메뉴 건너뛰기




Volumn 23, Issue 1-2, 1997, Pages 1-27

Laminin and the mechanism of neuronal outgrowth

Author keywords

Alzheimer's disease; growth cone; integrin receptor; laminin; laminin isoform; nerve regeneration; neuronal pathfinding; synapse formation

Indexed keywords

INTEGRIN; LAMININ;

EID: 0031053932     PISSN: 01650173     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0165-0173(96)00013-6     Document Type: Review
Times cited : (230)

References (98)
  • 1
    • 0028895717 scopus 로고
    • Absence of persistent spreading, branching, and adhesion in GAP-43-depleted growth cones
    • Aigner, L. and Caroni, P., Absence of persistent spreading, branching, and adhesion in GAP-43-depleted growth cones, J. Cell Biol., 128 (1995) 647-660.
    • (1995) J. Cell Biol. , vol.128 , pp. 647-660
    • Aigner, L.1    Caroni, P.2
  • 2
    • 0027970388 scopus 로고
    • Characterization of neural cell adhesion sites: Point contacts are the sites of interaction between integrins and the cytoskeleton in PC12 cells
    • Arregui, C.O., Carbonetto, S.T. and McKerracher, L., Characterization of neural cell adhesion sites: point contacts are the sites of interaction between integrins and the cytoskeleton in PC12 cells, J. Neurosci., 14 (1994) 6967-6977.
    • (1994) J. Neurosci. , vol.14 , pp. 6967-6977
    • Arregui, C.O.1    Carbonetto, S.T.2    McKerracher, L.3
  • 3
    • 0026732964 scopus 로고
    • LBL, a novel, developmental regulated, laminin-binding lectin
    • Bao, Z.-z., Muschler, J. and Horwitz, A., LBL, a novel, developmental regulated, laminin-binding lectin, J. Biol. Chem., 267 (1992) 4974-4980.
    • (1992) J. Biol. Chem. , vol.267 , pp. 4974-4980
    • Bao, Z.-Z.1    Muschler, J.2    Horwitz, A.3
  • 4
    • 0026703151 scopus 로고
    • Basement-membrane heparan sulfate proteoglycan binds to laminin by its heparan sulfate chains and to nidogen by sites in the protein core
    • Battaglia, C., Mayer, U., Aumailley, M. and Timpl, R., Basement-membrane heparan sulfate proteoglycan binds to laminin by its heparan sulfate chains and to nidogen by sites in the protein core, Eur. J. Biochem., 208 (1992) 359-366.
    • (1992) Eur. J. Biochem. , vol.208 , pp. 359-366
    • Battaglia, C.1    Mayer, U.2    Aumailley, M.3    Timpl, R.4
  • 5
    • 0025165018 scopus 로고
    • Structure and function of laminin: Anatomy of a multidomain glycoprotein
    • Beck, K., Hunter, I. and Engel, J., Structure and function of laminin: anatomy of a multidomain glycoprotein, FASEB J., 4 (1990) 149-160.
    • (1990) FASEB J. , vol.4 , pp. 149-160
    • Beck, K.1    Hunter, I.2    Engel, J.3
  • 6
    • 0025774515 scopus 로고
    • Laminin fragment E8 mediates PC12 cell neurite outgrowth by binding to cell surface β1,4 galactosyltransferase
    • Begovac, P.C., Hall, D.E. and Shur, B.D., Laminin fragment E8 mediates PC12 cell neurite outgrowth by binding to cell surface β1,4 galactosyltransferase, J. Cell Biol., 113 (1991) 37-644.
    • (1991) J. Cell Biol. , vol.113 , pp. 37-644
    • Begovac, P.C.1    Hall, D.E.2    Shur, B.D.3
  • 7
    • 0025019504 scopus 로고
    • Cell surface galactosyltransferase mediates the initiation of neurite outgrowth from PC12 cells on laminin
    • Begovac, P.C. and Shur, B.D., Cell surface galactosyltransferase mediates the initiation of neurite outgrowth from PC12 cells on laminin, J. Cell Biol., 110 (1991) 461-470.
    • (1991) J. Cell Biol. , vol.110 , pp. 461-470
    • Begovac, P.C.1    Shur, B.D.2
  • 8
    • 0027953386 scopus 로고
    • A role for extracellular matrix degradation and matrix metalloproteinases in senile dementia?
    • Bignami, A., LeBlanc, A. and Perides, G., A role for extracellular matrix degradation and matrix metalloproteinases in senile dementia? Acta Neuropathol. (Berl.), 87 (1994) 308-312.
    • (1994) Acta Neuropathol. (Berl.) , vol.87 , pp. 308-312
    • Bignami, A.1    LeBlanc, A.2    Perides, G.3
  • 9
    • 0024727218 scopus 로고
    • Protein kinase C is involved in laminin stimulation of neurite outgrowth
    • Bixby, J.L., Protein kinase C is involved in laminin stimulation of neurite outgrowth, Neuron, 3 (1989) 287-297.
    • (1989) Neuron , vol.3 , pp. 287-297
    • Bixby, J.L.1
  • 10
    • 0028170989 scopus 로고
    • 2+ influx and neurite growth in response to purified N-cadherin and laminin
    • 2+ influx and neurite growth in response to purified N-cadherin and laminin, J. Cell Biol., 127 (1994) 1461-1475.
    • (1994) J. Cell Biol. , vol.127 , pp. 1461-1475
    • Bixby, J.L.1    Grunwald, G.B.2    Bookman, R.J.3
  • 11
    • 0025768412 scopus 로고
    • Quantitative effects of laminin concentration on neurite outgrowth in vitro
    • Buettner, H.M. and Pittman, R.N., Quantitative effects of laminin concentration on neurite outgrowth in vitro, Dev. Biol., 145 (1991) 266-276.
    • (1991) Dev. Biol. , vol.145 , pp. 266-276
    • Buettner, H.M.1    Pittman, R.N.2
  • 12
    • 0029034002 scopus 로고
    • Growth cones are actively influenced by substrate-bound adhesion molecules
    • Burden-Gulley, S.M., Payne, H.R. and Lemmon, V., Growth cones are actively influenced by substrate-bound adhesion molecules, J. Neurosci., 15 (1995) 4370-4381.
    • (1995) J. Neurosci. , vol.15 , pp. 4370-4381
    • Burden-Gulley, S.M.1    Payne, H.R.2    Lemmon, V.3
  • 14
    • 0027991270 scopus 로고
    • Domain-specific activation of neuronal migration and neurite outgrowth-promoting activities of laminin
    • Calof, A.L., Campanero, M.R., O'Rear, J.J., Yurchenco, P.D. and Lander, A.D., Domain-specific activation of neuronal migration and neurite outgrowth-promoting activities of laminin, Neuron, 13 (1994) 117-130.
    • (1994) Neuron , vol.13 , pp. 117-130
    • Calof, A.L.1    Campanero, M.R.2    O'Rear, J.J.3    Yurchenco, P.D.4    Lander, A.D.5
  • 15
    • 0018348001 scopus 로고
    • Properties of a basement membrane-related glycoprotein synthesized in culture by a mouse embryonal carcinoma-derived cell line
    • Chung, A.E., Jaffe, R., Freeman, I.L., Vergnes, J.P., Braginski, J.E. and Carlin, B., Properties of a basement membrane-related glycoprotein synthesized in culture by a mouse embryonal carcinoma-derived cell line, Cell, 16 (1979) 277-287.
    • (1979) Cell , vol.16 , pp. 277-287
    • Chung, A.E.1    Jaffe, R.2    Freeman, I.L.3    Vergnes, J.P.4    Braginski, J.E.5    Carlin, B.6
  • 16
    • 0027286636 scopus 로고
    • Growth cone guidance and neuron morphology on micropatterned laminin surfaces
    • Clark, P., Britland, S. and Connolly, P., Growth cone guidance and neuron morphology on micropatterned laminin surfaces, J. Cell Sci., 105 (1993) 203-212.
    • (1993) J. Cell Sci. , vol.105 , pp. 203-212
    • Clark, P.1    Britland, S.2    Connolly, P.3
  • 17
    • 0028952738 scopus 로고
    • Mapping of network-forming, heparin-binding, and α1β1 integrin-recognition sites within the α-chain short arm of laminin-1
    • Colognato-Pyke, H., O'Rear, J.J., Yamada, Y., Carbonetto, S., Cheng, Y.-S. and Yurchenco, P.D., Mapping of network-forming, heparin-binding, and α1β1 integrin-recognition sites within the α-chain short arm of laminin-1, J. Biol. Chem., 270 (1995) 9398-9406.
    • (1995) J. Biol. Chem. , vol.270 , pp. 9398-9406
    • Colognato-Pyke, H.1    O'Rear, J.J.2    Yamada, Y.3    Carbonetto, S.4    Cheng, Y.-S.5    Yurchenco, P.D.6
  • 18
    • 0029931978 scopus 로고    scopus 로고
    • Perlecan and basement membrane-chondroitin sulfate proteoglycan (bamacan) are two basement membrane chondroitin-dermatan sulfate proteoglycans in the Engelbreth-Holm-Swarm Tumor matrix
    • Couchman, J.R., Kapoor, R., Sthanam, M. and Wu, R.-R., Perlecan and basement membrane-chondroitin sulfate proteoglycan (bamacan) are two basement membrane chondroitin-dermatan sulfate proteoglycans in the Engelbreth-Holm-Swarm Tumor matrix, J. Biol. Chem., 271 (1996) 9595-9602.
    • (1996) J. Biol. Chem. , vol.271 , pp. 9595-9602
    • Couchman, J.R.1    Kapoor, R.2    Sthanam, M.3    Wu, R.-R.4
  • 19
    • 0025289776 scopus 로고
    • A biological role of the carbohydrate moieties of laminin
    • Dean III, J.W., Chandrasekaran, S. and Tanzer, M.L., A biological role of the carbohydrate moieties of laminin, J. Biol. Chem., 265 (1990) 12553-12562.
    • (1990) J. Biol. Chem. , vol.265 , pp. 12553-12562
    • Dean J.W. III1    Chandrasekaran, S.2    Tanzer, M.L.3
  • 20
    • 0025315789 scopus 로고
    • Cell adhesion, spreading and neurite stimulation by laminin fragment E8 depends on maintenance of secondary and tertiary structure in its rod and globular domain
    • Deutzmann, R. Aumailley, M., Wiedemann, H., Pysny, W., Timpl, R. and Edgar, D., Cell adhesion, spreading and neurite stimulation by laminin fragment E8 depends on maintenance of secondary and tertiary structure in its rod and globular domain, Eur. J. Biochem., 191 (1990) 513-522.
    • (1990) Eur. J. Biochem. , vol.191 , pp. 513-522
    • Deutzmann, R.1    Aumailley, M.2    Wiedemann, H.3    Pysny, W.4    Timpl, R.5    Edgar, D.6
  • 21
    • 0026271943 scopus 로고
    • The expression and distribution of laminin in the developing nervous system
    • Edgar, D., The expression and distribution of laminin in the developing nervous system, J. Cell Sci., 15 (1991) 9-12.
    • (1991) J. Cell Sci. , vol.15 , pp. 9-12
    • Edgar, D.1
  • 22
    • 0027261511 scopus 로고
    • Multiple receptor systems promote CNS neural migration
    • Fishman, R.B. and Hatten, M.B., Multiple receptor systems promote CNS neural migration, J. Neurosci., 13 (1993) 3485-3495.
    • (1993) J. Neurosci. , vol.13 , pp. 3485-3495
    • Fishman, R.B.1    Hatten, M.B.2
  • 23
    • 0027321171 scopus 로고
    • Laminin-binding protein 120 from brain is closely related to the dystrophin-associated glycoprotein, dystroglycan, and binds with high affinity to the major heparin binding domain of laminin
    • Gee, S.H., Blacher, R.W., Douville, P.J., Provost, P.R., Yurchenco, P.D. and Carbonetto, S., Laminin-binding protein 120 from brain is closely related to the dystrophin-associated glycoprotein, dystroglycan, and binds with high affinity to the major heparin binding domain of laminin, J. Biol. Chem., 268 (1993) 14972-14980.
    • (1993) J. Biol. Chem. , vol.268 , pp. 14972-14980
    • Gee, S.H.1    Blacher, R.W.2    Douville, P.J.3    Provost, P.R.4    Yurchenco, P.D.5    Carbonetto, S.6
  • 24
    • 0028124120 scopus 로고
    • Filopodia initiate choices made by sensory neuron growth cones at laminin/fibronectin borders in vitro
    • Gomez, T.M. and Letourneau, P.C., Filopodia initiate choices made by sensory neuron growth cones at laminin/fibronectin borders in vitro, J. Neurosci., 14 (1994) 5959-5972.
    • (1994) J. Neurosci. , vol.14 , pp. 5959-5972
    • Gomez, T.M.1    Letourneau, P.C.2
  • 25
    • 0024244115 scopus 로고
    • Interference reflection microscopic study of dorsal root growth cones on different substrates: Assessment of growth cone-substrate contacts
    • Gundersen, R.W., Interference reflection microscopic study of dorsal root growth cones on different substrates: assessment of growth cone-substrate contacts, J. Neurosci. Res., 21 (1988) 298-306.
    • (1988) J. Neurosci. Res. , vol.21 , pp. 298-306
    • Gundersen, R.W.1
  • 26
    • 0024812992 scopus 로고
    • Laminin-like antigen in rat CNS neurons: Distribution and changes upon brain injury and nerve growth factor treatment
    • Hagg, T., Muir, D., Engvall, E., Varon, S. and Manthorpe, M., Laminin-like antigen in rat CNS neurons: distribution and changes upon brain injury and nerve growth factor treatment, Neuron, 3 (1989) 721-732.
    • (1989) Neuron , vol.3 , pp. 721-732
    • Hagg, T.1    Muir, D.2    Engvall, E.3    Varon, S.4    Manthorpe, M.5
  • 27
    • 0029118206 scopus 로고
    • Laminin β2 (S-laminin): A new player at the synapse
    • Hall, Z.W., Laminin β2 (S-laminin): a new player at the synapse, Science, 269 (1995) 362-363.
    • (1995) Science , vol.269 , pp. 362-363
    • Hall, Z.W.1
  • 28
    • 0023872779 scopus 로고
    • Growth cone guidance by substrate-bound laminin pathways is correlated with neuron-to-pathway adhesivity
    • Hammarback, J.A., McCarthy, J.B., Palm, S.K., Furcht, L.T. and Letourneau, P.C., Growth cone guidance by substrate-bound laminin pathways is correlated with neuron-to-pathway adhesivity, Dev. Biol., 126 (1988) 29-39.
    • (1988) Dev. Biol. , vol.126 , pp. 29-39
    • Hammarback, J.A.1    McCarthy, J.B.2    Palm, S.K.3    Furcht, L.T.4    Letourneau, P.C.5
  • 29
    • 0028027046 scopus 로고
    • Nature and the multiple functions of the 67-kD elastin-/laminin binding protein
    • Hinek, A., Nature and the multiple functions of the 67-kD elastin-/laminin binding protein, Cell Adhes. Commun., 2 (1994) 185-193.
    • (1994) Cell Adhes. Commun. , vol.2 , pp. 185-193
    • Hinek, A.1
  • 30
    • 0027465951 scopus 로고
    • Expression of laminin isoforms by peripheral nerve-derived connectice tissue cells in culture. Comparison with epitope distribution in normal human nerve and neural tumors in vivo
    • Hsiao, L.L., Engvall, E., Peltonen, J. and Uitto, J., Expression of laminin isoforms by peripheral nerve-derived connectice tissue cells in culture. Comparison with epitope distribution in normal human nerve and neural tumors in vivo, Lab. Invest., 68 (1993) 100-108.
    • (1993) Lab. Invest. , vol.68 , pp. 100-108
    • Hsiao, L.L.1    Engvall, E.2    Peltonen, J.3    Uitto, J.4
  • 31
    • 0026788499 scopus 로고
    • Expression of S-laminin and laminin in the developing rat central nervous system
    • Hunter, D.D., Llinas, R., Ard, M., Merlie J.P. and Sanes J.R., Expression of S-laminin and laminin in the developing rat central nervous system, J. Comp. Neurol., 323 (1992) 238-251.
    • (1992) J. Comp. Neurol. , vol.323 , pp. 238-251
    • Hunter, D.D.1    Llinas, R.2    Ard, M.3    Merlie, J.P.4    Sanes, J.R.5
  • 32
    • 0025807619 scopus 로고
    • Distinct immunoreactivity to 110 kDa laminin-binding protein in adult and lesioned rat forebrain
    • Jucker, M., Kleinman, H.K., Höhmann, C., Ordy, J.M. and Ingram, D.K., Distinct immunoreactivity to 110 kDa laminin-binding protein in adult and lesioned rat forebrain, Brain Res., 555 (1991) 305-312.
    • (1991) Brain Res. , vol.555 , pp. 305-312
    • Jucker, M.1    Kleinman, H.K.2    Höhmann, C.3    Ordy, J.M.4    Ingram, D.K.5
  • 35
    • 0020360978 scopus 로고
    • Isolation and characterization of type IV procollagen, laminin, and heparan sulfate proteoglycan from the EHS Sarcoma
    • Kleinman, H.K., McGarvey, M.L., Liotta, L.A., Robey, P.G., Tryggvason, K. and Martin, G.R., Isolation and characterization of type IV procollagen, laminin, and heparan sulfate proteoglycan from the EHS Sarcoma, Biochemistry, 24 (1982) 6188-6193.
    • (1982) Biochemistry , vol.24 , pp. 6188-6193
    • Kleinman, H.K.1    McGarvey, M.L.2    Liotta, L.A.3    Robey, P.G.4    Tryggvason, K.5    Martin, G.R.6
  • 37
    • 0025694881 scopus 로고
    • Developmental loss of laminin from the interstitial extracellular matrix correlates with decreased laminin gene expression
    • Kücherer-Ehret, A., Pottgiesser, J., Kreutzberg, G.W., Thoenen, H. and Edgar, D., Developmental loss of laminin from the interstitial extracellular matrix correlates with decreased laminin gene expression, Development, 110 (1990) 1285-1283.
    • (1990) Development , vol.110 , pp. 1285-11283
    • Kücherer-Ehret, A.1    Pottgiesser, J.2    Kreutzberg, G.W.3    Thoenen, H.4    Edgar, D.5
  • 38
    • 0025181679 scopus 로고
    • Immunoelectron microscopic localization of laminin in normal and regenerating mouse sciatic nerve
    • Kuecherer-Ehret, A., Graeber, M.B., Edgar, D., Thoenen, H. and Kreutzberg, G.W., Immunoelectron microscopic localization of laminin in normal and regenerating mouse sciatic nerve, J. Neurocytol., 19 (1990) 101-109.
    • (1990) J. Neurocytol. , vol.19 , pp. 101-109
    • Kuecherer-Ehret, A.1    Graeber, M.B.2    Edgar, D.3    Thoenen, H.4    Kreutzberg, G.W.5
  • 39
    • 0028872784 scopus 로고
    • Laminin and fibronectin guideposts signal sustained but opposite effects to passing growth cones
    • Kuhn, T.B., Schmidt, M.F. and Kater, S.B., Laminin and fibronectin guideposts signal sustained but opposite effects to passing growth cones, Neuron, 14 (1995) 275-285.
    • (1995) Neuron , vol.14 , pp. 275-285
    • Kuhn, T.B.1    Schmidt, M.F.2    Kater, S.B.3
  • 40
    • 0028247142 scopus 로고
    • Differential laminin gene expression in dorsal root ganglion neurons and nonneuronal cells
    • LeBeau, J.M., Liuzzi, F.J., Depto, A.S. and Vinik, A.I., Differential laminin gene expression in dorsal root ganglion neurons and nonneuronal cells, Exp. Neurol., 127 (1994) 1-8.
    • (1994) Exp. Neurol. , vol.127 , pp. 1-8
    • LeBeau, J.M.1    Liuzzi, F.J.2    Depto, A.S.3    Vinik, A.I.4
  • 41
    • 0026733686 scopus 로고
    • Laminin selectively enhances axonal growth accelerates the development of polarity by hippocampal neurons in culture
    • Lein, P.J., Banker, G.A. and Higgins, D., Laminin selectively enhances axonal growth accelerates the development of polarity by hippocampal neurons in culture, Dev. Brain Res., 69 (1992) 191-197.
    • (1992) Dev. Brain Res. , vol.69 , pp. 191-197
    • Lein, P.J.1    Banker, G.A.2    Higgins, D.3
  • 42
    • 0026538274 scopus 로고
    • Neurite growth on different substrates: Permissive versus instructive influences and the role of adhesive strength
    • Lemmon, V., Burden, S.M., Payne, H.R., Elmslie, G.J. and Hlavin, M.L., Neurite growth on different substrates: permissive versus instructive influences and the role of adhesive strength, J. Neurosci., 12 (1992) 818-826.
    • (1992) J. Neurosci. , vol.12 , pp. 818-826
    • Lemmon, V.1    Burden, S.M.2    Payne, H.R.3    Elmslie, G.J.4    Hlavin, M.L.5
  • 43
    • 0016736768 scopus 로고
    • Cell-to-substratum adhesion and guidance of axonal elongation
    • Letourneau, P.C., Cell-to-substratum adhesion and guidance of axonal elongation, Dev. Biol., 44 (1975) 92-101.
    • (1975) Dev. Biol. , vol.44 , pp. 92-101
    • Letourneau, P.C.1
  • 44
    • 0023884099 scopus 로고
    • Immunoreactivity for laminin in the developing ventral longitudinal pathway of the brain
    • Letourneau, P.C., Madsen, A.M., Palm, S.L. and Furcht, L.T., Immunoreactivity for laminin in the developing ventral longitudinal pathway of the brain, Dev. Biol., 125 (1988) 135-144.
    • (1988) Dev. Biol. , vol.125 , pp. 135-144
    • Letourneau, P.C.1    Madsen, A.M.2    Palm, S.L.3    Furcht, L.T.4
  • 45
    • 0022069874 scopus 로고
    • Do neurons in the vertebrate CNS migrate on laminin?
    • Liese, P., Do neurons in the vertebrate CNS migrate on laminin? EMBO J., 4 (1985) 1163-1170.
    • (1985) EMBO J. , vol.4 , pp. 1163-1170
    • Liese, P.1
  • 46
    • 0025054217 scopus 로고
    • Extracellular matrix and neuronal movement
    • Liesi, P., Extracellular matrix and neuronal movement, Experientia, 46 (1990) 900-907.
    • (1990) Experientia , vol.46 , pp. 900-907
    • Liesi, P.1
  • 47
    • 0026637886 scopus 로고
    • Neuronal migration on laminin involves neuronal contact formation followed by nuclear migration inside a preformed process
    • Liesi, P., Neuronal migration on laminin involves neuronal contact formation followed by nuclear migration inside a preformed process, Exp. Neurobiol., 111 (1992) 103-113.
    • (1992) Exp. Neurobiol. , vol.111 , pp. 103-113
    • Liesi, P.1
  • 48
    • 0028795727 scopus 로고
    • Domain-specific antibodies against the B2 chain of laminin inhibit neuronal migration in the neonatal rat cerebellum
    • Liesi, P., Hager, G., Dodt, H.U., Seppala, I. and Zieglgansberger, W., Domain-specific antibodies against the B2 chain of laminin inhibit neuronal migration in the neonatal rat cerebellum, J. Neurosci. Res., 40 (1995) 199-206.
    • (1995) J. Neurosci. Res. , vol.40 , pp. 199-206
    • Liesi, P.1    Hager, G.2    Dodt, H.U.3    Seppala, I.4    Zieglgansberger, W.5
  • 49
    • 0024375009 scopus 로고
    • Glial cells of mammalizn brain produce a variant form of laminin
    • Liesi, P. and Risteli, L., Glial cells of mammalizn brain produce a variant form of laminin, Exp. Neurol., 105 (1989) 86-92.
    • (1989) Exp. Neurol. , vol.105 , pp. 86-92
    • Liesi, P.1    Risteli, L.2
  • 50
    • 0024203038 scopus 로고
    • Is astrocyte laminin involved in axon guidance in the mammalian CNS?
    • Liesi, P. and Silver, J., Is astrocyte laminin involved in axon guidance in the mammalian CNS? Dev. Biol., 130 (1988) 774-785.
    • (1988) Dev. Biol. , vol.130 , pp. 774-785
    • Liesi, P.1    Silver, J.2
  • 51
    • 0027235994 scopus 로고
    • Tenascin and extracellular matrix glycoproteins: From promotion to polarization of neurite growth in vitro
    • Lochter, A. and Schachner, M., Tenascin and extracellular matrix glycoproteins: from promotion to polarization of neurite growth in vitro, J. Neurosci., 13 (1993) 3986-4000.
    • (1993) J. Neurosci. , vol.13 , pp. 3986-4000
    • Lochter, A.1    Schachner, M.2
  • 52
    • 0028798529 scopus 로고
    • Localization of the 110 kDa receptor for laminin in brains of embryonic and postnatal mice
    • Luckenbill-Edds, L., Kaiser, C.A., Rodgers, T.R. and Powell, D.D., Localization of the 110 kDa receptor for laminin in brains of embryonic and postnatal mice, Cell Tiss. Res., 279 (1995) 371-377.
    • (1995) Cell Tiss. Res. , vol.279 , pp. 371-377
    • Luckenbill-Edds, L.1    Kaiser, C.A.2    Rodgers, T.R.3    Powell, D.D.4
  • 53
    • 0023118128 scopus 로고
    • Peripheral nerve regeneration with entubulation repair: Comparison of biodegradeable nerve guides versus polyethylene tubes and the effects of a laminin-containing gel
    • Madison, R.D., Da Silva, C.F., Dikkes, P., Sidman, R.L. and Chiu T., Peripheral nerve regeneration with entubulation repair: comparison of biodegradeable nerve guides versus polyethylene tubes and the effects of a laminin-containing gel, Exp. Neurol., 95 (1987) 378-390.
    • (1987) Exp. Neurol. , vol.95 , pp. 378-390
    • Madison, R.D.1    Da Silva, C.F.2    Dikkes, P.3    Sidman, R.L.4    Chiu, T.5
  • 54
    • 0029122801 scopus 로고
    • A synaptic localization domain in the synaptic cleft protein laminin β2 (S-laminin)
    • Martin, P.T., Ettinger, A.J. and Sanes, J.R., A synaptic localization domain in the synaptic cleft protein laminin β2 (S-laminin), Science, 269 (1995) 413-416.
    • (1995) Science , vol.269 , pp. 413-416
    • Martin, P.T.1    Ettinger, A.J.2    Sanes, J.R.3
  • 55
    • 0028121111 scopus 로고
    • Expression and functional roles of neural cell surface molecules and extracellular matrix components during development and regeneration of peripheral nerves
    • Martini, R., Expression and functional roles of neural cell surface molecules and extracellular matrix components during development and regeneration of peripheral nerves, J. Neurocytol., 23 (1994) 1-28.
    • (1994) J. Neurocytol. , vol.23 , pp. 1-28
    • Martini, R.1
  • 56
    • 0026093621 scopus 로고
    • Receptors for laminin on mammalian cells
    • Mecham, R.P., Receptors for laminin on mammalian cells, FASEB J., 5 (1991) 2538-2546.
    • (1991) FASEB J. , vol.5 , pp. 2538-2546
    • Mecham, R.P.1
  • 57
    • 0024454709 scopus 로고
    • The elastin receptor shows structural and functional similarities to the 67-kDa tumor cell laminin receptor
    • Mecham, R.P., Hinek, A., Griffin, G.L., Senior, R.M. and Liotta, L.A., The elastin receptor shows structural and functional similarities to the 67-kDa tumor cell laminin receptor, J. Biol. Chem., 264 (1989) 16652-16657.
    • (1989) J. Biol. Chem. , vol.264 , pp. 16652-16657
    • Mecham, R.P.1    Hinek, A.2    Griffin, G.L.3    Senior, R.M.4    Liotta, L.A.5
  • 58
    • 0025805986 scopus 로고
    • Ligand affinity of the 67-kD elastin/laminin binding protein is modulated by the protein's lectin domain: Visualization of elastin/laminin-receptor complexes with gold-tagged ligands
    • Mecham, R.P., Ligand affinity of the 67-kD elastin/laminin binding protein is modulated by the protein's lectin domain: visualization of elastin/laminin-receptor complexes with gold-tagged ligands, J. Cell Biol., 113 (1991) 187-194.
    • (1991) J. Cell Biol. , vol.113 , pp. 187-194
    • Mecham, R.P.1
  • 59
    • 0025924138 scopus 로고
    • 1 72,000 cell surface concanavalin A binding glycoprotein is specifically involved in the spreading of chick embryo fibroblasts onto laminin substrate
    • 1 72,000 cell surface concanavalin A binding glycoprotein is specifically involved in the spreading of chick embryo fibroblasts onto laminin substrate, Exp. Cell. Res., 192 (1991) 236-242.
    • (1991) Exp. Cell. Res. , vol.192 , pp. 236-242
    • Moutsita, R.1    Aubery, M.2    Codogno, P.3
  • 60
    • 0026716274 scopus 로고
    • Laminin and its neurite outgrowth-promoting domain in the brain in Alzheimer's disease and Down's syndrome patients
    • Murtomäki, S., Risteli, L., Koivisto, U., Johansson, S. and Liesi, P., Laminin and its neurite outgrowth-promoting domain in the brain in Alzheimer's disease and Down's syndrome patients, J. Neurosci., 32 (1992) 261-273.
    • (1992) J. Neurosci. , vol.32 , pp. 261-273
    • Murtomäki, S.1    Risteli, L.2    Koivisto, U.3    Johansson, S.4    Liesi, P.5
  • 62
    • 0027942507 scopus 로고
    • Assembly of synthetic laminin peptides into a triple-stranded coiled-coil structure
    • Nomizu, M., Otaka, A., Utani, A., Roller, P.P. and Yamada, Y., Assembly of synthetic laminin peptides into a triple-stranded coiled-coil structure, J. Biol. Chem., 269 (1994) 30386-30392.
    • (1994) J. Biol. Chem. , vol.269 , pp. 30386-30392
    • Nomizu, M.1    Otaka, A.2    Utani, A.3    Roller, P.P.4    Yamada, Y.5
  • 63
    • 0029566272 scopus 로고
    • Galectin-3 binding potentials of mouse tumor EHS and human placental laminins
    • Ochieng, J. and Warfield, P., Galectin-3 binding potentials of mouse tumor EHS and human placental laminins, Biochem. Biophys. Res. Commun., 217 (1995) 402-406.
    • (1995) Biochem. Biophys. Res. Commun. , vol.217 , pp. 402-406
    • Ochieng, J.1    Warfield, P.2
  • 64
    • 0026332789 scopus 로고
    • Association between vascular basement membrane components and the lesions of Alzheimer's disease
    • Perlmutter, L.S., Barrón, E., Saperia, D. and Chui, H.C., Association between vascular basement membrane components and the lesions of Alzheimer's disease, J. Neurosci. Res., 30 (1991) 673-681.
    • (1991) J. Neurosci. Res. , vol.30 , pp. 673-681
    • Perlmutter, L.S.1    Barrón, E.2    Saperia, D.3    Chui, H.C.4
  • 65
    • 0028920977 scopus 로고
    • A mononeuron-selective stop signal in the synaptic protein S-laminin
    • Porter, B.E., Weis, J. and Sanes, J.R., A mononeuron-selective stop signal in the synaptic protein S-laminin, Neuron, 14 (1995) 549-559.
    • (1995) Neuron , vol.14 , pp. 549-559
    • Porter, B.E.1    Weis, J.2    Sanes, J.R.3
  • 66
    • 0343365608 scopus 로고    scopus 로고
    • Mini-review: Neuronal laminins and their cellular receptors
    • in press
    • Powell, S.K. and Kleinman, H.K., Mini-review: neuronal laminins and their cellular receptors, Int. J. Biochem. Cell Biol., (1996) in press.
    • (1996) Int. J. Biochem. Cell Biol.
    • Powell, S.K.1    Kleinman, H.K.2
  • 67
    • 0026020097 scopus 로고
    • Extracellular matrix molecules and their receptors: Functions in neural development
    • Reichardt, L.F. and Tomaselli, K.J., Extracellular matrix molecules and their receptors: functions in neural development, Ann. Rev. Neurosci., 14 (1991) 531-570.
    • (1991) Ann. Rev. Neurosci. , vol.14 , pp. 531-570
    • Reichardt, L.F.1    Tomaselli, K.J.2
  • 68
    • 0026571649 scopus 로고
    • Rapid effects of laminin on the growth cone
    • Rivas, R.J., Burmeister, D.W. and Goldberg, D.J., Rapid effects of laminin on the growth cone, Neuron, 8 (1992) 107-115.
    • (1992) Neuron , vol.8 , pp. 107-115
    • Rivas, R.J.1    Burmeister, D.W.2    Goldberg, D.J.3
  • 69
    • 0022486227 scopus 로고
    • Distribution of laminin in the developing peripheral nervous system of the chick
    • Rogers, S.L., Edson, K.J., Letourneau, P.C. and McLoon, S.C., Distribution of laminin in the developing peripheral nervous system of the chick, Dev. Biol., 113 (1986) 429-435.
    • (1986) Dev. Biol. , vol.113 , pp. 429-435
    • Rogers, S.L.1    Edson, K.J.2    Letourneau, P.C.3    McLoon, S.C.4
  • 70
    • 0027367064 scopus 로고
    • Inhibition of migration of neural crest-derived cells by the abnormal mesenchyme of the presumptive aganglionic bowel of ls/ls, mice: Analysis with aggregation and interspecies chimeras
    • Rothman, T.P., Goldowitz, D. and Gershon, M.D., Inhibition of migration of neural crest-derived cells by the abnormal mesenchyme of the presumptive aganglionic bowel of ls/ls, mice: analysis with aggregation and interspecies chimeras, Dev. Biol., 159 (1993) 559-573.
    • (1993) Dev. Biol. , vol.159 , pp. 559-573
    • Rothman, T.P.1    Goldowitz, D.2    Gershon, M.D.3
  • 72
    • 0018141960 scopus 로고
    • Reinnervation of muscle fiber basal lamina after removal of myofibers. Differentiation of regenerating axons at original synaptic sites
    • Sanes, J.R., Marshall, L.M. and McMahan, U.J., Reinnervation of muscle fiber basal lamina after removal of myofibers. Differentiation of regenerating axons at original synaptic sites, J. Cell Biol., 78 (1978) 176-198.
    • (1978) J. Cell Biol. , vol.78 , pp. 176-198
    • Sanes, J.R.1    Marshall, L.M.2    McMahan, U.J.3
  • 74
    • 0025049196 scopus 로고
    • Neuronal growth cones: An extended view
    • Smalheiser, N.R., Neuronal growth cones: an extended view, Neuroscience, 38 (1990) 1-11.
    • (1990) Neuroscience , vol.38 , pp. 1-11
    • Smalheiser, N.R.1
  • 75
    • 0025738084 scopus 로고
    • Role of laminin in stimulating rapid-onset neurites in NG108-15 cells: Relative contribution of attachment and motility responses
    • Smalheiser, N.R., Role of laminin in stimulating rapid-onset neurites in NG108-15 cells: relative contribution of attachment and motility responses, Dev. Brain Res., 2 (1991) 81-89.
    • (1991) Dev. Brain Res. , vol.2 , pp. 81-89
    • Smalheiser, N.R.1
  • 76
    • 0027447326 scopus 로고
    • Monensin-sensitive cellular events modulate neurite extension on laminin: An example of higher-order regulation of cell motility
    • Smalheiser, N.R., Monensin-sensitive cellular events modulate neurite extension on laminin: an example of higher-order regulation of cell motility, Cell Motil. Cytoskel., 24 (1993) 256-263.
    • (1993) Cell Motil. Cytoskel. , vol.24 , pp. 256-263
    • Smalheiser, N.R.1
  • 77
    • 0029072703 scopus 로고
    • Purification of cranin, a laminin binding membrane protein
    • Smalheiser, N.R. and Kim, E., Purification of cranin, a laminin binding membrane protein, J. Biol. Chem., 270 (1995) 15425-15433.
    • (1995) J. Biol. Chem. , vol.270 , pp. 15425-15433
    • Smalheiser, N.R.1    Kim, E.2
  • 78
    • 0023410821 scopus 로고
    • Cranin: A laminin-binding protein of cell membranes
    • Smalheiser, N.R. and Schwartz, N.B., Cranin: a laminin-binding protein of cell membranes, Proc. Natl. Acad. Sci. USA, 84 (1987) 6457-6461.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 6457-6461
    • Smalheiser, N.R.1    Schwartz, N.B.2
  • 79
    • 0028126824 scopus 로고
    • Relationship between injury-induced astrogliosis, laminin expression and axonal sprouting in the adult rat brain
    • Stichel, C.C. and Müller, H.-W., Relationship between injury-induced astrogliosis, laminin expression and axonal sprouting in the adult rat brain, J. Neurocytol., 23 (1994) 615-630.
    • (1994) J. Neurocytol. , vol.23 , pp. 615-630
    • Stichel, C.C.1    Müller, H.-W.2
  • 80
    • 0027520442 scopus 로고
    • Cell and heparin binding in the distal long arm of laminin: Identification of active and cryptic sites with recombinant and hybrid glycoprotein
    • Sung, U., O'Rear, J.J. and Yurchenco, P.D., Cell and heparin binding in the distal long arm of laminin: identification of active and cryptic sites with recombinant and hybrid glycoprotein, J. Cell Biol., 123 (1993) 1255-1268.
    • (1993) J. Cell Biol. , vol.123 , pp. 1255-1268
    • Sung, U.1    O'Rear, J.J.2    Yurchenco, P.D.3
  • 81
    • 0024443667 scopus 로고
    • A synthetic peptide containing the IKVAV sequence from the A chain of laminin mediates cell attachment, migration, and neurite outgrowth
    • Tashiro, K.-L, Sephel, G., Weeks, B.S., Sasaki, M., Martin, G.R., Kleinman, H.K. and Yamada, Y., A synthetic peptide containing the IKVAV sequence from the A chain of laminin mediates cell attachment, migration, and neurite outgrowth, J. Biol. Chem., 264 (1989) 16174-16182.
    • (1989) J. Biol. Chem. , vol.264 , pp. 16174-16182
    • Tashiro, K.-L.1    Sephel, G.2    Weeks, B.S.3    Sasaki, M.4    Martin, G.R.5    Kleinman, H.K.6    Yamada, Y.7
  • 83
    • 0023015217 scopus 로고
    • Structure, development, and molecular pathology of basement membranes
    • Timpl, R. and Dziadek, M., Structure, development, and molecular pathology of basement membranes, Int. Rev. Exp. Pathol., 29 (1986) 1-112.
    • (1986) Int. Rev. Exp. Pathol. , vol.29 , pp. 1-112
    • Timpl, R.1    Dziadek, M.2
  • 85
    • 0023813318 scopus 로고
    • Purification and characterization of mammalian integrins expressed by a rat neuronal cell line (PC12): Evidence that they function as alpha/beta heterodimeric receptors for laminin and type IV collagen
    • Tomaselli, K.J., Damsky, C.H. and Reichardt, L.F., Purification and characterization of mammalian integrins expressed by a rat neuronal cell line (PC12): evidence that they function as alpha/beta heterodimeric receptors for laminin and type IV collagen, J. Cell Biol., 107 (1988) 1241-1252.
    • (1988) J. Cell Biol. , vol.107 , pp. 1241-1252
    • Tomaselli, K.J.1    Damsky, C.H.2    Reichardt, L.F.3
  • 87
    • 0028989654 scopus 로고
    • β8 integrins mediate interactions of chick sensory neurons with laminin-1, collagen IV, and fibronectin
    • Venstrom, K. and Reichardt, L., β8 integrins mediate interactions of chick sensory neurons with laminin-1, collagen IV, and fibronectin, Mol. Biol. Cell, 6 (1995) 419-431.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 419-431
    • Venstrom, K.1    Reichardt, L.2
  • 90
    • 0027482396 scopus 로고
    • Assignment of laminin heavy chains using the lectin Ricinus communis, agglutinin-1
    • Wadsworth, D.F., Okuno, A. and Strong, P.N., Assignment of laminin heavy chains using the lectin Ricinus communis, agglutinin-1, Biochem. J., 295 (1993) 537-541.
    • (1993) Biochem. J. , vol.295 , pp. 537-541
    • Wadsworth, D.F.1    Okuno, A.2    Strong, P.N.3
  • 91
    • 0026598992 scopus 로고
    • The role of laminin, a component of Schwann cell basal lamina, in rat sciatic nerve regeneration within antiserum-treated nerve grafts
    • Wang, G.Y., Hirai, K. and Shimada, H., The role of laminin, a component of Schwann cell basal lamina, in rat sciatic nerve regeneration within antiserum-treated nerve grafts, Brain Res., 570 (1992) 116-125.
    • (1992) Brain Res. , vol.570 , pp. 116-125
    • Wang, G.Y.1    Hirai, K.2    Shimada, H.3
  • 92
    • 0025641374 scopus 로고
    • Laminin-mediated process formation in neuronal cells involves protein dephosphorylation
    • Weeks, B.S., DiSalvo, J. and Kleinman, H.K., Laminin-mediated process formation in neuronal cells involves protein dephosphorylation, J. Neurosci. Res., 27 (1990) 418-426.
    • (1990) J. Neurosci. Res. , vol.27 , pp. 418-426
    • Weeks, B.S.1    DiSalvo, J.2    Kleinman, H.K.3
  • 93
    • 0029054487 scopus 로고
    • Cell surface calreticulin is a putative mannoside lectin which triggers mouse melanoma cell spreading
    • White, T.K., Zhu, Q. and Tanzer, M.L., Cell surface calreticulin is a putative mannoside lectin which triggers mouse melanoma cell spreading, J. Biol. Chem., 270 (1995) 15926-15929.
    • (1995) J. Biol. Chem. , vol.270 , pp. 15926-15929
    • White, T.K.1    Zhu, Q.2    Tanzer, M.L.3
  • 94
    • 0026095012 scopus 로고
    • Carbohydrate-binding protein 35 (Mac-2), a laminin-binding lectin, forms functional dimers using cysteine-186
    • Woo, H.-J., Lotz, M.M., Jung, J.U. and Mercuric, A.M., Carbohydrate-binding protein 35 (Mac-2), a laminin-binding lectin, forms functional dimers using cysteine-186, J. Biol. Chem., 266 (1991) 18419-18422.
    • (1991) J. Biol. Chem. , vol.266 , pp. 18419-18422
    • Woo, H.-J.1    Lotz, M.M.2    Jung, J.U.3    Mercuric, A.M.4
  • 95
    • 0025353203 scopus 로고
    • Assembly of basement membranes
    • Yurchenco, P.D., Assembly of basement membranes, Ann. NY Acad. Sci., 580 (1990) 195-213.
    • (1990) Ann. NY Acad. Sci. , vol.580 , pp. 195-213
    • Yurchenco, P.D.1
  • 96
    • 0027416755 scopus 로고
    • Recombinant laminin G domain mediates myoblast adhesion and heparin binding
    • Yurchenco, P.D., Sung, U., Ward, M.D., Yamada, Y. and O'Rear, JJ., Recombinant laminin G domain mediates myoblast adhesion and heparin binding, J. Biol. Chem., 268 (1993) 8356-8365.
    • (1993) J. Biol. Chem. , vol.268 , pp. 8356-8365
    • Yurchenco, P.D.1    Sung, U.2    Ward, M.D.3    Yamada, Y.4    O'Rear, J.J.5
  • 97
    • 0028567840 scopus 로고
    • Measurements of growth cone adhesion to culture surfaces by micromanipulation
    • Zheng, J., Buxbaum, R.E. and Heidemann, S.R., Measurements of growth cone adhesion to culture surfaces by micromanipulation, J. Cell Biol., 127 (1994) 2049-2060.
    • (1994) J. Cell Biol. , vol.127 , pp. 2049-2060
    • Zheng, J.1    Buxbaum, R.E.2    Heidemann, S.R.3
  • 98
    • 0024995791 scopus 로고
    • Four patterns of laminin-immunoreactive structure in developing rat brain
    • Zhou, F.C., Four patterns of laminin-immunoreactive structure in developing rat brain, Dev. Brain Res., 55 (1990) 191-201.
    • (1990) Dev. Brain Res. , vol.55 , pp. 191-201
    • Zhou, F.C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.