메뉴 건너뛰기




Volumn 3, Issue 12, 2008, Pages

Cell surface sialylation and fucosylation are regulated by L1 via phospholipase Cγ and cooperate to modulate neurite outgrowth, cell survival and migration

Author keywords

[No Author keywords available]

Indexed keywords

CELL SURFACE MARKER; FUCOSYLTRANSFERASE; IMMUNOGLOBULIN G; LECTIN; MESSENGER RNA; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE INHIBITOR; PHOSPHOLIPASE C GAMMA; PHOSPHOLIPASE C INHIBITOR; POLYCLONAL ANTIBODY; SHORT HAIRPIN RNA; SIALIC ACID; SIALYLTRANSFERASE; BETA D GALACTOSIDE ALPHA 2 6 SIALYLTRANSFERASE; BETA-D-GALACTOSIDE ALPHA 2-6-SIALYLTRANSFERASE; FUCOSYLTRANSFERASE 9, MOUSE; NERVE CELL ADHESION MOLECULE L1; UNCLASSIFIED DRUG;

EID: 57349171403     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0003841     Document Type: Article
Times cited : (18)

References (41)
  • 1
    • 0024431691 scopus 로고
    • Glycosyltransferases: Structure, localization and control of cell type-specific glycosylation
    • Paulson JC, Colley JC (1989) Glycosyltransferases: structure, localization and control of cell type-specific glycosylation. J Biol Chem 264: 17615-17618.
    • (1989) J Biol Chem , vol.264 , pp. 17615-17618
    • Paulson, J.C.1    Colley, J.C.2
  • 2
    • 0032754473 scopus 로고    scopus 로고
    • On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database
    • Apweiler R, Hermjakob H, Sharon N (1999) On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database. Biochim Biophys Acta 1473: 4-8.
    • (1999) Biochim Biophys Acta , vol.1473 , pp. 4-8
    • Apweiler, R.1    Hermjakob, H.2    Sharon, N.3
  • 3
    • 33947724303 scopus 로고    scopus 로고
    • Complex N-glycan number and degree of branching cooperate to regulate cell proliferation and differentiation
    • Lau KS, Partridge EA, Grigorian A, Silvescu CI, Reinhold VN, et al. (2007) Complex N-glycan number and degree of branching cooperate to regulate cell proliferation and differentiation. Cell 29: 123-134.
    • (2007) Cell , vol.29 , pp. 123-134
    • Lau, K.S.1    Partridge, E.A.2    Grigorian, A.3    Silvescu, C.I.4    Reinhold, V.N.5
  • 4
    • 34247565506 scopus 로고    scopus 로고
    • Glycan-based interactions involving vertebrate sialic-acid-recognizing proteins
    • Varki A (2007) Glycan-based interactions involving vertebrate sialic-acid-recognizing proteins. Nature 446: 1023-1029.
    • (2007) Nature , vol.446 , pp. 1023-1029
    • Varki, A.1
  • 5
    • 33745381312 scopus 로고    scopus 로고
    • Genetic defects in the human glycome
    • Freeze HH (2006) Genetic defects in the human glycome. Nat Rev Genet 7: 537-551.
    • (2006) Nat Rev Genet , vol.7 , pp. 537-551
    • Freeze, H.H.1
  • 6
    • 0042266719 scopus 로고    scopus 로고
    • A genetic approach to mammalian glycan function
    • Lowe JB, Marth JD (2003) A genetic approach to mammalian glycan function. Annu Rev Biochem 72: 643-691.
    • (2003) Annu Rev Biochem , vol.72 , pp. 643-691
    • Lowe, J.B.1    Marth, J.D.2
  • 7
    • 1342310622 scopus 로고    scopus 로고
    • Glycans and neural cell interactions
    • Kleene R, Schachner M (2004) Glycans and neural cell interactions. Nat Rev Neurosci 5: 95-208.
    • (2004) Nat Rev Neurosci , vol.5 , pp. 95-208
    • Kleene, R.1    Schachner, M.2
  • 8
    • 0038495798 scopus 로고    scopus 로고
    • Fucose: Biosynthesis and biological function in mammals
    • Becker DJ, Lowe JB (2003) Fucose: biosynthesis and biological function in mammals. Glycobiology 13: 41R-53R.
    • (2003) Glycobiology , vol.13
    • Becker, D.J.1    Lowe, J.B.2
  • 9
    • 29444434177 scopus 로고    scopus 로고
    • The breast cancer susceptibility gene BRCA1 regulates progesterone receptor signaling in mammary epithelial cells
    • Ma Y, Katiyar P, Jones LP, Fan S, Zhang Y, et al. (2006) The breast cancer susceptibility gene BRCA1 regulates progesterone receptor signaling in mammary epithelial cells. Mol Endocrinol 20: 14-34.
    • (2006) Mol Endocrinol , vol.20 , pp. 14-34
    • Ma, Y.1    Katiyar, P.2    Jones, L.P.3    Fan, S.4    Zhang, Y.5
  • 10
    • 14844355836 scopus 로고    scopus 로고
    • Chaperone activity of protein O-fucosyltransferase 1 promotes notch receptor folding
    • Okajima T, Xu A, Lei L, Irvine KD (2005) Chaperone activity of protein O-fucosyltransferase 1 promotes notch receptor folding. Science 307: 1599-1603.
    • (2005) Science , vol.307 , pp. 1599-1603
    • Okajima, T.1    Xu, A.2    Lei, L.3    Irvine, K.D.4
  • 12
    • 0035877721 scopus 로고    scopus 로고
    • The neural recognition molecule L1 is a sialic acid-binding lectin for CD24, which induces promotion and inhibition of neurite outgrowth
    • Kleene R, Yang H, Kutsche M, Schachner M (2001) The neural recognition molecule L1 is a sialic acid-binding lectin for CD24, which induces promotion and inhibition of neurite outgrowth. J Biol Chem 276: 21656-21663.
    • (2001) J Biol Chem , vol.276 , pp. 21656-21663
    • Kleene, R.1    Yang, H.2    Kutsche, M.3    Schachner, M.4
  • 13
    • 33845882730 scopus 로고    scopus 로고
    • Neural recognition molecules of the immunoglobulin superfamily: Signaling transducers of axon guidance and neuronal migration
    • Maness PF, Schachner M (2007) Neural recognition molecules of the immunoglobulin superfamily: signaling transducers of axon guidance and neuronal migration. Nat Neurosci 10: 19-26.
    • (2007) Nat Neurosci , vol.10 , pp. 19-26
    • Maness, P.F.1    Schachner, M.2
  • 14
    • 0034639938 scopus 로고    scopus 로고
    • Neural cell recognition molecule L1: Relating biological complexity to human disease mutations
    • Kenwrick S, Watkins A, De Angelis E (2000) Neural cell recognition molecule L1: relating biological complexity to human disease mutations. Human Molecular Genetics 9: 879-886.
    • (2000) Human Molecular Genetics , vol.9 , pp. 879-886
    • Kenwrick, S.1    Watkins, A.2    De Angelis, E.3
  • 15
    • 0037164021 scopus 로고    scopus 로고
    • Lectin structure-activity: The story is never over
    • Goldstein IJ (2002) Lectin structure-activity: the story is never over. J Agric Food Chem 50: 6583-6585.
    • (2002) J Agric Food Chem , vol.50 , pp. 6583-6585
    • Goldstein, I.J.1
  • 16
    • 7244258916 scopus 로고    scopus 로고
    • History of lectins: From hemagglutinins to biological recognition molecules
    • Sharon N, Lis H (2004) History of lectins: from hemagglutinins to biological recognition molecules. Glycobiology 14: 53R-62R.
    • (2004) Glycobiology , vol.14
    • Sharon, N.1    Lis, H.2
  • 17
    • 0028786572 scopus 로고    scopus 로고
    • Appel F, Holm J, Conscience JF, Von Bohlen und Halbach F, Faissner A, et al. (1995) Identification of the border between fibronectin type III homologous repeats 2 and 3 of the neural cell adhesion molecule L1 as a neurite outgrowth promoting and signal transducing domain. J Neurobiol 28: 297-312.
    • Appel F, Holm J, Conscience JF, Von Bohlen und Halbach F, Faissner A, et al. (1995) Identification of the border between fibronectin type III homologous repeats 2 and 3 of the neural cell adhesion molecule L1 as a neurite outgrowth promoting and signal transducing domain. J Neurobiol 28: 297-312.
  • 18
    • 0025159279 scopus 로고
    • Two monoclonal antibodies recognizing carbohydrate epitopes on neural adhesion molecules interfere with cell interactions
    • Fahrig T, Schmitz B, Weber D, Kucherer-Ehret A, Faissner A, et al. (1990) Two monoclonal antibodies recognizing carbohydrate 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
  • 19
    • 0023279094 scopus 로고
    • The novel carbohydrate epitope L3 is shared by some neural cell adhesion molecules
    • Kucherer A, Faissner A, Schachner M (1987) The novel carbohydrate epitope L3 is shared by some neural cell adhesion molecules. J Cell Biol 104: 1597-1602.
    • (1987) J Cell Biol , vol.104 , pp. 1597-1602
    • Kucherer, A.1    Faissner, A.2    Schachner, M.3
  • 20
    • 0025054160 scopus 로고
    • Isolation and biochemical characterization of a neural proteoglycan expressing the L5 carbohydrate epitope
    • Streit A, Faissner A, Gehrig B, Schachner M (1990) Isolation and biochemical characterization of a neural proteoglycan expressing the L5 carbohydrate epitope. J Neurochem 55: 1494-1506.
    • (1990) J Neurochem , vol.55 , pp. 1494-1506
    • Streit, A.1    Faissner, A.2    Gehrig, B.3    Schachner, M.4
  • 21
    • 0029670645 scopus 로고    scopus 로고
    • x carbohydrate sequence is recognized by antibody to L5, a functional antigen in early neural development
    • x carbohydrate sequence is recognized by antibody to L5, a functional antigen in early neural development. J Neurochem 66: 834-844.
    • (1996) J Neurochem , vol.66 , pp. 834-844
    • Streit, A.1    Yuen, C.T.2    Wendy Loveless, R.3    Lawson, A.M.4    Finne, J.5
  • 22
    • 15244346626 scopus 로고    scopus 로고
    • Signal transduction pathways implicated in neural recognition molecule L1 triggered neuroprotection and neuritogenesis
    • Loers G, Chen S, Grumet M, Schachner M (2005) Signal transduction pathways implicated in neural recognition molecule L1 triggered neuroprotection and neuritogenesis. J Neurochem 92: 1463-1476.
    • (2005) J Neurochem , vol.92 , pp. 1463-1476
    • Loers, G.1    Chen, S.2    Grumet, M.3    Schachner, M.4
  • 23
    • 0022270860 scopus 로고
    • Differential inhibition of neurone-neurone, neurone-astrocyte and astrocyte-astrocyte adhesion by L1, L2 and N-CAM antibodies
    • Keilhauer G, Faissner A, Schachner M (1985) Differential inhibition of neurone-neurone, neurone-astrocyte and astrocyte-astrocyte adhesion by L1, L2 and N-CAM antibodies. Nature 316: 728-730.
    • (1985) Nature , vol.316 , pp. 728-730
    • Keilhauer, G.1    Faissner, A.2    Schachner, M.3
  • 24
    • 0030007495 scopus 로고    scopus 로고
    • Tenascin mediates human glioma cell migration and modulates cell migration on fibronectin
    • Deryugina EI, Bourdon MA (1996) Tenascin mediates human glioma cell migration and modulates cell migration on fibronectin. J Cell Sci 109: 643-652.
    • (1996) J Cell Sci , vol.109 , pp. 643-652
    • Deryugina, E.I.1    Bourdon, M.A.2
  • 25
    • 0021061819 scopus 로고
    • Rapid colorimetric assay for cellular growth and survival: Application to proliferation and cytotoxicity assays
    • Mosmann T (1983) Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays. J Immunol Methods 65: 55-63.
    • (1983) J Immunol Methods , vol.65 , pp. 55-63
    • Mosmann, T.1
  • 26
    • 45549095065 scopus 로고    scopus 로고
    • Sorting of the neuroendocrine secretory protein secretogranin II into the regulated secretory pathway: Role of amino- and carboxy-terminal alpha-helical domains
    • Courel M, Vasquez MS, Hook VY, Mahata SK, Taupenot L (2008) Sorting of the neuroendocrine secretory protein secretogranin II into the regulated secretory pathway: Role of amino- and carboxy-terminal alpha-helical domains. J Biol Chem 283: 11807-11822.
    • (2008) J Biol Chem , vol.283 , pp. 11807-11822
    • Courel, M.1    Vasquez, M.S.2    Hook, V.Y.3    Mahata, S.K.4    Taupenot, L.5
  • 27
    • 9244259627 scopus 로고    scopus 로고
    • Deletion of the Pleckstrin and Phosphotyrosine Binding Domains of Insulin Receptor Substrate-2 Does Not Impair Its Ability to Regulate Cell Proliferation in Myeloid Cells
    • Sun HZ, Baserga R (2004) Deletion of the Pleckstrin and Phosphotyrosine Binding Domains of Insulin Receptor Substrate-2 Does Not Impair Its Ability to Regulate Cell Proliferation in Myeloid Cells. Endocrinology 145: 5332-5343.
    • (2004) Endocrinology , vol.145 , pp. 5332-5343
    • Sun, H.Z.1    Baserga, R.2
  • 28
    • 0037301384 scopus 로고    scopus 로고
    • Single chain Fv antibodies against neural cell adhesion molecule L1 trigger L1 functions in cultured neurons
    • Dong L, Chen S, Schachner M (2003) Single chain Fv antibodies against neural cell adhesion molecule L1 trigger L1 functions in cultured neurons. Mol Cell Neurosci 2: 234-247.
    • (2003) Mol Cell Neurosci , vol.2 , pp. 234-247
    • Dong, L.1    Chen, S.2    Schachner, M.3
  • 29
    • 0032919002 scopus 로고    scopus 로고
    • Prevention of neuronal cell death by neural adhesion molecules L1 and CHL1
    • Chen S, Mantei N, Dong L, Schachner M (1999) Prevention of neuronal cell death by neural adhesion molecules L1 and CHL1. J Neurobiol 38: 428-439.
    • (1999) J Neurobiol , vol.38 , pp. 428-439
    • Chen, S.1    Mantei, N.2    Dong, L.3    Schachner, M.4
  • 30
    • 33748195979 scopus 로고    scopus 로고
    • Glycosylation in cellular mechanisms of health and disease
    • Ohtsubo K, Marth JD (2006) Glycosylation in cellular mechanisms of health and disease. Cell 126: 855-867.
    • (2006) Cell , vol.126 , pp. 855-867
    • Ohtsubo, K.1    Marth, J.D.2
  • 31
    • 3142695658 scopus 로고    scopus 로고
    • Effects of glycosylation on peptide conformation: A synergistic experimental and computational study
    • Bosques CJ, Tschampel SM, Woods RJ, Imperiali B (2004) Effects of glycosylation on peptide conformation: a synergistic experimental and computational study. J Am Chem Soc 126: 8421-8425.
    • (2004) J Am Chem Soc , vol.126 , pp. 8421-8425
    • Bosques, C.J.1    Tschampel, S.M.2    Woods, R.J.3    Imperiali, B.4
  • 32
    • 3943059566 scopus 로고    scopus 로고
    • Roles of N-linked glycans in the endoplasmic reticulum
    • Helenius A, Aebi M (2004) Roles of N-linked glycans in the endoplasmic reticulum. Annu Rev Biochem 73: 1019-1049.
    • (2004) Annu Rev Biochem , vol.73 , pp. 1019-1049
    • Helenius, A.1    Aebi, M.2
  • 33
    • 0029952934 scopus 로고    scopus 로고
    • Stereocontrolled syntheses of O-glycans of core class 2 with a linear tetrameric lactosamine chain and with three lactosamine branches
    • Wang ZG, Zhang XF, Ito Y, Nakahara Y, Ogawa T (1996) Stereocontrolled syntheses of O-glycans of core class 2 with a linear tetrameric lactosamine chain and with three lactosamine branches. Carbohydr Res 295: 25-39.
    • (1996) Carbohydr Res , vol.295 , pp. 25-39
    • Wang, Z.G.1    Zhang, X.F.2    Ito, Y.3    Nakahara, Y.4    Ogawa, T.5
  • 34
    • 0036815746 scopus 로고    scopus 로고
    • Siglecs: Sialic-acid-binding immunoglobulin-like lectins in cell-cell interactions and signalling
    • Crocker PR (2002) Siglecs: sialic-acid-binding immunoglobulin-like lectins in cell-cell interactions and signalling. Curr Opin Struct Biol 12: 609-615.
    • (2002) Curr Opin Struct Biol , vol.12 , pp. 609-615
    • Crocker, P.R.1
  • 35
    • 0035997376 scopus 로고    scopus 로고
    • Order out of chaos: Assembly of ligand binding sites in heparan sulfate
    • Esko JD, Selleck SB (2002) Order out of chaos: assembly of ligand binding sites in heparan sulfate. Annu Rev Biochem 71: 435-471.
    • (2002) Annu Rev Biochem , vol.71 , pp. 435-471
    • Esko, J.D.1    Selleck, S.B.2
  • 36
    • 0040620527 scopus 로고    scopus 로고
    • Glycosyltransferases and glycan structures contributing to the adhesive activities of L-, E- and P-selectin counter-receptors
    • Lowe JB (2002) Glycosyltransferases and glycan structures contributing to the adhesive activities of L-, E- and P-selectin counter-receptors. Biochem Soc Symp 69: 33-45.
    • (2002) Biochem Soc Symp , vol.69 , pp. 33-45
    • Lowe, J.B.1
  • 37
    • 0036587663 scopus 로고    scopus 로고
    • Unlocking the secrets of galectins: A challenge at the frontier of glyco-immunology
    • Rabinovich GA, Rubinstein N, Fainboim L (2002) Unlocking the secrets of galectins: a challenge at the frontier of glyco-immunology. J Leukoc Biol 71: 741-752.
    • (2002) J Leukoc Biol , vol.71 , pp. 741-752
    • Rabinovich, G.A.1    Rubinstein, N.2    Fainboim, L.3
  • 38
    • 0037524357 scopus 로고    scopus 로고
    • O-GlcNAc turns twenty: Functional implications for post-translational modification of nuclear and cytosolic proteins with a sugar
    • Wells L, Hart GW (2003) O-GlcNAc turns twenty: functional implications for post-translational modification of nuclear and cytosolic proteins with a sugar. FEBS Lett 546: 154-158.
    • (2003) FEBS Lett , vol.546 , pp. 154-158
    • Wells, L.1    Hart, G.W.2
  • 39
    • 34247585173 scopus 로고    scopus 로고
    • Recognition molecules and neural repair
    • Loers G, Schachner M (2007) Recognition molecules and neural repair. J Neurochem 101: 865-882.
    • (2007) J Neurochem , vol.101 , pp. 865-882
    • Loers, G.1    Schachner, M.2
  • 40
    • 1542374061 scopus 로고    scopus 로고
    • Deficiency of GDP-Man: GlcNAc2-PP-Dolichol mannosyltransferase causes congenital disorder of glycosylation type Ik
    • Schwarz M, Thiel C, Lübbehusen J, Dorland B, de Koning T, et al. (2004) Deficiency of GDP-Man: GlcNAc2-PP-Dolichol mannosyltransferase causes congenital disorder of glycosylation type Ik. Am J Hum Genet 74: 472-481.
    • (2004) Am J Hum Genet , vol.74 , pp. 472-481
    • Schwarz, M.1    Thiel, C.2    Lübbehusen, J.3    Dorland, B.4    de Koning, T.5
  • 41
    • 33645893191 scopus 로고    scopus 로고
    • Alterations of N-glycan branching and expression of sialic acid on amniotic fluid alpha-1-acid glycoprotein derived from second and third trimesters of normal and prolonged pregnancies
    • Orczyk-Pawilowicz M, Hirnle L, Katnik-Prastowska I (2006) Alterations of N-glycan branching and expression of sialic acid on amniotic fluid alpha-1-acid glycoprotein derived from second and third trimesters of normal and prolonged pregnancies. Clin Chem Acta 367: 86-92.
    • (2006) Clin Chem Acta , vol.367 , pp. 86-92
    • Orczyk-Pawilowicz, M.1    Hirnle, L.2    Katnik-Prastowska, I.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.