메뉴 건너뛰기




Volumn 79, Issue 3, 2004, Pages 137-144

Serine proteases regulating synaptic plasticity

Author keywords

Extracellular matrix; Learning and memory; Long term potentiation; Serine protease; Structural plasticity

Indexed keywords

ANKYRIN; BRAIN DERIVED NEUROTROPHIC FACTOR; LOW DENSITY LIPOPROTEIN RECEPTOR RELATED PROTEIN; NEUROPSIN; PROTHROMBIN; SCLEROPROTEIN; SERINE PROTEINASE; THROMBIN; TISSUE PLASMINOGEN ACTIVATOR; UROKINASE;

EID: 4544230337     PISSN: 14476959     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1447-073x.2004.00080.x     Document Type: Review
Times cited : (25)

References (80)
  • 1
    • 0036848631 scopus 로고    scopus 로고
    • Induction and experience-dependent consolidation of stable long-term potentiation lasting months in the hippocampus
    • Abraham WC, Logan B, Greenwood JM, Dragunow M (2002) Induction and experience-dependent consolidation of stable long-term potentiation lasting months in the hippocampus. J Neurosci 22, 9626-34.
    • (2002) J. Neurosci. , vol.22 , pp. 9626-9634
    • Abraham, W.C.1    Logan, B.2    Greenwood, J.M.3    Dragunow, M.4
  • 2
    • 0032192461 scopus 로고    scopus 로고
    • Tissue plasminogen activator contributes to the late phase of UP and to synaptic growth in the hippocampal mossy fiber pathway
    • Baranes D, Lederfein D, Huang YY, Chen M, Bailey CH, Kandel ER (1998) Tissue plasminogen activator contributes to the late phase of UP and to synaptic growth in the hippocampal mossy fiber pathway. Neuron 21, 813-25.
    • (1998) Neuron , vol.21 , pp. 813-825
    • Baranes, D.1    Lederfein, D.2    Huang, Y.Y.3    Chen, M.4    Bailey, C.H.5    Kandel, E.R.6
  • 3
    • 0022579766 scopus 로고
    • Long-term potentiation and kindling: Similar biochemical mechanisms?
    • Baudry M (1986) Long-term potentiation and kindling: Similar biochemical mechanisms?. Adv Neurol 44, 401-10.
    • (1986) Adv. Neurol. , vol.44 , pp. 401-410
    • Baudry, M.1
  • 4
    • 0027476024 scopus 로고
    • A synaptic model of memory: Long-term potentiation in the hippocampus
    • Bliss TV, Collingridge GL (1993) A synaptic model of memory: Long-term potentiation in the hippocampus. Nature 361, 31-9.
    • (1993) Nature , vol.361 , pp. 31-39
    • Bliss, T.V.1    Collingridge, G.L.2
  • 5
    • 0035479922 scopus 로고    scopus 로고
    • Immunoglobulin superfamily receptors: Cis interactions, intracellular adapters and alternative splicing regulate adhesion
    • Brummendorf T, Lemmon V (2001) Immunoglobulin superfamily receptors: Cis interactions, intracellular adapters and alternative splicing regulate adhesion. Curr Opin Cell Biol 13, 611-18.
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 611-618
    • Brummendorf, T.1    Lemmon, V.2
  • 6
    • 0034107402 scopus 로고    scopus 로고
    • Tissue plasminogen activator controls multiple forms of synaptic plasticity and memory
    • Calabresi P, Napolitano M, Centonze D et al. (2000) Tissue plasminogen activator controls multiple forms of synaptic plasticity and memory. Eur J Neurosci 12, 1002-12.
    • (2000) Eur. J. Neurosci. , vol.12 , pp. 1002-1012
    • Calabresi, P.1    Napolitano, M.2    Centonze, D.3
  • 7
    • 10744225521 scopus 로고    scopus 로고
    • The novel serine protease tumor-associated differentially expressed gene-14 (KLK8/Neuropsin/Ovasin) is highly overexpressed in cervical cancer
    • Cane S, Bignotti E, Bellone S et al. (2004) The novel serine protease tumor-associated differentially expressed gene-14 (KLK8/Neuropsin/Ovasin) is highly overexpressed in cervical cancer. Am J Obstet Gynecol 190, 60-6.
    • (2004) Am. J. Obstet. Gynecol. , vol.190 , pp. 60-66
    • Cane, S.1    Bignotti, E.2    Bellone, S.3
  • 8
    • 0025911764 scopus 로고
    • Plasmin cleavage of vitronectin. Identification of the site and consequent attenuation in binding plasminogen activator inhibitor-1
    • Chain D, Kreizman T, Shapira H, Shaltiel S (1991) Plasmin cleavage of vitronectin. Identification of the site and consequent attenuation in binding plasminogen activator inhibitor-1. FEBS Lett 285, 251-6.
    • (1991) FEBS Lett. , vol.285 , pp. 251-256
    • Chain, D.1    Kreizman, T.2    Shapira, H.3    Shaltiel, S.4
  • 9
    • 0031470554 scopus 로고    scopus 로고
    • Neuronal death in the hippocampus is promoted by plasmin-catalyzed degradation of laminin
    • Chen ZL, Strickland S (1997) Neuronal death in the hippocampus is promoted by plasmin-catalyzed degradation of laminin. Cell 91, 917-25.
    • (1997) Cell , vol.91 , pp. 917-925
    • Chen, Z.L.1    Strickland, S.2
  • 10
    • 4544221866 scopus 로고
    • A novel serine protease (neuropsin) specific to the limbic brain: Prominent expression in the hippocampus that can be depressed by direct electric stimulation
    • (Abstract)
    • Chen ZL, Momota Y, Shiosaka S (1994) A novel serine protease (neuropsin) specific to the limbic brain: Prominent expression in the hippocampus that can be depressed by direct electric stimulation. Neurosci Res 19 (Suppl.), S163 (Abstract).
    • (1994) Neurosci. Res. , vol.19 , Issue.SUPPL.
    • Chen, Z.L.1    Momota, Y.2    Shiosaka, S.3
  • 11
    • 0029050958 scopus 로고
    • Expression and activity-dependent changes of a novel limbic-serine protease gene in the hippocampus
    • Chen ZL, Yoshida S, Kato K et al. (1995) Expression and activity-dependent changes of a novel limbic-serine protease gene in the hippocampus. J Neurosci 15, 5088-97.
    • (1995) J. Neurosci. , vol.15 , pp. 5088-5097
    • Chen, Z.L.1    Yoshida, S.2    Kato, K.3
  • 12
    • 0037769931 scopus 로고    scopus 로고
    • The hippocampal laminin matrix is dynamic and critical for neuronal survival
    • Chen ZL, Indyk JA, Strickland S (2003) The hippocampal laminin matrix is dynamic and critical for neuronal survival. Mol Biol Cell 14, 2665-76.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 2665-2676
    • Chen, Z.L.1    Indyk, J.A.2    Strickland, S.3
  • 13
    • 0035115850 scopus 로고    scopus 로고
    • The expanded human kallikrein (KLK) gene family: Genomic organization, tissue-specific expression and potential functions
    • Clements J, Hooper J, Dong Y, Harvey T (2001) The expanded human kallikrein (KLK) gene family: Genomic organization, tissue-specific expression and potential functions. Biol Chem 382, 5-14.
    • (2001) Biol. Chem. , vol.382 , pp. 5-14
    • Clements, J.1    Hooper, J.2    Dong, Y.3    Harvey, T.4
  • 15
    • 0035885098 scopus 로고    scopus 로고
    • Loss of hippocampal serine protease BSP1/neuropsin predisposes to global seizure activity
    • Davies B, Kearns IR, Ure J, Davies CH, Lathe R (2001) Loss of hippocampal serine protease BSP1/neuropsin predisposes to global seizure activity. J Neurosci 21, 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
  • 16
    • 0033760167 scopus 로고    scopus 로고
    • New nomenclature for the human tissue kallikrein gene family
    • Diamandis EP, Yousef GM, Clements J et al. (2000) New nomenclature for the human tissue kallikrein gene family. Clin Chem 46, 1855-8.
    • (2000) Clin. Chem. , vol.46 , pp. 1855-1858
    • Diamandis, E.P.1    Yousef, G.M.2    Clements, J.3
  • 17
    • 0033529082 scopus 로고    scopus 로고
    • Dendritic spine changes associated with hippocampal long-term synaptic plasticity
    • Engert F, Bonhoeffer T (1999) Dendritic spine changes associated with hippocampal long-term synaptic plasticity. Nature 399, 66-70.
    • (1999) Nature , vol.399 , pp. 66-70
    • Engert, F.1    Bonhoeffer, T.2
  • 18
    • 0028049194 scopus 로고
    • Urokinase-type plasminogen activator and its receptor: New targets for anti-metastatic therapy?
    • Fazioli F, Blasi F (1994) Urokinase-type plasminogen activator and its receptor: New targets for anti-metastatic therapy? Trends Pharmacol Sci 15, 25-9.
    • (1994) Trends Pharmacol. Sci. , vol.15 , pp. 25-29
    • Fazioli, F.1    Blasi, F.2
  • 19
    • 0032906124 scopus 로고    scopus 로고
    • BDNF stimulates expression, activity and release of tissue-type plasminogen activator in mouse cortical neurons
    • Fiumelli H, Jabaudon D, Magistretti PJ, Martin JL (1999) BDNF stimulates expression, activity and release of tissue-type plasminogen activator in mouse cortical neurons. Eur J Neurosci 11, 1639-46.
    • (1999) Eur. J. Neurosci. , vol.11 , pp. 1639-1646
    • Fiumelli, H.1    Jabaudon, D.2    Magistretti, P.J.3    Martin, J.L.4
  • 20
    • 0029924091 scopus 로고    scopus 로고
    • A different form of long-lasting potentiation revealed in tissue plasminogen activator mutant mice
    • Frey U, Muller M, Kuhl D (1996) A different form of long-lasting potentiation revealed in tissue plasminogen activator mutant mice. J Neurosci 15, 2057-63.
    • (1996) J. Neurosci. , vol.15 , pp. 2057-2063
    • Frey, U.1    Muller, M.2    Kuhl, D.3
  • 21
    • 0038662761 scopus 로고    scopus 로고
    • Hippocampal LTP is accompanied by enhanced F-actin content within the dendritic spine that is essential for late LTP maintenance in vivo
    • Fukazawa Y, Saitoh Y, Ozawa F, Ohta Y, Mizuno K, Inokuchi K (2003) Hippocampal LTP is accompanied by enhanced F-actin content within the dendritic spine that is essential for late LTP maintenance in vivo. Neuron 38, 447-60.
    • (2003) Neuron , vol.38 , pp. 447-460
    • Fukazawa, Y.1    Saitoh, Y.2    Ozawa, F.3    Ohta, Y.4    Mizuno, K.5    Inokuchi, K.6
  • 22
    • 0034284153 scopus 로고    scopus 로고
    • Serine proteases and brain damage: Is there a link?
    • Gingrich MB, Traynelis SF (2000) Serine proteases and brain damage: Is there a link?. Trends Neurosci 23, 399-407.
    • (2000) Trends Neurosci. , vol.23 , pp. 399-407
    • Gingrich, M.B.1    Traynelis, S.F.2
  • 23
  • 24
    • 0034634470 scopus 로고    scopus 로고
    • Spatial regulation and activity modulation of plasmin by high affinity binding to the G domain of the alpha 3 subunit of laminin-5
    • Goldfinger LE, Jiang L, Hopkinson SB, Stack MS, Jones JC (2000) Spatial regulation and activity modulation of plasmin by high affinity binding to the G domain of the alpha 3 subunit of laminin-5. J Biol Chem 275, 34 887-93.
    • (2000) J. Biol. Chem. , vol.275 , Issue.34 , pp. 887-893
    • Goldfinger, L.E.1    Jiang, L.2    Hopkinson, S.B.3    Stack, M.S.4    Jones, J.C.5
  • 26
    • 0035066198 scopus 로고    scopus 로고
    • Abnormalities of synapses and neurons in the hippocampus of neuropsin-deficient mice
    • Hirata A, Yoshida S, Inoue N et al. (2001) Abnormalities of synapses and neurons in the hippocampus of neuropsin-deficient mice. Mol Cell Neurosci 17, 600-10.
    • (2001) Mol. Cell Neurosci. , vol.17 , pp. 600-610
    • Hirata, A.1    Yoshida, S.2    Inoue, N.3
  • 27
    • 0029080517 scopus 로고
    • Repeated confocal imaging of individual dendritic spines in the living hippocampal slice: Evidence for changes in length and orientation associated with chemically induced LTP
    • Hosokawa T, Rusakov DA, Bliss TV, Fine A (1995) Repeated confocal imaging of individual dendritic spines in the living hippocampal slice: Evidence for changes in length and orientation associated with chemically induced LTP. J Neurosci 15, 5560-73.
    • (1995) J. Neurosci. , vol.15 , pp. 5560-5573
    • Hosokawa, T.1    Rusakov, D.A.2    Bliss, T.V.3    Fine, A.4
  • 28
    • 9444240943 scopus 로고    scopus 로고
    • Mice lacking the gene encoding tissue-type plasminogen activator show a selective interference with late-phase long-term potentiation in both Schaffer collateral and mossy fiber pathways
    • Huang YY, Bach ME, Lipp HP et al. (1996) Mice lacking the gene encoding tissue-type plasminogen activator show a selective interference with late-phase long-term potentiation in both Schaffer collateral and mossy fiber pathways. Proc Natl Acad Sci USA 93, 8699-704.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 8699-8704
    • Huang, Y.Y.1    Bach, M.E.2    Lipp, H.P.3
  • 29
    • 0033586457 scopus 로고    scopus 로고
    • Expression of a serine protease (motopsin PRSS12) mRNA in the mouse brain: In situ hybridization histochemical study
    • Iijima N, Tanaka M, Mitsui S, Yamamura Y, Yamaguchi N, Ibata Y (1999) Expression of a serine protease (motopsin PRSS12) mRNA in the mouse brain: In situ hybridization histochemical study. Brain Res Mol Brain Res 66, 141-9.
    • (1999) Brain Res. Mol. Brain Res. , vol.66 , pp. 141-149
    • Iijima, N.1    Tanaka, M.2    Mitsui, S.3    Yamamura, Y.4    Yamaguchi, N.5    Ibata, Y.6
  • 30
    • 0008297599 scopus 로고    scopus 로고
    • Neuropsin regulates an early phase of Schaffer-collateral long-term potentiation in the murine hippocampus
    • Komai S, Matsuyama T, Matsumoto K et al. (2000) Neuropsin regulates an early phase of Schaffer-collateral long-term potentiation in the murine hippocampus. Eur J Neurosci 12, 1479-86.
    • (2000) Eur. J. Neurosci. , vol.12 , pp. 1479-1486
    • Komai, S.1    Matsuyama, T.2    Matsumoto, K.3
  • 31
    • 0035815656 scopus 로고    scopus 로고
    • The neural cell recognition molecule neurofascin interacts with syntenin-1 but not with syntenin-2, both of which reveal self-associating activity
    • Koroll M, Rathjen FG, Volkmer H (2001) The neural cell recognition molecule neurofascin interacts with syntenin-1 but not with syntenin-2, both of which reveal self-associating activity. J Biol Chem 276, 10 646-54.
    • (2001) J. Biol. Chem. , vol.276 , Issue.10 , pp. 646-654
    • Koroll, M.1    Rathjen, F.G.2    Volkmer, H.3
  • 32
    • 0019860445 scopus 로고
    • Plasminogen activator release at the neuronal growth cone
    • Krystosek A, Seeds NW (1981) Plasminogen activator release at the neuronal growth cone. Science 213, 1532-4.
    • (1981) Science , vol.213 , pp. 1532-1534
    • Krystosek, A.1    Seeds, N.W.2
  • 33
    • 0347915731 scopus 로고    scopus 로고
    • Structural plasticity and memory
    • Lamprecht R, LeDoux J (2004) Structural plasticity and memory. Nat Rev 5, 45-54.
    • (2004) Nat. Rev. , vol.5 , pp. 45-54
    • Lamprecht, R.1    LeDoux, J.2
  • 34
    • 0027379057 scopus 로고
    • Molecular interactions between tissue-type plasminogen activator and plasminogen
    • (Lorand L, Mann KG, eds). Academic Press, San Diego
    • Lunen HR, Collen D (1993) Molecular interactions between tissue-type plasminogen activator and plasminogen. In: Methods in Enzymology, Vol. 223 (Lorand L, Mann KG, eds). Academic Press, San Diego, 197-206.
    • (1993) Methods in Enzymology , vol.223 , pp. 197-206
    • Lunen, H.R.1    Collen, D.2
  • 35
    • 0029745079 scopus 로고    scopus 로고
    • Reduction of hippocampal long-term potentiation in transgenic mice ectopically expressing the neural cell adhesion molecule L1 in astrocytes
    • Lüthi A, Mohajeri H, Schachner M, Laurent JP (1996) Reduction of hippocampal long-term potentiation in transgenic mice ectopically expressing the neural cell adhesion molecule L1 in astrocytes. J Neurosci Res 46, 1-6.
    • (1996) J. Neurosci. Res. , vol.46 , pp. 1-6
    • Lüthi, A.1    Mohajeri, H.2    Schachner, M.3    Laurent, J.P.4
  • 36
    • 0033151831 scopus 로고    scopus 로고
    • Enhanced hippocampal long-term potentiation and learning by increased neuronal expression of tissue-type plasminogen activator in transgenic mice
    • Madani R, Hulo S, Toni N et al. (1999) Enhanced hippocampal long-term potentiation and learning by increased neuronal expression of tissue-type plasminogen activator in transgenic mice. EMBO J 18, 3007-12.
    • (1999) EMBO J. , vol.18 , pp. 3007-3012
    • Madani, R.1    Hulo, S.2    Toni, N.3
  • 37
    • 0037833494 scopus 로고    scopus 로고
    • Emotions are building up in the field of extracellular proteolysis
    • Madani R, Nef S, Vassalli JD (2003) Emotions are building up in the field of extracellular proteolysis. Trends Mol Med 9, 183-5.
    • (2003) Trends Mol. Med. , vol.9 , pp. 183-185
    • Madani, R.1    Nef, S.2    Vassalli, J.D.3
  • 38
    • 0033578855 scopus 로고    scopus 로고
    • Long-term potentiation: A decade of progress?
    • Malenka RC, Nicoll RA (1999) Long-term potentiation: A decade of progress? Science 285, 1870-4.
    • (1999) Science , vol.285 , pp. 1870-1874
    • Malenka, R.C.1    Nicoll, R.A.2
  • 39
    • 0033583022 scopus 로고    scopus 로고
    • Rapid dendritic morphogenesis in CA1 hippocampal dendrites induced by synaptic activity
    • Maletic-Savatic M, Malinow R, Svoboda K (1999) Rapid dendritic morphogenesis in CA1 hippocampal dendrites induced by synaptic activity. Science 283, 1923-7.
    • (1999) Science , vol.283 , pp. 1923-1927
    • Maletic-Savatic, M.1    Malinow, R.2    Svoboda, K.3
  • 41
    • 0037391807 scopus 로고    scopus 로고
    • Tissue plasminogen activator and NMDA receptor cleavage
    • Matys T, Strickland S (2003) Tissue plasminogen activator and NMDA receptor cleavage. Nat Med 9, 371-3.
    • (2003) Nat. Med. , vol.9 , pp. 371-373
    • Matys, T.1    Strickland, S.2
  • 42
    • 0028325747 scopus 로고
    • Overexpression of urokinase-type plasminogen activator in transgenic mice is correlated with impaired learning
    • Meiri N, Masos T, Rosenblum K, Miskin R, Dudai Y (1994) Overexpression of urokinase-type plasminogen activator in transgenic mice is correlated with impaired learning. Proc Natl Acad Sci USA 91, 3196-200.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 3196-3200
    • Meiri, N.1    Masos, T.2    Rosenblum, K.3    Miskin, R.4    Dudai, Y.5
  • 43
    • 0033559559 scopus 로고    scopus 로고
    • A novel form of human neuropsin, a brain-related serine protease, is generated by alternative splicing and is expressed preferentially in human adult brain
    • Mitsui S, Tsuruoka N, Yamashiro K, Nakazato H, Yamaguchi N (1999) A novel form of human neuropsin, a brain-related serine protease, is generated by alternative splicing and is expressed preferentially in human adult brain. Eur J Biochem 260, 627-34.
    • (1999) Eur. J. Biochem. , vol.260 , pp. 627-634
    • Mitsui, S.1    Tsuruoka, N.2    Yamashiro, K.3    Nakazato, H.4    Yamaguchi, N.5
  • 44
    • 18744371004 scopus 로고    scopus 로고
    • Truncating neurotrypsin mutation in autosomal recessive nonsyndromic mental retardation
    • Molinari F, Rio M, Meskenaite V et al. (2002) Truncating neurotrypsin mutation in autosomal recessive nonsyndromic mental retardation. Science 298, 1779-81.
    • (2002) Science , vol.298 , pp. 1779-1781
    • Molinari, F.1    Rio, M.2    Meskenaite, V.3
  • 45
    • 0141925717 scopus 로고    scopus 로고
    • Extracellular proteases and their inhibitors in genetic diseases of the central nervous system
    • (special no. 2)
    • Molinari F, Meskanaite V, Munnich A, Sonderegger P, Colleaux L (2003) Extracellular proteases and their inhibitors in genetic diseases of the central nervous system. Hum Mol Genet 12 (special no. 2), R195-200.
    • (2003) Hum. Mol. Genet. , vol.12
    • Molinari, F.1    Meskanaite, V.2    Munnich, A.3    Sonderegger, P.4    Colleaux, L.5
  • 46
    • 0031842366 scopus 로고    scopus 로고
    • Blockade of neuropsin, a serine protease, ameliorates kindling epilepsy
    • Momota Y, Yoshida S, Ito J et al. (1998) Blockade of neuropsin, a serine protease, ameliorates kindling epilepsy. Eur J Neurosci 10, 760-4.
    • (1998) Eur. J. Neurosci. , vol.10 , pp. 760-764
    • Momota, Y.1    Yoshida, S.2    Ito, J.3
  • 47
    • 0024373014 scopus 로고
    • Induction of morphological differentiation of human neuroblastoma cells is accompanied by induction of tissue-type plasminogen activator
    • Neuman T, Stephens RW, Salonen EM, Timmusk T, Vaheri A (1989) Induction of morphological differentiation of human neuroblastoma cells is accompanied by induction of tissue-type plasminogen activator. J Neurosci Res 23, 274-81.
    • (1989) J. Neurosci. Res. , vol.23 , pp. 274-281
    • Neuman, T.1    Stephens, R.W.2    Salonen, E.M.3    Timmusk, T.4    Vaheri, A.5
  • 48
    • 0034746189 scopus 로고    scopus 로고
    • The proteolytic activity of tissue-plasminogen activator enhances NMDA receptor-mediated signaling
    • Nicole O, Docagne F, Ali C et al. (2001) The proteolytic activity of tissue-plasminogen activator enhances NMDA receptor-mediated signaling. Nat Med 7, 59-64.
    • (2001) Nat. Med. , vol.7 , pp. 59-64
    • Nicole, O.1    Docagne, F.2    Ali, C.3
  • 49
    • 0037177876 scopus 로고    scopus 로고
    • Role of loop structures of neuropsin in the activity of serine protease and regulated secretion
    • Oka T, Hakoshima T, Itakura M et al. (2002) Role of loop structures of neuropsin in the activity of serine protease and regulated secretion. J Biol Chem 277, 14 724-30.
    • (2002) J. Biol. Chem. , vol.277 , Issue.14 , pp. 724-730
    • Oka, T.1    Hakoshima, T.2    Itakura, M.3
  • 50
    • 0030598059 scopus 로고    scopus 로고
    • Kindling induces neuropsin mRNA in the mouse brain
    • Okabe A, Momota Y, Yoshida S et al. (1996) Kindling induces neuropsin mRNA in the mouse brain. Brain Res 728, 116-20.
    • (1996) Brain Res. , vol.728 , pp. 116-120
    • Okabe, A.1    Momota, Y.2    Yoshida, S.3
  • 51
    • 0027980974 scopus 로고
    • Low density lipoprotein receptor-related protein is necessary for the internalization of both tissue-type plasminogen activator-inhibitor complexes and free tissue-type plasminogen activator
    • Orth K, Willnow T, Herz J, Gething MJ, Sambrook J (1994) Low density lipoprotein receptor-related protein is necessary for the internalization of both tissue-type plasminogen activator-inhibitor complexes and free tissue-type plasminogen activator. J Biol Chem 269, 21 117-22.
    • (1994) J. Biol. Chem. , vol.269 , Issue.21 , pp. 117-122
    • Orth, K.1    Willnow, T.2    Herz, J.3    Gething, M.J.4    Sambrook, J.5
  • 52
    • 0037056011 scopus 로고    scopus 로고
    • Rapid, specific and active site-catalyzed effect of tissue-plasminogen activator on hippocampus-dependent learning in mice
    • Pawlak R, Nagai N, Urano T et al. (2002) Rapid, specific and active site-catalyzed effect of tissue-plasminogen activator on hippocampus-dependent learning in mice. Neuroscience 113, 995-1001.
    • (2002) Neuroscience , vol.113 , pp. 995-1001
    • Pawlak, R.1    Nagai, N.2    Urano, T.3
  • 53
    • 0022102135 scopus 로고
    • Release of plasminogen activator and a calcium-dependent metalloprotease from cultured sympathetic and sensory neurons
    • Pittman RN (1985) Release of plasminogen activator and a calcium-dependent metalloprotease from cultured sympathetic and sensory neurons. Dev Biol 110, 91-101.
    • (1985) Dev. Biol. , vol.110 , pp. 91-101
    • Pittman, R.N.1
  • 54
    • 0024854138 scopus 로고
    • Neuronal plasminogen activators: Cell surface binding sites and involvement in neurite outgrowth
    • Pittman RN, Ivins JK, Buettner HM (1989) Neuronal plasminogen activators: Cell surface binding sites and involvement in neurite outgrowth. J Neurosci 9, 4269-86.
    • (1989) J. Neurosci. , vol.9 , pp. 4269-4286
    • Pittman, R.N.1    Ivins, J.K.2    Buettner, H.M.3
  • 55
    • 0033605650 scopus 로고    scopus 로고
    • Plasmin converts factor X from coagulation zymogen to fibrinolysis cofactor
    • Pryzdial EL, Lavigne N, Dupuis N, Kessler GE (1999) Plasmin converts factor X from coagulation zymogen to fibrinolysis cofactor. J Biol Chem 274, 8500-5.
    • (1999) J. Biol. Chem. , vol.274 , pp. 8500-8505
    • Pryzdial, E.L.1    Lavigne, N.2    Dupuis, N.3    Kessler, G.E.4
  • 56
    • 0027535364 scopus 로고
    • Tissue-plasminogen activator is induced as an immediate-early gene during seizure, kindling and long-term potentiation
    • Qian Z, Gilbert ME, Colicos MA, Kandel ER, Kuhl D (1993) Tissue-plasminogen activator is induced as an immediate-early gene during seizure, kindling and long-term potentiation. Nature 361, 453-7.
    • (1993) Nature , vol.361 , pp. 453-457
    • Qian, Z.1    Gilbert, M.E.2    Colicos, M.A.3    Kandel, E.R.4    Kuhl, D.5
  • 57
    • 0037016683 scopus 로고    scopus 로고
    • Reelin is a serine protease of the extracellular matrix
    • Quattrocchi CC, Wannenes F, Persico AM et al. (2002) Reelin is a serine protease of the extracellular matrix. J Biol Chem 277, 303-9.
    • (2002) J. Biol. Chem. , vol.277 , pp. 303-309
    • Quattrocchi, C.C.1    Wannenes, F.2    Persico, A.M.3
  • 58
    • 0025972053 scopus 로고
    • Substrate specificity of tissue-type and urokinase-type plasminogen activators
    • Rijken DC, Groeneveld E (1991) Substrate specificity of tissue-type and urokinase-type plasminogen activators. Biochem Biophys Res Commun 174, 432-8.
    • (1991) Biochem. Biophys. Res. Commun. , vol.174 , pp. 432-438
    • Rijken, D.C.1    Groeneveld, E.2
  • 59
    • 0037088905 scopus 로고    scopus 로고
    • Localization and regulation of the tissue plasminogen activator-plasmin system in the hippocampus
    • Salles FJ, Strickland S (2002) Localization and regulation of the tissue plasminogen activator-plasmin system in the hippocampus. J Neurosci 22, 2125-34.
    • (2002) J. Neurosci. , vol.22 , pp. 2125-2134
    • Salles, F.J.1    Strickland, S.2
  • 60
    • 0029556177 scopus 로고
    • Tissue plasminogen activator induction in Purkinje neurons after cerebellar motor learning
    • Seeds NW, Williams BL, Bickford PC (1995) Tissue plasminogen activator induction in Purkinje neurons after cerebellar motor learning. Science 270, 1992-4.
    • (1995) Science , vol.270 , pp. 1992-1994
    • Seeds, N.W.1    Williams, B.L.2    Bickford, P.C.3
  • 61
    • 0032079713 scopus 로고    scopus 로고
    • Characterization of recombinant and brain neuropsin, a plasticity-related serine protease
    • Shimizu C, Yoshida S, Shibata M et al. (1998) Characterization of recombinant and brain neuropsin, a plasticity-related serine protease. J Biol Chem 273, 11 189-96.
    • (1998) J. Biol. Chem. , vol.273 , Issue.11 , pp. 189-196
    • Shimizu, C.1    Yoshida, S.2    Shibata, M.3
  • 62
    • 0034213582 scopus 로고    scopus 로고
    • Synaptic microenvironments: Structural plasticity, adhesion molecules, proteases and their inhibitors
    • Shiosaka S, Yoshida S (2000) Synaptic microenvironments: Structural plasticity, adhesion molecules, proteases and their inhibitors. Neurosci Res 37, 85-9.
    • (2000) Neurosci. Res. , vol.37 , pp. 85-89
    • Shiosaka, S.1    Yoshida, S.2
  • 63
    • 1642402192 scopus 로고    scopus 로고
    • Prothrombin overexpressed in post-natal neurones requires blood factors for activation in the mouse brain
    • Sinnreich M, Meins M, Niclou SP, Suidan HS, Monard D (2004) Prothrombin overexpressed in post-natal neurones requires blood factors for activation in the mouse brain. J Neurochem 88, 1380-8.
    • (2004) J. Neurochem. , vol.88 , pp. 1380-1388
    • Sinnreich, M.1    Meins, M.2    Niclou, S.P.3    Suidan, H.S.4    Monard, D.5
  • 64
    • 0023948543 scopus 로고
    • Ankyrin and spectrin associate with voltage-dependent sodium channels in brain
    • Srinivasan Y, Elmer L, Davis J, Bennett V, Angelides K (1988) Ankyrin and spectrin associate with voltage-dependent sodium channels in brain. Nature 333, 177-80.
    • (1988) Nature , vol.333 , pp. 177-180
    • Srinivasan, Y.1    Elmer, L.2    Davis, J.3    Bennett, V.4    Angelides, K.5
  • 65
    • 0032980898 scopus 로고    scopus 로고
    • cDNA cloning and expression of a novel serine protease in the mouse brain
    • Suemoto T, Taniguchi M, Shiosaka S, Yoshida S (1999) cDNA cloning and expression of a novel serine protease in the mouse brain. Mol Brain Res 70, 273-81.
    • (1999) Mol. Brain Res. , vol.70 , pp. 273-281
    • Suemoto, T.1    Taniguchi, M.2    Shiosaka, S.3    Yoshida, S.4
  • 67
    • 0033604506 scopus 로고    scopus 로고
    • LTP promotes formation of multiple spine synapses between a single axon terminal and a dendrite
    • Toni N, Buchs PA, Nikonenko I, Povilaitite P, Bron CR, Muller D (1999) LTP promotes formation of multiple spine synapses between a single axon terminal and a dendrite. Nature 402, 421-5.
    • (1999) Nature , vol.402 , pp. 421-425
    • Toni, N.1    Buchs, P.A.2    Nikonenko, I.3    Povilaitite, P.4    Bron, C.R.5    Muller, D.6
  • 69
    • 0029088484 scopus 로고
    • Excitotoxin-induced neuronal degeneration and seizure are mediated by tissue plasminogen activator
    • Tsirka SE, Gualandris A, Amaral DG, Strickland S (1995) Excitotoxin-induced neuronal degeneration and seizure are mediated by tissue plasminogen activator. Nature 377, 340-4.
    • (1995) Nature , vol.377 , pp. 340-344
    • Tsirka, S.E.1    Gualandris, A.2    Amaral, D.G.3    Strickland, S.4
  • 70
    • 0033198458 scopus 로고    scopus 로고
    • Cloning of tumor-associated differentially expressed gene-14, a novel serine protease overexpressed by ovarian carcinoma
    • Underwood LJ, Tanimoto H, Wang Y, Shigemasa K, Parmley TH, O'Brien TJ (1999) Cloning of tumor-associated differentially expressed gene-14, a novel serine protease overexpressed by ovarian carcinoma. Cancer Res 59, 4435-9.
    • (1999) Cancer Res. , vol.59 , pp. 4435-4439
    • Underwood, L.J.1    Tanimoto, H.2    Wang, Y.3    Shigemasa, K.4    Parmley, T.H.5    O'Brien, T.J.6
  • 71
    • 0029151019 scopus 로고
    • Secretion of plasminogen activator and lysosomal enzymes from mouse skeletal muscle: Effect of denervation
    • von Steyern F, Josefsson JO (1995) Secretion of plasminogen activator and lysosomal enzymes from mouse skeletal muscle: Effect of denervation. J Cell Physiol 164, 555-61.
    • (1995) J. Cell Physiol. , vol.164 , pp. 555-561
    • von Steyern, F.1    Josefsson, J.O.2
  • 72
    • 0026035523 scopus 로고
    • Molecular cloning of a functional thrombin receptor reveals a novel proteolytic mechanism of receptor activation
    • Vu TK, Hung DT, Wheaton VI, Coughlin SR (1991) Molecular cloning of a functional thrombin receptor reveals a novel proteolytic mechanism of receptor activation. Cell 64, 1057-68.
    • (1991) Cell , vol.64 , pp. 1057-1068
    • Vu, T.K.1    Hung, D.T.2    Wheaton, V.I.3    Coughlin, S.R.4
  • 73
    • 0034689030 scopus 로고    scopus 로고
    • The tissue plasminogen activator (tPA)/plasmin extracellular proteolytic system regulates seizure-induced hippocampal mossy fiber outgrowth through a proteoglycan substrate
    • Wu YP, Siao CJ, Lu W et al. (2000) The tissue plasminogen activator (tPA)/plasmin extracellular proteolytic system regulates seizure-induced hippocampal mossy fiber outgrowth through a proteoglycan substrate. J Cell Biol 148, 1295-304.
    • (2000) J. Cell Biol. , vol.148 , pp. 1295-1304
    • Wu, Y.P.1    Siao, C.J.2    Lu, W.3
  • 74
    • 0031581061 scopus 로고    scopus 로고
    • Molecular cloning of a novel brain-specific serine protease with a kringle-like structure and three scavenger receptor cysteine-rich motifs
    • Yamamura Y, Yamashiro K, Tsuruolka N, Nakazato H, Tsujimura A, Yamaguchi IN (1997) Molecular cloning of a novel brain-specific serine protease with a kringle-like structure and three scavenger receptor cysteine-rich motifs. Biochem Biophys Res Commun 239, 386-92.
    • (1997) Biochem. Biophys. Res. Commun. , vol.239 , pp. 386-392
    • Yamamura, Y.1    Yamashiro, K.2    Tsuruolka, N.3    Nakazato, H.4    Tsujimura, A.5    Yamaguchi, I.N.6
  • 75
    • 0033112711 scopus 로고    scopus 로고
    • Plasticity-related serine proteases in the brain
    • Yoshida S, Shiosaka S (1999) Plasticity-related serine proteases in the brain. Int J Mol Med 3, 405-9.
    • (1999) Int. J. Mol. Med. , vol.3 , pp. 405-409
    • Yoshida, S.1    Shiosaka, S.2
  • 76
    • 0032525843 scopus 로고    scopus 로고
    • Sequence analysis and expression of human neuropsin cDNA and gene
    • Yoshida S, Taniguchi M, Hirata A, Shiosaka S (1998) Sequence analysis and expression of human neuropsin cDNA and gene. Gene 213, 9-16.
    • (1998) Gene , vol.213 , pp. 9-16
    • Yoshida, S.1    Taniguchi, M.2    Hirata, A.3    Shiosaka, S.4
  • 77
    • 0034065656 scopus 로고    scopus 로고
    • Assignment of the neuropsin gene (Prss19) to mouse chromosome band 7B4 by in situ hybridization
    • Yoshida S, Hirata A, Inoue N, Shiosaka S (2000) Assignment of the neuropsin gene (Prss19) to mouse chromosome band 7B4 by in situ hybridization. Cytogenet Cell Genet 88, 97-8.
    • (2000) Cytogenet. Cell Genet. , vol.88 , pp. 97-98
    • Yoshida, S.1    Hirata, A.2    Inoue, N.3    Shiosaka, S.4
  • 78
    • 0035018273 scopus 로고    scopus 로고
    • The new human tissue kallikrein gene family: Structure, function, and association to disease
    • Yousef GM, Diamandis EP (2001) The new human tissue kallikrein gene family: Structure, function, and association to disease. Endocr Rev 22, 184-204.
    • (2001) Endocr. Rev. , vol.22 , pp. 184-204
    • Yousef, G.M.1    Diamandis, E.P.2
  • 79
    • 0034928790 scopus 로고    scopus 로고
    • Morphological changes in dencritic spines associated with long-term synaptic plasticity
    • Yuste R, Bonhoeffer T (2001) Morphological changes in dencritic spines associated with long-term synaptic plasticity. Annu Rev Neurosci 24, 1071-89.
    • (2001) Annu. Rev. Neurosci. , vol.24 , pp. 1071-1089
    • Yuste, R.1    Bonhoeffer, T.2
  • 80
    • 0034651082 scopus 로고    scopus 로고
    • Role of tissue plasminogen activator receptor LRP in hippocampal long-term potentiation
    • Zhuo M, Holtzman DM, Li Y et al. (2000) Role of tissue plasminogen activator receptor LRP in hippocampal long-term potentiation. J Neurosci 20, 542-9.
    • (2000) J. Neurosci. , vol.20 , pp. 542-549
    • Zhuo, M.1    Holtzman, D.M.2    Li, Y.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.