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Volumn 7, Issue 10, 2012, Pages

Regulated Proteolytic Processing of Reelin through Interplay of Tissue Plasminogen Activator (tPA), ADAMTS-4, ADAMTS-5, and Their Modulators

Author keywords

[No Author keywords available]

Indexed keywords

AGGRECANASE 1; AGGRECANASE 2; ALPHA 2 MACROGLOBULIN; REELIN; SERINE PROTEINASE INHIBITOR; TISSUE PLASMINOGEN ACTIVATOR;

EID: 84867628829     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0047793     Document Type: Article
Times cited : (71)

References (63)
  • 1
    • 0036904755 scopus 로고    scopus 로고
    • The role of reelin in the development and evolution of the cerebral cortex
    • Tissir F, Lambert de Rouvroit C, Goffinet AM, (2002) The role of reelin in the development and evolution of the cerebral cortex. Braz J Med Biol Res 35: 1473-1484.
    • (2002) Braz J Med Biol Res , vol.35 , pp. 1473-1484
    • Tissir, F.1    Lambert de Rouvroit, C.2    Goffinet, A.M.3
  • 2
    • 39149102869 scopus 로고    scopus 로고
    • Patterns of neurogenesis and amplitude of Reelin expression are essential for making a mammalian-type cortex
    • Nomura T, Takahashi M, Hara Y, Osumi N, (2008) Patterns of neurogenesis and amplitude of Reelin expression are essential for making a mammalian-type cortex. PLoS One 3: e1454.
    • (2008) PLoS One , vol.3
    • Nomura, T.1    Takahashi, M.2    Hara, Y.3    Osumi, N.4
  • 5
    • 33750333569 scopus 로고    scopus 로고
    • Reelin, lipoprotein receptors and synaptic plasticity
    • Herz J, Chen Y, (2006) Reelin, lipoprotein receptors and synaptic plasticity. Nat Rev Neurosci 7: 850-859.
    • (2006) Nat Rev Neurosci , vol.7 , pp. 850-859
    • Herz, J.1    Chen, Y.2
  • 6
    • 70449723320 scopus 로고    scopus 로고
    • Reelin and apoE actions on signal transduction, synaptic function and memory formation
    • Rogers JT, Weeber EJ, (2008) Reelin and apoE actions on signal transduction, synaptic function and memory formation. Neuron Glia Biol 4: 259-270.
    • (2008) Neuron Glia Biol , vol.4 , pp. 259-270
    • Rogers, J.T.1    Weeber, E.J.2
  • 7
    • 0035968886 scopus 로고    scopus 로고
    • Altered levels of Reelin and its isoforms in schizophrenia and mood disorders
    • Fatemi SH, Kroll JL, Stary JM, (2001) Altered levels of Reelin and its isoforms in schizophrenia and mood disorders. Neuroreport 12: 3209-3215.
    • (2001) Neuroreport , vol.12 , pp. 3209-3215
    • Fatemi, S.H.1    Kroll, J.L.2    Stary, J.M.3
  • 10
    • 76149127988 scopus 로고    scopus 로고
    • Beta-amyloid controls altered Reelin expression and processing in Alzheimer's disease
    • Botella-López A, Cuchillo-Ibáñez I, Cotrufo T, Mok SS, Li QX, et al. (2010) Beta-amyloid controls altered Reelin expression and processing in Alzheimer's disease. Neurobiol Dis 37: 682-691.
    • (2010) Neurobiol Dis , vol.37 , pp. 682-691
    • Botella-López, A.1    Cuchillo-Ibáñez, I.2    Cotrufo, T.3    Mok, S.S.4    Li, Q.X.5
  • 12
    • 0033003134 scopus 로고    scopus 로고
    • Reeler/Disabled-like disruption of neuronal migration in knockout mice lacking the VLDL receptor and ApoE receptor 2
    • Trommsdorff M, Gotthardt M, Hiesberger T, Shelton J, Stockinger W, et al. (1999) Reeler/Disabled-like disruption of neuronal migration in knockout mice lacking the VLDL receptor and ApoE receptor 2. Cell 97: 689-701.
    • (1999) Cell , vol.97 , pp. 689-701
    • Trommsdorff, M.1    Gotthardt, M.2    Hiesberger, T.3    Shelton, J.4    Stockinger, W.5
  • 13
    • 0033213319 scopus 로고    scopus 로고
    • Direct binding of Reelin to VLDL receptor and ApoE receptor 2 induces tyrosine phosphorylation of disabled-1 and modulates tau phosphorylation
    • Hiesberger T, Trommsdorff M, Howell BW, Goffinet A, Mumby MC, et al. (1999) Direct binding of Reelin to VLDL receptor and ApoE receptor 2 induces tyrosine phosphorylation of disabled-1 and modulates tau phosphorylation. Neuron 24: 481-489.
    • (1999) Neuron , vol.24 , pp. 481-489
    • Hiesberger, T.1    Trommsdorff, M.2    Howell, B.W.3    Goffinet, A.4    Mumby, M.C.5
  • 15
    • 0141755223 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase interacts with the adaptor protein Dab1 in response to Reelin signaling and is required for normal cortical lamination
    • Bock HH, Jossin Y, Liu P, Förster E, May P, et al. (2003) Phosphatidylinositol 3-kinase interacts with the adaptor protein Dab1 in response to Reelin signaling and is required for normal cortical lamination. J Biol Chem 278: 38772-38779.
    • (2003) J Biol Chem , vol.278 , pp. 38772-38779
    • Bock, H.H.1    Jossin, Y.2    Liu, P.3    Förster, E.4    May, P.5
  • 16
    • 0345894331 scopus 로고    scopus 로고
    • Reelin-mediated signaling locally regulates protein kinase B/Akt and glycogen synthase kinase 3beta
    • Beffert U, Morfini G, Bock HH, Reyna H, Brady ST, et al. (2002) Reelin-mediated signaling locally regulates protein kinase B/Akt and glycogen synthase kinase 3beta. J Biol Chem 277: 49958-49964.
    • (2002) J Biol Chem , vol.277 , pp. 49958-49964
    • Beffert, U.1    Morfini, G.2    Bock, H.H.3    Reyna, H.4    Brady, S.T.5
  • 17
    • 0037313587 scopus 로고    scopus 로고
    • Apolipoprotein E and Reelin ligands modulate tau phosphorylation through an apolipoprotein E receptor/disabled-1/glycogen synthase kinase-3beta cascade
    • Ohkubo N, Lee YD, Morishima A, Terashima T, Kikkawa S, et al. (2003) Apolipoprotein E and Reelin ligands modulate tau phosphorylation through an apolipoprotein E receptor/disabled-1/glycogen synthase kinase-3beta cascade. FASEB J 17: 295-297.
    • (2003) FASEB J , vol.17 , pp. 295-297
    • Ohkubo, N.1    Lee, Y.D.2    Morishima, A.3    Terashima, T.4    Kikkawa, S.5
  • 18
    • 0001025605 scopus 로고    scopus 로고
    • Reelin, the extracellular matrix protein deficient in reeler mutant mice, is processed by a metalloproteinase
    • Lambert de Rouvroit C, de Bergeyck V, Cortvrindt C, Bar I, Eeckhout Y, et al. (1999) Reelin, the extracellular matrix protein deficient in reeler mutant mice, is processed by a metalloproteinase. Exp Neurol 156: 214-217.
    • (1999) Exp Neurol , vol.156 , pp. 214-217
    • Lambert de Rouvroit, C.1    de Bergeyck, V.2    Cortvrindt, C.3    Bar, I.4    Eeckhout, Y.5
  • 20
    • 0036312590 scopus 로고    scopus 로고
    • Secreted Reelin molecules form homodimers
    • Kubo K, Mikoshiba K, Nakajima K, (2002) Secreted Reelin molecules form homodimers. Neurosci Res 43: 381-388.
    • (2002) Neurosci Res , vol.43 , pp. 381-388
    • Kubo, K.1    Mikoshiba, K.2    Nakajima, K.3
  • 21
    • 1642540032 scopus 로고    scopus 로고
    • The central fragment of Reelin, generated by proteolytic processing in vivo, is critical to its function during cortical plate development
    • Jossin Y, Ignatova N, Hiesberger T, Herz J, Lambert de Rouvroit C, et al. (2004) The central fragment of Reelin, generated by proteolytic processing in vivo, is critical to its function during cortical plate development. J Neurosci 24: 514-521.
    • (2004) J Neurosci , vol.24 , pp. 514-521
    • Jossin, Y.1    Ignatova, N.2    Hiesberger, T.3    Herz, J.4    Lambert de Rouvroit, C.5
  • 22
    • 34247354614 scopus 로고    scopus 로고
    • Processing of Reelin by embryonic neurons is important for function in tissue but not in dissociated cultured neurons
    • Jossin Y, Gui L, Goffinet AM, (2007) Processing of Reelin by embryonic neurons is important for function in tissue but not in dissociated cultured neurons. J Neurosci 27: 4243-4252.
    • (2007) J Neurosci , vol.27 , pp. 4243-4252
    • Jossin, Y.1    Gui, L.2    Goffinet, A.M.3
  • 23
    • 80053422050 scopus 로고    scopus 로고
    • Functional importance of covalent homodimer of reelin protein linked via its central region
    • Yasui N, Kitago Y, Beppu A, Kohno T, Morishita S, et al. (2011) Functional importance of covalent homodimer of reelin protein linked via its central region. J Biol Chem 286: 35247-35256.
    • (2011) J Biol Chem , vol.286 , pp. 35247-35256
    • Yasui, N.1    Kitago, Y.2    Beppu, A.3    Kohno, T.4    Morishita, S.5
  • 24
    • 33845925306 scopus 로고    scopus 로고
    • DAB1 and Reelin effects on amyloid precursor protein and ApoE receptor 2 trafficking and processing
    • Hoe HS, Tran TS, Matsuoka Y, Howell BW, Rebeck GW, (2006) DAB1 and Reelin effects on amyloid precursor protein and ApoE receptor 2 trafficking and processing. J Biol Chem 281: 35176-35185.
    • (2006) J Biol Chem , vol.281 , pp. 35176-35185
    • Hoe, H.S.1    Tran, T.S.2    Matsuoka, Y.3    Howell, B.W.4    Rebeck, G.W.5
  • 25
    • 67049167155 scopus 로고    scopus 로고
    • Interaction of reelin with amyloid precursor protein promotes neurite outgrowth
    • Hoe HS, Lee KJ, Carney RS, Lee J, Markova A, et al. (2009) Interaction of reelin with amyloid precursor protein promotes neurite outgrowth. J Neurosci 29: 7459-7473.
    • (2009) J Neurosci , vol.29 , pp. 7459-7473
    • Hoe, H.S.1    Lee, K.J.2    Carney, R.S.3    Lee, J.4    Markova, A.5
  • 27
    • 34547115035 scopus 로고    scopus 로고
    • The extremely conserved C-terminal region of Reelin is not necessary for secretion but is required for efficient activation of downstream signaling
    • Nakano Y, Kohno T, Hibi T, Kohno S, Baba A, et al. (2007) The extremely conserved C-terminal region of Reelin is not necessary for secretion but is required for efficient activation of downstream signaling. J Biol Chem 282: 20544-20552.
    • (2007) J Biol Chem , vol.282 , pp. 20544-20552
    • Nakano, Y.1    Kohno, T.2    Hibi, T.3    Kohno, S.4    Baba, A.5
  • 28
    • 70449476622 scopus 로고    scopus 로고
    • C-terminal region-dependent change of antibody-binding to the Eighth Reelin repeat reflects the signaling activity of Reelin
    • Kohno T, Nakano Y, Kitoh N, Yagi H, Kato K, et al. (2009) C-terminal region-dependent change of antibody-binding to the Eighth Reelin repeat reflects the signaling activity of Reelin. J Neurosci Res 87: 3043-3053.
    • (2009) J Neurosci Res , vol.87 , pp. 3043-3053
    • Kohno, T.1    Nakano, Y.2    Kitoh, N.3    Yagi, H.4    Kato, K.5
  • 29
    • 0034662978 scopus 로고    scopus 로고
    • Reelin molecules assemble together to form a large protein complex, which is inhibited by the function-blocking CR-50 antibody
    • Utsunomiya-Tate N, Kubo K, Tate S, Kainosho M, Katayama E, et al. (2000) Reelin molecules assemble together to form a large protein complex, which is inhibited by the function-blocking CR-50 antibody. Proc Natl Acad Sci U S A 97: 9729-9734.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 9729-9734
    • Utsunomiya-Tate, N.1    Kubo, K.2    Tate, S.3    Kainosho, M.4    Katayama, E.5
  • 31
    • 15944413194 scopus 로고    scopus 로고
    • Reelin glycoprotein: structure, biology and roles in health and disease
    • Fatemi SH, (2005) Reelin glycoprotein: structure, biology and roles in health and disease. Mol Psychiatry 10: 251-257.
    • (2005) Mol Psychiatry , vol.10 , pp. 251-257
    • Fatemi, S.H.1
  • 32
    • 77954203843 scopus 로고    scopus 로고
    • Reelin-mediated signaling in neuropsychiatric and neurodegenerative diseases
    • Knuesel I, (2010) Reelin-mediated signaling in neuropsychiatric and neurodegenerative diseases. Prog Neurobiol 91: 257-274.
    • (2010) Prog Neurobiol , vol.91 , pp. 257-274
    • Knuesel, I.1
  • 33
    • 0042697305 scopus 로고    scopus 로고
    • Triple-transgenic model of Alzheimer's disease with plaques and tangles: intracellular Abeta and synaptic dysfunction
    • Oddo S, Caccamo A, Shepherd JD, Murphy MP, Golde TE, et al. (2003) Triple-transgenic model of Alzheimer's disease with plaques and tangles: intracellular Abeta and synaptic dysfunction. Neuron 39: 409-421.
    • (2003) Neuron , vol.39 , pp. 409-421
    • Oddo, S.1    Caccamo, A.2    Shepherd, J.D.3    Murphy, M.P.4    Golde, T.E.5
  • 34
    • 77951295962 scopus 로고    scopus 로고
    • Ceruloplasmin-induced aggregation of P19 neurons involves a serine protease activity and is accompanied by reelin cleavage
    • Ducharme P, Maltais D, Desroches D, Mateescu MA, Paquin J, (2010) Ceruloplasmin-induced aggregation of P19 neurons involves a serine protease activity and is accompanied by reelin cleavage. Neuroscience 167: 633-643.
    • (2010) Neuroscience , vol.167 , pp. 633-643
    • Ducharme, P.1    Maltais, D.2    Desroches, D.3    Mateescu, M.A.4    Paquin, J.5
  • 35
    • 38949162923 scopus 로고    scopus 로고
    • Genome-wide demethylation during neural differentiation of P19 embryonal carcinoma cells
    • Hatada I, Morita S, Kimura M, Horii T, Yamashita R, et al. (2008) Genome-wide demethylation during neural differentiation of P19 embryonal carcinoma cells. J Hum Genet 53: 185-191.
    • (2008) J Hum Genet , vol.53 , pp. 185-191
    • Hatada, I.1    Morita, S.2    Kimura, M.3    Horii, T.4    Yamashita, R.5
  • 36
    • 2942644528 scopus 로고    scopus 로고
    • Methodological factors influencing measurement and processing of plasma reelin in humans
    • Lugli G, Krueger JM, Davis JM, Persico AM, Keller F, et al. (2003) Methodological factors influencing measurement and processing of plasma reelin in humans. BMC Biochem 4: 9.
    • (2003) BMC Biochem , vol.4 , pp. 9
    • Lugli, G.1    Krueger, J.M.2    Davis, J.M.3    Persico, A.M.4    Keller, F.5
  • 37
    • 33644883338 scopus 로고    scopus 로고
    • Glycosaminoglycan-binding properties and aggrecanase activities of truncated ADAMTSs: comparative analyses with ADAMTS-5, -9, -16 and -18
    • Zeng W, Corcoran C, Collins-Racie LA, Lavallie ER, Morris EA, et al. (2006) Glycosaminoglycan-binding properties and aggrecanase activities of truncated ADAMTSs: comparative analyses with ADAMTS-5,-9,-16 and-18. Biochim Biophys Acta 1760: 517-524.
    • (2006) Biochim Biophys Acta , vol.1760 , pp. 517-524
    • Zeng, W.1    Corcoran, C.2    Collins-Racie, L.A.3    Lavallie, E.R.4    Morris, E.A.5
  • 39
    • 0037231877 scopus 로고    scopus 로고
    • Induction of aggrecanase 1 (ADAM-TS4) by interleukin-1 occurs through activation of constitutively produced protein
    • Pratta MA, Scherle PA, Yang G, Liu RQ, Newton RC, (2003) Induction of aggrecanase 1 (ADAM-TS4) by interleukin-1 occurs through activation of constitutively produced protein. Arthritis Rheum48: 119-133.
    • (2003) Arthritis Rheum , vol.48 , pp. 119-133
    • Pratta, M.A.1    Scherle, P.A.2    Yang, G.3    Liu, R.Q.4    Newton, R.C.5
  • 40
    • 38349140386 scopus 로고    scopus 로고
    • ADAMTS-4 and -8 are inflammatory regulated enzymes expressed in macrophage-rich areas of human atherosclerotic plaques
    • Wågsäter D, Björk H, Zhu C, Björkegren J, Valen G, et al. (2008) ADAMTS-4 and-8 are inflammatory regulated enzymes expressed in macrophage-rich areas of human atherosclerotic plaques. Atherosclerosis 196: 514-522.
    • (2008) Atherosclerosis , vol.196 , pp. 514-522
    • Wågsäter, D.1    Björk, H.2    Zhu, C.3    Björkegren, J.4    Valen, G.5
  • 41
    • 37149032447 scopus 로고    scopus 로고
    • Screening of potential a disintegrin and metalloproteinase with thrombospondin motifs-4 inhibitors using a collagen model fluorescence resonance energy transfer substrate
    • Lauer-Fields JL, Spicer TP, Chase PS, Cudic M, Burstein GD, et al. (2008) Screening of potential a disintegrin and metalloproteinase with thrombospondin motifs-4 inhibitors using a collagen model fluorescence resonance energy transfer substrate. Anal Biochem 373: 43-51.
    • (2008) Anal Biochem , vol.373 , pp. 43-51
    • Lauer-Fields, J.L.1    Spicer, T.P.2    Chase, P.S.3    Cudic, M.4    Burstein, G.D.5
  • 42
    • 0035853456 scopus 로고    scopus 로고
    • Inhibition of ADAMTS4 (aggrecanase-1) by tissue inhibitors of metalloproteinases (TIMP-1, 2, 3 and 4)
    • Hashimoto G, Aoki T, Nakamura H, Tanzawa K, Okada Y, (2001) Inhibition of ADAMTS4 (aggrecanase-1) by tissue inhibitors of metalloproteinases (TIMP-1, 2, 3 and 4). FEBS Lett 494: 192-195.
    • (2001) FEBS Lett , vol.494 , pp. 192-195
    • Hashimoto, G.1    Aoki, T.2    Nakamura, H.3    Tanzawa, K.4    Okada, Y.5
  • 43
    • 2342445246 scopus 로고    scopus 로고
    • Alpha2-macroglobulin is a novel substrate for ADAMTS-4 and ADAMTS-5 and represents an endogenous inhibitor of these enzymes
    • Tortorella MD, Arner EC, Hills R, Easton A, Korte-Sarfaty J, et al. (2004) Alpha2-macroglobulin is a novel substrate for ADAMTS-4 and ADAMTS-5 and represents an endogenous inhibitor of these enzymes. J Biol Chem 279: 17554-17561.
    • (2004) J Biol Chem , vol.279 , pp. 17554-17561
    • Tortorella, M.D.1    Arner, E.C.2    Hills, R.3    Easton, A.4    Korte-Sarfaty, J.5
  • 45
    • 2442595171 scopus 로고    scopus 로고
    • Proprotein convertase furin interacts with and cleaves pro-ADAMTS4 (Aggrecanase-1) in the trans-Golgi network
    • Wang P, Tortorella M, England K, Malfait AM, Thomas G, et al. (2004) Proprotein convertase furin interacts with and cleaves pro-ADAMTS4 (Aggrecanase-1) in the trans-Golgi network. J Biol Chem 279: 15434-15440.
    • (2004) J Biol Chem , vol.279 , pp. 15434-15440
    • Wang, P.1    Tortorella, M.2    England, K.3    Malfait, A.M.4    Thomas, G.5
  • 47
    • 39449131916 scopus 로고    scopus 로고
    • Will the real aggrecanase(s) step up: evaluating the criteria that define aggrecanase activity in osteoarthritis
    • Tortorella MD, Malfait AM, (2008) Will the real aggrecanase(s) step up: evaluating the criteria that define aggrecanase activity in osteoarthritis. Curr Pharm Biotechnol 9: 16-23.
    • (2008) Curr Pharm Biotechnol , vol.9 , pp. 16-23
    • Tortorella, M.D.1    Malfait, A.M.2
  • 48
    • 0031021357 scopus 로고    scopus 로고
    • An extracellular proteolytic cascade promotes neuronal degeneration in the mouse hippocampus
    • Tsirka SE, Rogove AD, Bugge TH, Degen JL, Strickland S, (1997) An extracellular proteolytic cascade promotes neuronal degeneration in the mouse hippocampus. J Neurosci 17: 543-552.
    • (1997) J Neurosci , vol.17 , pp. 543-552
    • Tsirka, S.E.1    Rogove, A.D.2    Bugge, T.H.3    Degen, J.L.4    Strickland, S.5
  • 49
    • 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: 2125-2134.
    • (2002) J Neurosci , vol.22 , pp. 2125-2134
    • Salles, F.J.1    Strickland, S.2
  • 50
    • 77950363927 scopus 로고    scopus 로고
    • Co-localization of Reelin and proteolytic AbetaPP fragments in hippocampal plaques in aged wild-type mice
    • Doehner J, Madhusudan A, Konietzko U, Fritschy JM, Knuesel I, (2010) Co-localization of Reelin and proteolytic AbetaPP fragments in hippocampal plaques in aged wild-type mice. J Alzheimers Dis 19: 1339-1357.
    • (2010) J Alzheimers Dis , vol.19 , pp. 1339-1357
    • Doehner, J.1    Madhusudan, A.2    Konietzko, U.3    Fritschy, J.M.4    Knuesel, I.5
  • 51
    • 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: 4269-4286.
    • (1989) J Neurosci , vol.9 , pp. 4269-4286
    • Pittman, R.N.1    Ivins, J.K.2    Buettner, H.M.3
  • 52
    • 84862658178 scopus 로고    scopus 로고
    • Extrusion of misfolded and aggregated proteins - a protective strategy of aging neurons?
    • Doehner J, Genoud C, Imhof C, Krstic D, Knuesel I, (2012) Extrusion of misfolded and aggregated proteins- a protective strategy of aging neurons? Eur J Neurosci 35: 1938-1950.
    • (2012) Eur J Neurosci , vol.35 , pp. 1938-1950
    • Doehner, J.1    Genoud, C.2    Imhof, C.3    Krstic, D.4    Knuesel, I.5
  • 53
    • 77954517681 scopus 로고    scopus 로고
    • Reduced Reelin expression accelerates amyloid-beta plaque formation and tau pathology in transgenic Alzheimer's disease mice
    • Kocherhans S, Madhusudan A, Doehner J, Breu KS, Nitsch RM, et al. (2010) Reduced Reelin expression accelerates amyloid-beta plaque formation and tau pathology in transgenic Alzheimer's disease mice. J Neurosci 30: 9228-9240.
    • (2010) J Neurosci , vol.30 , pp. 9228-9240
    • Kocherhans, S.1    Madhusudan, A.2    Doehner, J.3    Breu, K.S.4    Nitsch, R.M.5
  • 55
    • 64049110805 scopus 로고    scopus 로고
    • The N-terminal fragment of Reelin is generated after endocytosis and released through the pathway regulated by Rab11
    • Hibi T, Hattori M, (2009) The N-terminal fragment of Reelin is generated after endocytosis and released through the pathway regulated by Rab11. FEBS Lett 583: 1299-1303.
    • (2009) FEBS Lett , vol.583 , pp. 1299-1303
    • Hibi, T.1    Hattori, M.2
  • 56
    • 79952762804 scopus 로고    scopus 로고
    • Impaired reelin processing and secretion by Cajal-Retzius cells contributes to granule cell dispersion in a mouse model of temporal lobe epilepsy
    • Duveau V, Madhusudan A, Caleo M, Knuesel I, Fritschy JM, (2011) Impaired reelin processing and secretion by Cajal-Retzius cells contributes to granule cell dispersion in a mouse model of temporal lobe epilepsy. Hippocampus 21: 935-944.
    • (2011) Hippocampus , vol.21 , pp. 935-944
    • Duveau, V.1    Madhusudan, A.2    Caleo, M.3    Knuesel, I.4    Fritschy, J.M.5
  • 57
    • 0031031005 scopus 로고    scopus 로고
    • Reelin is a secreted glycoprotein recognized by the CR-50 monoclonal antibody
    • D'Arcangelo G, Nakajima K, Miyata T, Ogawa M, Mikoshiba K, et al. (1997) Reelin is a secreted glycoprotein recognized by the CR-50 monoclonal antibody. J Neurosci 17: 23-31.
    • (1997) J Neurosci , vol.17 , pp. 23-31
    • D'Arcangelo, G.1    Nakajima, K.2    Miyata, T.3    Ogawa, M.4    Mikoshiba, K.5
  • 58
    • 18944389722 scopus 로고    scopus 로고
    • Tissue plasminogen activator mediates amyloid-induced neurotoxicity via Erk1/2 activation
    • Medina MG, Ledesma MD, Domínguez JE, Medina M, Zafra D, et al. (2005) Tissue plasminogen activator mediates amyloid-induced neurotoxicity via Erk1/2 activation. EMBO J 24: 1706-1716.
    • (2005) EMBO J , vol.24 , pp. 1706-1716
    • Medina, M.G.1    Ledesma, M.D.2    Domínguez, J.E.3    Medina, M.4    Zafra, D.5
  • 59
    • 34547451637 scopus 로고    scopus 로고
    • Upregulation of tPA/plasminogen proteolytic system in the periphery of amyloid deposits in the Tg2576 mouse model of Alzheimer's disease
    • Lee JY, Kweon HS, Cho E, Lee JY, Byun HR, et al. (2007) Upregulation of tPA/plasminogen proteolytic system in the periphery of amyloid deposits in the Tg2576 mouse model of Alzheimer's disease. Neurosci Lett 423: 82-87.
    • (2007) Neurosci Lett , vol.423 , pp. 82-87
    • Lee, J.Y.1    Kweon, H.S.2    Cho, E.3    Lee, J.Y.4    Byun, H.R.5
  • 60
    • 77949312388 scopus 로고    scopus 로고
    • Processing of the matricellular protein hevin in mouse brain is dependent on ADAMTS4
    • Weaver MS, Workman G, Cardo-Vila M, Arap W, Pasqualini R, et al. (2010) Processing of the matricellular protein hevin in mouse brain is dependent on ADAMTS4. J Biol Chem 285: 5868-5877.
    • (2010) J Biol Chem , vol.285 , pp. 5868-5877
    • Weaver, M.S.1    Workman, G.2    Cardo-Vila, M.3    Arap, W.4    Pasqualini, R.5
  • 61
    • 80051475089 scopus 로고    scopus 로고
    • Altered versican cleavage in ADAMTS5 deficient mice; a novel etiology of myxomatous valve disease
    • Dupuis LE, McCulloch DR, McGarity JD, Bahan A, Wessels A, et al. (2011) Altered versican cleavage in ADAMTS5 deficient mice; a novel etiology of myxomatous valve disease. Dev Biol 357: 152-164.
    • (2011) Dev Biol , vol.357 , pp. 152-164
    • Dupuis, L.E.1    McCulloch, D.R.2    McGarity, J.D.3    Bahan, A.4    Wessels, A.5
  • 62
    • 67349155506 scopus 로고    scopus 로고
    • Adamts5, the gene encoding a proteoglycan-degrading metalloprotease, is expressed by specific cell lineages during mouse embryonic development and in adult tissues
    • McCulloch DR, Le Goff C, Bhatt S, Dixon LJ, Sandy JD, et al. (2009) Adamts5, the gene encoding a proteoglycan-degrading metalloprotease, is expressed by specific cell lineages during mouse embryonic development and in adult tissues. Gene Expr Patterns 9: 314-323.
    • (2009) Gene Expr Patterns , vol.9 , pp. 314-323
    • McCulloch, D.R.1    Le Goff, C.2    Bhatt, S.3    Dixon, L.J.4    Sandy, J.D.5
  • 63
    • 0036837361 scopus 로고    scopus 로고
    • Association between protease-specific proteolytic cleavage of brevican and synaptic loss in the dentate gyrus of kainate-treated rats
    • Yuan W, Matthews RT, Sandy JD, Gottschall PE, (2002) Association between protease-specific proteolytic cleavage of brevican and synaptic loss in the dentate gyrus of kainate-treated rats. Neuroscience 114: 1091-1101.
    • (2002) Neuroscience , vol.114 , pp. 1091-1101
    • Yuan, W.1    Matthews, R.T.2    Sandy, J.D.3    Gottschall, P.E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.