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Volumn 36, Issue 1, 2009, Pages 169-180

The role of MMP-9 in integrin-mediated hippocampal cell death after pilocarpine-induced status epilepticus

Author keywords

Integrins; Matrix metalloproteinase; Pilocarpine; Status epilepticus

Indexed keywords

BETA1 INTEGRIN; GELATINASE B; INTEGRIN LINKED KINASE; PILOCARPINE; PROTEIN KINASE B;

EID: 69649109317     PISSN: 09699961     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.nbd.2009.07.008     Document Type: Article
Times cited : (54)

References (68)
  • 1
    • 0035478029 scopus 로고    scopus 로고
    • Effects of matrix metalloproteinase-9 gene knock-out on the proteolysis of blood-brain barrier and white matter components after cerebral ischemia
    • Asahi M., Wang X., Mori T., Sumii T., Jung J.C., Moskowitz M.A., Fini M.E., and Lo E.H. Effects of matrix metalloproteinase-9 gene knock-out on the proteolysis of blood-brain barrier and white matter components after cerebral ischemia. J. Neurosci. 21 (2001) 7724-7732
    • (2001) J. Neurosci. , vol.21 , pp. 7724-7732
    • Asahi, M.1    Wang, X.2    Mori, T.3    Sumii, T.4    Jung, J.C.5    Moskowitz, M.A.6    Fini, M.E.7    Lo, E.H.8
  • 2
    • 0034601436 scopus 로고    scopus 로고
    • The integrin-linked kinase (ILK) suppresses anoikis
    • Attwell S., Roskelley C., and Dedhar S. The integrin-linked kinase (ILK) suppresses anoikis. Oncogene 19 (2000) 3811-3815
    • (2000) Oncogene , vol.19 , pp. 3811-3815
    • Attwell, S.1    Roskelley, C.2    Dedhar, S.3
  • 3
    • 0033528649 scopus 로고    scopus 로고
    • Differential regulation of apoptosis-related genes in resistant and vulnerable subfields of the rat epileptic hippocampus
    • Becker A.J., Gillardon F., Blumcke I., Langendorfer D., Beck H., and Wiestler O.D. Differential regulation of apoptosis-related genes in resistant and vulnerable subfields of the rat epileptic hippocampus. Brain Res. Mol. Brain Res. 67 (1999) 172-176
    • (1999) Brain Res. Mol. Brain Res. , vol.67 , pp. 172-176
    • Becker, A.J.1    Gillardon, F.2    Blumcke, I.3    Langendorfer, D.4    Beck, H.5    Wiestler, O.D.6
  • 4
    • 0030575294 scopus 로고    scopus 로고
    • Regional distribution and time-course of calpain activation following kainate-induced seizure activity in adult rat brain
    • Bi X., Chang V., Siman R., Tocco G., and Baudry M. Regional distribution and time-course of calpain activation following kainate-induced seizure activity in adult rat brain. Brain Res. 726 (1996) 98-108
    • (1996) Brain Res. , vol.726 , pp. 98-108
    • Bi, X.1    Chang, V.2    Siman, R.3    Tocco, G.4    Baudry, M.5
  • 6
    • 0036516460 scopus 로고    scopus 로고
    • Matrix metalloproteinases: a tail of a frog that became a prince
    • Brinckerhoff C.E., and Matrisian L.M. Matrix metalloproteinases: a tail of a frog that became a prince. Nat. Rev., Mol. Cell Biol. 3 (2002) 207-214
    • (2002) Nat. Rev., Mol. Cell Biol. , vol.3 , pp. 207-214
    • Brinckerhoff, C.E.1    Matrisian, L.M.2
  • 7
    • 0029014398 scopus 로고
    • The pilocarpine model of epilepsy
    • Cavalheiro E.A. The pilocarpine model of epilepsy. Ital. J. Neurol. Sci. 16 (1995) 33-37
    • (1995) Ital. J. Neurol. Sci. , vol.16 , pp. 33-37
    • Cavalheiro, E.A.1
  • 8
    • 0031470554 scopus 로고    scopus 로고
    • Neuronal death in the hippocampus is promoted by plasmin-catalyzed degradation of laminin
    • Chen Z.L., and Strickland S. Neuronal death in the hippocampus is promoted by plasmin-catalyzed degradation of laminin. Cell 91 (1997) 917-925
    • (1997) Cell , vol.91 , pp. 917-925
    • Chen, Z.L.1    Strickland, S.2
  • 9
    • 0037192458 scopus 로고    scopus 로고
    • Matrix metalloproteinase inhibitors and cancer: trials and tribulations
    • Coussens L.M., Fingleton B., and Matrisian L.M. Matrix metalloproteinase inhibitors and cancer: trials and tribulations. Science 295 (2002) 2387-2392
    • (2002) Science , vol.295 , pp. 2387-2392
    • Coussens, L.M.1    Fingleton, B.2    Matrisian, L.M.3
  • 10
    • 0033898797 scopus 로고    scopus 로고
    • Ultrastructural identification of dentate granule cell death from pilocarpine-induced seizures
    • Covolan L., et al. Ultrastructural identification of dentate granule cell death from pilocarpine-induced seizures. Epilepsy Res. 41 (2000) 9-21
    • (2000) Epilepsy Res. , vol.41 , pp. 9-21
    • Covolan, L.1
  • 11
    • 0035885098 scopus 로고    scopus 로고
    • Loss of hippocampal serine protease BSP1/neuropsin predisposes to global seizure activity
    • Davies B., Kearns I.R., Ure J., Davies C.H., and Lathe R. Loss of hippocampal serine protease BSP1/neuropsin predisposes to global seizure activity. J. Neurosci. 21 (2001) 6993-7000
    • (2001) J. Neurosci. , vol.21 , pp. 6993-7000
    • Davies, B.1    Kearns, I.R.2    Ure, J.3    Davies, C.H.4    Lathe, R.5
  • 12
    • 0029988699 scopus 로고    scopus 로고
    • Increased production of matrix metalloproteinases in enriched astrocyte and mixed hippocampal cultures treated with beta-amyloid peptides
    • Deb S., and Gottschall P.E. Increased production of matrix metalloproteinases in enriched astrocyte and mixed hippocampal cultures treated with beta-amyloid peptides. J. Neurochem. 66 (1996) 1641-1647
    • (1996) J. Neurochem. , vol.66 , pp. 1641-1647
    • Deb, S.1    Gottschall, P.E.2
  • 13
    • 0033821286 scopus 로고    scopus 로고
    • A metabolic and neuropathological approach to the understanding of plastic changes that occur in the immature and adult rat brain during lithium-pilocarpine-induced epileptogenesis
    • Dube C., Marescaux C., and Nehlig A. A metabolic and neuropathological approach to the understanding of plastic changes that occur in the immature and adult rat brain during lithium-pilocarpine-induced epileptogenesis. Epilepsia 41 Suppl. 6 (2000) S36-S43
    • (2000) Epilepsia , vol.41 , Issue.SUPPL. 6
    • Dube, C.1    Marescaux, C.2    Nehlig, A.3
  • 14
    • 0033053365 scopus 로고    scopus 로고
    • Proteolysis of neuronal cell adhesion molecule by the tissue plasminogen activator-plasmin system after kainate injection in the mouse hippocampus
    • Endo A., Nagai N., Urano T., Takada Y., Hashimoto K., and Takada A. Proteolysis of neuronal cell adhesion molecule by the tissue plasminogen activator-plasmin system after kainate injection in the mouse hippocampus. Neurosci. Res. 33 (1999) 1-8
    • (1999) Neurosci. Res. , vol.33 , pp. 1-8
    • Endo, A.1    Nagai, N.2    Urano, T.3    Takada, Y.4    Hashimoto, K.5    Takada, A.6
  • 15
    • 0142125762 scopus 로고    scopus 로고
    • Distribution of alpha and beta integrin subunits in the adult rat hippocampus after pilocarpine-induced neuronal cell loss, axonal reorganization and reactive astrogliosis
    • Fasen K., Elger C.E., and Lie A.A. Distribution of alpha and beta integrin subunits in the adult rat hippocampus after pilocarpine-induced neuronal cell loss, axonal reorganization and reactive astrogliosis. Acta Neuropathol. (Berl.) 106 (2003) 319-322
    • (2003) Acta Neuropathol. (Berl.) , vol.106 , pp. 319-322
    • Fasen, K.1    Elger, C.E.2    Lie, A.A.3
  • 16
    • 0033627968 scopus 로고    scopus 로고
    • Necrosis of hippocampus and piriform lobe in 38 domestic cats with seizures: a retrospective study on clinical and pathologic findings
    • Fatzer R., Gandini G., Jaggy A., Doherr M., and Vandevelde M. Necrosis of hippocampus and piriform lobe in 38 domestic cats with seizures: a retrospective study on clinical and pathologic findings. J. Vet. Intern. Med. 14 (2000) 100-104
    • (2000) J. Vet. Intern. Med. , vol.14 , pp. 100-104
    • Fatzer, R.1    Gandini, G.2    Jaggy, A.3    Doherr, M.4    Vandevelde, M.5
  • 17
    • 0033811496 scopus 로고    scopus 로고
    • Seizure-induced neuronal necrosis: implications for programmed cell death mechanisms
    • Fujikawa D.G., Shinmei S.S., and Cai B. Seizure-induced neuronal necrosis: implications for programmed cell death mechanisms. Epilepsia 41 Suppl. 6 (2000) S9-S13
    • (2000) Epilepsia , vol.41 , Issue.SUPPL. 6
    • Fujikawa, D.G.1    Shinmei, S.S.2    Cai, B.3
  • 18
    • 3242760652 scopus 로고    scopus 로고
    • Integrins, synaptic plasticity and epileptogenesis
    • Gall C.M., and Lynch G. Integrins, synaptic plasticity and epileptogenesis. Adv. Exp. Med. Biol. 548 (2004) 12-33
    • (2004) Adv. Exp. Med. Biol. , vol.548 , pp. 12-33
    • Gall, C.M.1    Lynch, G.2
  • 19
    • 0035094532 scopus 로고    scopus 로고
    • Integrin signaling via the PI3-kinase-Akt pathway increases neuronal resistance to glutamate-induced apoptosis
    • Gary D.S., and Mattson M.P. Integrin signaling via the PI3-kinase-Akt pathway increases neuronal resistance to glutamate-induced apoptosis. J. Neurochem. 76 (2001) 1485-1496
    • (2001) J. Neurochem. , vol.76 , pp. 1485-1496
    • Gary, D.S.1    Mattson, M.P.2
  • 20
    • 0037315101 scopus 로고    scopus 로고
    • Essential role for integrin linked kinase in Akt-mediated integrin survival signaling in hippocampal neurons
    • Gary D.S., Milhavet O., Camandola S., and Mattson M.P. Essential role for integrin linked kinase in Akt-mediated integrin survival signaling in hippocampal neurons. J. Neurochem. 84 (2003) 878-890
    • (2003) J. Neurochem. , vol.84 , pp. 878-890
    • Gary, D.S.1    Milhavet, O.2    Camandola, S.3    Mattson, M.P.4
  • 21
    • 0033505281 scopus 로고    scopus 로고
    • Early appearance of activated matrix metalloproteinase-9 after focal cerebral ischemia in mice: a possible role in blood-brain barrier dysfunction
    • Gasche Y., Fujimura M., Morita-Fujimura Y., Copin J.C., Kawase M., Massengale J., and Chan P.H. Early appearance of activated matrix metalloproteinase-9 after focal cerebral ischemia in mice: a possible role in blood-brain barrier dysfunction. J. Cereb. Blood Flow Metab. 19 (1999) 1020-1028
    • (1999) J. Cereb. Blood Flow Metab. , vol.19 , pp. 1020-1028
    • Gasche, Y.1    Fujimura, M.2    Morita-Fujimura, Y.3    Copin, J.C.4    Kawase, M.5    Massengale, J.6    Chan, P.H.7
  • 22
    • 0033551899 scopus 로고    scopus 로고
    • Integrin signaling
    • Giancotti F.G., and Ruoslahti E. Integrin signaling. Science 285 (1999) 1028-1032
    • (1999) Science , vol.285 , pp. 1028-1032
    • Giancotti, F.G.1    Ruoslahti, E.2
  • 24
    • 21844450866 scopus 로고    scopus 로고
    • A highly specific inhibitor of matrix metalloproteinase-9 rescues laminin from proteolysis and neurons from apoptosis in transient focal cerebral ischemia
    • Gu Z., Cui J., Brown S., Fridman R., Mobashery S., Strongin A.Y., and Lipton S.A. A highly specific inhibitor of matrix metalloproteinase-9 rescues laminin from proteolysis and neurons from apoptosis in transient focal cerebral ischemia. J. Neurosci. 25 (2005) 6401-6408
    • (2005) J. Neurosci. , vol.25 , pp. 6401-6408
    • Gu, Z.1    Cui, J.2    Brown, S.3    Fridman, R.4    Mobashery, S.5    Strongin, A.Y.6    Lipton, S.A.7
  • 26
    • 33646382411 scopus 로고    scopus 로고
    • Minocycline inhibits caspase-dependent and -independent cell death pathways and is neuroprotective against hippocampal damage after treatment with kainic acid in mice
    • Heo K., Cho Y.J., Cho K.J., Kim H.W., Kim H.J., Shin H.Y., Lee B.I., and Kim G.W. Minocycline inhibits caspase-dependent and -independent cell death pathways and is neuroprotective against hippocampal damage after treatment with kainic acid in mice. Neurosci. Lett. 398 (2006) 195-200
    • (2006) Neurosci. Lett. , vol.398 , pp. 195-200
    • Heo, K.1    Cho, Y.J.2    Cho, K.J.3    Kim, H.W.4    Kim, H.J.5    Shin, H.Y.6    Lee, B.I.7    Kim, G.W.8
  • 27
    • 0037069271 scopus 로고    scopus 로고
    • Epilepsy after brain insult: targeting epileptogenesis
    • Herman S.T. Epilepsy after brain insult: targeting epileptogenesis. Neurology 59 (2002) S21-S26
    • (2002) Neurology , vol.59
    • Herman, S.T.1
  • 28
    • 0023902887 scopus 로고
    • The nature and timing of excitotoxic neuronal necrosis in the cerebral cortex, hippocampus and thalamus due to flurothyl-induced status epilepticus
    • Ingvar M., Morgan P.F., and Auer R.N. The nature and timing of excitotoxic neuronal necrosis in the cerebral cortex, hippocampus and thalamus due to flurothyl-induced status epilepticus. Acta Neuropathol. 75 (1988) 362-369
    • (1988) Acta Neuropathol. , vol.75 , pp. 362-369
    • Ingvar, M.1    Morgan, P.F.2    Auer, R.N.3
  • 30
    • 0141869839 scopus 로고    scopus 로고
    • Neurodegeneration in striatum induced by the mitochondrial toxin 3-nitropropionic acid: role of matrix metalloproteinase-9 in early blood-brain barrier disruption?
    • Kim G.W., Gasche Y., Grzeschik S., Copin J.C., Maier C.M., and Chan P.H. Neurodegeneration in striatum induced by the mitochondrial toxin 3-nitropropionic acid: role of matrix metalloproteinase-9 in early blood-brain barrier disruption?. J. Neurosci. 23 (2003) 8733-8742
    • (2003) J. Neurosci. , vol.23 , pp. 8733-8742
    • Kim, G.W.1    Gasche, Y.2    Grzeschik, S.3    Copin, J.C.4    Maier, C.M.5    Chan, P.H.6
  • 31
    • 3042730654 scopus 로고    scopus 로고
    • Induction of caspase-mediated cell death by matrix metalloproteinases in cerebral endothelial cells after hypoxia-reoxygenation
    • Lee S.R., and Lo E.H. Induction of caspase-mediated cell death by matrix metalloproteinases in cerebral endothelial cells after hypoxia-reoxygenation. J. Cereb. Blood Flow Metab. 24 (2004) 720-727
    • (2004) J. Cereb. Blood Flow Metab. , vol.24 , pp. 720-727
    • Lee, S.R.1    Lo, E.H.2
  • 32
    • 10344233669 scopus 로고    scopus 로고
    • Extracellular proteolytic pathophysiology in the neurovascular unit after stroke
    • Lee S.R., Wang X., Tsuji K., and Lo E.H. Extracellular proteolytic pathophysiology in the neurovascular unit after stroke. Neurol. Res. 26 (2004) 854-861
    • (2004) Neurol. Res. , vol.26 , pp. 854-861
    • Lee, S.R.1    Wang, X.2    Tsuji, K.3    Lo, E.H.4
  • 33
    • 33644663413 scopus 로고    scopus 로고
    • Metalloporphyrin-based superoxide dismutase mimic attenuates the nuclear translocation of apoptosis-inducing factor and the subsequent DNA fragmentation after permanent focal cerebral ischemia in mice
    • Lee B.I., Chan P.H., and Kim G.W. Metalloporphyrin-based superoxide dismutase mimic attenuates the nuclear translocation of apoptosis-inducing factor and the subsequent DNA fragmentation after permanent focal cerebral ischemia in mice. Stroke 36 (2005) 2712-2717
    • (2005) Stroke , vol.36 , pp. 2712-2717
    • Lee, B.I.1    Chan, P.H.2    Kim, G.W.3
  • 34
    • 22544487228 scopus 로고    scopus 로고
    • Early nuclear translocation of endonuclease G and subsequent DNA fragmentation after transient focal cerebral ischemia in mice
    • Lee B.I., Lee D.J., Cho K.J., and Kim G.W. Early nuclear translocation of endonuclease G and subsequent DNA fragmentation after transient focal cerebral ischemia in mice. Neurosci. Lett. 386 (2005) 23-27
    • (2005) Neurosci. Lett. , vol.386 , pp. 23-27
    • Lee, B.I.1    Lee, D.J.2    Cho, K.J.3    Kim, G.W.4
  • 36
    • 12244295145 scopus 로고    scopus 로고
    • Activation of metalloproteinases and their association with integrins: an auxiliary apoptotic pathway in human endothelial cells
    • Levkau B., Kenagy R.D., Karsan A., Weitkamp B., Clowes A.W., Ross R., and Raines E.W. Activation of metalloproteinases and their association with integrins: an auxiliary apoptotic pathway in human endothelial cells. Cell Death Differ. 9 (2002) 1360-1367
    • (2002) Cell Death Differ. , vol.9 , pp. 1360-1367
    • Levkau, B.1    Kenagy, R.D.2    Karsan, A.3    Weitkamp, B.4    Clowes, A.W.5    Ross, R.6    Raines, E.W.7
  • 37
    • 5144224127 scopus 로고    scopus 로고
    • Differential alterations in the expression and activity of matrix metalloproteinases 2 and 9 after transient cerebral ischemia in mice
    • Magnoni S., Baker A., George S.J., Duncan W.C., Kerr L.E., McCulloch J., and Horsburgh K. Differential alterations in the expression and activity of matrix metalloproteinases 2 and 9 after transient cerebral ischemia in mice. Neurobiol. Dis. 17 (2004) 188-197
    • (2004) Neurobiol. Dis. , vol.17 , pp. 188-197
    • Magnoni, S.1    Baker, A.2    George, S.J.3    Duncan, W.C.4    Kerr, L.E.5    McCulloch, J.6    Horsburgh, K.7
  • 38
    • 0033749276 scopus 로고    scopus 로고
    • Selective neuronal necrosis associated with status epilepticus: MR findings
    • Men S., Lee D.H., Barron J.R., Munoz D.G., et al. Selective neuronal necrosis associated with status epilepticus: MR findings. AJNR Am. J. Neuroradiol. 21 (2000) 1837-1840
    • (2000) AJNR Am. J. Neuroradiol. , vol.21 , pp. 1837-1840
    • Men, S.1    Lee, D.H.2    Barron, J.R.3    Munoz, D.G.4
  • 41
    • 0033215979 scopus 로고    scopus 로고
    • Matrix metalloproteinase-9/gelatinase B is required for process outgrowth by oligodendrocytes
    • Oh L.Y., Larsen P.H., Krekoski C.A., Edwards D.R., Donovan F., Werb Z., and Yong V.W. Matrix metalloproteinase-9/gelatinase B is required for process outgrowth by oligodendrocytes. J. Neurosci. 19 (1999) 8464-8475
    • (1999) J. Neurosci. , vol.19 , pp. 8464-8475
    • Oh, L.Y.1    Larsen, P.H.2    Krekoski, C.A.3    Edwards, D.R.4    Donovan, F.5    Werb, Z.6    Yong, V.W.7
  • 42
    • 33947331893 scopus 로고    scopus 로고
    • Selective vulnerability of hippocampal NAAGergic neurons in experimental temporal lobe epilepsy
    • Pacheco Otalora L.F., Moffett J.R., and Garrido-Sanabria E.R. Selective vulnerability of hippocampal NAAGergic neurons in experimental temporal lobe epilepsy. Brain Res. 1144 (2007) 219-230
    • (2007) Brain Res. , vol.1144 , pp. 219-230
    • Pacheco Otalora, L.F.1    Moffett, J.R.2    Garrido-Sanabria, E.R.3
  • 43
    • 0038719715 scopus 로고    scopus 로고
    • Specific beta1 integrin site selectively regulates Akt/protein kinase B signaling via local activation of protein phosphatase 2A
    • Pankov R., Cukierman E., Clark K., Matsumoto K., Hahn C., Poulin B., and Yamada K.M. Specific beta1 integrin site selectively regulates Akt/protein kinase B signaling via local activation of protein phosphatase 2A. J. Biol. Chem. 278 (2003) 18671-18681
    • (2003) J. Biol. Chem. , vol.278 , pp. 18671-18681
    • Pankov, R.1    Cukierman, E.2    Clark, K.3    Matsumoto, K.4    Hahn, C.5    Poulin, B.6    Yamada, K.M.7
  • 44
    • 0001490738 scopus 로고    scopus 로고
    • Is epilepsy a progressive disorder? Prospects for new therapeutic approaches in temporal-lobe epilepsy
    • Pitkanen A., and Sutula T.P. Is epilepsy a progressive disorder? Prospects for new therapeutic approaches in temporal-lobe epilepsy. Lancet Neurol. 1 (2002) 173-181
    • (2002) Lancet Neurol. , vol.1 , pp. 173-181
    • Pitkanen, A.1    Sutula, T.P.2
  • 45
    • 0015309163 scopus 로고
    • Modification of seizure activity by electrical stimulation. II. Motor seizure
    • Racine R.J. Modification of seizure activity by electrical stimulation. II. Motor seizure. Electroencephalogr. Clin. Neurophysiol. 32 (1972) 281-294
    • (1972) Electroencephalogr. Clin. Neurophysiol. , vol.32 , pp. 281-294
    • Racine, R.J.1
  • 46
    • 0344824684 scopus 로고    scopus 로고
    • Matrix metalloproteinase inhibition alters functional and structural correlates of deafferentation-induced sprouting in the dentate gyrus
    • Reeves T.M., Prins M.L., Zhu J., Povlishock J.T., and Phillips L.L. Matrix metalloproteinase inhibition alters functional and structural correlates of deafferentation-induced sprouting in the dentate gyrus. J. Neurosci. 23 (2003) 10182-10189
    • (2003) J. Neurosci. , vol.23 , pp. 10182-10189
    • Reeves, T.M.1    Prins, M.L.2    Zhu, J.3    Povlishock, J.T.4    Phillips, L.L.5
  • 47
    • 0036460593 scopus 로고    scopus 로고
    • Gelatinase B and TIMP-1 are regulated in a cell- and time-dependent manner in association with neuronal death and glial reactivity after global forebrain ischemia
    • Rivera S., Ogier C., Jourquin J., Timsit S., Szklarczyk A.W., Miller K., Gearing A.J., Kaczmarek L., and Khrestchatisky M. Gelatinase B and TIMP-1 are regulated in a cell- and time-dependent manner in association with neuronal death and glial reactivity after global forebrain ischemia. Eur. J. Neurosci. 15 (2002) 19-32
    • (2002) Eur. J. Neurosci. , vol.15 , pp. 19-32
    • Rivera, S.1    Ogier, C.2    Jourquin, J.3    Timsit, S.4    Szklarczyk, A.W.5    Miller, K.6    Gearing, A.J.7    Kaczmarek, L.8    Khrestchatisky, M.9
  • 49
    • 0042838034 scopus 로고    scopus 로고
    • Interaction between XIAP and Smac/DIABLO in the mouse brain after transient focal cerebral ischemia
    • Saito A., Hayashi T., Okuno S., Ferrand-Drake M., and Chan P.H. Interaction between XIAP and Smac/DIABLO in the mouse brain after transient focal cerebral ischemia. J. Cereb. Blood Flow Metab. 23 (2003) 1010-1019
    • (2003) J. Cereb. Blood Flow Metab. , vol.23 , pp. 1010-1019
    • Saito, A.1    Hayashi, T.2    Okuno, S.3    Ferrand-Drake, M.4    Chan, P.H.5
  • 50
    • 7644237799 scopus 로고    scopus 로고
    • Oxidative stress affects the integrin-linked kinase signaling pathway after transient focal cerebral ischemia
    • Saito A., Hayashi T., Okuno S., Nishi T., and Chan P.H. Oxidative stress affects the integrin-linked kinase signaling pathway after transient focal cerebral ischemia. Stroke 35 (2004) 2560-2565
    • (2004) Stroke , vol.35 , pp. 2560-2565
    • Saito, A.1    Hayashi, T.2    Okuno, S.3    Nishi, T.4    Chan, P.H.5
  • 51
    • 33947373996 scopus 로고    scopus 로고
    • Suppression of NF-kappaB activation by curcumin leads to inhibition of expression of cyclo-oxygenase-2 and matrix metalloproteinase-9 in human articular chondrocytes: implications for the treatment of osteoarthritis
    • Shakibaei M., John T., Schulze-Tanzil G., Lehmann I., and Mobasheri A. Suppression of NF-kappaB activation by curcumin leads to inhibition of expression of cyclo-oxygenase-2 and matrix metalloproteinase-9 in human articular chondrocytes: implications for the treatment of osteoarthritis. Biochem. Pharmacol. 73 (2007) 1434-1445
    • (2007) Biochem. Pharmacol. , vol.73 , pp. 1434-1445
    • Shakibaei, M.1    John, T.2    Schulze-Tanzil, G.3    Lehmann, I.4    Mobasheri, A.5
  • 52
    • 0036278510 scopus 로고    scopus 로고
    • Pilocarpine-induced status epilepticus results in mossy fiber sprouting and spontaneous seizures in C57BL/6 and CD-1 mice
    • Shibley H., and Smith B.N. Pilocarpine-induced status epilepticus results in mossy fiber sprouting and spontaneous seizures in C57BL/6 and CD-1 mice. Epilepsy Res. 49 (2002) 109-120
    • (2002) Epilepsy Res. , vol.49 , pp. 109-120
    • Shibley, H.1    Smith, B.N.2
  • 54
    • 0035188727 scopus 로고    scopus 로고
    • How matrix metalloproteinases regulate cell behavior
    • Sternlicht M.D., and Werb Z. How matrix metalloproteinases regulate cell behavior. Annu. Rev. Cell Dev. Biol. 17 (2001) 463-516
    • (2001) Annu. Rev. Cell Dev. Biol. , vol.17 , pp. 463-516
    • Sternlicht, M.D.1    Werb, Z.2
  • 55
    • 0036470147 scopus 로고    scopus 로고
    • Matrix metalloproteinase-9 undergoes expression and activation during dendritic remodeling in adult hippocampus
    • Szklarczyk A., Lapinska J., Rylski M., McKay R.D., and Kaczmarek L. Matrix metalloproteinase-9 undergoes expression and activation during dendritic remodeling in adult hippocampus. J. Neurosci. 22 (2002) 920-930
    • (2002) J. Neurosci. , vol.22 , pp. 920-930
    • Szklarczyk, A.1    Lapinska, J.2    Rylski, M.3    McKay, R.D.4    Kaczmarek, L.5
  • 57
    • 0027248518 scopus 로고
    • Identification of a regulatory region of integrin beta 1 subunit using activating and inhibiting antibodies
    • Takada Y., and Puzon W. Identification of a regulatory region of integrin beta 1 subunit using activating and inhibiting antibodies. J. Biol. Chem. 268 (1993) 17597-17601
    • (1993) J. Biol. Chem. , vol.268 , pp. 17597-17601
    • Takada, Y.1    Puzon, W.2
  • 58
    • 0029088484 scopus 로고
    • Excitotoxin-induced neuronal degeneration and seizure are mediated by tissue plasminogen activator
    • Tsirka S.E., Gualandris A., Amaral D.G., and Strickland S. Excitotoxin-induced neuronal degeneration and seizure are mediated by tissue plasminogen activator. Nature 377 (1995) 340-344
    • (1995) Nature , vol.377 , pp. 340-344
    • Tsirka, S.E.1    Gualandris, A.2    Amaral, D.G.3    Strickland, S.4
  • 59
    • 0024510191 scopus 로고
    • Review: cholinergic mechanisms and epileptogenesis. The seizures induced by pilocarpine: a novel experimental model of intractable epilepsy
    • Turski L., Ikonomidou C., Turski W.A., Bortolotto Z.A., and Cavalheiro E.A. Review: cholinergic mechanisms and epileptogenesis. The seizures induced by pilocarpine: a novel experimental model of intractable epilepsy. Synapse 3 (1989) 154-171
    • (1989) Synapse , vol.3 , pp. 154-171
    • Turski, L.1    Ikonomidou, C.2    Turski, W.A.3    Bortolotto, Z.A.4    Cavalheiro, E.A.5
  • 60
    • 0034667542 scopus 로고    scopus 로고
    • Neutrophil gelatinase B potentiates interleukin-8 tenfold by aminoterminal processing, whereas it degrades CTAP-III, PF-4, and GRO-alpha and leaves RANTES and MCP-2 intact
    • Van den Steen P.E., Proost P., Wuyts A., Van Damme J., and Opdenakker G. Neutrophil gelatinase B potentiates interleukin-8 tenfold by aminoterminal processing, whereas it degrades CTAP-III, PF-4, and GRO-alpha and leaves RANTES and MCP-2 intact. Blood 96 (2000) 2673-2681
    • (2000) Blood , vol.96 , pp. 2673-2681
    • Van den Steen, P.E.1    Proost, P.2    Wuyts, A.3    Van Damme, J.4    Opdenakker, G.5
  • 62
    • 14744289621 scopus 로고    scopus 로고
    • Expression time course and spatial distribution of activated caspase-3 after experimental status epilepticus: contribution of delayed neuronal cell death to seizure-induced neuronal injury
    • Weise J., et al. Expression time course and spatial distribution of activated caspase-3 after experimental status epilepticus: contribution of delayed neuronal cell death to seizure-induced neuronal injury. Neurobiol. Dis. 18 (2005) 582-590
    • (2005) Neurobiol. Dis. , vol.18 , pp. 582-590
    • Weise, J.1
  • 63
    • 0030715322 scopus 로고    scopus 로고
    • ECM and cell surface proteolysis: regulating cellular ecology
    • Werb Z. ECM and cell surface proteolysis: regulating cellular ecology. Cell 91 (1997) 439-442
    • (1997) Cell , vol.91 , pp. 439-442
    • Werb, Z.1
  • 65
    • 28644435880 scopus 로고    scopus 로고
    • Metalloproteinases: mediators of pathology and regeneration in the CNS
    • Yong V.W. Metalloproteinases: mediators of pathology and regeneration in the CNS. Nat. Rev., Neurosci. 6 (2005) 931-944
    • (2005) Nat. Rev., Neurosci. , vol.6 , pp. 931-944
    • Yong, V.W.1
  • 66
    • 0035405886 scopus 로고    scopus 로고
    • Metalloproteinases in biology and pathology of the nervous system
    • Yong V.W., Power C., Forsyth P., and Edwards D.R. Metalloproteinases in biology and pathology of the nervous system. Nat. Rev., Neurosci. 2 (2001) 502-511
    • (2001) Nat. Rev., Neurosci. , vol.2 , pp. 502-511
    • Yong, V.W.1    Power, C.2    Forsyth, P.3    Edwards, D.R.4
  • 67
    • 0032457993 scopus 로고    scopus 로고
    • Regional and differential expression of gelatinases in rat brain after systemic kainic acid or bicuculline administration
    • Zhang J.W., Deb S., and Gottschall P.E. Regional and differential expression of gelatinases in rat brain after systemic kainic acid or bicuculline administration. Eur. J. Neurosci. 10 (1998) 3358-3368
    • (1998) Eur. J. Neurosci. , vol.10 , pp. 3358-3368
    • Zhang, J.W.1    Deb, S.2    Gottschall, P.E.3
  • 68
    • 3142543638 scopus 로고    scopus 로고
    • Kainic acid-mediated upregulation of matrix metalloproteinase-9 promotes retinal degeneration
    • Zhang X., Cheng M., and Chintala S.K. Kainic acid-mediated upregulation of matrix metalloproteinase-9 promotes retinal degeneration. Invest. Ophthalmol. Vis. Sci. 45 (2004) 2374-2383
    • (2004) Invest. Ophthalmol. Vis. Sci. , vol.45 , pp. 2374-2383
    • Zhang, X.1    Cheng, M.2    Chintala, S.K.3


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