메뉴 건너뛰기




Volumn 237, Issue , 2013, Pages 66-86

Spatiotemporal resolution of BDNF neuroprotection against glutamate excitotoxicity in cultured hippocampal neurons

Author keywords

Axons; Brain derived neurotrophic factor (BDNF); Dendrites; Excitotoxicity; Neuroprotection; Synapses

Indexed keywords

BRAIN DERIVED NEUROTROPHIC FACTOR; CALPAIN; CASPASE 3; GLUTAMIC ACID; MICROTUBULE ASSOCIATED PROTEIN 2; NEUROFILAMENT H PROTEIN; NEUROFILAMENT PROTEIN; PHOSPHATIDYLINOSITOL 3 KINASE; PHOSPHOLIPASE C GAMMA1; TRANSIENT RECEPTOR POTENTIAL CHANNEL 3; TRANSIENT RECEPTOR POTENTIAL CHANNEL 6; UNCLASSIFIED DRUG; VESICULAR GLUTAMATE TRANSPORTER 1; VESICULAR GLUTAMATE TRANSPORTER 2;

EID: 84874734906     PISSN: 03064522     EISSN: 18737544     Source Type: Journal    
DOI: 10.1016/j.neuroscience.2013.01.054     Document Type: Article
Times cited : (29)

References (101)
  • 4
    • 34248342249 scopus 로고    scopus 로고
    • TRPC3 channels are necessary for brain-derived neurotrophic factor to activate a nonselective cationic current and to induce dendritic spine formation
    • Amaral M.D., Pozzo-Miller L. TRPC3 channels are necessary for brain-derived neurotrophic factor to activate a nonselective cationic current and to induce dendritic spine formation. J Neurosci 2007, 27:5179-5189.
    • (2007) J Neurosci , vol.27 , pp. 5179-5189
    • Amaral, M.D.1    Pozzo-Miller, L.2
  • 6
    • 33646104431 scopus 로고    scopus 로고
    • Tubulin-mediated binding of human immunodeficiency virus-1 Tat to the cytoskeleton causes proteasomal-dependent degradation of microtubule-associated protein 2 and neuronal damage
    • Aprea S., Del Valle L., Mameli G., Sawaya B.E., Khalili K., Peruzzi F. Tubulin-mediated binding of human immunodeficiency virus-1 Tat to the cytoskeleton causes proteasomal-dependent degradation of microtubule-associated protein 2 and neuronal damage. J Neurosci 2006, 26:4054-4062.
    • (2006) J Neurosci , vol.26 , pp. 4054-4062
    • Aprea, S.1    Del Valle, L.2    Mameli, G.3    Sawaya, B.E.4    Khalili, K.5    Peruzzi, F.6
  • 7
    • 0030874793 scopus 로고    scopus 로고
    • Neuronal damage and MAP2 changes induced by the glutamate transport inhibitor dihydrokainate and by kainate in rat hippocampus in vivo
    • Arias C., Arrieta I., Massieu L., Tapia R. Neuronal damage and MAP2 changes induced by the glutamate transport inhibitor dihydrokainate and by kainate in rat hippocampus in vivo. Exp Brain Res 1997, 116:467-476.
    • (1997) Exp Brain Res , vol.116 , pp. 467-476
    • Arias, C.1    Arrieta, I.2    Massieu, L.3    Tapia, R.4
  • 8
    • 0034653131 scopus 로고    scopus 로고
    • Integrin-type signaling has a distinct influence on NMDA-induced cytoskeletal disassembly
    • Bahr B.A. Integrin-type signaling has a distinct influence on NMDA-induced cytoskeletal disassembly. J Neurosci Res 2000, 59:827-832.
    • (2000) J Neurosci Res , vol.59 , pp. 827-832
    • Bahr, B.A.1
  • 9
    • 38349014705 scopus 로고    scopus 로고
    • Wild-type but not FAD mutant presenilin-1 prevents neuronal degeneration by promoting phosphatidylinositol 3-kinase neuroprotective signaling
    • Baki L., Neve R.L., Shao Z., Shioi J., Georgakopoulos A., Robakis N.K. Wild-type but not FAD mutant presenilin-1 prevents neuronal degeneration by promoting phosphatidylinositol 3-kinase neuroprotective signaling. J Neurosci 2008, 28:483-490.
    • (2008) J Neurosci , vol.28 , pp. 483-490
    • Baki, L.1    Neve, R.L.2    Shao, Z.3    Shioi, J.4    Georgakopoulos, A.5    Robakis, N.K.6
  • 12
    • 65549115558 scopus 로고    scopus 로고
    • Platelet-derived growth factor selectively inhibits NR2B-containing N-methyl-d-aspartate receptors in CA1 hippocampal neurons
    • Beazely M.A., Lim A., Li H., Trepanier C., Chen X., Sidhu B., Macdonald J.F. Platelet-derived growth factor selectively inhibits NR2B-containing N-methyl-d-aspartate receptors in CA1 hippocampal neurons. J Biol Chem 2009, 284:8054-8063.
    • (2009) J Biol Chem , vol.284 , pp. 8054-8063
    • Beazely, M.A.1    Lim, A.2    Li, H.3    Trepanier, C.4    Chen, X.5    Sidhu, B.6    Macdonald, J.F.7
  • 13
    • 0038113310 scopus 로고    scopus 로고
    • Na-K-Cl cotransporter contributes to glutamate-mediated excitotoxicity
    • Beck J., Lenart B., Kintner D.B., Sun D. Na-K-Cl cotransporter contributes to glutamate-mediated excitotoxicity. J Neurosci 2003, 23:5061-5068.
    • (2003) J Neurosci , vol.23 , pp. 5061-5068
    • Beck, J.1    Lenart, B.2    Kintner, D.B.3    Sun, D.4
  • 14
    • 13944261492 scopus 로고    scopus 로고
    • Botulinum neurotoxin C initiates two different programs for neurite degeneration and neuronal apoptosis
    • Berliocchi L., Fava E., Leist M., Horvat V., Dinsdale D., Read D., Nicotera P. Botulinum neurotoxin C initiates two different programs for neurite degeneration and neuronal apoptosis. J Cell Biol 2005, 168:607-618.
    • (2005) J Cell Biol , vol.168 , pp. 607-618
    • Berliocchi, L.1    Fava, E.2    Leist, M.3    Horvat, V.4    Dinsdale, D.5    Read, D.6    Nicotera, P.7
  • 15
    • 0028838282 scopus 로고
    • Excitotoxic degeneration is initiated at non-random sites in cultured rat cerebellar neurons
    • Bindokas V.P., Miller R.J. Excitotoxic degeneration is initiated at non-random sites in cultured rat cerebellar neurons. J Neurosci 1995, 15:6999-7011.
    • (1995) J Neurosci , vol.15 , pp. 6999-7011
    • Bindokas, V.P.1    Miller, R.J.2
  • 16
    • 0035369623 scopus 로고    scopus 로고
    • Transcription-dependent and -independent control of neuronal survival by the PI3K-Akt signaling pathway
    • Brunet A., Datta S.R., Greenberg M.E. Transcription-dependent and -independent control of neuronal survival by the PI3K-Akt signaling pathway. Curr Opin Neurobiol 2001, 11:297-305.
    • (2001) Curr Opin Neurobiol , vol.11 , pp. 297-305
    • Brunet, A.1    Datta, S.R.2    Greenberg, M.E.3
  • 17
    • 0038433282 scopus 로고    scopus 로고
    • Microtubule-associated protein 2 (MAP2) associates with the NMDA receptor and is spatially redistributed within rat hippocampal neurons after oxygen-glucose deprivation
    • Buddle M., Eberhardt E., Ciminello L.H., Levin T., Wing R., DiPasquale K., Raley-Susman K.M. Microtubule-associated protein 2 (MAP2) associates with the NMDA receptor and is spatially redistributed within rat hippocampal neurons after oxygen-glucose deprivation. Brain Res 2003, 978:38-50.
    • (2003) Brain Res , vol.978 , pp. 38-50
    • Buddle, M.1    Eberhardt, E.2    Ciminello, L.H.3    Levin, T.4    Wing, R.5    DiPasquale, K.6    Raley-Susman, K.M.7
  • 19
    • 34249688577 scopus 로고    scopus 로고
    • Genetic modulation of BDNF signaling affects the outcome of axonal competition in vivo
    • Cao L., Dhilla A., Mukai J., Blazeski R., Lodovichi C., Mason C.A., Gogos J.A. Genetic modulation of BDNF signaling affects the outcome of axonal competition in vivo. Curr Biol 2007, 17:911-921.
    • (2007) Curr Biol , vol.17 , pp. 911-921
    • Cao, L.1    Dhilla, A.2    Mukai, J.3    Blazeski, R.4    Lodovichi, C.5    Mason, C.A.6    Gogos, J.A.7
  • 22
    • 0023753142 scopus 로고
    • Calcium-mediated neurotoxicity: relationship to specific channel types and role in ischemic damage
    • Choi D.W. Calcium-mediated neurotoxicity: relationship to specific channel types and role in ischemic damage. Trends Neurosci 1988, 11:465-469.
    • (1988) Trends Neurosci , vol.11 , pp. 465-469
    • Choi, D.W.1
  • 23
    • 18144416201 scopus 로고    scopus 로고
    • Glutamate induces rapid loss of axonal neurofilament proteins from cortical neurons in vitro
    • Chung R.S., McCormack G.H., King A.E., West A.K., Vickers J.C. Glutamate induces rapid loss of axonal neurofilament proteins from cortical neurons in vitro. Exp Neurol 2005, 193:481-488.
    • (2005) Exp Neurol , vol.193 , pp. 481-488
    • Chung, R.S.1    McCormack, G.H.2    King, A.E.3    West, A.K.4    Vickers, J.C.5
  • 24
    • 0029587224 scopus 로고
    • Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B
    • Cross D.A., Alessi D.R., Cohen P., Andjelkovich M., Hemmings B.A. Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B. Nature 1995, 378:785-789.
    • (1995) Nature , vol.378 , pp. 785-789
    • Cross, D.A.1    Alessi, D.R.2    Cohen, P.3    Andjelkovich, M.4    Hemmings, B.A.5
  • 25
    • 0030702123 scopus 로고    scopus 로고
    • Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery
    • Datta S.R., Dudek H., Tao X., Masters S., Fu H., Gotoh Y., Greenberg M.E. Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery. Cell 1997, 91:231-241.
    • (1997) Cell , vol.91 , pp. 231-241
    • Datta, S.R.1    Dudek, H.2    Tao, X.3    Masters, S.4    Fu, H.5    Gotoh, Y.6    Greenberg, M.E.7
  • 26
    • 10244241834 scopus 로고    scopus 로고
    • Deadly conversations: nuclear-mitochondrial cross-talk
    • Dawson V.L., Dawson T.M. Deadly conversations: nuclear-mitochondrial cross-talk. J Bioenerg Biomembr 2004, 36:287-294.
    • (2004) J Bioenerg Biomembr , vol.36 , pp. 287-294
    • Dawson, V.L.1    Dawson, T.M.2
  • 27
    • 0027956623 scopus 로고
    • Neurites can remain viable after destruction of the neuronal soma by programmed cell death (apoptosis)
    • Deckwerth T.L., Johnson E.M. Neurites can remain viable after destruction of the neuronal soma by programmed cell death (apoptosis). Dev Biol 1994, 165:63-72.
    • (1994) Dev Biol , vol.165 , pp. 63-72
    • Deckwerth, T.L.1    Johnson, E.M.2
  • 28
    • 1842333237 scopus 로고    scopus 로고
    • Interleukin-3-induced phosphorylation of BAD through the protein kinase Akt
    • del Peso L., Gonzalez-Garcia M., Page C., Herrera R., Nunez G. Interleukin-3-induced phosphorylation of BAD through the protein kinase Akt. Science 1997, 278:687-689.
    • (1997) Science , vol.278 , pp. 687-689
    • del Peso, L.1    Gonzalez-Garcia, M.2    Page, C.3    Herrera, R.4    Nunez, G.5
  • 29
    • 21344453509 scopus 로고    scopus 로고
    • The ubiquitin-proteasome system as a drug target in cerebrovascular disease: therapeutic potential of proteasome inhibitors
    • Di Napoli M., McLaughlin B. The ubiquitin-proteasome system as a drug target in cerebrovascular disease: therapeutic potential of proteasome inhibitors. Curr Opin Investig Drugs 2005, 6:686-699.
    • (2005) Curr Opin Investig Drugs , vol.6 , pp. 686-699
    • Di Napoli, M.1    McLaughlin, B.2
  • 30
    • 0023905661 scopus 로고
    • The establishment of polarity by hippocampal neurons in culture
    • Dotti C.G., Sullivan C.A., Banker G.A. The establishment of polarity by hippocampal neurons in culture. J Neurosci 1988, 8:1454-1468.
    • (1988) J Neurosci , vol.8 , pp. 1454-1468
    • Dotti, C.G.1    Sullivan, C.A.2    Banker, G.A.3
  • 31
    • 77957837438 scopus 로고    scopus 로고
    • Inhibition of TRPC6 degradation suppresses ischemic brain damage in rats
    • Du W., Huang J., Yao H., Zhou K., Duan B., Wang Y. Inhibition of TRPC6 degradation suppresses ischemic brain damage in rats. J Clin Invest 2010, 120:3480-3492.
    • (2010) J Clin Invest , vol.120 , pp. 3480-3492
    • Du, W.1    Huang, J.2    Yao, H.3    Zhou, K.4    Duan, B.5    Wang, Y.6
  • 33
    • 0034652278 scopus 로고    scopus 로고
    • Evidence that Wallerian degeneration and localized axon degeneration induced by local neurotrophin deprivation do not involve caspases
    • Finn J.T., Weil M., Archer F., Siman R., Srinivasan A., Raff M.C. Evidence that Wallerian degeneration and localized axon degeneration induced by local neurotrophin deprivation do not involve caspases. J Neurosci 2000, 20:1333-1341.
    • (2000) J Neurosci , vol.20 , pp. 1333-1341
    • Finn, J.T.1    Weil, M.2    Archer, F.3    Siman, R.4    Srinivasan, A.5    Raff, M.C.6
  • 34
    • 0142027116 scopus 로고    scopus 로고
    • Intracerebral injection of AMPA causes axonal damage in vivo
    • Fowler J.H., McCracken E., Dewar D., McCulloch J. Intracerebral injection of AMPA causes axonal damage in vivo. Brain Res 2003, 991:104-112.
    • (2003) Brain Res , vol.991 , pp. 104-112
    • Fowler, J.H.1    McCracken, E.2    Dewar, D.3    McCulloch, J.4
  • 36
    • 0024263542 scopus 로고
    • Selective localization of messenger RNA for cytoskeletal protein MAP2 in dendrites
    • Garner C.C., Tucker R.P., Matus A. Selective localization of messenger RNA for cytoskeletal protein MAP2 in dendrites. Nature 1988, 336:674-677.
    • (1988) Nature , vol.336 , pp. 674-677
    • Garner, C.C.1    Tucker, R.P.2    Matus, A.3
  • 37
    • 36448993027 scopus 로고    scopus 로고
    • Protein aggregation and proteasome dysfunction after brain ischemia
    • Ge P., Luo Y., Liu C.L., Hu B. Protein aggregation and proteasome dysfunction after brain ischemia. Stroke 2007, 38:3230-3236.
    • (2007) Stroke , vol.38 , pp. 3230-3236
    • Ge, P.1    Luo, Y.2    Liu, C.L.3    Hu, B.4
  • 38
    • 0027225572 scopus 로고
    • Prolonged survival of transected nerve fibres in C57BL/Ola mice is an intrinsic characteristic of the axon
    • Glass J.D., Brushart T.M., George E.B., Griffin J.W. Prolonged survival of transected nerve fibres in C57BL/Ola mice is an intrinsic characteristic of the axon. J Neurocytol 1993, 22:311-321.
    • (1993) J Neurocytol , vol.22 , pp. 311-321
    • Glass, J.D.1    Brushart, T.M.2    George, E.B.3    Griffin, J.W.4
  • 39
    • 0034658288 scopus 로고    scopus 로고
    • Caspase-mediated degradation of AMPA receptor subunits: a mechanism for preventing excitotoxic necrosis and ensuring apoptosis
    • Glazner G.W., Chan S.L., Lu C., Mattson M.P. Caspase-mediated degradation of AMPA receptor subunits: a mechanism for preventing excitotoxic necrosis and ensuring apoptosis. J Neurosci 2000, 20:3641-3649.
    • (2000) J Neurosci , vol.20 , pp. 3641-3649
    • Glazner, G.W.1    Chan, S.L.2    Lu, C.3    Mattson, M.P.4
  • 42
    • 79953008096 scopus 로고    scopus 로고
    • Cleavage of the vesicular GABA transporter under excitotoxic conditions is followed by accumulation of the truncated transporter in nonsynaptic sites
    • Gomes J.R., Lobo A.C., Melo C.V., Inacio A.R., Takano J., Iwata N., Saido T.C., de Almeida L.P., Wieloch T., Duarte C.B. Cleavage of the vesicular GABA transporter under excitotoxic conditions is followed by accumulation of the truncated transporter in nonsynaptic sites. J Neurosci 2011, 31:4622-4635.
    • (2011) J Neurosci , vol.31 , pp. 4622-4635
    • Gomes, J.R.1    Lobo, A.C.2    Melo, C.V.3    Inacio, A.R.4    Takano, J.5    Iwata, N.6    Saido, T.C.7    de Almeida, L.P.8    Wieloch, T.9    Duarte, C.B.10
  • 43
    • 0027193392 scopus 로고
    • Phosphorylation modulates calpain-mediated proteolysis and calmodulin binding of the 200-kDa and 160-kDa neurofilament proteins
    • Greenwood J.A., Troncoso J.C., Costello A.C., Johnson G.V. Phosphorylation modulates calpain-mediated proteolysis and calmodulin binding of the 200-kDa and 160-kDa neurofilament proteins. J Neurochem 1993, 61:191-199.
    • (1993) J Neurochem , vol.61 , pp. 191-199
    • Greenwood, J.A.1    Troncoso, J.C.2    Costello, A.C.3    Johnson, G.V.4
  • 44
    • 84855822399 scopus 로고    scopus 로고
    • Remarkable reduction of MAP2 in the brains of scrapie-infected rodents and human prion disease possibly correlated with the increase of calpain
    • Guo Y., Gong H.S., Zhang J., Xie W.L., Tian C., Chen C., Shi Q., Wang S.B., Xu Y., Zhang B.Y., Dong X.P. Remarkable reduction of MAP2 in the brains of scrapie-infected rodents and human prion disease possibly correlated with the increase of calpain. PLoS One 2012, 7:e30163.
    • (2012) PLoS One , vol.7
    • Guo, Y.1    Gong, H.S.2    Zhang, J.3    Xie, W.L.4    Tian, C.5    Chen, C.6    Shi, Q.7    Wang, S.B.8    Xu, Y.9    Zhang, B.Y.10    Dong, X.P.11
  • 45
    • 0027957063 scopus 로고
    • Competition between motor molecules (kinesin and cytoplasmic dynein) and fibrous microtubule-associated proteins in binding to microtubules
    • Hagiwara H., Yorifuji H., Sato-Yoshitake R., Hirokawa N. Competition between motor molecules (kinesin and cytoplasmic dynein) and fibrous microtubule-associated proteins in binding to microtubules. J Biol Chem 1994, 269:3581-3589.
    • (1994) J Biol Chem , vol.269 , pp. 3581-3589
    • Hagiwara, H.1    Yorifuji, H.2    Sato-Yoshitake, R.3    Hirokawa, N.4
  • 47
    • 17644393902 scopus 로고    scopus 로고
    • Distinct mechanistic roles of calpain and caspase activation in neurodegeneration as revealed in mice overexpressing their specific inhibitors
    • Higuchi M., Tomioka M., Takano J., Shirotani K., Iwata N., Masumoto H., Maki M., Itohara S., Saido T.C. Distinct mechanistic roles of calpain and caspase activation in neurodegeneration as revealed in mice overexpressing their specific inhibitors. J Biol Chem 2005, 280:15229-15237.
    • (2005) J Biol Chem , vol.280 , pp. 15229-15237
    • Higuchi, M.1    Tomioka, M.2    Takano, J.3    Shirotani, K.4    Iwata, N.5    Masumoto, H.6    Maki, M.7    Itohara, S.8    Saido, T.C.9
  • 48
    • 33744922406 scopus 로고    scopus 로고
    • Wlds protection distinguishes axon degeneration following injury from naturally occurring developmental pruning
    • Hoopfer E.D., McLaughlin T., Watts R.J., Schuldiner O., O'Leary D.D., Luo L. Wlds protection distinguishes axon degeneration following injury from naturally occurring developmental pruning. Neuron 2006, 50:883-895.
    • (2006) Neuron , vol.50 , pp. 883-895
    • Hoopfer, E.D.1    McLaughlin, T.2    Watts, R.J.3    Schuldiner, O.4    O'Leary, D.D.5    Luo, L.6
  • 49
    • 33846863358 scopus 로고    scopus 로고
    • Calcium-dependent NMDA-induced dendritic injury and MAP2 loss in acute hippocampal slices
    • Hoskison M.M., Yanagawa Y., Obata K., Shuttleworth C.W. Calcium-dependent NMDA-induced dendritic injury and MAP2 loss in acute hippocampal slices. Neuroscience 2007, 145:66-79.
    • (2007) Neuroscience , vol.145 , pp. 66-79
    • Hoskison, M.M.1    Yanagawa, Y.2    Obata, K.3    Shuttleworth, C.W.4
  • 50
    • 0242569337 scopus 로고    scopus 로고
    • Non-apoptotic neurite degeneration in apoptotic neuronal death: pivotal role of mitochondrial function in neurites
    • Ikegami K., Koike T. Non-apoptotic neurite degeneration in apoptotic neuronal death: pivotal role of mitochondrial function in neurites. Neuroscience 2003, 122:617-626.
    • (2003) Neuroscience , vol.122 , pp. 617-626
    • Ikegami, K.1    Koike, T.2
  • 51
    • 0029889986 scopus 로고    scopus 로고
    • Intracortical perfusion of glutamate in vivo induces alterations of tau and microtubule-associated protein 2 immunoreactivity in the rat
    • Irving E.A., McCulloch J., Dewar D. Intracortical perfusion of glutamate in vivo induces alterations of tau and microtubule-associated protein 2 immunoreactivity in the rat. Acta Neuropathol 1996, 92:186-196.
    • (1996) Acta Neuropathol , vol.92 , pp. 186-196
    • Irving, E.A.1    McCulloch, J.2    Dewar, D.3
  • 53
    • 34247466099 scopus 로고    scopus 로고
    • TRPC channels promote cerebellar granule neuron survival
    • Jia Y., Zhou J., Tai Y., Wang Y. TRPC channels promote cerebellar granule neuron survival. Nat Neurosci 2007, 10:559-567.
    • (2007) Nat Neurosci , vol.10 , pp. 559-567
    • Jia, Y.1    Zhou, J.2    Tai, Y.3    Wang, Y.4
  • 54
    • 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., Hayes R.L. Calpain inhibitors protect against depolarization-induced neurofilament protein loss of septo-hippocampal neurons in culture. Eur J Neurosci 1996, 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
  • 56
    • 35748950974 scopus 로고    scopus 로고
    • Role of proteasomes in the formation of neurofilamentous inclusions in spinal motor neurons of aluminum-treated rabbits
    • Kimura N., Kumamoto T., Ueyama H., Horinouchi H., Ohama E. Role of proteasomes in the formation of neurofilamentous inclusions in spinal motor neurons of aluminum-treated rabbits. Neuropathology 2007, 27:522-530.
    • (2007) Neuropathology , vol.27 , pp. 522-530
    • Kimura, N.1    Kumamoto, T.2    Ueyama, H.3    Horinouchi, H.4    Ohama, E.5
  • 57
    • 38349159840 scopus 로고    scopus 로고
    • Axon & dendrite degeneration: its mechanisms and protective experimental paradigms
    • Koike T., Yang Y., Suzuki K., Zheng X. Axon & dendrite degeneration: its mechanisms and protective experimental paradigms. Neurochem Int 2008, 52:751-760.
    • (2008) Neurochem Int , vol.52 , pp. 751-760
    • Koike, T.1    Yang, Y.2    Suzuki, K.3    Zheng, X.4
  • 58
    • 13244296953 scopus 로고    scopus 로고
    • Plasma membrane calcium ATPase deficiency causes neuronal pathology in the spinal cord: a potential mechanism for neurodegeneration in multiple sclerosis and spinal cord injury
    • Kurnellas M.P., Nicot A., Shull G.E., Elkabes S. Plasma membrane calcium ATPase deficiency causes neuronal pathology in the spinal cord: a potential mechanism for neurodegeneration in multiple sclerosis and spinal cord injury. FASEB J 2005, 19:298-300.
    • (2005) FASEB J , vol.19 , pp. 298-300
    • Kurnellas, M.P.1    Nicot, A.2    Shull, G.E.3    Elkabes, S.4
  • 59
    • 17244377058 scopus 로고    scopus 로고
    • Essential role of TRPC channels in the guidance of nerve growth cones by brain-derived neurotrophic factor
    • Li Y., Jia Y.C., Cui K., Li N., Zheng Z.Y., Wang Y.Z., Yuan X.B. Essential role of TRPC channels in the guidance of nerve growth cones by brain-derived neurotrophic factor. Nature 2005, 434:894-898.
    • (2005) Nature , vol.434 , pp. 894-898
    • Li, Y.1    Jia, Y.C.2    Cui, K.3    Li, N.4    Zheng, Z.Y.5    Wang, Y.Z.6    Yuan, X.B.7
  • 61
    • 0027533201 scopus 로고
    • Steric inhibition of cytoplasmic dynein and kinesin motility by MAP2
    • Lopez L.A., Sheetz M.P. Steric inhibition of cytoplasmic dynein and kinesin motility by MAP2. Cell Motil Cytoskeleton 1993, 24:1-16.
    • (1993) Cell Motil Cytoskeleton , vol.24 , pp. 1-16
    • Lopez, L.A.1    Sheetz, M.P.2
  • 62
    • 0036372055 scopus 로고    scopus 로고
    • Direct cleavage of AMPA receptor subunit GluR1 and suppression of AMPA currents by caspase-3: implications for synaptic plasticity and excitotoxic neuronal death
    • Lu C., Fu W., Salvesen G.S., Mattson M.P. Direct cleavage of AMPA receptor subunit GluR1 and suppression of AMPA currents by caspase-3: implications for synaptic plasticity and excitotoxic neuronal death. Neuromolecular Med 2002, 1:69-79.
    • (2002) Neuromolecular Med , vol.1 , pp. 69-79
    • Lu, C.1    Fu, W.2    Salvesen, G.S.3    Mattson, M.P.4
  • 64
    • 0024373441 scopus 로고
    • Absence of Wallerian degeneration does not hinder regeneration in peripheral nerve
    • Lunn E.R., Perry V.H., Brown M.C., Rosen H., Gordon S. Absence of Wallerian degeneration does not hinder regeneration in peripheral nerve. Eur J Neurosci 1989, 1:27-33.
    • (1989) Eur J Neurosci , vol.1 , pp. 27-33
    • Lunn, E.R.1    Perry, V.H.2    Brown, M.C.3    Rosen, H.4    Gordon, S.5
  • 65
    • 23244436227 scopus 로고    scopus 로고
    • Axon retraction and degeneration in development and disease
    • Luo L., O'Leary D.D. Axon retraction and degeneration in development and disease. Annu Rev Neurosci 2005, 28:127-156.
    • (2005) Annu Rev Neurosci , vol.28 , pp. 127-156
    • Luo, L.1    O'Leary, D.D.2
  • 67
    • 0034651078 scopus 로고    scopus 로고
    • BDNF promotes the regenerative sprouting, but not survival, of injured serotonergic axons in the adult rat brain
    • Mamounas L.A., Altar C.A., Blue M.E., Kaplan D.R., Tessarollo L., Lyons W.E. BDNF promotes the regenerative sprouting, but not survival, of injured serotonergic axons in the adult rat brain. J Neurosci 2000, 20:771-782.
    • (2000) J Neurosci , vol.20 , pp. 771-782
    • Mamounas, L.A.1    Altar, C.A.2    Blue, M.E.3    Kaplan, D.R.4    Tessarollo, L.5    Lyons, W.E.6
  • 69
    • 84858611096 scopus 로고    scopus 로고
    • Small GTPase Rab17 regulates dendritic morphogenesis and postsynaptic development of hippocampal neurons
    • Mori Y., Matsui T., Furutani Y., Yoshihara Y., Fukuda M. Small GTPase Rab17 regulates dendritic morphogenesis and postsynaptic development of hippocampal neurons. J Biol Chem 2012, 287:8963-8973.
    • (2012) J Biol Chem , vol.287 , pp. 8963-8973
    • Mori, Y.1    Matsui, T.2    Furutani, Y.3    Yoshihara, Y.4    Fukuda, M.5
  • 70
    • 0036939547 scopus 로고    scopus 로고
    • Positive modulation of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid-type glutamate receptors elicits neuroprotection after trimethyltin exposure in hippocampus
    • Munirathinam S., Rogers G., Bahr B.A. Positive modulation of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid-type glutamate receptors elicits neuroprotection after trimethyltin exposure in hippocampus. Toxicol Appl Pharmacol 2002, 185:111-118.
    • (2002) Toxicol Appl Pharmacol , vol.185 , pp. 111-118
    • Munirathinam, S.1    Rogers, G.2    Bahr, B.A.3
  • 71
  • 73
    • 18744428952 scopus 로고    scopus 로고
    • Lactacystin, a specific inhibitor of the proteasome, inhibits human platelet lysosomal cathepsin A-like enzyme
    • Ostrowska H., Wojcik C., Omura S., Worowski K. Lactacystin, a specific inhibitor of the proteasome, inhibits human platelet lysosomal cathepsin A-like enzyme. Biochem Biophys Res Commun 1997, 234:729-732.
    • (1997) Biochem Biophys Res Commun , vol.234 , pp. 729-732
    • Ostrowska, H.1    Wojcik, C.2    Omura, S.3    Worowski, K.4
  • 74
    • 0024237394 scopus 로고
    • Dephosphorylation of neurofilament proteins enhances their susceptibility to degradation by calpain
    • Pant H.C. Dephosphorylation of neurofilament proteins enhances their susceptibility to degradation by calpain. Biochem J 1988, 256:665-668.
    • (1988) Biochem J , vol.256 , pp. 665-668
    • Pant, H.C.1
  • 76
    • 53749093269 scopus 로고    scopus 로고
    • Review of the multiple aspects of neurofilament functions, and their possible contribution to neurodegeneration
    • Perrot R., Berges R., Bocquet A., Eyer J. Review of the multiple aspects of neurofilament functions, and their possible contribution to neurodegeneration. Mol Neurobiol 2008, 38:27-65.
    • (2008) Mol Neurobiol , vol.38 , pp. 27-65
    • Perrot, R.1    Berges, R.2    Bocquet, A.3    Eyer, J.4
  • 77
    • 0037012844 scopus 로고    scopus 로고
    • Axonal self-destruction and neurodegeneration
    • Raff M.C., Whitmore A.V., Finn J.T. Axonal self-destruction and neurodegeneration. Science 2002, 296:868-871.
    • (2002) Science , vol.296 , pp. 868-871
    • Raff, M.C.1    Whitmore, A.V.2    Finn, J.T.3
  • 78
    • 33645846638 scopus 로고    scopus 로고
    • Inhibition of calpain and caspase-3 prevented apoptosis and preserved electrophysiological properties of voltage-gated and ligand-gated ion channels in rat primary cortical neurons exposed to glutamate
    • Ray S.K., Karmakar S., Nowak M.W., Banik N.L. Inhibition of calpain and caspase-3 prevented apoptosis and preserved electrophysiological properties of voltage-gated and ligand-gated ion channels in rat primary cortical neurons exposed to glutamate. Neuroscience 2006, 139:577-595.
    • (2006) Neuroscience , vol.139 , pp. 577-595
    • Ray, S.K.1    Karmakar, S.2    Nowak, M.W.3    Banik, N.L.4
  • 80
    • 13844312400 scopus 로고    scopus 로고
    • Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex
    • Sarbassov D.D., Guertin D.A., Ali S.M., Sabatini D.M. Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex. Science 2005, 307:1098-1101.
    • (2005) Science , vol.307 , pp. 1098-1101
    • Sarbassov, D.D.1    Guertin, D.A.2    Ali, S.M.3    Sabatini, D.M.4
  • 81
    • 34748819496 scopus 로고    scopus 로고
    • Mechanisms of axon degeneration: from development to disease
    • Saxena S., Caroni P. Mechanisms of axon degeneration: from development to disease. Prog Neurobiol 2007, 83:174-191.
    • (2007) Prog Neurobiol , vol.83 , pp. 174-191
    • Saxena, S.1    Caroni, P.2
  • 83
    • 34848842158 scopus 로고    scopus 로고
    • The role of glutamate transporters in neurodegenerative diseases and potential opportunities for intervention
    • Sheldon A.L., Robinson M.B. The role of glutamate transporters in neurodegenerative diseases and potential opportunities for intervention. Neurochem Int 2007, 51:333-355.
    • (2007) Neurochem Int , vol.51 , pp. 333-355
    • Sheldon, A.L.1    Robinson, M.B.2
  • 85
    • 33746233381 scopus 로고    scopus 로고
    • Altered balance of glutamatergic/GABAergic synaptic input and associated changes in dendrite morphology after BDNF expression in BDNF-deficient hippocampal neurons
    • Singh B., Henneberger C., Betances D., Arevalo M.A., Rodriguez-Tebar A., Meier J.C., Grantyn R. Altered balance of glutamatergic/GABAergic synaptic input and associated changes in dendrite morphology after BDNF expression in BDNF-deficient hippocampal neurons. J Neurosci 2006, 26:7189-7200.
    • (2006) J Neurosci , vol.26 , pp. 7189-7200
    • Singh, B.1    Henneberger, C.2    Betances, D.3    Arevalo, M.A.4    Rodriguez-Tebar, A.5    Meier, J.C.6    Grantyn, R.7
  • 87
    • 4644301421 scopus 로고    scopus 로고
    • Synaptic and extrasynaptic localization of brain-derived neurotrophic factor and the tyrosine kinase B receptor in cultured hippocampal neurons
    • Swanwick C.C., Harrison M.B., Kapur J. Synaptic and extrasynaptic localization of brain-derived neurotrophic factor and the tyrosine kinase B receptor in cultured hippocampal neurons. J Comp Neurol 2004, 478:405-417.
    • (2004) J Comp Neurol , vol.478 , pp. 405-417
    • Swanwick, C.C.1    Harrison, M.B.2    Kapur, J.3
  • 88
    • 15444363122 scopus 로고    scopus 로고
    • Neuritic beading induced by activated microglia is an early feature of neuronal dysfunction toward neuronal death by inhibition of mitochondrial respiration and axonal transport
    • Takeuchi H., Mizuno T., Zhang G., Wang J., Kawanokuchi J., Kuno R., Suzumura A. Neuritic beading induced by activated microglia is an early feature of neuronal dysfunction toward neuronal death by inhibition of mitochondrial respiration and axonal transport. J Biol Chem 2005, 280:10444-10454.
    • (2005) J Biol Chem , vol.280 , pp. 10444-10454
    • Takeuchi, H.1    Mizuno, T.2    Zhang, G.3    Wang, J.4    Kawanokuchi, J.5    Kuno, R.6    Suzumura, A.7
  • 89
    • 79955723836 scopus 로고    scopus 로고
    • Dendrites have a rapid program of injury-induced degeneration that is molecularly distinct from developmental pruning
    • Tao J., Rolls M.M. Dendrites have a rapid program of injury-induced degeneration that is molecularly distinct from developmental pruning. J Neurosci 2011, 31:5398-5405.
    • (2011) J Neurosci , vol.31 , pp. 5398-5405
    • Tao, J.1    Rolls, M.M.2
  • 90
    • 33646584876 scopus 로고    scopus 로고
    • Ischemia opens neuronal gap junction hemichannels
    • Thompson R.J., Zhou N., MacVicar B.A. Ischemia opens neuronal gap junction hemichannels. Science 2006, 312:924-927.
    • (2006) Science , vol.312 , pp. 924-927
    • Thompson, R.J.1    Zhou, N.2    MacVicar, B.A.3
  • 91
    • 0034524665 scopus 로고    scopus 로고
    • The pathogenic activation of calpain: a marker and mediator of cellular toxicity and disease states
    • Vanderklish P.W., Bahr B.A. The pathogenic activation of calpain: a marker and mediator of cellular toxicity and disease states. Int J Exp Pathol 2000, 81:323-339.
    • (2000) Int J Exp Pathol , vol.81 , pp. 323-339
    • Vanderklish, P.W.1    Bahr, B.A.2
  • 93
    • 79957634907 scopus 로고    scopus 로고
    • Functional role of neurotrophin-3 in synapse regeneration by spiral ganglion neurons on inner hair cells after excitotoxic trauma in vitro
    • Wang Q., Green S.H. Functional role of neurotrophin-3 in synapse regeneration by spiral ganglion neurons on inner hair cells after excitotoxic trauma in vitro. J Neurosci 2011, 31:7938-7949.
    • (2011) J Neurosci , vol.31 , pp. 7938-7949
    • Wang, Q.1    Green, S.H.2
  • 94
    • 79956054104 scopus 로고    scopus 로고
    • TRPC6 channel protects retinal ganglion cells in a rat model of retinal ischemia/reperfusion-induced cell death
    • Wang X., Teng L., Li A., Ge J., Laties A.M., Zhang X. TRPC6 channel protects retinal ganglion cells in a rat model of retinal ischemia/reperfusion-induced cell death. Invest Ophthalmol Vis Sci 2010, 51:5751-5758.
    • (2010) Invest Ophthalmol Vis Sci , vol.51 , pp. 5751-5758
    • Wang, X.1    Teng, L.2    Li, A.3    Ge, J.4    Laties, A.M.5    Zhang, X.6
  • 95
    • 0037421670 scopus 로고    scopus 로고
    • Bidirectional changes in spatial dendritic integration accompanying long-term synaptic modifications
    • Wang Z., Xu N.L., Wu C.P., Duan S., Poo M.M. Bidirectional changes in spatial dendritic integration accompanying long-term synaptic modifications. Neuron 2003, 37:463-472.
    • (2003) Neuron , vol.37 , pp. 463-472
    • Wang, Z.1    Xu, N.L.2    Wu, C.P.3    Duan, S.4    Poo, M.M.5
  • 96
  • 98
    • 33846502748 scopus 로고    scopus 로고
    • Calpain-mediated mGluR1alpha truncation: a key step in excitotoxicity
    • Xu W., Wong T.P., Chery N., Gaertner T., Wang Y.T., Baudry M. Calpain-mediated mGluR1alpha truncation: a key step in excitotoxicity. Neuron 2007, 53:399-412.
    • (2007) Neuron , vol.53 , pp. 399-412
    • Xu, W.1    Wong, T.P.2    Chery, N.3    Gaertner, T.4    Wang, Y.T.5    Baudry, M.6
  • 99
    • 70449732194 scopus 로고    scopus 로고
    • TRPC channel-mediated neuroprotection by PDGF involves Pyk2/ERK/CREB pathway
    • Yao H., Peng F., Fan Y., Zhu X., Hu G., Buch S.J. TRPC channel-mediated neuroprotection by PDGF involves Pyk2/ERK/CREB pathway. Cell Death Differ 2009, 16:1681-1693.
    • (2009) Cell Death Differ , vol.16 , pp. 1681-1693
    • Yao, H.1    Peng, F.2    Fan, Y.3    Zhu, X.4    Hu, G.5    Buch, S.J.6
  • 101
    • 33645010267 scopus 로고    scopus 로고
    • Developmental changes in NMDA neurotoxicity reflect developmental changes in subunit composition of NMDA receptors
    • Zhou M., Baudry M. Developmental changes in NMDA neurotoxicity reflect developmental changes in subunit composition of NMDA receptors. J Neurosci 2006, 26:2956-2963.
    • (2006) J Neurosci , vol.26 , pp. 2956-2963
    • Zhou, M.1    Baudry, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.