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Volumn 4, Issue 4, 2005, Pages 239-245

The role of matrix metalloproteinases in the morphogenesis of the cerebellar cortex

Author keywords

Dendrites; Development; Extracellular matrix; Granule neurons; Migration; Proteinases

Indexed keywords

BLOCKING ANTIBODY; GELATINASE A; GELATINASE B; MATRIX METALLOPROTEINASE; PROTEINASE; STROMELYSIN; TISSUE INHIBITOR OF METALLOPROTEINASE; TISSUE INHIBITOR OF METALLOPROTEINASE 1; TISSUE INHIBITOR OF METALLOPROTEINASE 2; TISSUE INHIBITOR OF METALLOPROTEINASE 3; TISSUE INHIBITOR OF METALLOPROTEINASE 4;

EID: 33644796277     PISSN: 14734222     EISSN: 14734230     Source Type: Journal    
DOI: 10.1080/14734220500247646     Document Type: Review
Times cited : (40)

References (77)
  • 1
    • 0015384685 scopus 로고
    • Postnatal development of the cerebellar cortex in the rat. III. Maturation of the components of the granular layer
    • Altman J. Postnatal development of the cerebellar cortex in the rat. III. Maturation of the components of the granular layer. J Comp Neurol. 1972;145:465-513.
    • (1972) J Comp Neurol , vol.145 , pp. 465-513
    • Altman, J.1
  • 2
    • 0015364121 scopus 로고
    • Postnatal development of the cerebellar cortex in the rat. I. The external germinal layer and the transitional molecular layer
    • Altman J. Postnatal development of the cerebellar cortex in the rat. I. The external germinal layer and the transitional molecular layer. J Comp Neurol. 1972;145:353-97.
    • (1972) J Comp Neurol , vol.145 , pp. 353-397
    • Altman, J.1
  • 3
    • 0015383228 scopus 로고
    • Postnatal development of the cerebellar cortex in the rat. II. Phase in the maturation of Purkinje cells and of molecular layer
    • Altman J. Postnatal development of the cerebellar cortex in the rat. II. Phase in the maturation of Purkinje cells and of molecular layer. J Comp Neurol. 1972;145:399-463.
    • (1972) J Comp Neurol , vol.145 , pp. 399-463
    • Altman, J.1
  • 4
    • 2442566843 scopus 로고    scopus 로고
    • Cellular and genetic regulation of the development of the cerebellar system
    • Sotelo C. Cellular and genetic regulation of the development of the cerebellar system. Prog Neurobiol. 2004;72:295-339.
    • (2004) Prog Neurobiol , vol.72 , pp. 295-339
    • Sotelo, C.1
  • 7
    • 2542436756 scopus 로고    scopus 로고
    • Matrix metalloproteinases and their endogenous inhibitors in neuronal physiology of the adult brain
    • Dzwonek J, Rylski M, Kaczmarek L. Matrix metalloproteinases and their endogenous inhibitors in neuronal physiology of the adult brain. FEBS Lett. 2004;567:129-35.
    • (2004) FEBS Lett , vol.567 , pp. 129-135
    • Dzwonek, J.1    Rylski, M.2    Kaczmarek, L.3
  • 11
    • 0037121996 scopus 로고    scopus 로고
    • Matrix metalloproteinases in the adult brain physiology: A link between c-Fos, AP-1 and remodeling of neuronal connections?
    • Kaczmarek L, Lapinska-Dzwonek J, Szymczak S. Matrix metalloproteinases in the adult brain physiology: A link between c-Fos, AP-1 and remodeling of neuronal connections? EMBO J. 2002;21:6643-8.
    • (2002) EMBO J , vol.21 , pp. 6643-6648
    • Kaczmarek, L.1    Lapinska-Dzwonek, J.2    Szymczak, S.3
  • 13
    • 0036644958 scopus 로고    scopus 로고
    • Extracellular proteolysis in brain injury and inflammation: Role for plasminogen activators and matrix metalloproteinases
    • Lo EH, Wang X, Cuzner ML. Extracellular proteolysis in brain injury and inflammation: role for plasminogen activators and matrix metalloproteinases. J Neurosci Res. 2002;69:1-9.
    • (2002) J Neurosci Res , vol.69 , pp. 1-9
    • Lo, E.H.1    Wang, X.2    Cuzner, M.L.3
  • 14
    • 0028825270 scopus 로고
    • Matrix metalloproteinases in brain injury
    • Rosenberg GA. Matrix metalloproteinases in brain injury. J Neurotrauma. 1995;12:833-42.
    • (1995) J Neurotrauma , vol.12 , pp. 833-842
    • Rosenberg, G.A.1
  • 16
    • 0000030724 scopus 로고
    • An autoradiographic analysis of histogenesis in the mouse cerebellum
    • Miale IL, Sidman RL. An autoradiographic analysis of histogenesis in the mouse cerebellum. Exp Neurol. 1961;4:277-96.
    • (1961) Exp Neurol , vol.4 , pp. 277-296
    • Miale, I.L.1    Sidman, R.L.2
  • 17
    • 0015025916 scopus 로고
    • Neuron-glia relationship during granule cell migration in developing cerebellar cortex. A Golgi and electronmicroscopic study in Macacus Rhesus
    • Rakic P. Neuron-glia relationship during granule cell migration in developing cerebellar cortex. A Golgi and electronmicroscopic study in Macacus Rhesus. J Comp Neurol. 1971;141:283-312.
    • (1971) J Comp Neurol , vol.141 , pp. 283-312
    • Rakic, P.1
  • 18
    • 0025096007 scopus 로고
    • Principles of neural cell migration
    • Rakic P. Principles of neural cell migration. Experientia. 1990;46:882-91.
    • (1990) Experientia , vol.46 , pp. 882-891
    • Rakic, P.1
  • 19
    • 0025952928 scopus 로고
    • Complete structure of the human gene for 92-kDa type IV collagenase. Divergent regulation of expression for the 92- and 72-kilodalton enzyme genes in HT-1080 cells
    • Huhtala P, Tuuttila A, Chow LT, Lohi J, Keski-Oja J, Tryggvason K. Complete structure of the human gene for 92-kDa type IV collagenase. Divergent regulation of expression for the 92- and 72-kilodalton enzyme genes in HT-1080 cells. J Biol Chem. 1991;266:16485-90.
    • (1991) J Biol Chem , vol.266 , pp. 16485-16490
    • Huhtala, P.1    Tuuttila, A.2    Chow, L.T.3    Lohi, J.4    Keski-Oja, J.5    Tryggvason, K.6
  • 20
    • 0035101187 scopus 로고    scopus 로고
    • Expression of matrix metalloproteinases and tissue inhibitors of metalloproteinases in human optic nerve head astrocytes
    • Agapova OA, Ricard CS, Salvador-Silva M, Hernandez MR. Expression of matrix metalloproteinases and tissue inhibitors of metalloproteinases in human optic nerve head astrocytes. Glia. 2001;33:205-16.
    • (2001) Glia , vol.33 , pp. 205-216
    • Agapova, O.A.1    Ricard, C.S.2    Salvador-Silva, M.3    Hernandez, M.R.4
  • 21
    • 0034333458 scopus 로고    scopus 로고
    • Differential spatial distribution and temporal regulation of tissue inhibitor of metalloproteinase mRNA expression during rat central nervous system development
    • Fager N, Jaworski DM. Differential spatial distribution and temporal regulation of tissue inhibitor of metalloproteinase mRNA expression during rat central nervous system development. Mech Dev. 2000;98:105-9.
    • (2000) Mech Dev , vol.98 , pp. 105-109
    • Fager, N.1    Jaworski, D.M.2
  • 22
    • 0033836577 scopus 로고    scopus 로고
    • MMP-2 and MMP-9 increase the neurite-promoting potential of schwann cell basal laminae and are upregulated in degenerated nerve
    • Ferguson TA, Muir D. MMP-2 and MMP-9 increase the neurite-promoting potential of schwann cell basal laminae and are upregulated in degenerated nerve. Mol Cell Neurosci. 2000;16:157-67.
    • (2000) Mol Cell Neurosci , vol.16 , pp. 157-167
    • Ferguson, T.A.1    Muir, D.2
  • 23
    • 0033524845 scopus 로고    scopus 로고
    • Expression and modulation of matrix metalloproteinase-2 and tissue inhibitors of metalloproteinases in human embryonic CNS stem cells
    • Frolichsthal-Schoeller P, Vescovi AL, Krekoski CA, Murphy G, Edwards DR, Forsyth P. Expression and modulation of matrix metalloproteinase-2 and tissue inhibitors of metalloproteinases in human embryonic CNS stem cells. Neuroreport. 1999;10:345-51.
    • (1999) Neuroreport , vol.10 , pp. 345-351
    • Frolichsthal-Schoeller, P.1    Vescovi, A.L.2    Krekoski, C.A.3    Murphy, G.4    Edwards, D.R.5    Forsyth, P.6
  • 25
    • 0031964427 scopus 로고    scopus 로고
    • Oligodendrocytes utilize a matrix metalloproteinase, MMP-9, to extend processes along an astrocyte extracellular matrix
    • Uhm JH, Dooley NP, Oh LY, Yong VW. Oligodendrocytes utilize a matrix metalloproteinase, MMP-9, to extend processes along an astrocyte extracellular matrix. Glia. 1998;22:53-63.
    • (1998) Glia , vol.22 , pp. 53-63
    • Uhm, J.H.1    Dooley, N.P.2    Oh, L.Y.3    Yong, V.W.4
  • 26
    • 12444311673 scopus 로고    scopus 로고
    • Developmental expression of matrix metalloproteinases 2 and 9 and their potential role in the histogenesis of the cerebellar cortex
    • Ayoub AE, Cai TQ, Kaplan RA, Luo J. Developmental expression of matrix metalloproteinases 2 and 9 and their potential role in the histogenesis of the cerebellar cortex. J Comp Neurol. 2005;481:403-15.
    • (2005) J Comp Neurol , vol.481 , pp. 403-415
    • Ayoub, A.E.1    Cai, T.Q.2    Kaplan, R.A.3    Luo, J.4
  • 27
    • 0033564779 scopus 로고    scopus 로고
    • Spatiotemporal expression patterns of metalloproteinases and their inhibitors in the postnatal developing rat cerebellum
    • Vaillant C, Didier-Bazes M, Hutter A, Belin MF, Thomasset N. Spatiotemporal expression patterns of metalloproteinases and their inhibitors in the postnatal developing rat cerebellum. J Neurosci. 1999;19:4994-5004.
    • (1999) J Neurosci , vol.19 , pp. 4994-5004
    • Vaillant, C.1    Didier-Bazes, M.2    Hutter, A.3    Belin, M.F.4    Thomasset, N.5
  • 28
    • 0142188658 scopus 로고    scopus 로고
    • MMP-9 deficiency affects axonal outgrowth, migration, and apoptosis in the developing cerebellum
    • Vaillant C, Meissirel C, Mutin M, Belin MF, Lund LR, Thomasset N. MMP-9 deficiency affects axonal outgrowth, migration, and apoptosis in the developing cerebellum. Mol Cell Neurosci. 2003;24:395-408.
    • (2003) Mol Cell Neurosci , vol.24 , pp. 395-408
    • Vaillant, C.1    Meissirel, C.2    Mutin, M.3    Belin, M.F.4    Lund, L.R.5    Thomasset, N.6
  • 29
    • 0036616280 scopus 로고    scopus 로고
    • Cytodifferentiation of Bergmann glia and its relationship with Purkinje cells
    • Yamada K, Watanabe M. Cytodifferentiation of Bergmann glia and its relationship with Purkinje cells. Anat Sci Int. 2002;77:94-108.
    • (2002) Anat Sci Int , vol.77 , pp. 94-108
    • Yamada, K.1    Watanabe, M.2
  • 31
    • 0031913920 scopus 로고    scopus 로고
    • Immunohistochemistry of matrix metalloproteinases (MMP), their substrates, and their inhibitors (TIMP) during trophoblast invasion in the human placenta
    • Huppertz B, Kertschanska S, Demir AY, Frank HG, Kaufmann P. Immunohistochemistry of matrix metalloproteinases (MMP), their substrates, and their inhibitors (TIMP) during trophoblast invasion in the human placenta. Cell Tissue Res. 1998;291:133-48.
    • (1998) Cell Tissue Res , vol.291 , pp. 133-148
    • Huppertz, B.1    Kertschanska, S.2    Demir, A.Y.3    Frank, H.G.4    Kaufmann, P.5
  • 33
    • 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 RD, Kaczmarek L. Matrix metalloproteinase-9 undergoes expression and activation during dendritic remodeling in adult hippocampus. J Neurosci. 2002;22:920-30.
    • (2002) J Neurosci , vol.22 , pp. 920-930
    • Szklarczyk, A.1    Lapinska, J.2    Rylski, M.3    McKay, R.D.4    Kaczmarek, L.5
  • 34
    • 0030957218 scopus 로고    scopus 로고
    • Activation mechanisms of matrix metalloproteinases
    • Nagase H. Activation mechanisms of matrix metalloproteinases. Biol Chem. 1997;378:151-60.
    • (1997) Biol Chem , vol.378 , pp. 151-160
    • Nagase, H.1
  • 35
    • 0032854658 scopus 로고    scopus 로고
    • Activation of proMMP-9 by a plasmin/MMP-3 cascade in a tumor cell model. Regulation by tissue inhibitors of metalloproteinases
    • Hahn-Dantona E, Ramos-DeSimone N, Sipley J, Nagase H, French DL, Quigley JP. Activation of proMMP-9 by a plasmin/MMP-3 cascade in a tumor cell model. Regulation by tissue inhibitors of metalloproteinases. Ann NY Acad Sci. 1999;878:372-87.
    • (1999) Ann NY Acad Sci , vol.878 , pp. 372-387
    • Hahn-Dantona, E.1    Ramos-DeSimone, N.2    Sipley, J.3    Nagase, H.4    French, D.L.5    Quigley, J.P.6
  • 36
    • 0033598707 scopus 로고    scopus 로고
    • Neuronal migration is retarded in mice lacking the tissue plasminogen activator gene
    • USA
    • Seeds NW, Basham ME, Haffke SP. Neuronal migration is retarded in mice lacking the tissue plasminogen activator gene. Proc Natl Acad Sci USA. 1999;96:14118-23.
    • (1999) Proc Natl Acad Sci , vol.96 , pp. 14118-14123
    • Seeds, N.W.1    Basham, M.E.2    Haffke, S.P.3
  • 38
    • 0038297557 scopus 로고    scopus 로고
    • Tissue inhibitor of metalloproteinases-3 induces apoptosis in melanoma cells by stabilization of death receptors
    • Ahonen M, Poukkula M, Baker AH, Kashiwagi M, Nagase H, Eriksson JE, Kahari VM. Tissue inhibitor of metalloproteinases-3 induces apoptosis in melanoma cells by stabilization of death receptors. Oncogene. 2003;22:2121-34.
    • (2003) Oncogene , vol.22 , pp. 2121-2134
    • Ahonen, M.1    Poukkula, M.2    Baker, A.H.3    Kashiwagi, M.4    Nagase, H.5    Eriksson, J.E.6    Kahari, V.M.7
  • 40
    • 0344844997 scopus 로고    scopus 로고
    • Down-regulation of tissue inhibitor of matrix metalloprotease-1 (TIMP-1) in aged human skin contributes to matrix degradation and impaired cell growth and survival
    • Paris
    • Hornebeck W. Down-regulation of tissue inhibitor of matrix metalloprotease-1 (TIMP-1) in aged human skin contributes to matrix degradation and impaired cell growth and survival. Pathol Biol (Paris). 2003;51:569-73.
    • (2003) Pathol Biol , vol.51 , pp. 569-573
    • Hornebeck, W.1
  • 41
    • 0037192635 scopus 로고    scopus 로고
    • Complex roles of tissue inhibitors of metalloproteinases in cancer
    • Jiang Y, Goldberg ID, Shi YE. Complex roles of tissue inhibitors of metalloproteinases in cancer. Oncogene. 2002;21:2245-52.
    • (2002) Oncogene , vol.21 , pp. 2245-2252
    • Jiang, Y.1    Goldberg, I.D.2    Shi, Y.E.3
  • 43
    • 0029019867 scopus 로고
    • The gene structure of tissue inhibitor of metalloproteinases (TIMP)-3 and its inhibitory activities define the distinct TIMP gene family
    • Apte SS, Olsen BR, Murphy G. The gene structure of tissue inhibitor of metalloproteinases (TIMP)-3 and its inhibitory activities define the distinct TIMP gene family. J Biol Chem. 1995;270:14313-18.
    • (1995) J Biol Chem , vol.270 , pp. 14313-14318
    • Apte, S.S.1    Olsen, B.R.2    Murphy, G.3
  • 44
    • 0028244447 scopus 로고
    • Tissue inhibitor of metalloproteinases-3 (TIMP-3) is an extracellular matrix-associated protein with a distinctive pattern of expression in mouse cells and tissues
    • Leco KJ, Khokha R, Pavloff N, Hawkes SP, Edwards DR. Tissue inhibitor of metalloproteinases-3 (TIMP-3) is an extracellular matrix-associated protein with a distinctive pattern of expression in mouse cells and tissues. J Biol Chem. 1994;269:9352-60.
    • (1994) J Biol Chem , vol.269 , pp. 9352-9360
    • Leco, K.J.1    Khokha, R.2    Pavloff, N.3    Hawkes, S.P.4    Edwards, D.R.5
  • 45
    • 0030016342 scopus 로고    scopus 로고
    • The soluble catalytic domain of membrane type 1 matrix metalloproteinase cleaves the propeptide of progelatinase A and initiates autoproteolytic activation. Regulation by TIMP-2 and TIMP-3
    • Will H, Atkinson SJ, Butler GS, Smith B, Murphy G. The soluble catalytic domain of membrane type 1 matrix metalloproteinase cleaves the propeptide of progelatinase A and initiates autoproteolytic activation. Regulation by TIMP-2 and TIMP-3. J Biol Chem. 1996;271:17119-23.
    • (1996) J Biol Chem , vol.271 , pp. 17119-17123
    • Will, H.1    Atkinson, S.J.2    Butler, G.S.3    Smith, B.4    Murphy, G.5
  • 46
    • 0032101072 scopus 로고    scopus 로고
    • Adenovirus-mediated gene delivery of tissue inhibitor of metalloproteinases-3 inhibits invasion and induces apoptosis in melanoma cells
    • Ahonen M, Baker AH, Kahari VM. Adenovirus-mediated gene delivery of tissue inhibitor of metalloproteinases-3 inhibits invasion and induces apoptosis in melanoma cells. Cancer Res. 1998;58:2310-15.
    • (1998) Cancer Res , vol.58 , pp. 2310-2315
    • Ahonen, M.1    Baker, A.H.2    Kahari, V.M.3
  • 48
    • 0034737373 scopus 로고    scopus 로고
    • Developmental regulation of membrane type-5 matrix metalloproteinase (MT5-MMP) expression in the rat nervous system
    • Jaworski DM. Developmental regulation of membrane type-5 matrix metalloproteinase (MT5-MMP) expression in the rat nervous system. Brain Res. 2000;860:174-7.
    • (2000) Brain Res , vol.860 , pp. 174-177
    • Jaworski, D.M.1
  • 51
    • 0023807163 scopus 로고
    • Cytology and organization of rat cerebellar organ cultures
    • Jaeger CB, Kapoor R, Llinas R. Cytology and organization of rat cerebellar organ cultures. Neuroscience. 1988;26:509-38.
    • (1988) Neuroscience , vol.26 , pp. 509-538
    • Jaeger, C.B.1    Kapoor, R.2    Llinas, R.3
  • 52
    • 0030909239 scopus 로고    scopus 로고
    • Migration of granule neurons in cerebellar organorypic cultures is impaired by methylmercury
    • Kunimoto M, Suzuki T. Migration of granule neurons in cerebellar organorypic cultures is impaired by methylmercury. Neurosci Lett. 1997;226:183-6.
    • (1997) Neurosci Lett , vol.226 , pp. 183-186
    • Kunimoto, M.1    Suzuki, T.2
  • 53
    • 0036010813 scopus 로고    scopus 로고
    • Morphological study of organotypic cerebellar cultures
    • Takacs J, Metzger F. Morphological study of organotypic cerebellar cultures. Acta Biol Hung. 2002;53:187-204.
    • (2002) Acta Biol Hung , vol.53 , pp. 187-204
    • Takacs, J.1    Metzger, F.2
  • 54
    • 0028325047 scopus 로고
    • Observation of the highly organized development of granule cells in rat cerebellar organotypic cultures
    • Tanaka M, Tomita A, Yoshida S, Yano M, Shimizu H. Observation of the highly organized development of granule cells in rat cerebellar organotypic cultures. Brain Res. 1994;641:319-27.
    • (1994) Brain Res , vol.641 , pp. 319-327
    • Tanaka, M.1    Tomita, A.2    Yoshida, S.3    Yano, M.4    Shimizu, H.5
  • 55
    • 0023275590 scopus 로고    scopus 로고
    • Glial-guided granule neuron migration in vitro: A high-resolution time-lapse video microscopic study
    • Edmondson JC, Hatten ME. Glial-guided granule neuron migration in vitro: A high-resolution time-lapse video microscopic study. J Neurosci. 7:1928-34.
    • J Neurosci , vol.7 , pp. 1928-1934
    • Edmondson, J.C.1    Hatten, M.E.2
  • 56
    • 0035863132 scopus 로고    scopus 로고
    • Mode and tempo of tangential cell migration in the cerebellar external granular layer
    • Komuro H, Yacubova E, Yacubova E, Rakic P. Mode and tempo of tangential cell migration in the cerebellar external granular layer. J Neurosci. 2001;21:527-40.
    • (2001) J Neurosci , vol.21 , pp. 527-540
    • Komuro, H.1    Yacubova, E.2    Yacubova, E.3    Rakic, P.4
  • 57
    • 0032527889 scopus 로고    scopus 로고
    • Neuronal matrix metalloproteinase-2 degrades and inactivates a neurite-inhibiting chondroitin sulfate proteoglycan
    • Zuo J, Ferguson TA, Hernandez YJ, Stetler-Stevenson WG, Muir D. Neuronal matrix metalloproteinase-2 degrades and inactivates a neurite-inhibiting chondroitin sulfate proteoglycan. J Neurosci. 1998;18:5203-11.
    • (1998) J Neurosci , vol.18 , pp. 5203-5211
    • Zuo, J.1    Ferguson, T.A.2    Hernandez, Y.J.3    Stetler-Stevenson, W.G.4    Muir, D.5
  • 58
    • 0028913162 scopus 로고
    • The metalloproteinase stromelysin-1 (transin) mediates PC12 cell growth cone invasiveness through basal laminae
    • Nordstrom LA, Lochner J, Yeung W, Ciment G. The metalloproteinase stromelysin-1 (transin) mediates PC12 cell growth cone invasiveness through basal laminae. Mol Cell Neurosci. 1995;6:56-68.
    • (1995) Mol Cell Neurosci , vol.6 , pp. 56-68
    • Nordstrom, L.A.1    Lochner, J.2    Yeung, W.3    Ciment, G.4
  • 59
    • 0037107138 scopus 로고    scopus 로고
    • Metalloproteases and guidance of retinal axons in the developing visual system
    • Webber CA, Hocking JC, Yong VW, Stange CL, McFarlane S. Metalloproteases and guidance of retinal axons in the developing visual system. J Neurosci. 2002;22:8091-100.
    • (2002) J Neurosci , vol.22 , pp. 8091-8100
    • Webber, C.A.1    Hocking, J.C.2    Yong, V.W.3    Stange, C.L.4    McFarlane, S.5
  • 60
    • 0029930734 scopus 로고    scopus 로고
    • Role of neuron-glial junctional domain proteins in the maintenance and termination of neuronal migration across the embryonic cerebral wall
    • Anton ES, Cameron RS, Rakic P. Role of neuron-glial junctional domain proteins in the maintenance and termination of neuronal migration across the embryonic cerebral wall. J Neurosci. 1996;16:2283-93.
    • (1996) J Neurosci , vol.16 , pp. 2283-2293
    • Anton, E.S.1    Cameron, R.S.2    Rakic, P.3
  • 61
    • 0030722709 scopus 로고    scopus 로고
    • Developmental expression, pattern of distribution, and effect on cell aggregation implicate a neuron-glial junctional domain protein in neuronal migration
    • Cameron RS, Ruffin JW, Cho NK, Cameron PL, Rakic P. Developmental expression, pattern of distribution, and effect on cell aggregation implicate a neuron-glial junctional domain protein in neuronal migration. J Comp Neurol. 1997;387:467-88.
    • (1997) J Comp Neurol , vol.387 , pp. 467-488
    • Cameron, R.S.1    Ruffin, J.W.2    Cho, N.K.3    Cameron, P.L.4    Rakic, P.5
  • 62
    • 0025990092 scopus 로고
    • Astrotactin provides a receptor system for CNS neuronal migration
    • Fishell G, Hatten ME. Astrotactin provides a receptor system for CNS neuronal migration. Development. 1991;113:755-65.
    • (1991) Development , vol.113 , pp. 755-765
    • Fishell, G.1    Hatten, M.E.2
  • 63
    • 0027261511 scopus 로고
    • Multiple receptor systems promote CNS neural migration
    • Fishman RB, Hatten ME. Multiple receptor systems promote CNS neural migration. J Neurosci. 1993;13:3485-95.
    • (1993) J Neurosci , vol.13 , pp. 3485-3495
    • Fishman, R.B.1    Hatten, M.E.2
  • 64
    • 0032965534 scopus 로고    scopus 로고
    • Central nervous system neuronal migration
    • Hatten ME. Central nervous system neuronal migration. Annu Rev Neurosci. 1999;22:511-39.
    • (1999) Annu Rev Neurosci , vol.22 , pp. 511-539
    • Hatten, M.E.1
  • 65
    • 0038048005 scopus 로고    scopus 로고
    • Recent advances in cerebellar granule cell migration
    • Komuro H, Yacubova E. Recent advances in cerebellar granule cell migration. Cell Mol Life Sci. 2003;60:1084-98.
    • (2003) Cell Mol Life Sci , vol.60 , pp. 1084-1098
    • Komuro, H.1    Yacubova, E.2
  • 66
    • 0028944942 scopus 로고
    • Motility and cytoskeletal organization of migrating cerebellar granule neurons
    • Rivas RJ, Hatten ME. Motility and cytoskeletal organization of migrating cerebellar granule neurons. J Neurosci. 1995;15:981-9.
    • (1995) J Neurosci , vol.15 , pp. 981-989
    • Rivas, R.J.1    Hatten, M.E.2
  • 67
    • 0037101640 scopus 로고    scopus 로고
    • Intrinsic program for migration of cerebellar granule cells in vitro
    • Yacubova E, Komuro H. Intrinsic program for migration of cerebellar granule cells in vitro. J Neurosci. 2002;22:5966-81.
    • (2002) J Neurosci , vol.22 , pp. 5966-5981
    • Yacubova, E.1    Komuro, H.2
  • 68
    • 0029081738 scopus 로고
    • Degradation of vitronectin by matrix metalloproteinases-1, -2, -3, -7 and -9
    • Imai K, Shikata H, Okada Y. Degradation of vitronectin by matrix metalloproteinases-1, -2, -3, -7 and -9. FEBS Lett. 1995;369:249-51.
    • (1995) FEBS Lett , vol.369 , pp. 249-251
    • Imai, K.1    Shikata, H.2    Okada, Y.3
  • 69
    • 0029959437 scopus 로고    scopus 로고
    • Matrix metalloproteinase 2 releases active soluble ectodomain of fibroblast growth factor receptor 1
    • USA
    • Levi E, Fridman R, Miao HQ, Ma YS, Yayon A, Vlodavsky I. Matrix metalloproteinase 2 releases active soluble ectodomain of fibroblast growth factor receptor 1. Proc Natl Acad Sci USA. 1996;93:7069-74.
    • (1996) Proc Natl Acad Sci , vol.93 , pp. 7069-7074
    • Levi, E.1    Fridman, R.2    Miao, H.Q.3    Ma, Y.S.4    Yayon, A.5    Vlodavsky, I.6
  • 70
    • 0034650486 scopus 로고    scopus 로고
    • Cell surface-localized matrix metalloproteinase-9 proteolytically activates TGF-beta and promotes tumor invasion and angiogenesis
    • Yu Q, Stamenkovic I. Cell surface-localized matrix metalloproteinase-9 proteolytically activates TGF-beta and promotes tumor invasion and angiogenesis. Genes Dev. 2000;14:163-76.
    • (2000) Genes Dev , vol.14 , pp. 163-176
    • Yu, Q.1    Stamenkovic, I.2
  • 71
    • 9544231789 scopus 로고    scopus 로고
    • Astrocytes promote process outgrowth by adult human oligodendrocytes in vitro through interaction between bFGF and astrocyte extracellular matrix
    • Oh LY, Yong VW. Astrocytes promote process outgrowth by adult human oligodendrocytes in vitro through interaction between bFGF and astrocyte extracellular matrix. Glia. 1996;17:237-53.
    • (1996) Glia , vol.17 , pp. 237-253
    • Oh, L.Y.1    Yong, V.W.2
  • 72
    • 0029906468 scopus 로고    scopus 로고
    • Glioma invasion in vitro: Regulation by matrix metalloprotease-2 and protein kinase C
    • Uhm JH, Dooley NP, Villemure JG, Yong VW. Glioma invasion in vitro: Regulation by matrix metalloprotease-2 and protein kinase C. Clin Exp Metastasis. 1996;14:421-33.
    • (1996) Clin Exp Metastasis , vol.14 , pp. 421-433
    • Uhm, J.H.1    Dooley, N.P.2    Villemure, J.G.3    Yong, V.W.4
  • 73
    • 0020626162 scopus 로고
    • Alterations in the postnatal development of the cerebellar cortex due to zinc deficiency. I. Impaired acquisition of granule cells
    • Dvergsten CL, Fosmire GJ, Ollerich DA, Sandstead HH. Alterations in the postnatal development of the cerebellar cortex due to zinc deficiency. I. Impaired acquisition of granule cells. Brain Res. 1983;271:217-26.
    • (1983) Brain Res , vol.271 , pp. 217-226
    • Dvergsten, C.L.1    Fosmire, G.J.2    Ollerich, D.A.3    Sandstead, H.H.4
  • 74
    • 0022921106 scopus 로고
    • Effects of methylmercury on the morphogenesis of the rat cerebellum
    • Howard JD, Mottet NK. Effects of methylmercury on the morphogenesis of the rat cerebellum. Teratology. 1986;34:89-95.
    • (1986) Teratology , vol.34 , pp. 89-95
    • Howard, J.D.1    Mottet, N.K.2
  • 75
    • 0019992233 scopus 로고
    • Effects of methylmercury on developing mouse cerebellar cortex
    • Sager PR, Doherty RA, Rodier PM. Effects of methylmercury on developing mouse cerebellar cortex. Exp Neurol. 1982;77:179-93.
    • (1982) Exp Neurol , vol.77 , pp. 179-193
    • Sager, P.R.1    Doherty, R.A.2    Rodier, P.M.3
  • 76
    • 0034156663 scopus 로고    scopus 로고
    • Inhibition of human gingival gelatinases (MMP-2 and MMP-9) by metal salts
    • de Souza AP, Gerlach RF, Line SR. Inhibition of human gingival gelatinases (MMP-2 and MMP-9) by metal salts. Dent Mater. 2000;16:103-08.
    • (2000) Dent Mater , vol.16 , pp. 103-108
    • De Souza, A.P.1    Gerlach, R.F.2    Line, S.R.3
  • 77
    • 0018666035 scopus 로고
    • A latent gelatin specific proteinase of human leucocytes and its activation
    • Sopata I, Wize J. A latent gelatin specific proteinase of human leucocytes and its activation. Biochim Biophys Acta. 1979;571:305-12.
    • (1979) Biochim Biophys Acta , vol.571 , pp. 305-312
    • Sopata, I.1    Wize, J.2


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