McINTOSH, T.K., SMITH, D.H., and GARDE, E. (1996). Therapeutic approaches for the prevention of secondary brain injury. Europ. J. of Anaes. 13, 291-309.
    • (1996) Europ. J. of Anaes. , vol.13 , pp. 291-309
    • McIntosh, T.K.1    Smith, D.H.2    Garde, E.3
  • 63
    • 0026705186 scopus 로고
    • Enduring suppression of hippocampal long-term potentiation following traumatic brain injury in rat
    • MIYAZAKI, S., KATAYAMA, Y., LYETH, B.G., and HAYES, R.L. (1992). Enduring suppression of hippocampal long-term potentiation following traumatic brain injury in rat. Brain Res. 585, 335-339.
    • (1992) Brain Res. , vol.585 , pp. 335-339
    • Miyazaki, S.1    Katayama, Y.2    Lyeth, B.G.3    Hayes, R.L.4
  • 64
    • 0026764487 scopus 로고
    • 2+/calmodulin-dependent protein kinase II and calcineurin in the hippocampus of rat brain after transient forebrain ischemia
    • 2+/calmodulin-dependent protein kinase II and calcineurin in the hippocampus of rat brain after transient forebrain ischemia. J. Neurochem. 58, 1798-1809.
    • (1992) J. Neurochem. , vol.58 , pp. 1798-1809
    • Morioka, M.1    Fukunaga, K.2    Yasugawa, S.3    Nagahiro, S.4    Ushio, Y.5    Miyamoto6
  • 65
    • 0028981424 scopus 로고
    • Ca accumulation in rat brain after closed head injury: Attentuation by the novel neurorpotective agent HU-211
    • NADLER, V., BIEGON, A., BETI-YANNAI, E., ADAMCHIK, J., and SHOHAMI, E. (1995). Ca accumulation in rat brain after closed head injury: attentuation by the novel neurorpotective agent HU-211. Brain Res. 685, 1-11.
    • (1995) Brain Res. , vol.685 , pp. 1-11
    • Nadler, V.1    Biegon, A.2    Beti-Yannai, E.3    Adamchik, J.4    Shohami, E.5
  • 66
    • 0026612609 scopus 로고
    • Differential distribution of 68kD and 200kD neurofilament proteins in gerbil hippocampus and their early distributional changes following transient forebrain ischemia
    • NAKAMURA, M., ARAKI, M., OGURO, K., and MASUZAWA, T. (1992). Differential distribution of 68kD and 200kD neurofilament proteins in gerbil hippocampus and their early distributional changes following transient forebrain ischemia. Exp. Brain Res. 89, 31-39.
    • (1992) Exp. Brain Res. , vol.89 , pp. 31-39
    • Nakamura, M.1    Araki, M.2    Oguro, K.3    Masuzawa, T.4
  • 67
    • 0029854806 scopus 로고    scopus 로고
    • α-spectrin breakdown by calpain and ICE-like proteases in apoptotic celldeath: Contributory roles of both proteases families in neuronal apoptosis
    • NATH, R., RASER, K., STAFFORD, D., HAJIMOHAMMADREZA, II, POSNER, A., ALLEN, H., TALANIAN, R.V., YUEN, P.W., GILBERTSEN, B., and WANG, K.K.W. (1996a). α-spectrin breakdown by calpain and ICE-like proteases in apoptotic celldeath: contributory roles of both proteases families in neuronal apoptosis. Biochemical J. 319, 683-690.
    • (1996) Biochemical J. , vol.319 , pp. 683-690
    • Nath, R.1    Raser, K.2    Stafford, D.3    Hajimohammadreza II4    Posner, A.5    Allen, H.6    Talanian, R.V.7    Yuen, P.W.8    Gilbertsen, B.9    Wang, K.K.W.10
  • 70
    • 0029068871 scopus 로고
    • Identification and inhibition of the ICE/CED-3 protease necessary for mammalian apoptosis
    • NICHOLSON, D.W., AMBEREEN, A.N., THORNBERRY, N.A., VALLANCOURT, J.P. et al. (1995). Identification and inhibition of the ICE/CED-3 protease necessary for mammalian apoptosis. Nature 376, 37-43.
    • (1995) Nature , vol.376 , pp. 37-43
    • Nicholson, D.W.1    Ambereen, A.N.2    Thornberry, N.A.3    Vallancourt, J.P.4
  • 72
    • 0028238507 scopus 로고
    • Brain ischemia decreases phophatidylcholine-phospholipase D but not phosphatidylinositol-phospholipase C in rats
    • NISHIDA, A., EMOTO, K., SHIMIZU, M., UOZUMI, T., and YAMAWAKI, S. (1994). Brain ischemia decreases phophatidylcholine-phospholipase D but not phosphatidylinositol-phospholipase C in rats. Stroke 25, 1247-1251.
    • (1994) Stroke , vol.25 , pp. 1247-1251
    • Nishida, A.1    Emoto, K.2    Shimizu, M.3    Uozumi, T.4    Yamawaki, S.5
  • 73
    • 0025943790 scopus 로고
    • Neurofilament phosphorylation: A new look at regulation and function
    • NIXON, R.A., and SIHAG, R.K. (1991). Neurofilament phosphorylation: a new look at regulation and function. Trends Neurosci. 14, 501-506.
    • (1991) Trends Neurosci. , vol.14 , pp. 501-506
    • Nixon, R.A.1    Sihag, R.K.2
  • 74
    • 0021260066 scopus 로고
    • Degradation of neurofilament proteins by purified human brain cathepsin D
    • NIXON, R.A., and MAROTTA, C.A. (1984). Degradation of neurofilament proteins by purified human brain cathepsin D. J. Neurochem. 43, 507-516.
    • (1984) J. Neurochem. , vol.43 , pp. 507-516
    • Nixon, R.A.1    Marotta, C.A.2
  • 75
    • 0024953749 scopus 로고
    • Calcium activated neutral proteinases as regulators of cellular function. Implications for Alzheimers disease pathogenesis
    • NIXON, R.A. (1989). Calcium activated neutral proteinases as regulators of cellular function. Implications for Alzheimers disease pathogenesis. Ann. N.Y. Acad. Sci. 568, 198-208.
    • (1989) Ann. N.Y. Acad. Sci. , vol.568 , pp. 198-208
    • Nixon, R.A.1
  • 76
    • 0027934386 scopus 로고
    • Subcellular distribution of calpain and calpastatin immunoreactivity and fodrin proteolysis in rabbit hippocampus after hypoxia and glucocorticoid treatment
    • OSTWALD, K., HAYASHI, M., NAKAMURA, M., and KAWASHIMA, S. (1994). Subcellular distribution of calpain and calpastatin immunoreactivity and fodrin proteolysis in rabbit hippocampus after hypoxia and glucocorticoid treatment. J. Neurochem. 63, 1069-1076.
    • (1994) J. Neurochem. , vol.63 , pp. 1069-1076
    • Ostwald, K.1    Hayashi, M.2    Nakamura, M.3    Kawashima, S.4
  • 77
    • 0023866466 scopus 로고
    • The ultrastructural localization of calcium activated protease "Calpain" in rat brain
    • PERLMUTTER, L.S., SIMAN, R., GALL, C., SEUBERT, P., BAUDRY, M., and LYNCH, G. (1988). The ultrastructural localization of calcium activated protease "Calpain" in rat brain. Synapse 2, 79-88.
    • (1988) Synapse , vol.2 , pp. 79-88
    • Perlmutter, L.S.1    Siman, R.2    Gall, C.3    Seubert, P.4    Baudry, M.5    Lynch, G.6
  • 78
    • 0025285178 scopus 로고
    • Distribution of calcium-activated protease in the rat brain
    • PERLMUTTER, L.S., GALL, C., BAUDRY, M., and LYNCH, G. (1990). Distribution of calcium-activated protease 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
  • 79
    • 0028152764 scopus 로고
    • Traumatically induced altered membrane permeability: Its relationship to traumatically induced reactive axonal change
    • PETTUS, E.H., CHRISTMAN, C.W., GIEBEL, M.L., and POVLISHOCK, J.T. (1994). Traumatically induced altered membrane permeability: Its relationship to traumatically induced reactive axonal change. J. Neurotrauma 11, 507-521.
    • (1994) J. Neurotrauma , vol.11 , pp. 507-521
    • Pettus, E.H.1    Christman, C.W.2    Giebel, M.L.3    Povlishock, J.T.4
  • 80
    • 0029896102 scopus 로고    scopus 로고
    • Characterization of a disstinct set of intra-axonal ultrastructural changes associated with traumatically induced alteration in axolemmal permeability
    • PETTUS, E.H., and POVLISHOCK, J.T. (1996). Characterization of a disstinct set of intra-axonal ultrastructural changes associated with traumatically induced alteration in axolemmal permeability. Brain Research 722, 1-11.
    • (1996) Brain Research , vol.722 , pp. 1-11
    • Pettus, E.H.1    Povlishock, J.T.2
  • 81
    • 0028135244 scopus 로고
    • Neurofilament 68 and neurofilament 200 protein levels decrease after traumatic brain injury
    • POSMANTUR, R., HAYES, R.L., DIXON, C.E., and TAFT, W.C. (1994). Neurofilament 68 and neurofilament 200 protein levels decrease after traumatic brain injury. J. Neurotrauma 11, 533-545.
    • (1994) J. Neurotrauma , vol.11 , pp. 533-545
    • Posmantur, R.1    Hayes, R.L.2    Dixon, C.E.3    Taft, W.C.4
  • 82
    • 0030063506 scopus 로고    scopus 로고
    • Cytoskeletal derangements of cortical neuronal processes three hours after traumatic brain injury in rats: An immunofluorescence study
    • POSMANTUR, R.M., KAMPFL, A., LIU, S.J., HECK, K., TAFT, W.C., CLIFTON, G.L., and HAYES, R.L. (1996a). Cytoskeletal derangements of cortical neuronal processes three hours after traumatic brain injury in rats: an immunofluorescence study. J. Neuropath. Exp. Neurol. 55, 68-90.
    • (1996) J. Neuropath. Exp. Neurol. , vol.55 , pp. 68-90
    • Posmantur, R.M.1    Kampfl, A.2    Liu, S.J.3    Heck, K.4    Taft, W.C.5    Clifton, G.L.6    Hayes, R.L.7
  • 83
  • 84
    • 10144253093 scopus 로고    scopus 로고
    • A calpain inhibitor attenuates cortical cytoskeletal protein loss after experimental traumatic brain injury in the rat
    • in press
    • POSMANTUR, R., KAMPFL, A., SIMAN, R., LIU, S.J., ZHAO, X., CLIFTON, G.L., and HAYES, R.L. (1996c). A calpain inhibitor attenuates cortical cytoskeletal protein loss after experimental traumatic brain injury in the rat. Neuroscience, in press.
    • (1996) Neuroscience
    • Posmantur, R.1    Kampfl, A.2    Siman, R.3    Liu, S.J.4    Zhao, X.5    Clifton, G.L.6    Hayes, R.L.7
  • 85
    • 1842277636 scopus 로고    scopus 로고
    • A one and two-dimensional immunoblot analyses of putative calpain medicated neurofilament BDPs following traumatic brain injury in rats
    • POSMANTUR, R.M., ZHAO, X., KAMPFL, A., LIU, J.S., CLIFTON, G.L., and HAYES, R.L. (1996d). A one and two-dimensional immunoblot analyses of putative calpain medicated neurofilament BDPs following traumatic brain injury in rats. Soc. for Neurosci. 22, 1903.
    • (1996) Soc. for Neurosci. , vol.22 , pp. 1903
    • Posmantur, R.M.1    Zhao, X.2    Kampfl, A.3    Liu, J.S.4    Clifton, G.L.5    Hayes, R.L.6
  • 86
    • 0028793071 scopus 로고
    • The pathobiology of traumatically induced axonal injury in animals and humans: A review of current thoughts
    • POVLISHOCK, J.T., and CHRISTMAN, C.W. (1995). The pathobiology of traumatically induced axonal injury in animals and humans: a review of current thoughts. J. Neurotrauma 12, 555-564.
    • (1995) J. Neurotrauma , vol.12 , pp. 555-564
    • Povlishock, J.T.1    Christman, C.W.2
  • 88
    • 0027215039 scopus 로고
    • Protective effects of calpain inhibitors against neuronal damage caused by cytotoxic hypoxia in vitro and ischemia in vivo
    • RAMI, A., and KRIEGLSTEIN, J. (1993). Protective effects of calpain inhibitors against neuronal damage caused by cytotoxic hypoxia in vitro and ischemia in vivo. Brain Res. 609, 67-70.
    • (1993) Brain Res. , vol.609 , pp. 67-70
    • Rami, A.1    Krieglstein, J.2
  • 89
    • 0028820892 scopus 로고
    • Long-term potentiation deficits and excitability changes following traumatic brain injury
    • REEVES, T.M., LYETH, B.G., and POVLISHOCK, J.T. (1995). Long-term potentiation deficits and excitability changes following traumatic brain injury. Exp. Brain Res. 106, 248-256.
    • (1995) Exp. Brain Res. , vol.106 , pp. 248-256
    • Reeves, T.M.1    Lyeth, B.G.2    Povlishock, J.T.3
  • 91
  • 92
    • 0028282502 scopus 로고
    • Immunolocalization of calpain 1 mediated spectrin degradation to vulnerable neurons in ischemic gerbil brain
    • ROBERTS-LEWIS, J.M., SAVAGE, M.J., MARCY, V.R., PINSKER L.R., and SIMAN, R. (1994). Immunolocalization of calpain 1 mediated spectrin degradation to vulnerable neurons in ischemic gerbil brain. J. Neurosci. 14, 3934-3944.
    • (1994) J. Neurosci. , vol.14 , pp. 3934-3944
    • Roberts-Lewis, J.M.1    Savage, M.J.2    Marcy, V.R.3    Pinsker, L.R.4    Siman, R.5
  • 93
    • 0030025099 scopus 로고    scopus 로고
    • Inhibiting calpain, rescuing cells
    • ROBINSON, A. (1996). Inhibiting calpain, rescuing cells. Can. Med. Assoc. J. 154, 193-195.
    • (1996) Can. Med. Assoc. J. , vol.154 , pp. 193-195
    • Robinson, A.1
  • 94
    • 0028825270 scopus 로고
    • Matrix metalloproteinases in brain injury
    • ROSENBERG, G. (1995). Matrix metalloproteinases in brain injury. J. Neurotrauma 12, 833-840.
    • (1995) J. Neurotrauma , vol.12 , pp. 833-840
    • Rosenberg, G.1
  • 95
    • 0028872674 scopus 로고
    • Excitotoxicity and the NMDA receptor-still lethal after eight years
    • ROTHMAN, S.M., and OLNEY, J.W. (1995). Excitotoxicity and the NMDA receptor-still lethal after eight years. Trends Neurosci. 18, 57-58.
    • (1995) Trends Neurosci. , vol.18 , pp. 57-58
    • Rothman, S.M.1    Olney, J.W.2
  • 96
    • 0030037390 scopus 로고    scopus 로고
    • Prolonged calpain-mediated spectrin breakdown occurs regionally following experimental brain injury in the rat
    • T.K.
    • SAATMAN, K.E., BOZYCZKO-COYNE, D., SIMAN, R., MARCY V., and, T.K. (1996a). Prolonged calpain-mediated spectrin breakdown occurs regionally following experimental brain injury in the rat. J. Neuropathol. Exp. Neurol. 55, 852-862.
    • (1996) J. Neuropathol. Exp. Neurol. , vol.55 , pp. 852-862
    • Saatman, K.E.1    Bozyczko-Coyne, D.2    Siman, R.3    Marcy, V.4
  • 98
    • 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
  • 99
    • 0026542341 scopus 로고
    • Autolytic transition of μ-calpain upon activation as resolved by antibodies distinguishing between pre- and post-autolysis forms
    • SAIDO, T.C., NAGAO, S., SHIRAMINE, M., TSUKAGUCHI, M., SORIMACHI, H., MUROFUCSHI, H., TSUCHCHIYA, T., ITO, H., and SUZUKI K. (1992). Autolytic transition of μ-calpain upon activation as resolved by antibodies distinguishing between pre- and post-autolysis forms. J. Biochem. 111, 81-86.
    • (1992) J. Biochem. , vol.111 , pp. 81-86
    • Saido, T.C.1    Nagao, S.2    Shiramine, M.3    Tsukaguchi, M.4    Sorimachi, H.5    Murofucshi, H.6    Tsuchchiya, T.7    Ito, H.8    Suzuki, K.9
  • 100
    • 0026454458 scopus 로고
    • Positive regulation of μ-calpain action by polyphosphoinositides
    • SAIDO, T.C., SHUBATA, M., TAKENAWA, T., MUROFUSH, H., SUZUKI, K. (1992). Positive regulation of μ-calpain action by polyphosphoinositides. J. Biol. Chem. 264(34), 24585-24590.
    • (1992) J. Biol. Chem. , vol.264 , Issue.34 , pp. 24585-24590
    • Saido, T.C.1    Shubata, M.2    Takenawa, T.3    Murofush, H.4    Suzuki, K.5
  • 102
    • 0027365768 scopus 로고
    • Spatial resolution of fodrin proteolysis in postischemic brain
    • SAIDO, T.C., YOKOTA, M., NAGAO, S., et al. (1993b). Spatial resolution of fodrin proteolysis in postischemic brain. J. Biol. Chem. 33, 25239-25243.
    • (1993) J. Biol. Chem. , vol.33 , pp. 25239-25243
    • Saido, T.C.1    Yokota, M.2    Nagao, S.3
  • 103
    • 0027474051 scopus 로고
    • Widespread activation of calcium-activated neutral proteinase (calpain) in the brain in Alzheimer disease: A potential molecular basis for neuronal degeneration
    • SAITO, K.I., ELCE, J.S., HAMOS, J.E., and NIXON, R.A. (1993). Widespread activation of calcium-activated neutral proteinase (calpain) in the brain in Alzheimer disease: a potential molecular basis for neuronal degeneration. Proc. Natl. Acad. Sci. USA. 90, 2628-2632.
    • (1993) Proc. Natl. Acad. Sci. USA. , vol.90 , pp. 2628-2632
    • Saito, K.I.1    Elce, J.S.2    Hamos, J.E.3    Nixon, R.A.4
  • 104
    • 0024332791 scopus 로고
    • Quantitation and immunohistochemical localization of cathepsins E and D in rat tissues and blood cells
    • SAKAI, H., SAKU, T., KATO, Y., and YAMAMOTO et al. (1989). Quantitation and immunohistochemical localization of cathepsins E and D in rat tissues and blood cells. Biochim Biophys Acta 991, 367-375.
    • (1989) Biochim Biophys Acta , vol.991 , pp. 367-375
    • Sakai, H.1    Saku, T.2    Kato, Y.3    Yamamoto4
  • 105
    • 0023126417 scopus 로고
    • Neurofilaments: Structure, metabolism, and implications in disease
    • SCHLAEPFER, W. (1987). Neurofilaments: Structure, metabolism, and implications in disease. J. Neuropath. Exp. Neurol. 46, 117-129.
    • (1987) J. Neuropath. Exp. Neurol. , vol.46 , pp. 117-129
    • Schlaepfer, W.1
  • 106
    • 0022300365 scopus 로고
    • Mechanisms underlying the neuronal response to ischemic injury. Calcium-activated proteolysis of neurofilaments
    • SCHLAEPFER, W.W., and ZIMMERMAN, U.J. (1985). Mechanisms underlying the neuronal response to ischemic injury. Calcium-activated proteolysis of neurofilaments. Prog. Brain Res. 63, 185-196.
    • (1985) Prog. Brain Res. , vol.63 , pp. 185-196
    • Schlaepfer, W.W.1    Zimmerman, U.J.2
  • 107
    • 0021931262 scopus 로고
    • An immunoblot study of neurofilament degradation in situ and during calcium activated proteolysis
    • SCHLAEPFER, W.W., LEE, C., LEE, V.W., and ZIMMERMAN, U.J. (1985). An immunoblot study of neurofilament degradation in situ and during calcium activated proteolysis. J. Neurochem. 44, 502-509.
    • (1985) J. Neurochem. , vol.44 , pp. 502-509
    • Schlaepfer, W.W.1    Lee, C.2    Lee, V.W.3    Zimmerman, U.J.4
  • 108
    • 0024347477 scopus 로고
    • Ischemia triggers NMDA receptor-linked cytoskeletal proteolysis in hippocampus
    • SEUBERT, P., LEE, K., and LYNCH, G. (1989). Ischemia triggers NMDA receptor-linked cytoskeletal proteolysis in hippocampus. Brain Res. 492, 366-370.
    • (1989) Brain Res. , vol.492 , pp. 366-370
    • Seubert, P.1    Lee, K.2    Lynch, G.3
  • 109
    • 0024349953 scopus 로고
    • Accumulation of calcium in the brain following head trauma
    • SHAPIRA, Y., YADID, G., COTEX, S., and SHAHOAMI, E. (1989). Accumulation of calcium in the brain following head trauma. Neurological Res. 11, 169-172.
    • (1989) Neurological Res. , vol.11 , pp. 169-172
    • Shapira, Y.1    Yadid, G.2    Cotex, S.3    Shahoami, E.4
  • 110
    • 0022700342 scopus 로고
    • Neurofilaments: Abundant but mysterious structures
    • SHAW, G. (1986). Neurofilaments: Abundant but mysterious structures. Bioessays 4, 161-166.
    • (1986) Bioessays , vol.4 , pp. 161-166
    • Shaw, G.1
  • 111
    • 0024556434 scopus 로고
    • Calcium fluxes, calcium antagonists, and calcium related pathology in brain ischemia, hypoglycemia, and spreading depression: A unifying hypothesis
    • SIESJOE, B.K., and BENGTSSON F. (1989). Calcium fluxes, calcium antagonists, and calcium related pathology in brain ischemia, hypoglycemia, and spreading depression: a unifying hypothesis. J. Cereb. Blood Flow Metab. 9, 127-140.
    • (1989) J. Cereb. Blood Flow Metab. , vol.9 , pp. 127-140
    • Siesjoe, B.K.1    Bengtsson, F.2
  • 112
    • 0021273261 scopus 로고
    • Brain fodrin: Substrate for calpain 1, an endogenous calcium-activated protease
    • SIMAN, R., BAUDRY, M., and LYNCH, G. (1984). Brain fodrin: Substrate for calpain 1, an endogenous calcium-activated protease. Proc. Natl. Acad. Sci. USA. 81, 3572-3575.
    • (1984) Proc. Natl. Acad. Sci. USA. , vol.81 , pp. 3572-3575
    • Siman, R.1    Baudry, M.2    Lynch, G.3
  • 113
    • 0024020782 scopus 로고
    • Excitatory amino acids activate calpain 1 and induce structural protein breakdown in vivo
    • SIMAN, R., and NOSZEK, J.C. (1988). Excitatory amino acids activate calpain 1 and induce structural protein breakdown in vivo. Neuron 1, 279-287.
    • (1988) Neuron , vol.1 , pp. 279-287
    • Siman, R.1    Noszek, J.C.2
  • 114
    • 0024363137 scopus 로고
    • Calpain 1 activation is specifically related to excitatory amino acid induction of hippocampal damage
    • SIMAN, R., NOSZEK, J.C., and KEGERISE, C. (1989). Calpain 1 activation is specifically related to excitatory amino acid induction of hippocampal damage. J. Neurosci. 9, 1579-1590.
    • (1989) J. Neurosci. , vol.9 , pp. 1579-1590
    • Siman, R.1    Noszek, J.C.2    Kegerise, C.3
  • 115
    • 0028347283 scopus 로고
    • New era of calpain research: Discovery of tissue-specific calpains
    • SORIMACHI, H., SAIDO, T.C., and SUZUKI, K. (1994). New era of calpain research: Discovery of tissue-specific calpains. FEBS Ltrs 343, 1-5.
    • (1994) FEBS Ltrs , vol.343 , pp. 1-5
    • Sorimachi, H.1    Saido, T.C.2    Suzuki, K.3
  • 119
    • 0028024908 scopus 로고
    • Triggering and execution of neuronal death in brain ischemia: Two phases of glutamate release by different mechanisms
    • SZATKOWSKI, M., and ATWELL, D. (1994). Triggering and execution of neuronal death in brain ischemia: two phases of glutamate release by different mechanisms. Trends Neurosci. 17, 359-365.
    • (1994) Trends Neurosci. , vol.17 , pp. 359-365
    • Szatkowski, M.1    Atwell, D.2
  • 120
    • 0026489693 scopus 로고
    • Microtubule associated protein 2 level in hippocampus following traumatic brain injury
    • TAFT, W.C., YANG, K., DIXON, C.E., and HAYES, R.L. (1992). Microtubule associated protein 2 level in hippocampus following traumatic brain injury. J. Neurotrauma 9, 281-290.
    • (1992) J. Neurotrauma , vol.9 , pp. 281-290
    • Taft, W.C.1    Yang, K.2    Dixon, C.E.3    Hayes, R.L.4
  • 121
    • 0027199244 scopus 로고
    • Hypothermia attenuates the loss of hippocampal microtubule-associated protein 2 (MAP2) following traumatic brain injury
    • TAFT, W.C., YANG, K., DIXON, C.E., CLIFTON, G.L., and HAYES, R.L. (1993). Hypothermia attenuates the loss of hippocampal microtubule-associated protein 2 (MAP2) following traumatic brain injury. J. Cereb. Blood. Flow. Metab. 13, 796-802.
    • (1993) J. Cereb. Blood. Flow. Metab. , vol.13 , pp. 796-802
    • Taft, W.C.1    Yang, K.2    Dixon, C.E.3    Clifton, G.L.4    Hayes, R.L.5
  • 122
    • 0028990125 scopus 로고
    • Yama/CPP32B, a mammalian homolog of CED-3, is a CmA-inhibitable protease that cleaves the death substrate Poly (ADP-Ribose) Polymerase
    • TEWART, M., QUAN, L., O'ROURKE, K., DESNOYERS, S., ZENG, Z., BEIDLER, D., POIRIER, G., SALVESEN, G., and DIXIT, V.M. (1995). Yama/CPP32B, a mammalian homolog of CED-3, is a CmA-inhibitable protease that cleaves the death substrate Poly (ADP-Ribose) Polymerase. Cell 81, 801-809.
    • (1995) Cell , vol.81 , pp. 801-809
    • Tewart, M.1    Quan, L.2    O'Rourke, K.3    Desnoyers, S.4    Zeng, Z.5    Beidler, D.6    Poirier, G.7    Salvesen, G.8    Dixit, V.M.9
  • 124
  • 125
    • 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
  • 126
    • 0027988820 scopus 로고
    • Calpain inhibition: An overview of its therapeutic potential
    • WANG, K.K.W., and YUEN, P.-W. (1994). Calpain inhibition: An overview of its therapeutic potential. Trends. Pharmacol. Sci. 15, 412-419.
    • (1994) Trends. Pharmacol. Sci. , vol.15 , pp. 412-419
    • Wang, K.K.W.1    Yuen, P.-W.2
  • 127
    • 0029095275 scopus 로고
    • Brief potassium depolarization decreases levels of neurofilament proteins in CNS culture
    • WHITSON, J.S., KAMPFL, A., ZHAO, X., DIXON, C.E., and HAYES, R.L. (1995a). Brief potassium depolarization decreases levels of neurofilament proteins in CNS culture. Brain Res. 694, 213-222.
    • (1995) Brain Res. , vol.694 , pp. 213-222
    • Whitson, J.S.1    Kampfl, A.2    Zhao, X.3    Dixon, C.E.4    Hayes, R.L.5
  • 128
    • 0029147614 scopus 로고
    • Transient loss of neurofilament proteins following brief potassium depolarization in CNS culture
    • WHITSON, J.S., KAMPFL A., ZHAO, X., and HAYES, R.L. (1995b). Transient loss of neurofilament proteins following brief potassium depolarization in CNS culture. Neurosci. Lett. 197, 159-163.
    • (1995) Neurosci. Lett. , vol.197 , pp. 159-163
    • Whitson, J.S.1    Kampfl, A.2    Zhao, X.3    Hayes, R.L.4
  • 129
    • 0026073294 scopus 로고
    • Changes in the activity of protein kinase C and the differential subcellular redistribution of its isoenzymes in the rat striatum during and following transient forebrain ischemia
    • WIELOCH, T., CARDELL, M., BINGREN, H., ZIVIN, J., and SAITOH, T. (1992). Changes in the activity of protein kinase C and the differential subcellular redistribution of its isoenzymes in the rat striatum during and following transient forebrain ischemia. J. Neurochem. 56, 1227-1233.
    • (1992) J. Neurochem. , vol.56 , pp. 1227-1233
    • Wieloch, T.1    Cardell, M.2    Bingren, H.3    Zivin, J.4    Saitoh, T.5
  • 130
    • 0026598116 scopus 로고
    • Traumatically induced reactive change as visualized through the use of monoclonal antibodies targeted to neurofilament subunits
    • YAGHMAI, A., and POVLISHOCK, J. (1992). Traumatically induced reactive change as visualized through the use of monoclonal antibodies targeted to neurofilament subunits. J. Neuropath. Exp. Neurol. 51, 158-176.
    • (1992) J. Neuropath. Exp. Neurol. , vol.51 , pp. 158-176
    • Yaghmai, A.1    Povlishock, J.2
  • 132
    • 0026715839 scopus 로고
    • Alteration in the immunoreactivity of the calcineurin subunits after ischemia hippocampal damage
    • YAMASAKI, Y., ONODERA, H., ADACHI, K., SHOZUHARA, H., and KOGURE, K. (1992). Alteration in the immunoreactivity of the calcineurin subunits after ischemia hippocampal damage. Neuroscience 49, 545-556.
    • (1992) Neuroscience , vol.49 , pp. 545-556
    • Yamasaki, Y.1    Onodera, H.2    Adachi, K.3    Shozuhara, H.4    Kogure, K.5
  • 133
    • 0028113774 scopus 로고
    • Endogenous phosphorylation of a 61000 dalton hippocampal protein increases following TBI
    • YANG, K.Y., TAFT, W.C., DIXON, C.E., YU, R.K., and HAYES, R.L. (1994). Endogenous phosphorylation of a 61000 dalton hippocampal protein increases following TBI. J. Neurotrauma 11, 523-532.
    • (1994) J. Neurotrauma , vol.11 , pp. 523-532
    • Yang, K.Y.1    Taft, W.C.2    Dixon, C.E.3    Yu, R.K.4    Hayes, R.L.5
  • 134
    • 0029825747 scopus 로고    scopus 로고
    • Therapeutic potential of calpain inhibitors in neurodegeneerative disorders
    • YUEN, P.-W., and WANG, K.K.W. (1996). Therapeutic potential of calpain inhibitors in neurodegeneerative disorders. Exp. Opin. Invest. Drugs 5(10), 1291-1304.
    • (1996) Exp. Opin. Invest. Drugs , vol.5 , Issue.10 , pp. 1291-1304
    • Yuen, P.-W.1    Wang, K.K.W.2
  • 135
    • 0028169924 scopus 로고
    • Calcium accumulations in dendrites of neocortical pyramidal neurons: An apical band and evidence for two functional compartments
    • YUSTE, R., GUTNICK, M.J., SAAR, D., DELANEY, K.R., and TANK, D.W. (1994). Calcium accumulations in dendrites of neocortical pyramidal neurons: an apical band and evidence for two functional compartments. Neuron 13, 23-43.
    • (1994) Neuron , vol.13 , pp. 23-43
    • Yuste, R.1    Gutnick, M.J.2    Saar, D.3    Delaney, K.R.4    Tank, D.W.5
  • 136
    • 0029763766 scopus 로고    scopus 로고
    • The Major Calpain Isozymes Are Long-lived Proteins
    • ZHANG, W., LANE, R.D., MELLGRAN, R.L. (1996). The Major Calpain Isozymes Are Long-lived Proteins. J Biological Chem, (271) 31, 18825-18830.
    • (1996) J Biological Chem , vol.31 , Issue.271 , pp. 18825-18830
    • Zhang, W.1    Lane, R.D.2    Mellgran, R.L.3
  • 137
    • 0025911090 scopus 로고
    • Two stage autolysis of the catalytic subunit inititates autolysis of μ-calpain
    • ZIMMERMAN, U.J.P., and SCHLAEPFER, W.W. (1991). Two stage autolysis of the catalytic subunit inititates autolysis of μ-calpain. Biochem. Biophys. Acta. 1078, 192-198.
    • (1991) Biochem. Biophys. Acta. , vol.1078 , pp. 192-198
    • Zimmerman, U.J.P.1    Schlaepfer, W.W.2


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