메뉴 건너뛰기




Volumn 9, Issue 8, 1999, Pages 823-831

Glycosylation of a CNS-specific extracellular matrix glycoprotein, tenascin-R, is dominated by O-linked sialylated glycans and 'brain-type' neutral N-glycans

Author keywords

CNS; Extracellular matrix; N and O glycans; Sialylation; Tenascin R

Indexed keywords

GLYCOPROTEIN; SCLEROPROTEIN; SIALOGLYCOPROTEIN; TENASCIN;

EID: 0032789158     PISSN: 09596658     EISSN: None     Source Type: Journal    
DOI: 10.1093/glycob/9.8.823     Document Type: Article
Times cited : (41)

References (62)
  • 1
    • 0032529346 scopus 로고    scopus 로고
    • Tenascin-R is antiadhesive for activated microglia that induce downregulation of the protein after peripheral nerve injury: A new role in neuronal protection
    • Angelov, D.N., Walther, M., Streppel, M., Guntinas-Lichius, O., Neiss, W.F., Probstmeier, R. and Pesheva, P. (1998) Tenascin-R is antiadhesive for activated microglia that induce downregulation of the protein after peripheral nerve injury: a new role in neuronal protection. J.Neurosci., 18, 6218-6229.
    • (1998) J.Neurosci. , vol.18 , pp. 6218-6229
    • Angelov, D.N.1    Walther, M.2    Streppel, M.3    Guntinas-Lichius, O.4    Neiss, W.F.5    Probstmeier, R.6    Pesheva, P.7
  • 3
    • 0028783449 scopus 로고
    • The versican C-type lectin domain recognizes the adhesion protein tenascin-R
    • Aspberg, A., Binkert, C. and Ruoslahti, E. (1995) The versican C-type lectin domain recognizes the adhesion protein tenascin-R. Proc. Natl Acad. Sci. USA, 92, 10590-10594.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 10590-10594
    • Aspberg, A.1    Binkert, C.2    Ruoslahti, E.3
  • 4
    • 0030963839 scopus 로고    scopus 로고
    • The C-type lectin domains of lecticans, a family of aggregating chondroitin sulfate proteoglycans, bind tenascin-R by protein-protein interactions independent of carbohydrate moiety
    • Aspberg, A., Miura, R., Bourdoulous, S., Shimonaka, M., Heinegard, D., Schachner, M., Ruoslahti, E. and Yamaguchi, Y. (1997) The C-type lectin domains of lecticans, a family of aggregating chondroitin sulfate proteoglycans, bind tenascin-R by protein-protein interactions independent of carbohydrate moiety. Proc. Natl Acad. Sci. USA, 94, 10116-10121.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 10116-10121
    • Aspberg, A.1    Miura, R.2    Bourdoulous, S.3    Shimonaka, M.4    Heinegard, D.5    Schachner, M.6    Ruoslahti, E.7    Yamaguchi, Y.8
  • 5
    • 0026529925 scopus 로고
    • Immunohistological localization of tenascin in the developing and lesioned adult mouse optic nerve
    • Bartsch, U., Bartsch, S., Dorries, U. and Schachner, M. (1992) Immunohistological localization of tenascin in the developing and lesioned adult mouse optic nerve. Eur. J. Neurosci., 4, 338-352.
    • (1992) Eur. J. Neurosci. , vol.4 , pp. 338-352
    • Bartsch, U.1    Bartsch, S.2    Dorries, U.3    Schachner, M.4
  • 6
    • 0027669963 scopus 로고
    • Expression of janusin (J1-160/180) in the retina and optic nerve of the developing and adult mouse
    • Bartsch, U., Pesheva, P., Raff, M. and Schachner, M. (1993) Expression of janusin (J1-160/180) in the retina and optic nerve of the developing and adult mouse. Glia, 9, 57-69.
    • (1993) Glia , vol.9 , pp. 57-69
    • Bartsch, U.1    Pesheva, P.2    Raff, M.3    Schachner, M.4
  • 7
    • 0029164230 scopus 로고
    • Non-selective and efficient fluorescent labeling of glycans using 2-aminobenzamide and anthranillic acid
    • Bigge, J.C., Patel, T.P., Bruce, J.A., Goulding, P.N., Charles, S.M. and Parekh, R.B. (1995) Non-selective and efficient fluorescent labeling of glycans using 2-aminobenzamide and anthranillic acid. Anal. Biochem., 230, 229-238.
    • (1995) Anal. Biochem. , vol.230 , pp. 229-238
    • Bigge, J.C.1    Patel, T.P.2    Bruce, J.A.3    Goulding, P.N.4    Charles, S.M.5    Parekh, R.B.6
  • 8
    • 0029935338 scopus 로고    scopus 로고
    • Human tenascin-R. Complete primary structure, pre-mRNA alternative splicing and gene localization on chromosome 1q23-q24
    • Carnemolla, B., Leprini, A., Borsi, L., Querze, G., Urbini, S. and Zardi, L. (1996) Human tenascin-R. Complete primary structure, pre-mRNA alternative splicing and gene localization on chromosome 1q23-q24. J.Biol. Chem., 271, 8157-8160.
    • (1996) J.Biol. Chem. , vol.271 , pp. 8157-8160
    • Carnemolla, B.1    Leprini, A.2    Borsi, L.3    Querze, G.4    Urbini, S.5    Zardi, L.6
  • 9
    • 0028158115 scopus 로고
    • Perineuronal nets - A specialized form of extracellular matrix in the adult nervous system
    • Celio, M.R. and Blumcke, I. (1994) Perineuronal nets - a specialized form of extracellular matrix in the adult nervous system. Brain Res. Rev., 19, 128-145.
    • (1994) Brain Res. Rev. , vol.19 , pp. 128-145
    • Celio, M.R.1    Blumcke, I.2
  • 10
    • 0032007314 scopus 로고    scopus 로고
    • Neutral N-glycans in adult rat brain tissue; complete characterisation reveals fucosylated hybrid and complex structures
    • Chen, Y-J., Wing, D.R., Guile, G.R., Dwek, R.A., Harvey, D.J. and Zamze, S. (1998) Neutral N-glycans in adult rat brain tissue; complete characterisation reveals fucosylated hybrid and complex structures. Eur. J. Biochem., 251, 691-703.
    • (1998) Eur. J. Biochem. , vol.251 , pp. 691-703
    • Chen, Y.-J.1    Wing, D.R.2    Guile, G.R.3    Dwek, R.A.4    Harvey, D.J.5    Zamze, S.6
  • 11
    • 0028859440 scopus 로고
    • Tenascins, a growing family of extracellular matrix proteins
    • Chiquet-Ehrismann, R. (1995) Tenascins, a growing family of extracellular matrix proteins. Experientia, 51, 853-862.
    • (1995) Experientia , vol.51 , pp. 853-862
    • Chiquet-Ehrismann, R.1
  • 12
    • 0031745290 scopus 로고    scopus 로고
    • Identification of lectin-purified neural glycoproteins, GPs, 180, 116 and 110 with NMDA and AMPA receptor subunits - Conservation of glycosylation at the synapse
    • Clark, R.A.C., Gurd, J.W., Bissoon, N., Tricaud, N., Molnar, E., Zamze, S., Dwek, R.A., McIlhinney, R.A.J. and Wing, D.R. (1998) Identification of lectin-purified neural glycoproteins, GPs, 180, 116 and 110 with NMDA and AMPA receptor subunits - conservation of glycosylation at the synapse. J. Neurochem., 70, 2594-2605.
    • (1998) J. Neurochem. , vol.70 , pp. 2594-2605
    • Clark, R.A.C.1    Gurd, J.W.2    Bissoon, N.3    Tricaud, N.4    Molnar, E.5    Zamze, S.6    Dwek, R.A.7    McIlhinney, R.A.J.8    Wing, D.R.9
  • 13
    • 0025780182 scopus 로고
    • Purification and properties of sialoadhesin, a sialic acid binding receptor of murine tissue macrophages
    • Crocker, P.R., Kelm, S., Dubois, C., Martin, B., McWilliam, A.S., Shotton, D.M, Paulson, J.C. and Gordon, S. (1991) Purification and properties of sialoadhesin, a sialic acid binding receptor of murine tissue macrophages. EMBO J., 10, 1661-1669.
    • (1991) EMBO J. , vol.10 , pp. 1661-1669
    • Crocker, P.R.1    Kelm, S.2    Dubois, C.3    Martin, B.4    McWilliam, A.S.5    Shotton, D.M.6    Paulson, J.C.7    Gordon, S.8
  • 14
    • 0027685702 scopus 로고
    • Tenascin-C, tenascin-R and tenascin-X: A family of talented proteins in search of functions
    • Erickson, H.P. (1993) Tenascin-C, tenascin-R and tenascin-X: a family of talented proteins in search of functions. Curr. Opin. Cell Biol., 5, 869-876.
    • (1993) Curr. Opin. Cell Biol. , vol.5 , pp. 869-876
    • Erickson, H.P.1
  • 15
    • 0025159279 scopus 로고
    • Two monoclonal antibodies recognizing epitopes on neural adhesion molecules interfere with cell interactions
    • Fahrig, T. Schmitz, B., Weber, D., Kucherer-Ehret, A., Faissner, A. and Schachner, M. (1990) Two monoclonal antibodies recognizing epitopes on neural adhesion molecules interfere with cell interactions. Eur. J. Neurosci., 2, 153-161.
    • (1990) Eur. J. Neurosci. , vol.2 , pp. 153-161
    • Fahrig, T.1    Schmitz, B.2    Weber, D.3    Kucherer-Ehret, A.4    Faissner, A.5    Schachner, M.6
  • 16
    • 0025259964 scopus 로고
    • J1/tenascin is a repulsive substrate for central nervous system neurons
    • Faissner, A. and Kruse, J. (1990) J1/tenascin is a repulsive substrate for central nervous system neurons. Neuron, 5, 627-637.
    • (1990) Neuron , vol.5 , pp. 627-637
    • Faissner, A.1    Kruse, J.2
  • 17
    • 0003087130 scopus 로고
    • Tenascin and Janusin: Glial recognition molecules involved in neural development and recognition
    • Kettenmann, H. and Ransom, B.R. (eds.), Oxford University Press, New York
    • Faissner, A. and Schachner, M. (1995) Tenascin and Janusin: Glial recognition molecules involved in neural development and recognition. In Kettenmann, H. and Ransom, B.R. (eds.), Neuroglia, Oxford University Press, New York, pp. 422-426.
    • (1995) Neuroglia , pp. 422-426
    • Faissner, A.1    Schachner, M.2
  • 19
    • 0343765721 scopus 로고    scopus 로고
    • Concerted action of tenascin-C domains in cell adhesion, anti-adhesion and promotion of neurite outgrowth
    • Fischer, D., Brown-Lüdi, M., Schulthess, T. and Chiquet-Ehrismann, R. (1997) Concerted action of tenascin-C domains in cell adhesion, anti-adhesion and promotion of neurite outgrowth. J. Cell Sci., 110, 1513-1522.
    • (1997) J. Cell Sci. , vol.110 , pp. 1513-1522
    • Fischer, D.1    Brown-Lüdi, M.2    Schulthess, T.3    Chiquet-Ehrismann, R.4
  • 20
    • 0027397492 scopus 로고
    • Molecular characterisation and in situ mRNA localization of the neural recognition molecule J1-160/180: A modular structure similar to tenascin
    • Fuss, B., Wintergerst, E.-S., Bartsch, U. and Schachner, M. (1993) Molecular characterisation and in situ mRNA localization of the neural recognition molecule J1-160/180: a modular structure similar to tenascin. J.Cell Biol., 120, 1237-1249.
    • (1993) J.Cell Biol. , vol.120 , pp. 1237-1249
    • Fuss, B.1    Wintergerst, E.-S.2    Bartsch, U.3    Schachner, M.4
  • 21
    • 0028053975 scopus 로고
    • Analytical and preparative separation of anionic oligosaccharides by weak anion-exchange high-performance liquid chromatography on an inert polymer column
    • Guile, G.R., Wong, S.Y.C. and Dwek, R.A. (1994) Analytical and preparative separation of anionic oligosaccharides by weak anion-exchange high-performance liquid chromatography on an inert polymer column. Anal. Biochem., 222, 231-235.
    • (1994) Anal. Biochem. , vol.222 , pp. 231-235
    • Guile, G.R.1    Wong, S.Y.C.2    Dwek, R.A.3
  • 22
    • 0030571019 scopus 로고    scopus 로고
    • A rapid high-resolution high-performance liquid chromatographic method for separating glycan mixtures and analysing oligosaccharide profiles
    • Guile, G.R., Rudd, P.M., Wing, D.R., Prime, S. and Dwek, R.A. (1996) A rapid high-resolution high-performance liquid chromatographic method for separating glycan mixtures and analysing oligosaccharide profiles. Anal. Biochem., 230, 210-226.
    • (1996) Anal. Biochem. , vol.230 , pp. 210-226
    • Guile, G.R.1    Rudd, P.M.2    Wing, D.R.3    Prime, S.4    Dwek, R.A.5
  • 23
    • 0027243414 scopus 로고
    • The 4th immunoglobulin-like domain of N-CAM contains a carbohydrate recognition domain for oligomannosidic glycans implicated in association with L1 and neurite outgrowth
    • Horstkorte, R., Schachner, M., Magyar, J.R. Vorherr, T. and Schmitz, B. (1993) The 4th immunoglobulin-like domain of N-CAM contains a carbohydrate recognition domain for oligomannosidic glycans implicated in association with L1 and neurite outgrowth. J. Cell Biol., 121, 1409-1421.
    • (1993) J. Cell Biol. , vol.121 , pp. 1409-1421
    • Horstkorte, R.1    Schachner, M.2    Magyar, J.R.3    Vorherr, T.4    Schmitz, B.5
  • 24
    • 0025297888 scopus 로고
    • Why are proteins O-glycosylated?
    • Jentoft, N. (1990) Why are proteins O-glycosylated? Trends Biol. Sci., 15, 291-294.
    • (1990) Trends Biol. Sci. , vol.15 , pp. 291-294
    • Jentoft, N.1
  • 25
    • 0027688857 scopus 로고
    • Astrocytes and neurons regulate the expression of the neural recognition molecule janusin by cultured oligodendrocytes
    • Jung, M., Pesheva, P., Schachner, M. and Trotter, J. (1993) Astrocytes and neurons regulate the expression of the neural recognition molecule janusin by cultured oligodendrocytes. Glia, 9, 163-175.
    • (1993) Glia , vol.9 , pp. 163-175
    • Jung, M.1    Pesheva, P.2    Schachner, M.3    Trotter, J.4
  • 27
    • 0021800963 scopus 로고
    • The J1 glycoprotein - A novel nervous system cell adhesion molecule of the L2/HNK-1 family
    • 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.
    • (1985) Nature , vol.316 , pp. 146-148
    • Kruse, J.1    Keilhauer, G.2    Faissner, A.3    Timpl, R.4    Schachner, M.5
  • 28
    • 0031586351 scopus 로고    scopus 로고
    • Inhibitors of protein kinases abolish ECM-mediated promotion of neuronal polarity
    • Lochter, A. and Schachner, M. (1997) Inhibitors of protein kinases abolish ECM-mediated promotion of neuronal polarity. Exp. Cell Res., 235, 124-129.
    • (1997) Exp. Cell Res. , vol.235 , pp. 124-129
    • Lochter, A.1    Schachner, M.2
  • 29
    • 0025836594 scopus 로고
    • J1/Tenascin in substrate-bound and soluble form displays contrary effects on neurite outgrowth
    • Lochter, A., Vaughan, L., Kaplony, A., Prochiantz, A., Schachner, M. and Faissner, A. (1991) J1/Tenascin in substrate-bound and soluble form displays contrary effects on neurite outgrowth. J.Cell Biol., 113, 1159-1171.
    • (1991) J.Cell Biol. , vol.113 , pp. 1159-1171
    • Lochter, A.1    Vaughan, L.2    Kaplony, A.3    Prochiantz, A.4    Schachner, M.5    Faissner, A.6
  • 30
    • 0031915973 scopus 로고    scopus 로고
    • The glycosylation and structure of human serum IgA1, Fab and Fc regions and the role of N-glycosylation in Fca receptor interactions
    • Mattu, T.S., Pleass, R.J., Willis, A.C, Killian, M., Wormald, M.R., Lellouch, A.C., Rudd, P.M., Woof, J.M. and Dwek, R.A. (1998) The glycosylation and structure of human serum IgA1, Fab and Fc regions and the role of N-glycosylation in Fca receptor interactions. J. Biol. Chem., 273, 2260-2272.
    • (1998) J. Biol. Chem. , vol.273 , pp. 2260-2272
    • Mattu, T.S.1    Pleass, R.J.2    Willis, A.C.3    Killian, M.4    Wormald, M.R.5    Lellouch, A.C.6    Rudd, P.M.7    Woof, J.M.8    Dwek, R.A.9
  • 31
    • 0032549591 scopus 로고    scopus 로고
    • High affinity binding and overlapping localization of neurocan amd phosphacan/protein-tyrosine phosphatase-zeta/beta with tenascin-R, amphoterin and the heparin-binding growth-associated molecule
    • Milev, P., Chiba, A., Haring, M., Rauvala, H., Schachner, M., Ranscht, B., Margolis, R.K. and Margolis, R.U. (1998) High affinity binding and overlapping localization of neurocan amd phosphacan/protein-tyrosine phosphatase-zeta/beta with tenascin-R, amphoterin and the heparin-binding growth-associated molecule. J. Biol. Chem., 273, 6998-7005.
    • (1998) J. Biol. Chem. , vol.273 , pp. 6998-7005
    • Milev, P.1    Chiba, A.2    Haring, M.3    Rauvala, H.4    Schachner, M.5    Ranscht, B.6    Margolis, R.K.7    Margolis, R.U.8
  • 32
    • 0025338819 scopus 로고
    • Oligodendrocyte-derived J1-160/180 extracellular matrix glycoproteins are adhesive or repulsive depending on the partner cell type and time of interaction
    • Morganti, M.C., Taylor, J., Pesheva, P. and Schachner, M. (1990) Oligodendrocyte-derived J1-160/180 extracellular matrix glycoproteins are adhesive or repulsive depending on the partner cell type and time of interaction. Exp. Neurol., 109, 98-110.
    • (1990) Exp. Neurol. , vol.109 , pp. 98-110
    • Morganti, M.C.1    Taylor, J.2    Pesheva, P.3    Schachner, M.4
  • 33
    • 0026633247 scopus 로고
    • The chicken neural extracellular matrix molecule restrictin: Similarity with EGF-, fibronectin type III- and fibrinogen-like motifs
    • Norenberg, U., Wille, H., Wolff, M., Frank, R. and Rathjen, F.G. (1992) The chicken neural extracellular matrix molecule restrictin: similarity with EGF-, fibronectin type III- and fibrinogen-like motifs. Neuron, 8, 849-863.
    • (1992) Neuron , vol.8 , pp. 849-863
    • Norenberg, U.1    Wille, H.2    Wolff, M.3    Frank, R.4    Rathjen, F.G.5
  • 34
    • 0030175346 scopus 로고    scopus 로고
    • Structural and functional characterization of tenascin-R (restrictin), an extracellular matrix glycoprotein of glial cells and neurons
    • Norenberg, U., Hubert, M. and Rathjen, F.G. (1996) Structural and functional characterization of tenascin-R (restrictin), an extracellular matrix glycoprotein of glial cells and neurons. Int. J. Dev. Neurosci., 14, 217-231.
    • (1996) Int. J. Dev. Neurosci. , vol.14 , pp. 217-231
    • Norenberg, U.1    Hubert, M.2    Rathjen, F.G.3
  • 35
    • 0032516205 scopus 로고    scopus 로고
    • The molecular elasticity of the extracellular matrix protein tenascin
    • Oberhauser, A.F., Marszalek, P.E., Erickson, H.P. and Fernandez, J.M. (1998) The molecular elasticity of the extracellular matrix protein tenascin. Nature, 393, 181-185.
    • (1998) Nature , vol.393 , pp. 181-185
    • Oberhauser, A.F.1    Marszalek, P.E.2    Erickson, H.P.3    Fernandez, J.M.4
  • 36
    • 0023338172 scopus 로고
    • Tissue-specific N-glycosylation, site-specific oligosaccharide patterns and lentil lectin recognition of rat Thy-1
    • Parekh, R.B., Tse, A.G.D., Dwek, R.A., Williams, A.F. and Rademacher, T.W. (1987) Tissue-specific N-glycosylation, site-specific oligosaccharide patterns and lentil lectin recognition of rat Thy-1. EMBO J., 6, 1233-1244.
    • (1987) EMBO J. , vol.6 , pp. 1233-1244
    • Parekh, R.B.1    Tse, A.G.D.2    Dwek, R.A.3    Williams, A.F.4    Rademacher, T.W.5
  • 37
    • 0027441378 scopus 로고
    • Use of hydrazine to release in intact and unreduced form both N- and O-linked oligosaccharides from glycoproteins
    • Patel, T., Bruce, J., Merry, A., Bigge, C., Wormald, M., Jaques, A. and Parekh, R. (1993) Use of hydrazine to release in intact and unreduced form both N- and O-linked oligosaccharides from glycoproteins. Biochemistry, 32, 679-693.
    • (1993) Biochemistry , vol.32 , pp. 679-693
    • Patel, T.1    Bruce, J.2    Merry, A.3    Bigge, C.4    Wormald, M.5    Jaques, A.6    Parekh, R.7
  • 38
    • 0026564842 scopus 로고
    • The blood-brain barrier regulates the expression of a macrophage sialic acid-binding receptor on microglia
    • Perry, V.H., Crocker, P.R. and Gordon, S. (1992) The blood-brain barrier regulates the expression of a macrophage sialic acid-binding receptor on microglia. J. Cell Sci., 101, 201-207.
    • (1992) J. Cell Sci. , vol.101 , pp. 201-207
    • Perry, V.H.1    Crocker, P.R.2    Gordon, S.3
  • 39
    • 0024424947 scopus 로고
    • J1-160 and J1-180 are oligodendrocyte-secreted nonpermissive substrates for cell adhesion
    • Pesheva, P., Spiess, E. and Schachner, M. (1989) J1-160 and J1-180 are oligodendrocyte-secreted nonpermissive substrates for cell adhesion. J. Cell Biol., 109, 1765-1778.
    • (1989) J. Cell Biol. , vol.109 , pp. 1765-1778
    • Pesheva, P.1    Spiess, E.2    Schachner, M.3
  • 40
    • 0027526588 scopus 로고
    • The F3/F11 cell adhesion molecule mediates the repulsion of neurons by the extracellular matrix glycoprotein J1-160/180
    • Pesheva, P., Gennarini, G., Goridis, C. and Schachner, M. (1993) The F3/F11 cell adhesion molecule mediates the repulsion of neurons by the extracellular matrix glycoprotein J1-160/180. Neuron, 10, 69-82.
    • (1993) Neuron , vol.10 , pp. 69-82
    • Pesheva, P.1    Gennarini, G.2    Goridis, C.3    Schachner, M.4
  • 41
    • 0030919911 scopus 로고    scopus 로고
    • Tenascin-R is an intrinsic autocrine factor for oligodendrocyte differentiation and promotes cell adhesion by a sulfatide-mediated mechanism
    • Pesheva, P., Gloor, S., Schachner, M. and Probstmeier, R. (1997) Tenascin-R is an intrinsic autocrine factor for oligodendrocyte differentiation and promotes cell adhesion by a sulfatide-mediated mechanism. J. Neurosci., 17, 4642-4651.
    • (1997) J. Neurosci. , vol.17 , pp. 4642-4651
    • Pesheva, P.1    Gloor, S.2    Schachner, M.3    Probstmeier, R.4
  • 42
    • 0032940329 scopus 로고    scopus 로고
    • I-type lectins in the nervous system
    • Probstmeier, R. and Pesheva, P. (1999) I-type lectins in the nervous system. Prog. Neurobiol., 58, 163-184.
    • (1999) Prog. Neurobiol. , vol.58 , pp. 163-184
    • Probstmeier, R.1    Pesheva, P.2
  • 43
    • 0025744729 scopus 로고
    • A chick neural extracellular matrix protein involved in cell attachment co-purifies with the cell recognition molecule F11
    • Rathjen, F.G., Wolff, J.M. and Chiquet-Ehrismann, R. (1991) A chick neural extracellular matrix protein involved in cell attachment co-purifies with the cell recognition molecule F11. Development, 13, 151-164.
    • (1991) Development , vol.13 , pp. 151-164
    • Rathjen, F.G.1    Wolff, J.M.2    Chiquet-Ehrismann, R.3
  • 44
    • 0026020097 scopus 로고
    • Extracellular matrix molecules and their receptors: Functions in neural development
    • Reichardt, L.F. and Tomaselli, K.J. (1991) Extracellular matrix molecules and their receptors: functions in neural development. Annu. Rev. Neurosci., 14, 531-570.
    • (1991) Annu. Rev. Neurosci. , vol.14 , pp. 531-570
    • Reichardt, L.F.1    Tomaselli, K.J.2
  • 45
    • 0029823181 scopus 로고    scopus 로고
    • Brain extracellular matrix
    • Ruoslahti, E. (1996) Brain extracellular matrix. Glycobiology, 6, 489-492.
    • (1996) Glycobiology , vol.6 , pp. 489-492
    • Ruoslahti, E.1
  • 46
    • 0028965141 scopus 로고
    • Glycans and the modulation of neural-recognition molecule function
    • Schachner, M. and Martini, R. (1995) Glycans and the modulation of neural-recognition molecule function. Trends Neurosci., 18, 183-191.
    • (1995) Trends Neurosci. , vol.18 , pp. 183-191
    • Schachner, M.1    Martini, R.2
  • 47
    • 0028704499 scopus 로고
    • The perplexing multifunctionality of janusin, a tenascin-related molecule
    • Schachner, M., Taylor, J., Bartsch, U. and Pesheva, P. (1994) The perplexing multifunctionality of janusin, a tenascin-related molecule. Perspect. Dev. Neurobiol., 2, 33-41.
    • (1994) Perspect. Dev. Neurobiol. , vol.2 , pp. 33-41
    • Schachner, M.1    Taylor, J.2    Bartsch, U.3    Pesheva, P.4
  • 48
    • 0027429703 scopus 로고
    • Structures of N-linked sugar chains expressed mainly in mouse brain
    • Shimizu, H., Ochai, K., Ikenaka, K., Mikoshiba, K. and Hase, S. (1993) Structures of N-linked sugar chains expressed mainly in mouse brain. J. Biochem. (Tokyo), 114, 334-338.
    • (1993) J. Biochem. (Tokyo) , vol.114 , pp. 334-338
    • Shimizu, H.1    Ochai, K.2    Ikenaka, K.3    Mikoshiba, K.4    Hase, S.5
  • 49
    • 0032402696 scopus 로고    scopus 로고
    • Glycan specificity of myelin-associated glycoprotein and sialoadhesin deduced from interactions with synthetic oligosaccharides
    • Strenge, K., Schauer, R., Bovin, N., Hasegawa, A., Ishida, H., Kiso, M. and Kelm, S. (1998) Glycan specificity of myelin-associated glycoprotein and sialoadhesin deduced from interactions with synthetic oligosaccharides. Eur. J. Biochem., 258, 677-685.
    • (1998) Eur. J. Biochem. , vol.258 , pp. 677-685
    • Strenge, K.1    Schauer, R.2    Bovin, N.3    Hasegawa, A.4    Ishida, H.5    Kiso, M.6    Kelm, S.7
  • 50
    • 0027190321 scopus 로고
    • Influence of janusin and tenascin on growth cone behaviour in vitro
    • Taylor, J., Pesheva, P. and Schachner, M. (1993) Influence of janusin and tenascin on growth cone behaviour in vitro. J. Neurosci. Res., 35, 347-362.
    • (1993) J. Neurosci. Res. , vol.35 , pp. 347-362
    • Taylor, J.1    Pesheva, P.2    Schachner, M.3
  • 51
    • 0025865091 scopus 로고
    • Amino acid distributions around O-linked glycosylation sites
    • Wilson, I.B.H., Gavel, Y. and von Heijne, G. (1991) Amino acid distributions around O-linked glycosylation sites. Biochem. J., 275, 529-534.
    • (1991) Biochem. J. , vol.275 , pp. 529-534
    • Wilson, I.B.H.1    Gavel, Y.2    Von Heijne, G.3
  • 52
    • 0027401599 scopus 로고
    • Localisation of janusin mRNA in the central nervous system of the developing and adult mouse
    • Wintergerst, E.-S., Fuss, B. and Bartsch, U. (1993) Localisation of janusin mRNA in the central nervous system of the developing and adult mouse. Eur. J .Neurosci., 5, 299-310.
    • (1993) Eur. J. Neurosci. , vol.5 , pp. 299-310
    • Wintergerst, E.-S.1    Fuss, B.2    Bartsch, U.3
  • 53
    • 0029978087 scopus 로고    scopus 로고
    • Distinct effects of recombinant tenascin-R domains in neuronal cell functions and identification of the domain interacting with the neuronal recognition molecule F3/F11
    • Xiao, Z.C., Taylor, J., Montag, D., Rougon, G. and Schachner, M. (1996) Distinct effects of recombinant tenascin-R domains in neuronal cell functions and identification of the domain interacting with the neuronal recognition molecule F3/F11. Eur. J. Neurosci., 8, 766-782.
    • (1996) Eur. J. Neurosci. , vol.8 , pp. 766-782
    • Xiao, Z.C.1    Taylor, J.2    Montag, D.3    Rougon, G.4    Schachner, M.5
  • 54
    • 0031449805 scopus 로고    scopus 로고
    • Isolation of a tenascin-R binding protein from mouse brain membranes. A phosphacan-related chondroitin sulfate proteoglycan
    • Xiao, Z.C., Bartsch, U., Margolis, R.K., Rougon, G., Montag, D. and Schachner, M. (1997a) Isolation of a tenascin-R binding protein from mouse brain membranes. A phosphacan-related chondroitin sulfate proteoglycan. J. Biol. Chem., 272, 32092-32101.
    • (1997) J. Biol. Chem. , vol.272 , pp. 32092-32101
    • Xiao, Z.C.1    Bartsch, U.2    Margolis, R.K.3    Rougon, G.4    Montag, D.5    Schachner, M.6
  • 55
    • 0030960984 scopus 로고    scopus 로고
    • Signaling events following the interaction of the neuronal adhesion molecule F3 with the N-terminal domain of tenascin-R
    • Xiao, Z.C., Hillenbrand, R., Schachner, M., Thermes, S., Rougon, G. and Gomez, S. (1997b) Signaling events following the interaction of the neuronal adhesion molecule F3 with the N-terminal domain of tenascin-R. J. Neurosci. Res., 49, 698-709.
    • (1997) J. Neurosci. Res. , vol.49 , pp. 698-709
    • Xiao, Z.C.1    Hillenbrand, R.2    Schachner, M.3    Thermes, S.4    Rougon, G.5    Gomez, S.6
  • 56
    • 0032524781 scopus 로고    scopus 로고
    • Defasciculation of neurites is mediated by tenascin-R and its neuronal receptor F3/F11
    • Xiao, Z.C., Revest, J.M., Laeng, R. Rougon, G., Schachner, M. and Montag, D. (1998) Defasciculation of neurites is mediated by tenascin-R and its neuronal receptor F3/F11. J. Neurosci. Res., 52, 390-404.
    • (1998) J. Neurosci. Res. , vol.52 , pp. 390-404
    • Xiao, Z.C.1    Revest, J.M.2    Laeng, R.3    Rougon, G.4    Schachner, M.5    Montag, D.6
  • 58
    • 0020479801 scopus 로고
    • Structural studies of the sugar chains of hen ovomucoid
    • Yamashita, K., Kamerling, J.P. and Kobata, A. (1992) Structural studies of the sugar chains of hen ovomucoid. J. Biol. Chem., 257, 12809-12814.
    • (1992) J. Biol. Chem. , vol.257 , pp. 12809-12814
    • Yamashita, K.1    Kamerling, J.P.2    Kobata, A.3
  • 60
    • 0031004767 scopus 로고    scopus 로고
    • Brain contains HNK-1 immunoreactive O-glycans of the sulfoglucuronyl lactosamine series that terminate in 2-linked or, 2,6-linked hexose (mannose)
    • Yuen, C.T., Chai, W., Loveless, R.W., Lawson, A.M., Margolis, R.U. and Feizi, T. (1997) Brain contains HNK-1 immunoreactive O-glycans of the sulfoglucuronyl lactosamine series that terminate in 2-linked or, 2,6-linked hexose (mannose). J. Biol. Chem., 272, 8924-8931.
    • (1997) J. Biol. Chem. , vol.272 , pp. 8924-8931
    • Yuen, C.T.1    Chai, W.2    Loveless, R.W.3    Lawson, A.M.4    Margolis, R.U.5    Feizi, T.6
  • 61
    • 0032533383 scopus 로고    scopus 로고
    • Sialylated N-glycans in adult rat brain tissue. A widespread distribution of disialylated antennae in complex and hybrid structures
    • Zamze, S., Harvey, D.J., Chen, Y.-J., Guile, G.R., Dwek, R.A. and Wing, D.R. (1998) Sialylated N-glycans in adult rat brain tissue. A widespread distribution of disialylated antennae in complex and hybrid structures. Eur. J. Biochem., 258, 243-270.
    • (1998) Eur. J. Biochem. , vol.258 , pp. 243-270
    • Zamze, S.1    Harvey, D.J.2    Chen, Y.-J.3    Guile, G.R.4    Dwek, R.A.5    Wing, D.R.6
  • 62
    • 0026688638 scopus 로고
    • Neuronal cell adhesion molecule contactin/F11 binds to tenascin via its immunoglobulin-like domains
    • Zisch, A.H., D'Alessandri, L., Ranscht, B., Falchetto, R., Winterhalter, K.H. and Vaughan, L. (1992) Neuronal cell adhesion molecule contactin/F11 binds to tenascin via its immunoglobulin-like domains. J. Cell Biol., 119, 203-213.
    • (1992) J. Cell Biol. , vol.119 , pp. 203-213
    • Zisch, A.H.1    D'Alessandri, L.2    Ranscht, B.3    Falchetto, R.4    Winterhalter, K.H.5    Vaughan, L.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.