Abstract
The extracellular space occupies about 40% of the immature brain (Bondareff and Pysh, 1968), decreasing to 20% in the adult (van Harreveld et al., 1971; Nevis and Collins, 1967). This space is filled with a matrix (ECM) of insoluble glycoconjugates (glycoproteins, proteoglycans) through which neural cell precursors migrate to take up their final positions in the central nervous system (CNS). In the adult peripheral nervous system, regenerating axons must also make their way through the ECM to reach their targets. In these and other instances, adhesion of cells to a matrix or other cells is essential for motility, which results in large part from contractile processes in the cell. A common feature of such adhesions is that they involve interaction of glycoconjugates in the ECM with others (glycoproteins, proteoglycans, and glycolipids) at the cell surface; for example, the adhesive ECM glycoproteins laminin, fibronectin, and collagens bind to receptors on the cell surface. The ramifications of these ECM—receptor interactions in the nervous system may be profound. In some instances they rival those of hormones and growth factors (Edgar et al., 1984) by modifying gene expression (Bissell et al., 1982) and leading to neural cell differentiation (Reh et al., 1987), proliferation (Kleinman et al.,1984), synaptogenesis (Nitkin et al.,1983), neuroblast migration (Newgreen and Thiery, 1980; Boucaut et al.,1984; Liesi, 1985a), Schwann cell ensheathment of peripheral axons (Bunge et al.,1986), and possibly formation of the blood—brain barrier (Arthur et al.,1987).
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References
Achseon, A., Edgar, D., Timpl, P., and Theonen, H,. 1986, Laminin increases both levels and activity of tyrosine hydroxylase in calf adrenal chromaffin cells, J. cell Biol. 102: 151–159.
Akers, R. M., Mosher, D. F., and Lilien, J. E., 1981, Promotion of retinal neurite outgrowth by substratum-bound fibronectin, Del,. Biol. 86:179–188.
Akeson, R., and Warren, S. L., 1986, PC12 adhesion and neurite formation on selected substrates are inhibited by some glycosaminoglycans and a fibronectin-derived tetrapeptide, Exp. Cell Res. 162: 347–362.
Akiyama, S. K., and Yamada, K. M., 1985, The interaction of plasma fibronectin with fibroblastic cells in suspension, J. Biol. Chem. 260: 4492–4500.
Akiyama, S. K., Yamada, S. S., and Yamada, K. M., 1986, Characterization of a 140-kD avian cell surface antigen as a fibronectin-binding molecule, J. Cell Biol. 102: 442–448.
Aquino, D. A., Margolis, R. U., and Margolis, R. K., 1984, Immunocytochemical localization of a chondroitin sulfate proteoglycan in nervous tissue. I. Adult brain, retina, and peripheral nerve, J. Cell Biol. 99: 1117–1119.
Arthur, F. E., Shivers, R. R., and Bowman, P. D., 1987, Astrocyte-mediated induction of tight junctions in brain capillary endothelium: An efficient in vitro model, Dey. Brain Res. 36: 155–159.
Aumailley, M., Nurcombe, V., Edgar, D., Paulsson, M., and Timpl, R., 1987, The cellular interactions of laminin fragments, J. Biol. Chem. 262: 11532–11538.
Barlow, D. P., Green, N. M., Kurkinen, M., and Hogan, B., 1984, Sequencing of laminin B chain cDNA, reveals C-terminal regions of coiled-coil alpha-helix, EMBO J. 3: 2355–2362.
Barsky, S. H., Rao, C. N., Hyams, D., and Liotta, L. A., 1984, Characterization of a laminin receptor from human breast carcinoma tissue, Breast Cancer Res. Treat. 4: 181–188.
Bissell, M. J., Hall, G. H., and Parry, G., 1982, How does the extracellular matrix direct gene expression? J. Theor. Biol. 99: 31–68.
Bixby, J. L., Pratt, R. S., Lilien, J ., and Reichardt, L. F., 1987, Neurite outgrowth on muscle cell surfaces involves extracellular matrix receptors as well as Cat+-dependent and -independent cell adhesion molecules, Proc. Natl. Acad. Sci. USA 84: 2555–2559.
Bondareff, W., and Pysh, J. J., 1968, Distribution of the extracellular space during postnatal maturation of rat cerebral cortex, Anat. Rec. 160: 773–780.
Boucaut, J.-C., Darribere, T., Poole, T. J., Aoyama, H., Yamada, K. M., and Thiery, J.-P., 1984, Biologically active synthetic peptides as probes of embryonic development: A competitive peptide inhibitor of fibronectin function inhibits gastrulation in amphibian embryos and neural crest cell migration in avian embryos, J. Cell Biol. 99: 1822–1830.
Bozyczko, D., and Horwitz, A. F., 1986, The participation of a putative cell surface receptor for laminin and fibronectin in peripheral neurite extension, J. Neurosci. 65: 1241–1251.
Branner-Fraser, M., 1986, An antibody to a receptor for fibronectin and laminin perturbs cranial neural crest cell development in vivo, Dey. Biol. 117: 528–536.
Brown, S. S., Malinoff, H. L., and Wicha, M. S., 1983, Connectin, a cell surface protein that binds both laminin and actin, Proc. Natl. Acad. Sci. USA 80: 5927–5930.
Buck, C. A., and Horwitz, A. F., 1987, Cell surface receptors for extracellular matrix molecules, Annu. Rev. Cell Biol. 3: 179–205.
Buck, C. A., Shea, E., Duggan, K., and Horwitz, A. F., 1986, Integrin (the CSAT antigen) functionality requires oligomeric integrity, J. Cell Biol. 103: 2421–2428.
Bunge, R. P., Bunge, M. B., and Eldridge, C. F., 1986, Linkage between axonal ensheathment and basal lamina production by Schwann cells, Annu. Rev. Neurosci. 9: 305–328.
Burridge, K., 1987, Substrate adhesions in normal and transformed fibroblasts: Organization and regulation of cytoskeletal, membrane and extracellular matrix components at focal contacts, Cancer Rev. 4: 18–78.
Carbonetto, S., 1984, The extracellular matrix of the nervous system, Trends Neurosci. 7: 382–387.
Carbonetto, S. T., Gruver, M. M., and Turner, D. C., 1982, Nerve fiber growth on defined hydrogel substrates, Science 216: 897–899.
Carbonetto, S., Gruver, M. M., and Turner, D. C., 1983, Nerve fiber growth in culture on fibronectin, collagen, and glycosaminoglycan substrates, J. Neurosci. 3: 2324–2335.
Carbonetto, S., Evans, D., and Cochard, P., 1987, Nerve fiber growth in culture on tissue substrata from central and peripheral nervous systems, J. Neurosci. 7: 610–620.
Carlin, B., Jaffe, R., Bender, B., and Chung, A. E., 1981, Entactin, a novel basal lamina-associated sulfated glycoprotein, J. Biol. Chem. 256: 5209–5214.
Chen, W.-T., Hasegawa, E., Hasegawa, T., Weinstock, C., and Yamada, K. M., 1985, Development of cell surface linkage complexes in cultured fibroblasts, J. Cell Biol. 100: 1103–1114.
Cheresh, D. A., and Harper, J. R., 1987, Arg-Gly-Asp recognition by a cell adhesion receptor requires its 130-kDa a subunit, J. Biol. Chem. 262: 1434–1437.
Cheresh, D. A., Pierschbacher, M. D., Herzig, M. A., and Mujoo, K., 1986, Disialogangliosides GD2 and GD3 are involved in the attachment of human melanoma and neuroblastoma cells to extracellular matrix proteins, J. Cell Biol. 102: 688–696.
Chiquet-Ehrismann, R., Mackie, E. J., Pearson, C. A., and Sakakura, T., 1986, Tenascin: An extracellular matrix protein involved in tissue interactions during fetal development and oncogenesis, Cell 47:131-139.
Chiquet, M., 1989, Tenascin/J1/Cytotactin: The potential function of hexabrachion protein in neural development, Dev. Neurosci. 11:in press.
Chiu, A. Y., and Sanes, J. R., 1984, Development of basal lamina in synaptic and extrasynaptic portions of embryonic rat muscle, Dev. Biol. 103: 456–467.
Chung, A. E., Jaffe, R., Freeman, I. L., Vergnes, J. P., Braginski, J. E., and Carlin, B., 1979, Properties of a basement membrane related glycoprotein synthesized in culture by a mouse embryonal carcinoma-derived cell line, Cell 16: 277–287.
Chuong, C.-M., Crossin, K. L., and Edelman, G. M., 1987, Sequential expression and differential function of multiple adhesion molecules during the formation of cerebellar cortical layers, J. Cell Biol. 104: 331–342.
Clegg, D. O., Helder, J. C., Hann, B. C., Hall, D. E., and Reichardt, L. F., 1988, Amino acid sequence and distribution of mRNA encoding a major skeletal muscle laminin binding protein: an extracellular matrix-associated protein with an unusual COOH-terminal polyaspartate domain, J. Cell Biol. 107: 699–705.
Cohen, J., Bume, J. F., Winter, J., and Bartlett, P., 1986, Retinal ganglion cells lose response to laminin with maturation, Nature 322: 465–467.
Cohen, J., Bume, J. F., McKinlay, C., and Winter, J., 1987, The role of laminin and the laminin/fibronectin receptor complex in the outgrowth of retinal ganglion cell axons, Dev. Biol. 122: 407–418.
Cole, G. C., and Glaser, L., 1986, A heparin-binding domain from N-CAM is involved in neuron—substratum adhesion, J. Cell Biol. 102: 403–412.
Crossin, K. L., Hoffman, S., Grumet, M., Thiery, J.-P., and Edelman, G. M., 1986, Site-restricted expression of cytotactin during development of the chicken embryo, J. Cell Biol. 102: 1917–1930.
Damsky, C. H., Knudsen, K. A., Bradley, D., Buck, C. A., and Horwitz, A. F., 1985, Distribution of the cell substratum (CSAT) antigen on myogenic and fibroblastic cells in culture, J. Cell Biol. 100:1528-1539.
Davis, G. E., Manthorpe, M., Engvall, E., and Varon, S., 1985a, Isolation and characterization of rat Schwannoma neurite-promoting factor: Evidence that the factor contains laminin, J. Neurosci. 5: 2662–2671.
Davis, G. E., Varon, S., Engvall, E., and Manthorpe, M., 1985b, Substratum-binding neurite-promoting factors: Relationships to laminin, Trends Neurosci. 8: 528–532.
Dedhar, S., Ruoslahti, E., and Pierschbacher, M. D., 1987, A cell surface receptor complex for collagen type I recognizes the Arg-Gly-Asp sequence, J. Cell Biol. 104: 585–593.
Douville, P., Harvey, W., and Carbonetto, S., 1987, Identification and purification of a high affinity laminin receptor from embryonic chick brain: Evidence for developmental regulation in the CNS, Soc. Neurosci. Abstr. 13: 14–82.
Douville, P. J., Harvey, W. J., and Carbonetto, S., 1988, Isolation and characterization of high affinity laminin receptors in neural cells, J. Biol. Chem. 263: 14964–14969.
Dow, K. E., Musky, S. E. L., Roder, J. C., Riopelle, R. G., 1988, Neuronal proteoglycans: Biosynthesis and functional interaction with neurons in vitro, J. Neurosci. 8: 3278–3289.
Dräger, U. C., and Rabacchi, S. A., 1988, A positional marker in the dorsal eye of the embryo, Soc. Neurosci. Abs. 14: 769.
Duband, J.-L., Rocher, S., Chen, W.-T., Yamada, K. M., and Thiery, J.-P., 1986, Cell adhesion and migration in the early vertebrate embryo: Location and possible role of the putative fibronectin receptor complex, J. Cell Biol. 102: 160–178.
Dziadek, M., and Timpl, R., 1985, Expression of nidogen and laminin in basement membranes during mouse embryogenesis and in teratocarcinoma cells, Dey. Biol. 111: 372–382.
Dziadek, M., Paulsson, M., and Timpl, R., 1985, Identification and interaction repertoire of large forms of the basement membrane protein nidogen, EMBO J. 4: 2513–2518.
Edgar, D., Timpl, R., and Theonen, H., 1984, The heparin-binding domain of laminin is responsible for its effects on neurite outgrowth and neuronal survival, EMBO J. 3: 1463–1468.
Ehrismann, R., Roth, D. E., Eppenberger, H. M., and Turner, D. C., 1982, Arrangement of attachment-promoting, self-association, and heparin-binding sites in horse serum fibronectin, J. Biol. Chem. 257: 7381–7387.
Enenstein, J., and Furcht, L. T., 1984, Isolation and characterization of epinectin, a novel adhesion protein for epithelial cells, J. Cell Biol. 99: 464–470.
Engel, J., Odermatt, E., Engle, A., Madri, J. A., Furthmayr, H., Rohde, H., and Timpl, R., 1981, Shapes, domain organizations and flexibility of laminin and fibronectin, two multifunctional proteins of the extracellular matrix, J. Mol. Biol. 150: 97–120.
Engvall, E., Davis, G. E., Dickerson, K., Ruoslahti, E., Varon, S., and Manthorpe, M., 1986, Mapping of domains in human laminin using monoclonal antibodies: localization of the neurite-promoting site, J. Cell Biol. 103: 2457–2465.
Erickson, H. P., and Inglesias, J. L., 1984, A six-armed oligomer isolated from cell surface fibronectin preparations, Nature 311: 267–269.
Fahrig, T., Landa, C., Pesheva, P., Kühn, K., and Schachner, M., 1987, Characterization of binding properties of the myelin-associated glycoprotein to extracellular matrix constituents, EMBO J. 6: 2875–2883.
Fakuda, T., and Hashimoto, P. H., 1987, Distribution and fine structure of ependymal cells possessing intracellular cysts in the aqueductal wall of the rat brain, Cell Tissue Res. 247: 555–564.
Fitzgerald, L. A., Steiner, B., Rall, S. C., Jr., Lo, S., and Phillips, D. R., 1987, Protein sequence of endothelial glycoprotein IIIa derived from a cDNA clone, J. Biol. Chem. 262: 3936–3939.
Gardner, J. M., and Hynes, R. O., 1985, Interaction of fibronectin with its receptor on platelets, Cell 42: 439–448.
Giftochristos, N., and David, S., 1988, Laminin and heparan sulfate proteoglycan in the lesioned adult mammaliam central nervous system and their possible relationship to axonal sprouting, J. Neurocyt. 17: 385–397.
Ginsberg, M., Pierschbacher, M. D., Ruoslahti, E., Marguerie, G., and Plow, E., 1985, Inhibition of fibronectin binding to platelets by proteolytic fragments and synthetic peptides which support fibroblast adhesion, J. Biol. Chem. 260: 3931–3936.
Ginsberg, M. H., Loftus, J., Ryckwaert, J., Pierschbacher, M., Pytela, R., Ruoslahti, E., and Plow, E. F., 1987, Immunochemical and amino-terminal sequence comparison of two cytoadhesins indicates they contain similar or identical ß subunits and distinct a subunits, J. Biol. Chem. 262: 5437–5440.
Goodman, S. L., Deutzmann, R., and von der Mark, K., 1987, Two distinct cell-binding domains can independently promote nonneuronal cell adhesion and spreading, J. Cell Biol. 105: 589–598.
Graf, J., Iwamoto, Y., Sasaki, M., Martin, G. R., Kleinman, H. K., Robey, F. A., and Yamada, Y., 1987a, Identification of an amino acid sequence in laminin mediating cell attachment, chemotaxis, and receptor binding, Cell 48: 989–996.
Graf, J., Ogle, R. C., Robey, F. A., Sasaki, M., Martin, G. R., Yamada, Y., and Kleinman, H. K., 1987b, A pentapeptide from the laminin B1 chain mediates cell adhesion and binds the 67,000 laminin receptor, Biochemistry 26: 6896–6900.
Greve, J. M., and Gottlieb, D. I., 1982, Monoclonal antibodies which alter the morphology of cultured chick myogenic cells, J. Cell Biochem. 18: 221–229.
Grinnell, F., 1978, Cellular adhesiveness and extracellular substrata, Int. Rev. Cytol. 53: 65–144.
Grumet, M., Hoffman, S., Crossin, K. L., and Edelman, G. M., 1985, Cytotactin, an extracellular matrix protein of neural and non-neural tissues that mediates glia-neuron interaction, Proc. Natl. Acad. Sci.USA 82: 8075–8079.
Hall, D. E., Neugebauer, K. M., and Reichardt, L. F., 1987, Embryonic neural retinal cell response to extracellular matrix proteins: Developmental changes and effects of the cell substratum attachment antibody (CSAT), J. Cell Biol. 104: 623–634.
Hall, D. E., Frazer, K. A., Hann, B. C., and Reichardt, L. F., 1988, Isolation and characterization of a laminin-binding protein from rat and chick muscle, J. Cell Biol. 107: 687–697.
Harvey, W., and Carbonetto, S., 1986, Specific binding of 125í-laminin to neural cells in culture, Soc. Neurosci. Abstr. 12: 1109.
Hatten, M. E., Furie, M. B., and Rifkin, D. B., 1982, Binding of developing mouse cerebellar cells to fibronectin: A possible mechanism for the formation of the external granular layer, J. Neurosci. 2: 1195–1206.
Hauschka, S. D., and Konigsberg, I. R., 1966, The influence of collagen on the development of muscle clones, Proc. Natl. Acad. Sci. USA 55: 119–126.
Hemler, M. E., Huang, C., and Schwarz, L., 1987, The VLA protein family: Characterization of five distinct cell surface heterodimers each with a common 130,000 MT subunit, J. Biol. Chem. 262: 3300–3309.
Hewitt, A. T., Kleinman, H. K., Pennypacker, J. P., and Martin, G. R., 1980, Identification of an adhesion factor for chondrocytes, Proc. Natl. Acad. Sci. USA 77: 385–388.
Hinek, A., Wrenn, D. S., Mecham, R. P., and Barondes, S. H., 1988, The elastin receptor: a galactosidebinding protein, Science 239: 1539–1541.
Hirst, R., Horwitz, A., Buck, C., and Rohrschneider, L., 1986, Phosphorylation of the fibronectin receptor complex in cells transformed by oncogenes that encode tyrosine kinases, Proc. Natl. Acad. Sci. USA 83: 6470–6474.
Hopkins, J. M., Ford-Holevinski, T. S., McCoy, J. P., and Agranoff, B. W., 1985, Laminin and optic nerve regeneration in the goldfish, J. Neurosci. 5:3030–3038.
Horwitz, A., Duggan, K., Greggs, R., Decker, C., and Buck, C., 1985, The cell substrate attachment (CSAT) antigen has properties of a receptor for laminin and fibronectin, J. Cell Biol. 101: 2134–2144.
Horwitz, A., Duggan, K., Buck, C., Beckerle, M. C., and Burridge, K., 1986, Interaction of plasma membrane fibronectin receptor with talin—A transmembrane linkage, Nature 320: 531–533.
Hostikka, S. L., Kurkinen, M., and Trygvason, K., 1987, Nucleotide sequence coding for the human type IV collagen a2 chain cDNA reveals extensive homology with the NC-1 domain of al(IV) but not with the collagenous domain or 3’-untranslated region, FEBS Lett. 216: 281–286.
Huard, T. M., Malinoff, H. L., and Wicha, M. S., 1986, Macrophages express a plasma membrane receptor for basement membrane laminin, Am. J. Pathol. 123: 365–370.
Humphries, M. J., Olden, K., and Yamada, K. M., 1986a, A synthetic peptide from fibronectin inhibits experimental metastasis of murine melanoma cells, Science 233: 467–470.
Humphries, M. J., Akiyama, S. K., Komoriya, A., Olden, K., and Yamada, K. M., 1986b, Identification of an alternatively spliced site in human plasma fibronectin that mediates cell type-specific adhesion, J. Cell Biol. 103: 2637–2647.
Hynes, R. O., 1985, Molecular biology of fibronectin, Annu. Rev. Cell Biol. 1: 67–90.
Hynes, R. O., 1987, Integrins: A family of cell surface receptors, Cell 48: 549–554.
Hynes, R. O., Patel, R., and Miller, R. H., 1986, Migration of neuroblasts along preexisting axonal tracts during prenatal cerebellar development, J. Neurosci. 6: 867–876.
Ide, C., Tohyama, K., Yokota, R., Nitatori, T., and Onodera, S., 1983, Schwann cell basal lamina and nerve regeneration, Brain Res. 288: 61–75.
Iwamoto, Y., Robey, F. A., Graf, J., Sasaki, M., Kleinman, H. K., Yamada, Y., and Martin, G., 1987, YIGSR, a synthetic laminin pentapeptide, inhibits experimental metastasis formation, Science 238: 1132–1134.
Keene, D. R., Sakai, L. Y., Lunstrum, G. P., Moms, N. P., and Burgeson, R. E., 1987, Type VII collagen forms an extended network of anchoring fibrils, J. Cell Biol. 104: 611–621.
Kefalides, N. A., Alper, R., and Clark, C. C., 1979, Biochemistry and metabolism of basement membranes, Int. Rev. Cytol. 61: 167–221.
Kleinman, H. K., McGarvey, M. L., Hassell, J. R., Martin, G. R., Baron van Evercooren, A., and DuboisDalcq, M., 1984, The role of laminin in basement membranes and in the growth, adhesion, and differentiation of cells, in: The Role of Extracellular Matrix in Development ( R. L. Trelstad, ed.), pp. 123–143, Liss, New York.
Kleinman, H. K., Ogle, R. C., Cannon, F. B., Little, C. C., Sweeney, T. M., and Luckenbill-Edds, L., 1988, Laminin receptors for neurite formation, Proc. Natl. Acad. Sci. USA 85: 1282–1286.
Kleitman, N., Wood, P., Johnson, M. I., and Bunge, R. P., 1988, Schwann cell surfaces but not extracellular matrix organized by Schwann cells support neurite outgrowth from embryonic rat retina, J. Neurosci. 8: 653–663.
Knudsen, K. A., Horwitz, A. F., and Buck, C. A., 1985, A monoclonal antibody identifies a glycoprotein complex involved in cell–substratum adhesion, Exp. Cell Res. 157: 218–226.
Komblihtt, A. R., Umezawa, K., Vibe-Pedersen, K., and Baralle, F. E., 1985, Primary structure of human fibronectin: Differential splicing may generate at least 10 polypeptides from a single gene, EMBO J. 4: 1755–1759.
Kruse, J., Keilhauer, G., Faissner, A., Timpl, R., and Schachner, M., 1985, The J1 glycoprotein—A novel nervous system cell adhesion molecule of the L2/HNK-1 family, Nature 316: 146–148.
Kühn, K., Glanville, R. W., Babel, W., Qian, R.-Q., Dieringer, H., Voss, T., Siebold, B., Oberbäumer, J., Schwarz, U., and Yamada, Y., 1985, The structure of type IV collagen, Ann. N.Y. Acad. Sci. 460: 14–24.
Lander, A. D., Fujii, D. K., and Reichardt, L. F., 1985, Laminin is associated with the “neurite outgrowth promoting factors” found in conditioned media, Proc. Natl. Acad. Sci. USA 82: 2183–2187.
Landis, S. C., 1983, Neuronal growth cones, Annu. Rev. Physiol. 45: 567–580.
Laurie, G. W., Leblond, C. P., and Martin, G. R., 1982, Localization of type IV collagen, laminin, heparan sulfate proteoglycan, and fibronectin to the basal lamina of basement membranes, J. Cell Biol. 95: 340–344.
Laurie, G. W., Leblond, C. P., and Martin, G. R., 1983, Light microscopic immunolocalization of type IV collagen, laminin, heparan sulfate proteoglycan, and fibronectin in basement membranes of a variety of rat organs, Am. J. Anat. 167: 71–82.
Law, S. K. A., Gagnon, J., Hildreth, J. E. K., Wells, C. E., Willis, A. C., and Wong, A. J., 1987, The primary structure of the ß subunit of the cell surface adhesion glycoproteins LFA-1, CR3 and p150,95 and its relationship to the fibronectin receptor, EMBO J. 64: 915–919.
Lesot, H., Kuhl, U., and von der Mark, K., 1983, Isolation of a laminin-binding protein from muscle cell membranes, EMBO J. 2: 861–865.
Letoumeau, P. C., 1981, Immunocytochemical evidence for colocalization in neurite growth cones of actin and myosin and their relationship to cell–substratum adhesions, Dev. Biol. 85: 113–122.
Letourneau, P. C., 1983, Axonal growth and guidance, Trends Neurosci. 6: 451–455.
Letourneau, P. C., 1988, Interaction of growing axons with fibronectin and laminin, in: The Current Status of Peripheral Nerve Regeneration ( V. Chan-Palay and S. L. Palay, eds.), pp. 99–110, Liss, New York.
Liesi, P., 1985a, Do neurons in the vertebrate CNS migrate on laminin? EMBO J. 4: 1163–1170.
Liesi, P., 1985b, Laminin-inmwnoreactive glia distinguish adult CNS systems from non-regenerative ones, EMBO J. 4: 2505–2511.
Linsenmayer, T. F., 1981, Collagen, in: Cell Biology of Extracellular Matrix ( E. Hay, ed.), pp. 5–37, Plenum Press, New York.
Liotta, L. A., Hand, P. H., Rao, C. N., Bryant, G., Barsky, S. H., and Schlom, J., 1985, Monoclonal antibodies to the human laminin receptor recognize structurally distinct sites, Exp. Cell Res. 156: 117–126.
Liotta, L. A., Rao, C. N., and Wewer, U. M., 1986, Biochemical interactions of tumor cells with the basement membrane, Annu. Rev. Biochem. 55: 1037–1057.
Low, F. N., 1976, The perineurium and connective tissue of peripheral nerve, in: The Peripheral Nerve (D. N. Landon, ed.), pp. 159–187, Chapman & Hall, London.
Luckenbill-Edds, L., Ogle, R. C., and Kleinman, H. K., 1986, Laminin binds to cell membrane receptors on a neuroblastoma x glioma cell line (NG108–15), J. Cell Biol. 103: 261a.
Madri, J. A., Pratt, B. M., Yurchenko, P. D., and Furthmayr, H., 1984, The ultrastructural organization and architecture of basement membranes, in: Basement Membranes and Cell Movement, pp. 6–24, Pitman, London.
Makgoba, M. W., Sanders, M. E., Luce, G. E. G., Dustin, M. L., Springer, T. A., Clark, E. A., Mannoni, P., and Shaw, S., 1988, ICAM-1 a ligand for LFA-1-dependent adhesion of B, T and myeloid cells, Nature 331: 86–88.
Malinoff, H. L., and Wicha, M. S., 1983, Isolation of a cell surface receptor protein for laminin from murine fibrosarcoma cells, J. Cell Biol. 96: 1475–1479.
Manthorpe, M., Engvall, E., Ruoslahti, E., Longo, F. M., Davis, G. E., and Varon, S., 1983, Laminin promotes neuritic regeneration from cultured peripheral and central neurons, J. Cell Biol. 97: 1882–1890.
Manthorpe, M., Hagg, T., Engvall, E., and Varon, S., 1988, Luminin-like immunoreactivity in adult rat brain neurons Soc. Neurosci. Abs. 14: 364.
Martin, G. R., and Timpl, R., 1987, Laminin and other basement membrane components, Annu. Rev. Cell Biol. 3: 57–85.
McCarthy, J. B., Palm, S. L., and Furcht, L. T., 1984, Migration by haptotaxis of a Schwalm cell tumor line to the basement membrane glycoprotein laminin, J. Cell Biol. 97: 772–777.
Naidet, C., Séméríra, M., Yamada, K. M., and Thiery, J.-P., 1987, Peptides containing the cell-attachment recognition signal Arg-Gly-Asp prevent gastrulation in Drosophila embryos, Nature 325: 348–350.
Neff, N. T., Lowrey, C., Decker, C., Tovar, A., Damsky, C., Buck, C., and Horwitz, A. F., 1982, A monoclonal antibody detaches embryonic skeletal muscle from extracellular matrices, J. Cell Biol. 95: 654–666.
Nevis, A. H., and Collins, G. H., 1967, Electrical impedance and volume changes in brain during development, Brain Res. 5 :57–85.
Newgreen, D., and Thiery, J.-P., 1980, Fibronectin in early avian embryos: Synthesis and distribution along the migration pathways of neural crest cells, Cell Tissue Res. 211: 269–291.
Nitkin, R. M., Wallace, B. G., Spira, M. E., Godfrey, E. W., and McMahon, U. J., 1983, Molecular components of the synaptic basal lamina that direct differentiation of regenerating neuromuscular junctions, Cold Spring Harbor Symp. Quant. Biol. 48: 653–665.
Oberbäumer, I., Laurent, M., Schwarz, U., Sakurai, Y., Yamada, Y., Vogeli, G., Voss, T., Siebold, B., Glanville, R. W., and Kühn, K., 1985, Amino acid sequence of the non-collagenous globular domain (NCI) of the a1(IV) chain of basement membrane collagen derived from complementary DNA, Eur. J. Biochem. 14: 217–224.
Odermatt, E., Tamkun, J. W., and Hynes, R. 0., 1985, Repeating modular structure of the fibronectin gene: Relationship to protein structure and subunit variation, Proc. Natl. Acad. Sci. USA 82: 6571–6575.
Ogle, R. C., and Little, C. D., 1989, Collagen binding proteins derived from the embryonic fibroblast cell surface recognize arginine-glycine-aspartic acid, Biosci. Rep., in press.
Ogle, R. C., Laurie, G. W., Kitten, G. T., Kandel, S. L., and Bing, J. T., 1987, Isolation of a cell surface receptor for collagen type IV, J. Cell Biol. 105: 136a.
Oldberg, A., and Ruoslahti, E., 1986, Evolution of the fibronectin gene, J. Biol. Chem. 261: 2113–2116.
Ott, U., Odermatt, E., Engel, J., Furthmayr, H., and Timpl, R., 1982, Protease resistance and conformation of laminin, Eur. J. Biochem. 123: 63–72.
Palm, S. L., and Furcht, L. T., 1983, Production of laminin and fibronectin by Schwannoma cells: Cell—protein interactions in vitro and protein localization in peripheral nerve in vivo, J. Cell Biol. 96:1218-1226.
Patel, V. P., and Lodish, H. F., 1986, The fibronectin receptor on mammalian erythroid precursor cells: Characterization and developmental regulation, J. Cell Biol. 86: 449–456.
Patterson, P. H., 1985, On the role of proteases, their inhibitors and the extracellular matrix in promoting neurite outgrowth, J. Physiol. (Paris) 80: 207–211.
Paulsson, M., Aumailley, M., Deutzmann, R., Timpl, R., Beck, K., and Engel, J., 1987, Lamininnidogen complex: Extraction with chelating agents and structural characterization, Eur. J. Biochem. 166: 11–19.
Peters, A., Palay, S. L., and Webster, H., 1976, The Fine Structure of the Nervous System: The Neurons and Supporting Cells, Saunders, Philadelphia.
Petersen, T. E., Thogersen, H. C., Skorstengaard, K., Vibe-Pedersen, K., Sahl, P., Sottrup-Jensen, L., and Magnusson, S., 1983, Partial primary structure of bovine plasma fibronectin: Three types of internal homology, Proc. Natl. Acad. Sci. USA 80: 137–141.
Pierschbacher, M. D., and Ruoslahti, E., 1984, Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule, Nature 309: 30–33.
Pierschbacher, M. D., Hayman, E. G., and Ruoslahti, E., 1981, Location of the cell-attachment site in fibronectin with monoclonal antibodies and proteolytic fragments of the molecule, Cell 26: 259–267.
Plow, E. F., Loftus, J. C., Levin, E. G., Fair, D. S., Dixon, D., Forsyth, J., and Ginsberg, M. H., 1986, Immunologic relationship between platelet membrane glycoprotein GPIIb/IIIa and cell surface molecules expressed by a variety of cells, Proc. Natl. Acad. Sci. USA 83: 6002–6006.
Pollard, T. D., 1980, Platelet contractile proteins, Thromb. Haemostasis 42: 1634–1637.
Pytela, R., Pierschbacher, M. D., and Ruoslahti, E., 1985a, Identification and isolation of a 140 kd cell surface glycoprotein with properties expected of a fibronectin receptor, Cell 40: 191–198.
Pytela, R., Pierschbacher, M. D., and Ruoslahti, E., 1985b, A 125/115-kDa cell surface receptor for vitronectin interacts with the arginine-glycine-aspartic acid adhesion sequence from fibronectin, Proc. Natl. Acad. Sci. USA 82: 5766–5770.
Pytela, R., Pierschbacher, M. D., Ginsberg, M. H., Plow, E. F., and Ruoslahti, E., 1986, Platelet membrane glycoprotein IIb/IIIa: Member of a family of Arg-Gly-Asp-specific adhesion receptors, Science 231: 1559–1562.
Rabacchi, S. A., Neve, R. L., and Dräger, U. C., 1988, Molecular cloning of the “dorsal eye antigen”: homology to the high-affinity laminin receptor, Soc. Neurosci. Abs. 14: 769.
Rakic, P., 1985, Contact regulation of neuronal migration, in: The Cell in Contact: Adhesions and Junctions as Morphogenetic Determinants ( G. M. Edelman and J.-P. Thiery, eds.), pp. 67–92, Wiley, New York.
Rao, C. N., Margulies, I. M. K., Troika, T. S., Terranova, V. P., Madri, J. A., and Liotta, L. A., 1982, Isolation of a subunit of laminin and its role in molecular structure and tumor cell attachment, J. Biol. Chem. 257: 9740–9744.
Rao, C. N., Barsky, S. H., Terranova, V. P., and Liotta, L. A., 1983, Isolation of a tumor cell laminin receptor, Biochem. Biophys. Res. Commun. 111: 804–808.
Rauvala, H., and Hakomori, S.-I., 1981, Studies on cell adhesion and recognition. III. The occurrence of amannosidase at the fibroblast cell surface, and its possible role in cell recognition, J. Cell Biol. 88: 149159.
Reichardt, L. F., Bixby, J. L., Hall, D. E., Ignatius, M. J., Neugebauer, K. M., and Tomaselli, K. J., 1989, Integrins and cell adhesion molecules: Neuronal receptors that regulate axon growth on extra-cellular matrices and cell surfaces, Dey. Neurosci. 11:in press.
Reh, T. A., Nagy, T., and Gretton, H., 1987, Retinal pigmented epithelial cells induced to transdifferentiate to neurons by laminin, Nature 330: 68–71.
Roberts, D. D., Rao, C. N., Magini, J. L., Spitalnik, S. L., Liotta, L. A., and Ginsberg, V., 1985, Laminin binds specifically to sulfated glycolipids, Proc. Natl. Acad. Sci. USA 82: 1306–1310.
Rogers, S. L., Letoumeau, P. C., Palm, S. L., McCarthy, J. B., and Furcht, L. T., 1983, Neurite extension by peripheral and central nervous system neurons in response to substratum-bound fibronectin and laminin, Dey. Biol. 98: 212–220.
Rogers, S. L., McCarthy, J. B., Palm, S. L., Furcht, L. T., and Letoumeau, P. C., 1985, Neuron-specific interactions with two neurite-promoting fragments of fibronectin, J. Neurosci. 5: 369–378.
Rogers, S. L., Edson, K. J., Letoumeau, P. C., and McLoon, S. C., 1986, Distribution of laminin in the developing peripheral nervous system of the chick, Dey. Biol. 113: 429–435.
Runyan, R. B., Maxwell, G. D., and Shur, B. D., 1986, Evidence for a novel enzymatic mechanism of neural crest cell migration on extracellular glycoconjugate matrices, J. Cell Biol. 102: 432–441.
Ruoslahti, E., and Pierschbacher, M. D., 1987, New perspectives in cell adhesion: RGD and integrins, Science 238: 491–497.
Sakurai, Y., Sullivan, M., and Yamada, Y., 1986, al type IV collagen gene evolved differently from fibrillar collagen genes, J. Biol. Chem. 261: 6654–6657.
Sandrock, A. W., Jr., and Matthew, W. D., 1987, An in vitro neurite promoting antigen functions in axonal regeneration in vivo, Science 237: 1605–1608.
Sanes, J. R., Schachner, M., and Covault, J., 1986, Expression of several adhesive macromolecules (N-CAM, Ll, J1, NILE, uvomorulin, laminin, fibronectin and a heparan sulfate proteoglycan) in embryonic, adult and denervated adult skeletal muscle, J. Cell Biol. 102: 420–431.
Santoro, S. A., 1986, Identification of a 160,000 dalton platelet membrane protein that mediates the initial divalent cation-dependent adhesion of platelets to collagen, Cell 46: 913–920.
Sasaki, M., and Yamada, Y., 1987, The laminin B2 chain has a multidomain structure homologous to the B1 chain, J. Biol. Chem. 262: 17111–17117.
Sasaki, M., Kato, S., Kohno, K., Martin, G. R., and Yamada, Y., 1987, Sequence of the cDNA encoding the laminin B1 chain reveals a multidomain protein containing cysteine-rich repeats, Proc. Natl. Acad. Sci. USA 84: 935–939.
Schachner, M., Schoonmaker, G., and Hynes, R. O., 1978, Cellular and subcellular localization of LETS protein in the nervous system, Brain Res. 158: 149–158.
Schwarzbauer, J. E., Paul, J. I., and Hynes, R. O., 1985, On the origin of species of fibronectin, Proc. Natl. Acad. Sci. USA 82: 1424–1428.
Segui-Real, B., Savagner, P., Ogle, R. C., Huang, T., Martin, G. R., and Yamada, Y., 1988, Unusual features of the laminin receptor predicted from cDNA clones, Fed. Proc. 2: A1551.
Sephel, G. C., Burrows,B. A., and Kleinman, H. K., 1989, Laminin neural activity and binding proteins, Dev. Neurosci. 11:in press.
Shadle, P. J., Ginsberg, M. H., Plow, E. F., and Barondes, S. H., 1984, Platelet–collagen adhesion: Inhibition by a monoclonal antibody that binds glycoprotein Ilb, J. Cell Biol. 99: 2056–2060.
Smalheiser, N. R., and Schwartz, N. B., 1987, Cranin: A laminin binding protein of cell membranes, Proc. Natl. Acad. Sci. USA 84: 6457–6461.
Smith, D. E., and Furcht, L. T., 1982, Localization of two unique heparin binding domains of human plasma fibronectin with monoclonal antibodies, J. Biol. Chem. 257: 6518–6523.
Sternberg, J., and Kimber, S. J., 1986, Distribution of fibronectin, laminin and entactin in the environment of migrating neural crest cells in early mouse embryos, J. Embryol. Exp. Morphol. 91: 267–282.
Stewart, G. R., and Pearlman, A. L., 1987, Fibronectin-like immunoreactivity in the developing cerebral cortex, J. Neurosci. 7: 3325–3333.
Suzuki, S., Oldberg, A., Hayman, E. G., Pierschbacher, M. D., and Ruoslahti, E., 1985, Complete amino acid sequence of human vitronectin deduced from cDNA. Similarity of cell attachment sites in vitronectin and fibronectin, EMBO J. 4: 2519–2529.
Suzuki, S., Argraves, W. S., Pytela, R., Arai, H., Krusius, T., Pierschbacher, M. D., and Ruoslahti, E., 1986, cDNA and amino acid sequences of the cell adhesion protein receptor recognizing vitronectin reveal a transmembrane domain and homologies with other adhesion protein receptors, Proc. Natl. Acad. Sci. USA 83: 8614–8618.
Tamkun, J. W., DeSimone, D. W., Fonda, D., Patel, R. S., Buck, C., Horwitz, A. F., and Hynes, R. O., 1986, Structure of integrin, a glycoprotein involved in the transmembrane linkage between fibronectin and actin, Cell 46: 271–282.
Tan, S.-S., Crossin, K. L., Hoffman, S., and Edelman, G. M., 1987, Asymmetric expression in somites of cytotactin and its proteoglycan ligand is correlated with neural crest distribution, Proc. Natl. Acad. Sci. USA 84: 7977–7981.
Tapley, P., Horwitz, A., Buck, C., Burridge, K., Duggan, K., Hirst, R., and Rohrschneider, L., 1989, Integrins isolated from rous sarcoma virus transformed chicken embryo fibroblasts, Oncogene,in press.
Termine, J. D., Kleinman, H. K., William-Whitsu, S., Conn, K. M., McGarvey, M. L., and Martin, G. R., 1981, Osteonectin, a bone-specific protein linking mineral to collagen, Cell 26: 99–105.
Terranova, V. P., Rao, C. N., Kalebic, T., Margulies, I. M., and Liotta, L. A., 1983, Laminin receptor on human breast carcinoma cells, Proc. Natl. Acad. Sci. USA 80: 444–448.
Timpl, R., Rohde, H., Robey, P. G., Rennard, S. I., Foidart, J.-M., and Martin, G. R., 1979, Laminin—A glycoprotein from basement membranes, J. Biol. Chem. 254: 9933–9937.
Timpl, R., Johansson, S., van Delden, V., Oberbaumer, I., and Hook, M., 1983, Characterization of protease-resistant fragments of laminin mediating attachment and spreading of rat hepatocytes, J. Biol. Chem. 258: 8922–8927.
Timpl, R., Fujiwara, S., Dziadek, M., Aumailley, M., Weber, S., and Engel, J., 1984, Laminin, proteoglycan, nidogen and collagen IV: Structural models and molecular interactions, in: Basement Membranes and Cell Movement, pp. 25–43, Pitman, London.
Timpl, R., Oberbäumer, I., von der Mark, K., Bode, W., Wick, G., Weber, S., and Engel, J., 1985, Structure and biology of the globular domain of basement membrane type IV collagen, Ann. N.Y. Acad. Sci. 460: 58–72.
Tomaselli, K. J., Reichardt, L. F., and Bixby, J. L., 1986, Distinct molecular interactions mediate neuronal process outgrowth on nonneuronal cell surfaces and extracellular matrices, J. Cell Biol. 103: 2659–2672.
Tomaselli, K. J., Damsky, C. H., and Reichardt, L. F., 1987, Interaction of a neuronal cell line (PC12) with laminin, collagen IV, and fibronectin: Identification of integrin-related glycoproteins involved in attachment and process outgrowth, J. Cell Biol. 105: 2347–2358.
Tomaselli, K. J., Damsky, C. H., and Reichardt, L. F., 1988, Purification and characterization of mam-malian integrins expressed by a rat neuronal cell line (PC12): evidence that they function as a/13 heterodimeric receptors for laminin and type IV collagen, J. Cell Biol. 107: 1241–1252.
Toyota, B., Carbonetto, S., and David, S., 1988, Involvement of laminin in nerve regeneration in vivo, Soc. Neurosci. Abs. 14: 498.
Trimmer, J. S., and Vacquier, V. D., 1986, Activation of sea urchin gametes, Annu. Rev. Cell Biol. 2: 126.
Trüeb, B., Gröbli, B., Spiess, M., Odermatt, B. F., and Winterhalter, K. H., 1982, Basement membrane (type IV) collagen is a heteropolymer, J. Biol. Chem. 257: 5239–5245.
Tuckett, F., and Morriss-Kay, G. M., 1986, The distribution of fibronectin, laminin and entactin in the neurulating rat embryo by indirect immunofluorescence, J. Embryol. Exp. Morphol. 94: 95–112.
Turner, D. C., Flier, L. A., and Carbonetto, S., 1987, Magnesium-dependent attachment and neurite outgrowth by PC12 cells on collagen and laminin substrata, Del,. Biol. 121: 510–525.
Turner, D. C., Flier, L. A., and Carbonetto, S., 1989, Identification of a cell-surface protein involved in PC12 cell—substratum adhesion and neurite outgrowth on collagen and laminin, J. Neurosci., in press.
Van Harreveld, A., Dafny, N., and Khattab, F. I., 1971, Effects of calcium on the electrical resistance and extracellular space of cerebral cortex, Exp. Neurol. 31: 358–367.
von der Mark, K., and Kühl, U., 1985, Laminin and its receptor, Biochim. Biophys. Acta 823: 147–160.
Waite, K. A., Munai, G., and Culp, L. A., 1987, A second cell-binding domain on fibronectin (RGDS-independent) for neurite extension of human neuroblastoma cells, Exp. Cell Res. 169: 311–327.
Wayner, E. A., and Carter, W. G., 1987, Identification of multiple cell adhesion receptors for collagen and fibronectin in human fibrosarcoma cells possessing unique a and 13 subunits, J. Cell Biol. 105: 1873–1884.
Wewer, U. M., Liotta, L. A., Jaye, M., Ricca, G. A., Drohan, W. N., Claysmith, A. P., Rao, C. N., Wirth, P., Coligan, J. E., Albrechtsen, R., Mudryj, M., and Sobel, M. E., 1986, Altered levels of laminin receptor in various carcinoma cells that have different abilities to bind laminin, Proc. Natl. Acad. Sci. USA 83: 7137–7141.
Yamada, K. M., 1983, Cell surface interactions with extracellular materials, Annu. Rev. Biochem. 52: 76 1799.
Yamada, K. M., and Kennedy, D. W., 1984, Dualistic nature of adhesive protein function: Fibronectin and its biologically active peptide fragments can autoinhibit fibronectin function, J. Cell Biol. 99: 29–36.
Yamada, K. M., and Kennedy, D. W., 1987, Peptide inhibitors of fibronectin, laminin, and other adhesion molecules: Unique and shared features, J. Cell Physiol. 130: 21–28.
Yamada, K. M., Critchley, D. R., Fishman, P. H., and Moss, J., 1983, Exogenous gangliosides enhance the interaction of fibronectin with ganglioside-deficient cells, Exp. Cell Res. 143: 295–302.
Yow, H., Wang, J. M., Chen, H. S., Lee, C., Steele, G. D., Jr., and Chen, L. B., 1988, Increased mRNA expression of a laminin-binding protein in human colon carcinoma: complete sequence of a full-length cDNA encoding the protein, Proc. Natl. Acad. Sci. USA 85: 6394–6398.
Zanetta, J. P., Dontenwill, M., Meyer, A., and Roussel, G., 1985, Isolation and immunohistochemical localization of a lectin-like molecule from the rat cerebellum, Dey. Brain Res. 17: 233–243.
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Douville, P., Carbonetto, S. (1989). Extracellular Matrix Adhesive Glycoproteins and Their Receptors in the Nervous System. In: Margolis, R.U., Margolis, R.K. (eds) Neurobiology of Glycoconjugates. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-5955-6_13
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