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Volumn 41, Issue 2-3, 2010, Pages 314-340

Deregulated sphingolipid metabolism and membrane organization in neurodegenerative disorders

Author keywords

Alzheimer's disease; Gangliosides; Glycosphingolipids; Parkinson's disease; Prion diseases; Sphingolipid storage diseases; Sphingolipids; Sphingomyelin

Indexed keywords

1 DEOXYNOJIRIMYCIN DERIVATIVE; ALPHA SYNUCLEIN; AMYLOID BETA PROTEIN; GANGLIOSIDE GM1; GANGLIOSIDE GM2; GLYCOSPHINGOLIPID; MYELIN; N BUTYL DEOXYNOJIRIMYCIN; PRION PROTEIN; SPHINGOLIPID; UNCLASSIFIED DRUG;

EID: 77955088249     PISSN: 08937648     EISSN: None     Source Type: Journal    
DOI: 10.1007/s12035-009-8096-6     Document Type: Conference Paper
Times cited : (113)

References (330)
  • 1
    • 0032211143 scopus 로고    scopus 로고
    • Nomenclature of glycolipids
    • IUPAC-IUBMB Joint Commission on Biochemical Nomenclature
    • IUPAC-IUBMB Joint Commission on Biochemical Nomenclature (1998) Nomenclature of glycolipids. Carbohydr Res 312:167-175
    • (1998) Carbohydr Res , vol.312 , pp. 167-175
  • 2
    • 0019816914 scopus 로고
    • Ganglioside stimulation of axonal sprouting in vitro
    • Roisen FJ, Bartfeld H, Nagele R, Yorke G (1981) Ganglioside stimulation of axonal sprouting in vitro. Science 214:577-578
    • (1981) Science , vol.214 , pp. 577-578
    • Roisen, F.J.1    Bartfeld, H.2    Nagele, R.3    Yorke, G.4
  • 3
    • 0020348005 scopus 로고
    • Chemistry, metabolism, and biological functions of sialic acids
    • Schauer R (1982) Chemistry, metabolism, and biological functions of sialic acids. Adv Carbohydr Chem Biochem 40:131-234
    • (1982) Adv Carbohydr Chem Biochem , vol.40 , pp. 131-234
    • Schauer, R.1
  • 4
    • 1542399850 scopus 로고    scopus 로고
    • Lipid raft proteins have a random distribution during localized activation of the T-cell receptor
    • Glebov OO, Nichols BJ (2004) Lipid raft proteins have a random distribution during localized activation of the T-cell receptor. Nat Cell Biol 6:238-243
    • (2004) Nat Cell Biol , vol.6 , pp. 238-243
    • Glebov, O.O.1    Nichols, B.J.2
  • 5
    • 0014868653 scopus 로고
    • On the chemistry and occurrence of sphingolipid long-chain bases
    • Karlsson KA (1970) On the chemistry and occurrence of sphingolipid long-chain bases. Chem Phys Lipids 5:6-43
    • (1970) Chem Phys Lipids , vol.5 , pp. 6-43
    • Karlsson, K.A.1
  • 6
    • 20444428731 scopus 로고    scopus 로고
    • Getting downstream without a raft
    • Lin J, Shaw AS (2005) Getting downstream without a raft. Cell 121:815-816
    • (2005) Cell , vol.121 , pp. 815-816
    • Lin, J.1    Shaw, A.S.2
  • 7
  • 8
    • 33745753441 scopus 로고    scopus 로고
    • Dynamic and structural properties of sphingolipids as driving forces for the formation of membrane domains
    • Sonnino S, Prinetti A, Mauri L, Chigorno V, Tettamanti G (2006) Dynamic and structural properties of sphingolipids as driving forces for the formation of membrane domains. Chem Rev 106:2111-2125
    • (2006) Chem Rev , vol.106 , pp. 2111-2125
    • Sonnino, S.1    Prinetti, A.2    Mauri, L.3    Chigorno, V.4    Tettamanti, G.5
  • 9
    • 0026357863 scopus 로고
    • 1H-NMR study of GM2 ganglioside: Evidence that an interresidue amide-carboxyl hydrogen bond contributes to stabilization of a preferred conformation
    • Levery SB (1991) 1H-NMR study of GM2 ganglioside: evidence that an interresidue amide-carboxyl hydrogen bond contributes to stabilization of a preferred conformation. Glycoconj J 8:484-492
    • (1991) Glycoconj J , vol.8 , pp. 484-492
    • Levery, S.B.1
  • 10
    • 0027990661 scopus 로고
    • Geometrical and conformational properties of ganglioside GalNAc-GD1a, IV4GalNAcIV3Neu5AcII3Neu5AcGgOse4Cer
    • Acquotti D, Cantu L, Ragg E, Sonnino S (1994) Geometrical and conformational properties of ganglioside GalNAc-GD1a, IV4GalNAcIV3Neu5AcII3Neu5AcGgOse4Cer. Eur J Biochem 225:271-288
    • (1994) Eur J Biochem , vol.225 , pp. 271-288
    • Acquotti, D.1    Cantu, L.2    Ragg, E.3    Sonnino, S.4
  • 11
    • 0026077153 scopus 로고
    • Three dimensional structure of GD1b and GD1b-monolactone ganglio-sides in dimethylsulphoxide: A nuclear Overhauser effect investigation supported by molecular dynamics calculations
    • Acquotti D, Fronza G, Ragg E, Sonnino S (1991) Three dimensional structure of GD1b and GD1b-monolactone ganglio-sides in dimethylsulphoxide: a nuclear Overhauser effect investigation supported by molecular dynamics calculations. Chem Phys Lipids 59:107-125
    • (1991) Chem Phys Lipids , vol.59 , pp. 107-125
    • Acquotti, D.1    Fronza, G.2    Ragg, E.3    Sonnino, S.4
  • 12
    • 0025007355 scopus 로고
    • Three-dimensional structure of the oligosaccaride chain of GM1 ganglioside revealed by a distance-mapping procedure: A rotating and laboratory frame nuclear overhauser enhancement investigation of native glycolipid in dimethyl sulfoxide and in water-dodecylphosphocholine solutions
    • Acquotti D, Poppe L, Dabrowski J, von der Lieth GW, Sonnino S, Tettamanti G (1990) Three-dimensional structure of the oligosaccaride chain of GM1 ganglioside revealed by a distance-mapping procedure: a rotating and laboratory frame nuclear overhauser enhancement investigation of native glycolipid in dimethyl sulfoxide and in water-dodecylphosphocholine solutions. J Am Chem Soc 112:7772-7778
    • (1990) J Am Chem Soc , vol.112 , pp. 7772-7778
    • Acquotti, D.1    Poppe, L.2    Dabrowski, J.3    Von Der Lieth, G.W.4    Sonnino, S.5    Tettamanti, G.6
  • 13
    • 0029864602 scopus 로고    scopus 로고
    • Nuclear Overhauser effect investigation on GM1 ganglioside containing N-glycolyl-neuraminic acid (II3Neu5GcGgOse4Cer
    • Brocca P, Acquotti D, Sonnino S (1996) Nuclear Overhauser effect investigation on GM1 ganglioside containing N-glycolyl-neuraminic acid (II3Neu5GcGgOse4Cer). Glycoconj J 13:57-62
    • (1996) Glycoconj J , vol.13 , pp. 57-62
    • Brocca, P.1    Acquotti, D.2    Sonnino, S.3
  • 14
    • 0031972866 scopus 로고    scopus 로고
    • Conformation of the oligosaccharide chain of G(M1) ganglioside in a carbohydrate-enriched surface
    • Brocca P, Berthault P, Sonnino S (1998) Conformation of the oligosaccharide chain of G(M1) ganglioside in a carbohydrate-enriched surface. Biophys J 74:309-318
    • (1998) Biophys J , vol.74 , pp. 309-318
    • Brocca, P.1    Berthault, P.2    Sonnino, S.3
  • 15
    • 0029162657 scopus 로고
    • Aggregation properties of semisynthetic GD1a ganglioside (IV3Neu5AcII3Neu5AcG-gOse4Cer) containing an acetyl group as acyl moiety
    • Brocca P, Cantu L, Sonnino S (1995) Aggregation properties of semisynthetic GD1a ganglioside (IV3Neu5AcII3Neu5AcG-gOse4Cer) containing an acetyl group as acyl moiety. Chem Phys Lipids 77:41-49
    • (1995) Chem Phys Lipids , vol.77 , pp. 41-49
    • Brocca, P.1    Cantu, L.2    Sonnino, S.3
  • 16
    • 0026333058 scopus 로고
    • Aggregation properties of GD1b, II3Neu5Ac2GgOse4Cer, and of GD1b-lactone, II3[alpha-Neu5Ac-(2-8, 1-9)-alpha-Neu5Ac] GgOse4Cer, in aqueous solution
    • Cantù L, Corti M, Casellato R, Acquotti D, Sonnino S (1991) Aggregation properties of GD1b, II3Neu5Ac2GgOse4Cer, and of GD1b-lactone, II3[alpha-Neu5Ac-(2-8, 1-9)-alpha-Neu5Ac] GgOse4Cer, in aqueous solution. Chem Phys Lipids 60:111-118
    • (1991) Chem Phys Lipids , vol.60 , pp. 111-118
    • Cantù, L.1    Corti, M.2    Casellato, R.3    Acquotti, D.4    Sonnino, S.5
  • 17
    • 0025000463 scopus 로고
    • Evidence for spontaneous segregation phenomena in mixed micelles of gangliosides
    • Cantu L, Corti M, Sonnino S, Tettamanti G (1990) Evidence for spontaneous segregation phenomena in mixed micelles of gangliosides. Chem Phys Lipids 55:223-229
    • (1990) Chem Phys Lipids , vol.55 , pp. 223-229
    • Cantu, L.1    Corti, M.2    Sonnino, S.3    Tettamanti, G.4
  • 18
    • 0022573422 scopus 로고
    • Thermotropic characterization of phosphatidylcholine vesicles containing ganglioside GM1 with homogeneous ceramide chain length
    • Masserini M, Freire E (1986) Thermotropic characterization of phosphatidylcholine vesicles containing ganglioside GM1 with homogeneous ceramide chain length. Biochemistry 25:1043-1049
    • (1986) Biochemistry , vol.25 , pp. 1043-1049
    • Masserini, M.1    Freire, E.2
  • 19
    • 0024316313 scopus 로고
    • Influence of glycolipid oligosaccharide and long-chain base composition on the thermo-tropic properties of dipalmitoylphosphatidylcholine large unilamellar vesicles containing gangliosides
    • Masserini M, Palestini P, Freire E (1989) Influence of glycolipid oligosaccharide and long-chain base composition on the thermo-tropic properties of dipalmitoylphosphatidylcholine large unilamellar vesicles containing gangliosides. Biochemistry 28:5029-5034
    • (1989) Biochemistry , vol.28 , pp. 5029-5034
    • Masserini, M.1    Palestini, P.2    Freire, E.3
  • 20
    • 0023682466 scopus 로고
    • Interactions of proteins with ganglioside-enriched microdomains on the membrane: The lateral phase separation of molecular species of GD1a ganglioside, having homogeneous long-chain base composition, is recognized by Vibrio cholerae sialidase
    • Masserini M, Palestini P, Venerando B, Fiorilli A, Acquotti D, Tettamanti G (1988) Interactions of proteins with ganglioside-enriched microdomains on the membrane: the lateral phase separation of molecular species of GD1a ganglioside, having homogeneous long-chain base composition, is recognized by Vibrio cholerae sialidase. Biochemistry 27:7973-7978
    • (1988) Biochemistry , vol.27 , pp. 7973-7978
    • Masserini, M.1    Palestini, P.2    Venerando, B.3    Fiorilli, A.4    Acquotti, D.5    Tettamanti, G.6
  • 21
    • 0028328601 scopus 로고
    • Carbohydrate dynamics at a micellar surface: GD1a headgroup transformations revealed by NMR spectroscopy
    • Poppe L, van Halbeek H, Acquotti D, Sonnino S (1994) Carbohydrate dynamics at a micellar surface: GD1a headgroup transformations revealed by NMR spectroscopy. Biophys J 66:1642-1652
    • (1994) Biophys J , vol.66 , pp. 1642-1652
    • Poppe, L.1    Van Halbeek, H.2    Acquotti, D.3    Sonnino, S.4
  • 22
    • 0025110455 scopus 로고
    • NMR and computational studies of interactions between remote residues in gangliosides
    • Scarsdale JN, Prestegard JH, Yu RK (1990) NMR and computational studies of interactions between remote residues in gangliosides. Biochemistry 29:9843-9855
    • (1990) Biochemistry , vol.29 , pp. 9843-9855
    • Scarsdale, J.N.1    Prestegard, J.H.2    Yu, R.K.3
  • 23
    • 0026742506 scopus 로고
    • Solution conformations of GM3 gangliosides containing different sialic acid residues as revealed by NOE-based distance mapping, molecular mechanics, and molecular dynamics calculations
    • Siebert HC, Reuter G, Schauer R, von der Lieth CW, Dabrowski J (1992) Solution conformations of GM3 gangliosides containing different sialic acid residues as revealed by NOE-based distance mapping, molecular mechanics, and molecular dynamics calculations. Biochemistry 31:6962-6971
    • (1992) Biochemistry , vol.31 , pp. 6962-6971
    • Siebert, H.C.1    Reuter, G.2    Schauer, R.3    Von Der Lieth, C.W.4    Dabrowski, J.5
  • 24
    • 0025012620 scopus 로고
    • Aggregation properties of GM3 ganglioside (II3Neu5AcLacCer) in aqueous solutions
    • Sonnino S, Cantu L, Acquotti D, Corti M, Tettamanti G (1990) Aggregation properties of GM3 ganglioside (II3Neu5AcLacCer) in aqueous solutions. Chem Phys Lipids 52:231-241
    • (1990) Chem Phys Lipids , vol.52 , pp. 231-241
    • Sonnino, S.1    Cantu, L.2    Acquotti, D.3    Corti, M.4    Tettamanti, G.5
  • 25
    • 0025634378 scopus 로고
    • Aggregation properties of semisynthetic GM1 ganglioside (II3Neu5AcGgOse4Cer) containing an acetyl group as acyl moiety
    • Sonnino S, Cantu L, Corti M, Acquotti D, Kirschner G, Tettamanti G (1990) Aggregation properties of semisynthetic GM1 ganglioside (II3Neu5AcGgOse4Cer) containing an acetyl group as acyl moiety. Chem Phys Lipids 56:49-57
    • (1990) Chem Phys Lipids , vol.56 , pp. 49-57
    • Sonnino, S.1    Cantu, L.2    Corti, M.3    Acquotti, D.4    Kirschner, G.5    Tettamanti, G.6
  • 27
    • 0024378717 scopus 로고
    • Role of the hydrophobic effect in stability of site-specific protein-DNA complexes
    • Ha JH, Spolar RS, Record MT Jr (1989) Role of the hydrophobic effect in stability of site-specific protein-DNA complexes. J Mol Biol 209:801-816
    • (1989) J Mol Biol , vol.209 , pp. 801-816
    • Ha, J.H.1    Spolar, R.S.2    Record Jr., M.T.3
  • 28
    • 0020439499 scopus 로고
    • Compositional aspects of lipid hydration
    • Bach D, Sela B, Miller IR (1982) Compositional aspects of lipid hydration. Chem Phys Lipids 31:381-394
    • (1982) Chem Phys Lipids , vol.31 , pp. 381-394
    • Bach, D.1    Sela, B.2    Miller, I.R.3
  • 29
    • 0029034829 scopus 로고
    • Gel phase preference of ganglioside GM1 at low concentration in two-component, two-phase phosphatidylcholine bilayers depends upon the ceramide moiety
    • Palestini P, Allietta M, Sonnino S, Tettamanti G, Thompson TE, Tillack TW (1995) Gel phase preference of ganglioside GM1 at low concentration in two-component, two-phase phosphatidylcholine bilayers depends upon the ceramide moiety. Biochim Biophys Acta 1235:221-230
    • (1995) Biochim Biophys Acta , vol.1235 , pp. 221-230
    • Palestini, P.1    Allietta, M.2    Sonnino, S.3    Tettamanti, G.4    Thompson, T.E.5    Tillack, T.W.6
  • 30
    • 0023901368 scopus 로고
    • Ganglioside-modulated protein phosphorylation. Partial purification and characterization of a ganglioside-inhibited protein kinase in brain
    • Chan KF (1988) Ganglioside-modulated protein phosphorylation. Partial purification and characterization of a ganglioside-inhibited protein kinase in brain. J Biol Chem 263:568-574
    • (1988) J Biol Chem , vol.263 , pp. 568-574
    • Chan, K.F.1
  • 31
    • 0024464077 scopus 로고
    • Ganglioside-modulated protein phosphorylation in muscle. Activation of phosphorylase b kinase by gangliosides
    • Chan KF (1989) Ganglioside-modulated protein phosphorylation in muscle. Activation of phosphorylase b kinase by gangliosides. J Biol Chem 264:18632-18637
    • (1989) J Biol Chem , vol.264 , pp. 18632-18637
    • Chan, K.F.1
  • 32
    • 0026095894 scopus 로고
    • Exogenous gangliosides GD1b and GD1b-lactone, stably associated to rat brain P2 subcellular fraction, modulate differently the process of protein phosphorylation
    • Bassi R, Chigorno V, Fiorilli A, Sonnino S, Tettamanti G (1991) Exogenous gangliosides GD1b and GD1b-lactone, stably associated to rat brain P2 subcellular fraction, modulate differently the process of protein phosphorylation. J Neurochem 57:1207-1211
    • (1991) J Neurochem , vol.57 , pp. 1207-1211
    • Bassi, R.1    Chigorno, V.2    Fiorilli, A.3    Sonnino, S.4    Tettamanti, G.5
  • 33
    • 0021186166 scopus 로고
    • Ganglioside-mediated modulation of cell growth, growth factor binding, and receptor phosphorylation
    • Bremer EG, Hakomori S, Bowen-Pope DF, Raines E, Ross R (1984) Ganglioside-mediated modulation of cell growth, growth factor binding, and receptor phosphorylation. J Biol Chem 259:6818-6825
    • (1984) J Biol Chem , vol.259 , pp. 6818-6825
    • Bremer, E.G.1    Hakomori, S.2    Bowen-Pope, D.F.3    Raines, E.4    Ross, R.5
  • 34
    • 0021919509 scopus 로고
    • Calcium/ganglioside-dependent protein kinase activity in rat brain membrane
    • Goldenring JR, Otis LC, Yu RK, DeLorenzo RJ (1985) Calcium/ganglioside- dependent protein kinase activity in rat brain membrane. J Neurochem 44:1229-1234
    • (1985) J Neurochem , vol.44 , pp. 1229-1234
    • Goldenring, J.R.1    Otis, L.C.2    Yu, R.K.3    Delorenzo, R.J.4
  • 35
    • 0029609895 scopus 로고
    • Functional role of glycosphin-golipids in cell recognition and signaling
    • Hakomori S, Igarashi Y (1995) Functional role of glycosphin-golipids in cell recognition and signaling. J Biochem (Tokyo) 118:1091-1103
    • (1995) J Biochem (Tokyo) , vol.118 , pp. 1091-1103
    • Hakomori, S.1    Igarashi, Y.2
  • 36
    • 0022626028 scopus 로고
    • Gangliosides inhibit phospholipid-sensitive Ca2+-dependent kinase phosphorylation of rat myelin basic proteins
    • Kim JY, Goldenring JR, DeLorenzo RJ, Yu RK (1986) Gangliosides inhibit phospholipid-sensitive Ca2+-dependent kinase phosphorylation of rat myelin basic proteins. J Neurosci Res 15:159-166
    • (1986) J Neurosci Res , vol.15 , pp. 159-166
    • Kim, J.Y.1    Goldenring, J.R.2    Delorenzo, R.J.3    Yu, R.K.4
  • 37
    • 0022486132 scopus 로고
    • Bioactive gangliosides: Analysis of functional structures of the tetrasialoganglioside GQ1b which promotes neurite outgrowth
    • Nakajima J, Tsuji S, Nagai Y (1986) Bioactive gangliosides: analysis of functional structures of the tetrasialoganglioside GQ1b which promotes neurite outgrowth. Biochim Biophys Acta 876:65-71
    • (1986) Biochim Biophys Acta , vol.876 , pp. 65-71
    • Nakajima, J.1    Tsuji, S.2    Nagai, Y.3
  • 38
    • 0020955702 scopus 로고
    • GQ1b, a bioactive ganglioside that exhibits novel nerve growth factor (NGF)-like activities in the two neuroblastoma cell lines
    • Tsuji S, Arita M, Nagai Y (1983) GQ1b, a bioactive ganglioside that exhibits novel nerve growth factor (NGF)-like activities in the two neuroblastoma cell lines. J Biochem (Tokyo) 94:303-306
    • (1983) J Biochem (Tokyo) , vol.94 , pp. 303-306
    • Tsuji, S.1    Arita, M.2    Nagai, Y.3
  • 39
    • 0021912362 scopus 로고
    • Bioactive gangliosides. IV. Ganglioside GQ1b/Ca2+ dependent protein kinase activity exists in the plasma membrane fraction of neuroblastoma cell line, GOTO
    • Tsuji S, Nakajima J, Sasaki T, Nagai Y (1985) Bioactive gangliosides. IV. Ganglioside GQ1b/Ca2+ dependent protein kinase activity exists in the plasma membrane fraction of neuroblastoma cell line, GOTO. J Biochem 97:969-972
    • (1985) J Biochem , vol.97 , pp. 969-972
    • Tsuji, S.1    Nakajima, J.2    Sasaki, T.3    Nagai, Y.4
  • 40
    • 0031904515 scopus 로고    scopus 로고
    • Sphingolipids as receptor modulators An overview
    • Yates AJ, Rampersaud A (1998) Sphingolipids as receptor modulators. An overview. Ann N Y Acad Sci 845:57-71
    • (1998) Ann N y Acad Sci , vol.845 , pp. 57-71
    • Yates, A.J.1    Rampersaud, A.2
  • 42
    • 3543085572 scopus 로고    scopus 로고
    • Ganglioside/glycosphingolipid turnover: New concepts
    • Tettamanti G (2004) Ganglioside/glycosphingolipid turnover: new concepts. Glycoconj J 20:301-317
    • (2004) Glycoconj J , vol.20 , pp. 301-317
    • Tettamanti, G.1
  • 43
    • 0037135608 scopus 로고    scopus 로고
    • Combinatorial ganglioside biosynthesis
    • Kolter T, Proia RL, Sandhoff K (2002) Combinatorial ganglioside biosynthesis. J Biol Chem 277:25859-25862
    • (2002) J Biol Chem , vol.277 , pp. 25859-25862
    • Kolter, T.1    Proia, R.L.2    Sandhoff, K.3
  • 44
    • 0027467490 scopus 로고
    • Ganglioside metabolism. Enzymology, topology, and regulation
    • van Echten G, Sandhoff K (1993) Ganglioside metabolism. Enzymology, topology, and regulation. J Biol Chem 268:5341-5344
    • (1993) J Biol Chem , vol.268 , pp. 5341-5344
    • Van Echten, G.1    Sandhoff, K.2
  • 45
    • 33748746334 scopus 로고    scopus 로고
    • When do Lasses (longevity assurance genes) become CerS (ceramide synthases)?: Insights into the regulation of ceramide synthesis
    • Pewzner-Jung Y, Ben-Dor S, Futerman AH (2006) When do Lasses (longevity assurance genes) become CerS (ceramide synthases)?: insights into the regulation of ceramide synthesis. J Biol Chem 281:25001-25005
    • (2006) J Biol Chem , vol.281 , pp. 25001-25005
    • Pewzner-Jung, Y.1    Ben-Dor, S.2    Futerman, A.H.3
  • 46
    • 2442423192 scopus 로고    scopus 로고
    • Expression cloning of a human cDNA restoring sphingomyelin synthesis and cell growth in sphingomyelin synthase-defective lymphoid cells
    • Yamaoka S, Miyaji M, Kitano T, Umehara H, Okazaki T (2004) Expression cloning of a human cDNA restoring sphingomyelin synthesis and cell growth in sphingomyelin synthase-defective lymphoid cells. J Biol Chem 279:18688-18693
    • (2004) J Biol Chem , vol.279 , pp. 18688-18693
    • Yamaoka, S.1    Miyaji, M.2    Kitano, T.3    Umehara, H.4    Okazaki, T.5
  • 48
    • 0032475872 scopus 로고    scopus 로고
    • UDP-galactose:ceramide galactosyltransferase is a class i integral membrane protein of the endoplasmic reticulum
    • Sprong H, Kruithof B, Leijendekker R, Slot JW, van Meer G, van der Sluijs P (1998) UDP-galactose:ceramide galactosyltransferase is a class I integral membrane protein of the endoplasmic reticulum, J Biol Chem, 273, 25880-25888
    • (1998) J Biol Chem , vol.273 , pp. 25880-25888
    • Sprong, H.1    Kruithof, B.2    Leijendekker, R.3    Slot, J.W.4    Van Meer, G.5    Van Der Sluijs, P.6
  • 49
    • 52049122869 scopus 로고    scopus 로고
    • Two sphingolipid transfer proteins CERT and FAPP2: Their roles in sphingolipid metabolism
    • Yamaji T, Kumagai K, Tomishige N, Hanada K (2008) Two sphingolipid transfer proteins, CERT and FAPP2: their roles in sphingolipid metabolism. IUBMB Life 60:511-518
    • (2008) IUBMB Life , vol.60 , pp. 511-518
    • Yamaji, T.1    Kumagai, K.2    Tomishige, N.3    Hanada, K.4
  • 51
    • 0030581275 scopus 로고    scopus 로고
    • Salvage of catabolic products in ganglioside metabolism: A study on rat cerebellar granule cells in culture
    • Riboni L, Bassi R, Prinetti A, Tettamanti G (1996) Salvage of catabolic products in ganglioside metabolism: a study on rat cerebellar granule cells in culture. FEBS Lett 391:336-340
    • (1996) FEBS Lett , vol.391 , pp. 336-340
    • Riboni, L.1    Bassi, R.2    Prinetti, A.3    Tettamanti, G.4
  • 52
    • 0027989296 scopus 로고
    • Effect of brefeldin A on ganglioside metabolism in cultured neurons: Implications for the intracellular traffic of gangliosides
    • Riboni L, Bassi R, Tettamanti G (1994) Effect of brefeldin A on ganglioside metabolism in cultured neurons: implications for the intracellular traffic of gangliosides. J Biochem (Tokyo) 116:140-146
    • (1994) J Biochem (Tokyo) , vol.116 , pp. 140-146
    • Riboni, L.1    Bassi, R.2    Tettamanti, G.3
  • 53
    • 0027994349 scopus 로고
    • The sphingomyelin cycle and the second messenger function of ceramide
    • Hannun YA (1994) The sphingomyelin cycle and the second messenger function of ceramide. J Biol Chem 269:3125-3128
    • (1994) J Biol Chem , vol.269 , pp. 3125-3128
    • Hannun, Y.A.1
  • 54
    • 0037201939 scopus 로고    scopus 로고
    • Sphingomyelinases: Enzymology and membrane activity
    • Goni FM, Alonso A (2002) Sphingomyelinases: enzymology and membrane activity. FEBS Lett 531:38-46
    • (2002) FEBS Lett , vol.531 , pp. 38-46
    • Goni, F.M.1    Alonso, A.2
  • 55
    • 0344349001 scopus 로고    scopus 로고
    • Signalling sphingomyelinases: Which, where, how and why?
    • Levade T, Jaffrezou JP (1999) Signalling sphingomyelinases: which, where, how and why? Biochim Biophys Acta 1438:1-17
    • (1999) Biochim Biophys Acta , vol.1438 , pp. 1-17
    • Levade, T.1    Jaffrezou, J.P.2
  • 57
    • 0024356723 scopus 로고
    • Free sphingosine formation from endogenous substrates by a liver plasma membrane system with a divalent cation dependence and a neutral pH optimum
    • Slife CW, Wang E, Hunter R, Wang S, Burgess C, Liotta DC, Merrill AH Jr (1989) Free sphingosine formation from endogenous substrates by a liver plasma membrane system with a divalent cation dependence and a neutral pH optimum. J Biol Chem 264:10371-10377
    • (1989) J Biol Chem , vol.264 , pp. 10371-10377
    • Slife, C.W.1    Wang, E.2    Hunter, R.3    Wang, S.4    Burgess, C.5    Liotta, D.C.6    Merrill Jr., A.H.7
  • 58
    • 0038193634 scopus 로고    scopus 로고
    • O-glycosylation of mucin-like domain retains the neutral ceramidase on the plasma membranes as a type II integral membrane protein
    • Tani M, Iida H, Ito M (2003) O-glycosylation of mucin-like domain retains the neutral ceramidase on the plasma membranes as a type II integral membrane protein. J Biol Chem 278:10523-10530
    • (2003) J Biol Chem , vol.278 , pp. 10523-10530
    • Tani, M.1    Iida, H.2    Ito, M.3
  • 59
    • 27444446836 scopus 로고    scopus 로고
    • Mechanisms of sphingosine and sphingosine 1-phosphate generation in human platelets
    • Tani M, Sano T, Ito M, Igarashi Y (2005) Mechanisms of sphingosine and sphingosine 1-phosphate generation in human platelets. J Lipid Res 46:2458-2467
    • (2005) J Lipid Res , vol.46 , pp. 2458-2467
    • Tani, M.1    Sano, T.2    Ito, M.3    Igarashi, Y.4
  • 60
    • 0014962937 scopus 로고
    • Intracellular location and properties of bovine brain sialidase
    • Schengrund CL, Rosenberg A (1970) Intracellular location and properties of bovine brain sialidase. J Biol Chem 245:6196-6200
    • (1970) J Biol Chem , vol.245 , pp. 6196-6200
    • Schengrund, C.L.1    Rosenberg, A.2
  • 62
    • 0015795372 scopus 로고
    • Parallelism of subcellular location of major particulate neuraminidase and gangliosides in rabbit brain cortex
    • Tettamanti G, Preti A, Lombardo A, Bonali F, Zambotti V (1973) Parallelism of subcellular location of major particulate neuraminidase and gangliosides in rabbit brain cortex. Biochim Biophys Acta 306:466-477
    • (1973) Biochim Biophys Acta , vol.306 , pp. 466-477
    • Tettamanti, G.1    Preti, A.2    Lombardo, A.3    Bonali, F.4    Zambotti, V.5
  • 63
    • 0016816193 scopus 로고
    • Membrane-bound neuraminidase in the brain of different animals: Behaviour of the enzyme on endogenous sialo derivatives and rationale for its assay
    • Tettamanti G, Preti A, Lombardo A, Suman T, Zambotti V (1975) Membrane-bound neuraminidase in the brain of different animals: behaviour of the enzyme on endogenous sialo derivatives and rationale for its assay. J Neurochem 25:451-456
    • (1975) J Neurochem , vol.25 , pp. 451-456
    • Tettamanti, G.1    Preti, A.2    Lombardo, A.3    Suman, T.4    Zambotti, V.5
  • 64
    • 0018952049 scopus 로고
    • Occurrence of sialyltransferase activity in the synaptosomal membranes prepared from calf brain cortex
    • Preti A, Fiorilli A, Lombardo A, Caimi L, Tettamanti G (1980) Occurrence of sialyltransferase activity in the synaptosomal membranes prepared from calf brain cortex. J Neurochem 35:281-296
    • (1980) J Neurochem , vol.35 , pp. 281-296
    • Preti, A.1    Fiorilli, A.2    Lombardo, A.3    Caimi, L.4    Tettamanti, G.5
  • 65
    • 0022622670 scopus 로고
    • Surface glycosyltransferase activities during development of neuronal cell cultures
    • Matsui Y, Lombard D, Massarelli R, Mandel P, Dreyfus H (1986) Surface glycosyltransferase activities during development of neuronal cell cultures. J Neurochem 46:144-150
    • (1986) J Neurochem , vol.46 , pp. 144-150
    • Matsui, Y.1    Lombard, D.2    Massarelli, R.3    Mandel, P.4    Dreyfus, H.5
  • 66
    • 0024323878 scopus 로고
    • Anabolic sialosylation of gangliosides in situ in rat brain cortical slices
    • Durrie R, Rosenberg A (1989) Anabolic sialosylation of gangliosides in situ in rat brain cortical slices. J Lipid Res 30:1259-1266
    • (1989) J Lipid Res , vol.30 , pp. 1259-1266
    • Durrie, R.1    Rosenberg, A.2
  • 67
    • 0023951018 scopus 로고
    • Endogenous glycosphingolipid acceptor specificity of sialosyltransferase systems in intact Golgi membranes, synaptosomes, and synaptic plasma membranes from rat brain
    • Durrie R, Saito M, Rosenberg A (1988) Endogenous glycosphingolipid acceptor specificity of sialosyltransferase systems in intact Golgi membranes, synaptosomes, and synaptic plasma membranes from rat brain. Biochemistry 27:3759-3764
    • (1988) Biochemistry , vol.27 , pp. 3759-3764
    • Durrie, R.1    Saito, M.2    Rosenberg, A.3
  • 68
    • 23844431674 scopus 로고    scopus 로고
    • Changes in the glycolipid composition and characteristic activation of GM3 synthase in the thymus of mouse after administration of dexamethasone
    • Iwamori M, Iwamori Y (2005) Changes in the glycolipid composition and characteristic activation of GM3 synthase in the thymus of mouse after administration of dexamethasone. Glycoconj J 22:119-126
    • (2005) Glycoconj J , vol.22 , pp. 119-126
    • Iwamori, M.1    Iwamori, Y.2
  • 69
    • 0343487873 scopus 로고    scopus 로고
    • Effects of cell surface ganglioside sialidase inhibition on growth control and differentiation of human neuroblastoma cells
    • Kopitz J, Muhl C, Ehemann V, Lehmann C, Cantz M (1997) Effects of cell surface ganglioside sialidase inhibition on growth control and differentiation of human neuroblastoma cells. Eur J Cell Biol 73:1-9
    • (1997) Eur J Cell Biol , vol.73 , pp. 1-9
    • Kopitz, J.1    Muhl, C.2    Ehemann, V.3    Lehmann, C.4    Cantz, M.5
  • 70
    • 0030987611 scopus 로고    scopus 로고
    • Partial characterization and enrichment of a membrane-bound sialidase specific for gangliosides from human brain tissue
    • Kopitz J, Sinz K, Brossmer R, Cantz M (1997) Partial characterization and enrichment of a membrane-bound sialidase specific for gangliosides from human brain tissue. Eur J Biochem 248:527-534
    • (1997) Eur J Biochem , vol.248 , pp. 527-534
    • Kopitz, J.1    Sinz, K.2    Brossmer, R.3    Cantz, M.4
  • 71
    • 0025883136 scopus 로고
    • Cerebellar granule cells in culture exhibit a ganglioside-sialidase presumably linked to the plasma membrane
    • Riboni L, Prinetti A, Bassi R, Tettamanti G (1991) Cerebellar granule cells in culture exhibit a ganglioside-sialidase presumably linked to the plasma membrane. FEBS Lett 287:42-46
    • (1991) FEBS Lett , vol.287 , pp. 42-46
    • Riboni, L.1    Prinetti, A.2    Bassi, R.3    Tettamanti, G.4
  • 72
    • 0029666071 scopus 로고    scopus 로고
    • Selective ganglioside desialylation in the plasma membrane of human neuroblastoma cells
    • Kopitz J, von Reitzenstein C, Sinz K, Cantz M (1996) Selective ganglioside desialylation in the plasma membrane of human neuroblastoma cells. Glycobiology 6:367-376
    • (1996) Glycobiology , vol.6 , pp. 367-376
    • Kopitz, J.1    Von Reitzenstein, C.2    Sinz, K.3    Cantz, M.4
  • 73
    • 0031959479 scopus 로고    scopus 로고
    • Purification and characterization of a membrane-associated ganglioside sialidase from bovine brain
    • Hata K, Wada T, Hasegawa A, Kiso M, Miyagi T (1998) Purification and characterization of a membrane-associated ganglioside sialidase from bovine brain. J Biochem (Tokyo) 123:899-905
    • (1998) J Biochem (Tokyo) , vol.123 , pp. 899-905
    • Hata, K.1    Wada, T.2    Hasegawa, A.3    Kiso, M.4    Miyagi, T.5
  • 75
    • 0033582517 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a plasma membrane-associated sialidase specific for gangliosides
    • Miyagi T, Wada T, Iwamatsu A, Hata K, Yoshikawa Y, Tokuyama S, Sawada M (1999) Molecular cloning and characterization of a plasma membrane-associated sialidase specific for gangliosides. J Biol Chem 274:5004-5011
    • (1999) J Biol Chem , vol.274 , pp. 5004-5011
    • Miyagi, T.1    Wada, T.2    Iwamatsu, A.3    Hata, K.4    Yoshikawa, Y.5    Tokuyama, S.6    Sawada, M.7
  • 76
    • 0034678126 scopus 로고    scopus 로고
    • Molecular cloning of mouse ganglioside sialidase and its increased expression in neuro2a cell differentiation
    • Hasegawa T, Yamaguchi K, Wada T, Takeda A, Itoyama Y, Miyagi T (2000) Molecular cloning of mouse ganglioside sialidase and its increased expression in neuro2a cell differentiation. J Biol Chem 275:14778
    • (2000) J Biol Chem , vol.275 , pp. 14778
    • Hasegawa, T.1    Yamaguchi, K.2    Wada, T.3    Takeda, A.4    Itoyama, Y.5    Miyagi, T.6
  • 80
    • 0035958557 scopus 로고    scopus 로고
    • Plasma membrane repair is mediated by Ca(2+)-regulated exocytosis of lysosomes
    • Reddy A, Caler EV, Andrews NW (2001) Plasma membrane repair is mediated by Ca(2+)-regulated exocytosis of lysosomes. Cell 106:157-169
    • (2001) Cell , vol.106 , pp. 157-169
    • Reddy, A.1    Caler, E.V.2    Andrews, N.W.3
  • 81
    • 13244259437 scopus 로고    scopus 로고
    • Sphingolipid uptake by cultured cells: Complex aggregates of cell sphingolipids with serum proteins and lipoproteins are rapidly catabolized
    • Chigorno V, Giannotta C, Ottico E, Sciannamblo M, Mikulak J, Prinetti A, Sonnino S (2005) Sphingolipid uptake by cultured cells: complex aggregates of cell sphingolipids with serum proteins and lipoproteins are rapidly catabolized. J Biol Chem 280:2668-2675
    • (2005) J Biol Chem , vol.280 , pp. 2668-2675
    • Chigorno, V.1    Giannotta, C.2    Ottico, E.3    Sciannamblo, M.4    Mikulak, J.5    Prinetti, A.6    Sonnino, S.7
  • 82
    • 0034616635 scopus 로고    scopus 로고
    • Influence of cellular ganglioside depletion on tumor formation
    • Deng W, Li R, Ladisch S (2000) Influence of cellular ganglioside depletion on tumor formation. J Natl Cancer Inst 92:912-917
    • (2000) J Natl Cancer Inst , vol.92 , pp. 912-917
    • Deng, W.1    Li, R.2    Ladisch, S.3
  • 84
    • 0031656924 scopus 로고    scopus 로고
    • Natural forms of shed tumor gangliosides
    • Kong Y, Li R, Ladisch S (1998) Natural forms of shed tumor gangliosides. Biochim Biophys Acta 1394:43-56
    • (1998) Biochim Biophys Acta , vol.1394 , pp. 43-56
    • Kong, Y.1    Li, R.2    Ladisch, S.3
  • 85
    • 0033213878 scopus 로고    scopus 로고
    • Tumor gangliosides inhibit the tumor-specific immune response
    • McKallip R, Li R, Ladisch S (1999) Tumor gangliosides inhibit the tumor-specific immune response. J Immunol 163:3718-3726
    • (1999) J Immunol , vol.163 , pp. 3718-3726
    • McKallip, R.1    Li, R.2    Ladisch, S.3
  • 87
    • 0034304915 scopus 로고    scopus 로고
    • Biomolecule function: No reliable prediction from cell culture
    • Kolter T, Magin TM, Sandhoff K (2000) Biomolecule function: no reliable prediction from cell culture. Traffic 1:803-804
    • (2000) Traffic , vol.1 , pp. 803-804
    • Kolter, T.1    Magin, T.M.2    Sandhoff, K.3
  • 90
    • 36448995805 scopus 로고    scopus 로고
    • Developmental changes of glycosphingolipids and expression of glycogenes in mouse brains
    • Ngamukote S, Yanagisawa M, Ariga T, Ando S, Yu RK (2007) Developmental changes of glycosphingolipids and expression of glycogenes in mouse brains. J Neurochem 103:2327-2341
    • (2007) J Neurochem , vol.103 , pp. 2327-2341
    • Ngamukote, S.1    Yanagisawa, M.2    Ariga, T.3    Ando, S.4    Yu, R.K.5
  • 91
    • 0024341819 scopus 로고
    • Human brain gangliosides: Developmental changes from early fetal stage to advanced age
    • Svennerholm L,BostromK,FredmanP, Mansson JE, Rosengren B, Rynmark BM (1989) Human brain gangliosides: developmental changes from early fetal stage to advanced age. Biochim Biophys Acta 1005:109-117
    • (1989) Biochim Biophys Acta , vol.1005 , pp. 109-117
    • Lbostromkfredmanp, S.1    Mansson, J.E.2    Rosengren, B.3    Rynmark, B.M.4
  • 92
    • 0035877706 scopus 로고    scopus 로고
    • Changes in the lipid turnover, composition, and organization, as sphingolipid-enriched membrane domains, in rat cerebellar granule cells developing in vitro
    • Prinetti A, Chigorno V, Prioni S, Loberto N, Marano N, Tettamanti G, Sonnino S (2001) Changes in the lipid turnover, composition, and organization, as sphingolipid-enriched membrane domains, in rat cerebellar granule cells developing in vitro. J Biol Chem 276:21136-21145
    • (2001) J Biol Chem , vol.276 , pp. 21136-21145
    • Prinetti, A.1    Chigorno, V.2    Prioni, S.3    Loberto, N.4    Marano, N.5    Tettamanti, G.6    Sonnino, S.7
  • 93
    • 0034852030 scopus 로고    scopus 로고
    • Immunoseparation of sphingolipid-enriched membrane domains enriched in Src family protein tyrosine kinases and in the neuronal adhesion molecule TAG-1 by anti-GD3 ganglioside monoclonal antibody
    • Prinetti A, Prioni S, Chigorno V, Karagogeos D, Tettamanti G, Sonnino S (2001) Immunoseparation of sphingolipid-enriched membrane domains enriched in Src family protein tyrosine kinases and in the neuronal adhesion molecule TAG-1 by anti-GD3 ganglioside monoclonal antibody. J Neurochem 78:1162-1167
    • (2001) J Neurochem , vol.78 , pp. 1162-1167
    • Prinetti, A.1    Prioni, S.2    Chigorno, V.3    Karagogeos, D.4    Tettamanti, G.5    Sonnino, S.6
  • 94
    • 0036694905 scopus 로고    scopus 로고
    • Sphingolipid metabolism and caveolin expression in gonadotropin-releasing hormone-expressing GN11 and gonadotropin-releasing hormone-secreting GT1-7 neuronal cells
    • Prioni S, Loberto N, Prinetti A, Chigorno V, Guzzi F, Maggi R, Parenti M, Sonnino S (2002) Sphingolipid metabolism and caveolin expression in gonadotropin-releasing hormone-expressing GN11 and gonadotropin-releasing hormone-secreting GT1-7 neuronal cells. Neurochem Res 27:831-840
    • (2002) Neurochem Res , vol.27 , pp. 831-840
    • Prioni, S.1    Loberto, N.2    Prinetti, A.3    Chigorno, V.4    Guzzi, F.5    Maggi, R.6    Parenti, M.7    Sonnino, S.8
  • 95
    • 0025543251 scopus 로고
    • Patterns of endogenous gangliosides and metabolic processing of exogenous gangliosides in cerebellar granule cells during differentiation in culture
    • Riboni L, Prinetti A, Pitto M, Tettamanti G (1990) Patterns of endogenous gangliosides and metabolic processing of exogenous gangliosides in cerebellar granule cells during differentiation in culture. Neurochem Res 15:1175-1183
    • (1990) Neurochem Res , vol.15 , pp. 1175-1183
    • Riboni, L.1    Prinetti, A.2    Pitto, M.3    Tettamanti, G.4
  • 96
    • 0026700494 scopus 로고
    • Developmental patterns of ganglioside sialosylation coincident with neuritogenesis in cultured embryonic chick brain neurons
    • Rosenberg A, Sauer A, Noble EP, Gross HJ, Chang R, Brossmer R (1992) Developmental patterns of ganglioside sialosylation coincident with neuritogenesis in cultured embryonic chick brain neurons. J Biol Chem 267:10607-10612
    • (1992) J Biol Chem , vol.267 , pp. 10607-10612
    • Rosenberg, A.1    Sauer, A.2    Noble, E.P.3    Gross, H.J.4    Chang, R.5    Brossmer, R.6
  • 97
    • 0018216692 scopus 로고
    • Immunofluorescent patterns of dissociated rat embryo cerebral cells during development in surface culture: Distinctive reactions with neurite and perikaryon cell membranes
    • Yavin Z, Yavin E (1978) Immunofluorescent patterns of dissociated rat embryo cerebral cells during development in surface culture: distinctive reactions with neurite and perikaryon cell membranes. Dev Neurosci 1:31-40
    • (1978) Dev Neurosci , vol.1 , pp. 31-40
    • Yavin, Z.1    Yavin, E.2
  • 98
    • 0024451962 scopus 로고
    • Changes of mouse brain gangliosides during aging from young adult until senescence
    • Ohsawa T (1989) Changes of mouse brain gangliosides during aging from young adult until senescence. Mech Ageing Dev 50:169-177
    • (1989) Mech Ageing Dev , vol.50 , pp. 169-177
    • Ohsawa, T.1
  • 99
    • 35148814075 scopus 로고    scopus 로고
    • Genotype-related changes of ganglioside composition in brain regions of transgenic mouse models of Alzheimer's disease
    • Barrier L, Ingrand S, Damjanac M, Rioux Bilan A, Hugon J, Page G (2007) Genotype-related changes of ganglioside composition in brain regions of transgenic mouse models of Alzheimer's disease. Neurobiol Aging 28:1863-1872
    • (2007) Neurobiol Aging , vol.28 , pp. 1863-1872
    • Barrier, L.1    Ingrand, S.2    Damjanac, M.3    Rioux Bilan, A.4    Hugon, J.5    Page, G.6
  • 101
    • 0028099263 scopus 로고
    • Membrane lipids of adult human brain: Lipid composition of frontal and temporal lobe in subjects of age 20 to 100 years
    • Svennerholm L, Bostrom K, Jungbjer B, Olsson L (1994) Membrane lipids of adult human brain: lipid composition of frontal and temporal lobe in subjects of age 20 to 100 years. J Neurochem 63:1802-1811
    • (1994) J Neurochem , vol.63 , pp. 1802-1811
    • Svennerholm, L.1    Bostrom, K.2    Jungbjer, B.3    Olsson, L.4
  • 102
    • 0028157335 scopus 로고
    • Membrane lipids, selectively diminished in Alzheimer brains, suggest synapse loss as a primary event in early-onset form (type I) and demyelination in late-onset form (type II
    • Svennerholm L, Gottfries CG (1994) Membrane lipids, selectively diminished in Alzheimer brains, suggest synapse loss as a primary event in early-onset form (type I) and demyelination in late-onset form (type II). J Neurochem 62:1039-1047
    • (1994) J Neurochem , vol.62 , pp. 1039-1047
    • Svennerholm, L.1    Gottfries, C.G.2
  • 104
    • 0021026958 scopus 로고
    • Ganglioside-induced neuritogenesis: Verification that ganglio-sides are the active agents, and comparison of molecular species
    • Byrne MC, Ledeen RW, Roisen FJ, Yorke G, Sclafani JR (1983) Ganglioside-induced neuritogenesis: verification that ganglio-sides are the active agents, and comparison of molecular species. J Neurochem 41:1214-1222
    • (1983) J Neurochem , vol.41 , pp. 1214-1222
    • Byrne, M.C.1    Ledeen, R.W.2    Roisen, F.J.3    Yorke, G.4    Sclafani, J.R.5
  • 105
    • 0021327310 scopus 로고
    • Promotion of neuritogenesis in mouse neuroblastoma cells by exogenous gangliosides. Relationship between the effect and the cell association of ganglioside GM1
    • Facci L, Leon A, Toffano G, Sonnino S, Ghidoni R, Tettamanti G (1984) Promotion of neuritogenesis in mouse neuroblastoma cells by exogenous gangliosides. Relationship between the effect and the cell association of ganglioside GM1. J Neurochem 42:299-305
    • (1984) J Neurochem , vol.42 , pp. 299-305
    • Facci, L.1    Leon, A.2    Toffano, G.3    Sonnino, S.4    Ghidoni, R.5    Tettamanti, G.6
  • 106
    • 0025293655 scopus 로고
    • Effect of differentiation and cell density on glycosphingolipid class and molecular species composition of mouse neuroblastoma NB2a cells
    • Kadowaki H, Evans JE, Rys-Sikora KE, Koff RS (1990) Effect of differentiation and cell density on glycosphingolipid class and molecular species composition of mouse neuroblastoma NB2a cells. J Neurochem 54:2125-2137
    • (1990) J Neurochem , vol.54 , pp. 2125-2137
    • Kadowaki, H.1    Evans, J.E.2    Rys-Sikora, K.E.3    Koff, R.S.4
  • 107
    • 0028211544 scopus 로고
    • Gangliosides turnover and neural cells function: A new perspective
    • Tettamanti G, Riboni L (1994) Gangliosides turnover and neural cells function: a new perspective. Prog Brain Res 101:77-100
    • (1994) Prog Brain Res , vol.101 , pp. 77-100
    • Tettamanti, G.1    Riboni, L.2
  • 108
    • 0023933272 scopus 로고
    • Synthetic sialyl compounds as well as natural gangliosides induce neuritogenesis in a mouse neuroblastoma cell line (Neuro2a
    • Tsuji S, Yamashita T, Tanaka M, Nagai Y (1988) Synthetic sialyl compounds as well as natural gangliosides induce neuritogenesis in a mouse neuroblastoma cell line (Neuro2a). J Neurochem 50:414-423
    • (1988) J Neurochem , vol.50 , pp. 414-423
    • Tsuji, S.1    Yamashita, T.2    Tanaka, M.3    Nagai, Y.4
  • 109
    • 0020776508 scopus 로고
    • Gangliosides enhance neurite outgrowth in PC12 cells
    • Ferrari G, Fabris M, Gorio A (1983) Gangliosides enhance neurite outgrowth in PC12 cells. Brain Res 284:215-221
    • (1983) Brain Res , vol.284 , pp. 215-221
    • Ferrari, G.1    Fabris, M.2    Gorio, A.3
  • 110
    • 0036694862 scopus 로고    scopus 로고
    • Stable transfection of GM1 synthase gene into GM1-deficient NG108-15 cells, CR-72 cells, rescues the responsiveness of Trk-neurotrophin receptor to its ligand, NGF
    • Mutoh T, Hamano T, Yano S, Koga H, Yamamoto H, Furukawa K, Ledeen RW (2002) Stable transfection of GM1 synthase gene into GM1-deficient NG108-15 cells, CR-72 cells, rescues the responsiveness of Trk-neurotrophin receptor to its ligand, NGF. Neurochem Res 27:801-806
    • (2002) Neurochem Res , vol.27 , pp. 801-806
    • Mutoh, T.1    Hamano, T.2    Yano, S.3    Koga, H.4    Yamamoto, H.5    Furukawa, K.6    Ledeen, R.W.7
  • 112
    • 0030007255 scopus 로고    scopus 로고
    • GM1 ganglioside modulates prostaglandin E1 stimulated adenylyl cyclase in neuro-2A cells
    • Wu G, Lu ZH, Ledeen RW (1996) GM1 ganglioside modulates prostaglandin E1 stimulated adenylyl cyclase in neuro-2A cells. Glycoconj J 13:235-239
    • (1996) Glycoconj J , vol.13 , pp. 235-239
    • Wu, G.1    Lu, Z.H.2    Ledeen, R.W.3
  • 113
    • 0025912858 scopus 로고
    • Correlation of gangliotetraose gangliosides with neurite forming potential of neuroblastoma cells
    • Wu GS, Lu ZH, Ledeen RW (1991) Correlation of gangliotetraose gangliosides with neurite forming potential of neuroblastoma cells. Brain Res Dev Brain Res 61:217-228
    • (1991) Brain Res Dev Brain Res , vol.61 , pp. 217-228
    • Wu, G.S.1    Lu, Z.H.2    Ledeen, R.W.3
  • 114
    • 0033597907 scopus 로고    scopus 로고
    • Glycosphingolipid-enriched signaling domain in mouse neuroblastoma Neuro2a cells. Mechanism of ganglioside-dependent neuritogenesis
    • Prinetti A, Iwabuchi K, Hakomori S (1999) Glycosphingolipid-enriched signaling domain in mouse neuroblastoma Neuro2a cells. Mechanism of ganglioside-dependent neuritogenesis. J Biol Chem 274:20916-20924
    • (1999) J Biol Chem , vol.274 , pp. 20916-20924
    • Prinetti, A.1    Iwabuchi, K.2    Hakomori, S.3
  • 115
    • 9644254296 scopus 로고    scopus 로고
    • Membrane cholesterol content modulates activation of BK channels in colonic epithelia
    • Lam RS, Shaw AR, Duszyk M (2004) Membrane cholesterol content modulates activation of BK channels in colonic epithelia. Biochim Biophys Acta 1667:241-248
    • (2004) Biochim Biophys Acta , vol.1667 , pp. 241-248
    • Lam, R.S.1    Shaw, A.R.2    Duszyk, M.3
  • 116
    • 0033597931 scopus 로고    scopus 로고
    • Sphingolipid depletion increases formation of the scrapie prion protein in neuroblastoma cells infected with prions
    • Naslavsky N, Shmeeda H, Friedlander G, Yanai A, Futerman AH, Barenholz Y, Taraboulos A (1999) Sphingolipid depletion increases formation of the scrapie prion protein in neuroblastoma cells infected with prions. J Biol Chem 274:20763-20771
    • (1999) J Biol Chem , vol.274 , pp. 20763-20771
    • Naslavsky, N.1    Shmeeda, H.2    Friedlander, G.3    Yanai, A.4    Futerman, A.H.5    Barenholz, Y.6    Taraboulos, A.7
  • 117
    • 0034602253 scopus 로고    scopus 로고
    • Involvement of gangliosides in glycosylphosphatidylinositol-anchored neuronal cell adhesion molecule TAG-1 signaling in lipid rafts
    • Kasahara K, Watanabe K, Takeuchi K, Kaneko H, Oohira A, Yamamoto T, Sanai Y (2000) Involvement of gangliosides in glycosylphosphatidylinositol-anchored neuronal cell adhesion molecule TAG-1 signaling in lipid rafts. J Biol Chem 275:34701-34709
    • (2000) J Biol Chem , vol.275 , pp. 34701-34709
    • Kasahara, K.1    Watanabe, K.2    Takeuchi, K.3    Kaneko, H.4    Oohira, A.5    Yamamoto, T.6    Sanai, Y.7
  • 118
    • 0034534277 scopus 로고    scopus 로고
    • Glycosphingolipid deficiency affects functional microdomain formation in Lewis lung carcinoma cells
    • Inokuchi JI, Uemura S, Kabayama K, Igarashi Y (2000) Glycosphingolipid deficiency affects functional microdomain formation in Lewis lung carcinoma cells. Glycoconj J 17:239-245
    • (2000) Glycoconj J , vol.17 , pp. 239-245
    • Inokuchi, J.I.1    Uemura, S.2    Kabayama, K.3    Igarashi, Y.4
  • 119
    • 27444438906 scopus 로고    scopus 로고
    • A specific microdomain ("glycosynapse 3") controls phenotypic conversion and reversion of bladder cancer cells through GM3-mediated interaction of alpha3beta1 integrin with CD9
    • Mitsuzuka K, Handa K, Satoh M, Arai Y, Hakomori S (2005) A specific microdomain ("glycosynapse 3") controls phenotypic conversion and reversion of bladder cancer cells through GM3-mediated interaction of alpha3beta1 integrin with CD9. J Biol Chem 280:35545-35553
    • (2005) J Biol Chem , vol.280 , pp. 35545-35553
    • Mitsuzuka, K.1    Handa, K.2    Satoh, M.3    Arai, Y.4    Hakomori, S.5
  • 120
    • 9144272911 scopus 로고    scopus 로고
    • Reduction of glycosphingolipid levels in lipid rafts affects the expression state and function of glycosylphosphatidylinositol-anchored proteins but does not impair signal transduction via the T cell receptor
    • Nagafuku M, Kabayama K, Oka D, Kato A, Tani-ichi S, Shimada Y, Ohno-Iwashita Y, Yamasaki S, Saito T, Iwabuchi K, Hamaoka T, Inokuchi J, Kosugi A (2003) Reduction of glycosphingolipid levels in lipid rafts affects the expression state and function of glycosylphosphatidylinositol-anchored proteins but does not impair signal transduction via the T cell receptor. J Biol Chem 278:51920-51927
    • (2003) J Biol Chem , vol.278 , pp. 51920-51927
    • Nagafuku, M.1    Kabayama, K.2    Oka, D.3    Kato, A.4    Tani-Ichi, S.5    Shimada, Y.6    Ohno-Iwashita, Y.7    Yamasaki, S.8    Saito, T.9    Iwabuchi, K.10    Hamaoka, T.11    Inokuchi, J.12    Kosugi, A.13
  • 121
    • 26444469673 scopus 로고    scopus 로고
    • Role for up-regulated ganglioside biosynthesis and association of Src family kinases with microdomains in retinoic acid-induced differentiation of F9 embryonal carcinoma cells
    • Sato T, Zakaria AM, Uemura S, Ishii A, Ohno-Iwashita Y, Igarashi Y, Inokuchi J (2005) Role for up-regulated ganglioside biosynthesis and association of Src family kinases with microdomains in retinoic acid-induced differentiation of F9 embryonal carcinoma cells. Glycobiology 15:687-699
    • (2005) Glycobiology , vol.15 , pp. 687-699
    • Sato, T.1    Zakaria, A.M.2    Uemura, S.3    Ishii, A.4    Ohno-Iwashita, Y.5    Igarashi, Y.6    Inokuchi, J.7
  • 122
    • 4544250815 scopus 로고    scopus 로고
    • Cell growth regulation through GM3-enriched microdomain (glycosynapse) in human lung embryonal fibroblast WI38 and its oncogenic transformant VA13
    • Toledo MS, Suzuki E, Handa K, Hakomori S (2004) Cell growth regulation through GM3-enriched microdomain (glycosynapse) in human lung embryonal fibroblast WI38 and its oncogenic transformant VA13. J Biol Chem 279:34655-34664
    • (2004) J Biol Chem , vol.279 , pp. 34655-34664
    • Toledo, M.S.1    Suzuki, E.2    Handa, K.3    Hakomori, S.4
  • 123
    • 26644433655 scopus 로고    scopus 로고
    • Glycosphingolipid synthesis inhibitor represses cytokine-induced activation of the Ras-MAPK pathway in embryonic neural precursor cells
    • Yanagisawa M, Nakamura K, Taga T (2005) Glycosphingolipid synthesis inhibitor represses cytokine-induced activation of the Ras-MAPK pathway in embryonic neural precursor cells. J Biochem (Tokyo) 138:285-291
    • (2005) J Biochem (Tokyo) , vol.138 , pp. 285-291
    • Yanagisawa, M.1    Nakamura, K.2    Taga, T.3
  • 124
    • 33644816561 scopus 로고    scopus 로고
    • Inhibition of sphingolipid synthesis affects kinetics but not fidelity of L1/NgCAM transport along direct but not transcytotic axonal pathways
    • Chang MC, Wisco D, Ewers H, Norden C, Winckler B (2006) Inhibition of sphingolipid synthesis affects kinetics but not fidelity of L1/NgCAM transport along direct but not transcytotic axonal pathways. Mol Cell Neurosci 31:525-538
    • (2006) Mol Cell Neurosci , vol.31 , pp. 525-538
    • Chang, M.C.1    Wisco, D.2    Ewers, H.3    Norden, C.4    Winckler, B.5
  • 125
    • 3042609777 scopus 로고    scopus 로고
    • Lipid rafts: Microenvironments for integrin-growth factor interactions in neural development
    • Decker L, Baron W, Ffrench-Constant C (2004) Lipid rafts: microenvironments for integrin-growth factor interactions in neural development. Biochem Soc Trans 32:426-430
    • (2004) Biochem Soc Trans , vol.32 , pp. 426-430
    • Decker, L.1    Baron, W.2    Ffrench-Constant, C.3
  • 126
    • 0037381124 scopus 로고    scopus 로고
    • Ceramide in rafts (detergent-insoluble fraction) mediates cell death in neurotumor cell lines
    • Kilkus J, Goswami R, Testai FD, Dawson G (2003) Ceramide in rafts (detergent-insoluble fraction) mediates cell death in neurotumor cell lines. J Neurosci Res 72:65-75
    • (2003) J Neurosci Res , vol.72 , pp. 65-75
    • Kilkus, J.1    Goswami, R.2    Testai, F.D.3    Dawson, G.4
  • 127
    • 0032584212 scopus 로고    scopus 로고
    • Neuronal polarity: Essential role of protein-lipid complexes in axonal sorting
    • Ledesma MD, Simons K, Dotti CG (1998) Neuronal polarity: essential role of protein-lipid complexes in axonal sorting. Proc Natl Acad Sci USA 95:3966-3971
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 3966-3971
    • Ledesma, M.D.1    Simons, K.2    Dotti, C.G.3
  • 128
    • 0027278513 scopus 로고
    • Inhibition of sphingolipid synthesis affects axonal outgrowth in cultured hippocampal neurons
    • Harel R, Futerman AH (1993) Inhibition of sphingolipid synthesis affects axonal outgrowth in cultured hippocampal neurons. J Biol Chem 268:14476-14481
    • (1993) J Biol Chem , vol.268 , pp. 14476-14481
    • Harel, R.1    Futerman, A.H.2
  • 129
    • 0028933977 scopus 로고
    • A regulatory role for sphingolipids in neuronal growth. Inhibition of sphingolipid synthesis and degradation have opposite effects on axonal branching
    • Schwarz A, Rapaport E, Hirschberg K, Futerman AH (1995) A regulatory role for sphingolipids in neuronal growth. Inhibition of sphingolipid synthesis and degradation have opposite effects on axonal branching. J Biol Chem 270:10990-10998
    • (1995) J Biol Chem , vol.270 , pp. 10990-10998
    • Schwarz, A.1    Rapaport, E.2    Hirschberg, K.3    Futerman, A.H.4
  • 130
    • 0029800629 scopus 로고    scopus 로고
    • Induction of ganglioside biosynthesis and neurite outgrowth of primary cultured neurons by L-threo-1-phenyl-2-decanoylamino-3-morpholino-1-propanol
    • Usuki S, Hamanoue M, Kohsaka S, Inokuchi J (1996) Induction of ganglioside biosynthesis and neurite outgrowth of primary cultured neurons by L-threo-1-phenyl-2-decanoylamino-3-morpholino-1-propanol. J Neurochem 67:1821-1830
    • (1996) J Neurochem , vol.67 , pp. 1821-1830
    • Usuki, S.1    Hamanoue, M.2    Kohsaka, S.3    Inokuchi, J.4
  • 132
    • 0031928545 scopus 로고    scopus 로고
    • Significance of gangliosides in neuronal differentiation of neuroblastoma cells and neurite growth in tissue culture
    • Rosner H (1998) Significance of gangliosides in neuronal differentiation of neuroblastoma cells and neurite growth in tissue culture. Ann N Y Acad Sci 845:200-214
    • (1998) Ann N y Acad Sci , vol.845 , pp. 200-214
    • Rosner, H.1
  • 133
    • 0023812102 scopus 로고
    • Nerve growth factor, a differentiating agent, and epidermal growth factor, a mitogen, increase the activities of different S6 kinases in PC12 cells
    • Mutoh T, Rudkin BB, Koizumi S, Guroff G (1988) Nerve growth factor, a differentiating agent, and epidermal growth factor, a mitogen, increase the activities of different S6 kinases in PC12 cells. J Biol Chem 263:15853-15856
    • (1988) J Biol Chem , vol.263 , pp. 15853-15856
    • Mutoh, T.1    Rudkin, B.B.2    Koizumi, S.3    Guroff, G.4
  • 135
    • 0027970181 scopus 로고
    • Induction of cholinergic differentiation with neurite sprouting by de novo biosynthesis and expression of GD3 and b-series gangliosides in Neuro2a cells
    • Kojima N, Kurosawa N, Nishi T, Hanai N, Tsuji S (1994) Induction of cholinergic differentiation with neurite sprouting by de novo biosynthesis and expression of GD3 and b-series gangliosides in Neuro2a cells. J Biol Chem 269:30451-30456
    • (1994) J Biol Chem , vol.269 , pp. 30451-30456
    • Kojima, N.1    Kurosawa, N.2    Nishi, T.3    Hanai, N.4    Tsuji, S.5
  • 136
    • 0028894347 scopus 로고
    • Effect of nerve growth factor and forskolin on glycosyltransferase activities and expression of a globo-series glycosphingolipid in PC12D pheochromocytoma cells
    • Kanda T, Ariga T, Yamawaki M, Pal S, Katoh-Semba R, Yu RK (1995) Effect of nerve growth factor and forskolin on glycosyltransferase activities and expression of a globo-series glycosphingolipid in PC12D pheochromocytoma cells. J Neurochem 64:810-817
    • (1995) J Neurochem , vol.64 , pp. 810-817
    • Kanda, T.1    Ariga, T.2    Yamawaki, M.3    Pal, S.4    Katoh-Semba, R.5    Yu, R.K.6
  • 137
    • 0034616293 scopus 로고    scopus 로고
    • Up-regulation of glucosylcer-amide synthesis upon stimulation of axonal growth by basic fibroblast growth factor. Evidence for post-translational modification of glucosylceramide synthase
    • Boldin SA, Futerman AH (2000) Up-regulation of glucosylcer-amide synthesis upon stimulation of axonal growth by basic fibroblast growth factor. Evidence for post-translational modification of glucosylceramide synthase. J Biol Chem 275:9905-9909
    • (2000) J Biol Chem , vol.275 , pp. 9905-9909
    • Boldin, S.A.1    Futerman, A.H.2
  • 138
    • 0023951111 scopus 로고
    • Developmental changes in ganglioside composition and synthesis in embryonic rat brain
    • Yu RK, Macala LJ, Taki T, Weinfield HM, Yu FS (1988) Developmental changes in ganglioside composition and synthesis in embryonic rat brain. J Neurochem 50:1825-1829
    • (1988) J Neurochem , vol.50 , pp. 1825-1829
    • Yu, R.K.1    MacAla, L.J.2    Taki, T.3    Weinfield, H.M.4    Yu, F.S.5
  • 139
    • 66349103103 scopus 로고    scopus 로고
    • The role of glycosphingolipid metabolism in the developing brain
    • Yu RK, Nakatani Y, Yanagisawa M (2009) The role of glycosphingolipid metabolism in the developing brain. J Lipid Res 50(Suppl):S440-445
    • (2009) J Lipid Res , vol.50 , Issue.SUPPL.
    • Yu, R.K.1    Nakatani, Y.2    Yanagisawa, M.3
  • 140
    • 0036695474 scopus 로고    scopus 로고
    • Modulation of neuritogenesis by ganglioside-specific sialidase (Neu 3) in human neuroblastoma NB-1 cells
    • Proshin S, Yamaguchi K, Wada T, Miyagi T (2002) Modulation of neuritogenesis by ganglioside-specific sialidase (Neu 3) in human neuroblastoma NB-1 cells. Neurochem Res 27:841-846
    • (2002) Neurochem Res , vol.27 , pp. 841-846
    • Proshin, S.1    Yamaguchi, K.2    Wada, T.3    Miyagi, T.4
  • 141
    • 0034826059 scopus 로고    scopus 로고
    • Differential functional relevance of a plasma membrane ganglioside sialidase in cholinergic and adrenergic neuroblastoma cell lines
    • von Reitzenstein C, Kopitz J, Schuhmann V, Cantz M (2001) Differential functional relevance of a plasma membrane ganglioside sialidase in cholinergic and adrenergic neuroblastoma cell lines. Eur J Biochem 268:326-333
    • (2001) Eur J Biochem , vol.268 , pp. 326-333
    • Von Reitzenstein, C.1    Kopitz, J.2    Schuhmann, V.3    Cantz, M.4
  • 143
    • 0035503727 scopus 로고    scopus 로고
    • Plasma membrane ganglioside sialidase regulates axonal growth and regeneration in hippocampal neurons in culture
    • Rodriguez JA, Piddini E, Hasegawa T, Miyagi T, Dotti CG (2001) Plasma membrane ganglioside sialidase regulates axonal growth and regeneration in hippocampal neurons in culture. J Neurosci 21:8387-8395
    • (2001) J Neurosci , vol.21 , pp. 8387-8395
    • Rodriguez, J.A.1    Piddini, E.2    Hasegawa, T.3    Miyagi, T.4    Dotti, C.G.5
  • 144
    • 29144483525 scopus 로고    scopus 로고
    • Toward understanding the dynamics of membrane-raft-based molecular interactions
    • Kusumi A, Suzuki K (2005) Toward understanding the dynamics of membrane-raft-based molecular interactions. Biochim Biophys Acta 1746:234-251
    • (2005) Biochim Biophys Acta , vol.1746 , pp. 234-251
    • Kusumi, A.1    Suzuki, K.2
  • 145
    • 38449090335 scopus 로고    scopus 로고
    • Modulation of cell functions by glycosphingolipid metabolic remodeling in the plasma membrane
    • Prinetti A, Chigorno V, Mauri L, Loberto N, Sonnino S (2007) Modulation of cell functions by glycosphingolipid metabolic remodeling in the plasma membrane. J Neurochem 103(Suppl 1):113-125
    • (2007) J Neurochem , vol.103 , Issue.SUPPL. 1 , pp. 113-125
    • Prinetti, A.1    Chigorno, V.2    Mauri, L.3    Loberto, N.4    Sonnino, S.5
  • 146
    • 17244380947 scopus 로고    scopus 로고
    • Lipid rafts and membrane dynamics
    • Rajendran L, Simons K (2005) Lipid rafts and membrane dynamics. J Cell Sci 118:1099-1102
    • (2005) J Cell Sci , vol.118 , pp. 1099-1102
    • Rajendran, L.1    Simons, K.2
  • 148
    • 0035426416 scopus 로고    scopus 로고
    • GDNF recruits the signaling crew into lipid rafts
    • Saarma M (2001) GDNF recruits the signaling crew into lipid rafts. Trends Neurosci 24:427-429
    • (2001) Trends Neurosci , vol.24 , pp. 427-429
    • Saarma, M.1
  • 149
    • 2342451911 scopus 로고    scopus 로고
    • G-protein coupled receptors in lipid rafts and caveolae: How when and why do they go theré
    • Chini B, Parenti M (2004) G-protein coupled receptors in lipid rafts and caveolae: how, when and why do they go theré J Mol Endocrinol 32:325-338
    • (2004) J Mol Endocrinol , vol.32 , pp. 325-338
    • Chini, B.1    Parenti, M.2
  • 150
    • 0030664824 scopus 로고    scopus 로고
    • Association of Src family tyrosine kinase Lyn with ganglioside GD3 in rat brain. Possible regulation of Lyn by glycosphingolipid in caveolae-like domains
    • Kasahara K, Watanabe Y, YamamotoT,Sanai Y (1997) Association of Src family tyrosine kinase Lyn with ganglioside GD3 in rat brain. Possible regulation of Lyn by glycosphingolipid in caveolae-like domains. J Biol Chem 272:29947-29953
    • (1997) J Biol Chem , vol.272 , pp. 29947-29953
    • Kasahara, K.1    Watanabe, Y.2    Yamamototsanai, Y.3
  • 151
    • 23944445784 scopus 로고    scopus 로고
    • Activity-dependent modulation of the BDNF receptor TrkB: Mechanisms and implications
    • Nagappan G, Lu B (2005) Activity-dependent modulation of the BDNF receptor TrkB: mechanisms and implications. Trends Neurosci 28:464-471
    • (2005) Trends Neurosci , vol.28 , pp. 464-471
    • Nagappan, G.1    Lu, B.2
  • 152
    • 0036801360 scopus 로고    scopus 로고
    • Lipid rafts and the control of neurotrophic factor signaling in the nervous system: Variations on a theme
    • Paratcha G, Ibanez CF (2002) Lipid rafts and the control of neurotrophic factor signaling in the nervous system: variations on a theme. Curr Opin Neurobiol 12:542-549
    • (2002) Curr Opin Neurobiol , vol.12 , pp. 542-549
    • Paratcha, G.1    Ibanez, C.F.2
  • 153
    • 0034697010 scopus 로고    scopus 로고
    • Sphingolipid-enriched membrane domains from rat cerebellar granule cells differentiated in culture. A compositional study
    • Prinetti A, Chigorno V, Tettamanti G, Sonnino S (2000) Sphingolipid-enriched membrane domains from rat cerebellar granule cells differentiated in culture. A compositional study. J Biol Chem 275:11658-11665
    • (2000) J Biol Chem , vol.275 , pp. 11658-11665
    • Prinetti, A.1    Chigorno, V.2    Tettamanti, G.3    Sonnino, S.4
  • 154
    • 0034528068 scopus 로고    scopus 로고
    • Association of Src-family protein tyrosine kinases with sphingolipids in rat cerebellar granule cells differentiated in culture
    • Prinetti A, Marano N, Prioni S, Chigorno V, Mauri L, Casellato R, Tettamanti G, Sonnino S (2000) Association of Src-family protein tyrosine kinases with sphingolipids in rat cerebellar granule cells differentiated in culture. Glycoconj J 17:223-232
    • (2000) Glycoconj J , vol.17 , pp. 223-232
    • Prinetti, A.1    Marano, N.2    Prioni, S.3    Chigorno, V.4    Mauri, L.5    Casellato, R.6    Tettamanti, G.7    Sonnino, S.8
  • 155
    • 0031034679 scopus 로고    scopus 로고
    • Tyrosine kinase receptors concentrated in caveolae-like domains from neuronal plasma membrane
    • Wu C, Butz S, Ying Y, Anderson RG (1997) Tyrosine kinase receptors concentrated in caveolae-like domains from neuronal plasma membrane. J Biol Chem 272:3554-3559
    • (1997) J Biol Chem , vol.272 , pp. 3554-3559
    • Wu, C.1    Butz, S.2    Ying, Y.3    Anderson, R.G.4
  • 156
    • 1942425583 scopus 로고    scopus 로고
    • Lipid rafts and integrin activation regulate oligodendrocyte survival
    • Decker L, Ffrench-Constant C (2004) Lipid rafts and integrin activation regulate oligodendrocyte survival. J Neurosci 24:3816-3825
    • (2004) J Neurosci , vol.24 , pp. 3816-3825
    • Decker, L.1    Ffrench-Constant, C.2
  • 157
    • 18544376071 scopus 로고    scopus 로고
    • Prion protein recruits its neuronal receptor NCAM to lipid rafts to activate p59fyn and to enhance neurite outgrowth
    • Santuccione A, Sytnyk V, Leshchyns'ka I, Schachner M (2005) Prion protein recruits its neuronal receptor NCAM to lipid rafts to activate p59fyn and to enhance neurite outgrowth. J Cell Biol 169:341-354
    • (2005) J Cell Biol , vol.169 , pp. 341-354
    • Santuccione, A.1    Sytnyk, V.2    Leshchyns'Ka, I.3    Schachner, M.4
  • 158
  • 159
    • 0037062501 scopus 로고    scopus 로고
    • Ganglioside rafts as MAG receptors that mediate blockade of axon growth
    • McKerracher L (2002) Ganglioside rafts as MAG receptors that mediate blockade of axon growth. Proc Natl Acad Sci USA 99:7811-7813
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 7811-7813
    • McKerracher, L.1
  • 162
    • 53749085118 scopus 로고    scopus 로고
    • The role and metabolism of sulfatide in the nervous system
    • Eckhardt M (2008) The role and metabolism of sulfatide in the nervous system. Mol Neurobiol 37:93-103
    • (2008) Mol Neurobiol , vol.37 , pp. 93-103
    • Eckhardt, M.1
  • 163
    • 0037137492 scopus 로고    scopus 로고
    • Galactolipids are molecular determinants of myelin development and axo-glial organization
    • Marcus J, Popko B (2002) Galactolipids are molecular determinants of myelin development and axo-glial organization. Biochim Biophys Acta 1573:406-413
    • (2002) Biochim Biophys Acta , vol.1573 , pp. 406-413
    • Marcus, J.1    Popko, B.2
  • 164
    • 0029851157 scopus 로고    scopus 로고
    • Functional breakdown of the lipid bilayer of the myelin membrane in central and peripheral nervous system by disrupted galactocerebroside synthesis
    • Bosio A, Binczek E, Stoffel W (1996) Functional breakdown of the lipid bilayer of the myelin membrane in central and peripheral nervous system by disrupted galactocerebroside synthesis. Proc Natl Acad Sci USA 93:13280-13285
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 13280-13285
    • Bosio, A.1    Binczek, E.2    Stoffel, W.3
  • 165
    • 0030602822 scopus 로고    scopus 로고
    • Myelination in the absence of galactocerebroside and sulfatide: Normal structure with abnormal function and regional instability
    • Coetzee T, Fujita N, Dupree J, Shi R, Blight A, Suzuki K, Popko B (1996) Myelination in the absence of galactocerebroside and sulfatide: normal structure with abnormal function and regional instability. Cell 86:209-219
    • (1996) Cell , vol.86 , pp. 209-219
    • Coetzee, T.1    Fujita, N.2    Dupree, J.3    Shi, R.4    Blight, A.5    Suzuki, K.6    Popko, B.7
  • 166
    • 1242314377 scopus 로고    scopus 로고
    • Sulfatide is a negative regulator of oligodendrocyte differentiation: Development in sulfatide-null mice
    • Hirahara Y, Bansal R, Honke K, Ikenaka K, Wada Y (2004) Sulfatide is a negative regulator of oligodendrocyte differentiation: development in sulfatide-null mice. Glia 45:269-277
    • (2004) Glia , vol.45 , pp. 269-277
    • Hirahara, Y.1    Bansal, R.2    Honke, K.3    Ikenaka, K.4    Wada, Y.5
  • 167
    • 40849086666 scopus 로고    scopus 로고
    • Myelin glycosphingolipids, galactosylceramide and sulfatide, participate in carbohydrate-carbohydrate interactions between apposed membranes and may form glycosynapses between oligodendrocyte and/or myelin membranes
    • Boggs JM, Gao W, Hirahara Y (2008) Myelin glycosphingolipids, galactosylceramide and sulfatide, participate in carbohydrate-carbohydrate interactions between apposed membranes and may form glycosynapses between oligodendrocyte and/or myelin membranes. Biochim Biophys Acta 1780:445-455
    • (2008) Biochim Biophys Acta , vol.1780 , pp. 445-455
    • Boggs, J.M.1    Gao, W.2    Hirahara, Y.3
  • 168
    • 0036319382 scopus 로고    scopus 로고
    • Detergent-insoluble glycosphingolipid/cholesterol microdomains of the myelin membrane
    • Taylor CM, Coetzee T, Pfeiffer SE (2002) Detergent-insoluble glycosphingolipid/cholesterol microdomains of the myelin membrane. J Neurochem 81:993-1004
    • (2002) J Neurochem , vol.81 , pp. 993-1004
    • Taylor, C.M.1    Coetzee, T.2    Pfeiffer, S.E.3
  • 169
    • 23644441748 scopus 로고    scopus 로고
    • Myelin-associated glycoprotein and complementary axonal ligands, gangliosides, mediate axon stability in the CNS and PNS: Neuropathology and behavioral deficits in single-and double-null mice
    • Pan B, Fromholt SE, Hess EJ, Crawford TO, Griffin JW, Sheikh KA, Schnaar RL (2005) Myelin-associated glycoprotein and complementary axonal ligands, gangliosides, mediate axon stability in the CNS and PNS: neuropathology and behavioral deficits in single-and double-null mice. Exp Neurol 195:208-217
    • (2005) Exp Neurol , vol.195 , pp. 208-217
    • Pan, B.1    Fromholt, S.E.2    Hess, E.J.3    Crawford, T.O.4    Griffin, J.W.5    Sheikh, K.A.6    Schnaar, R.L.7
  • 170
    • 70449379468 scopus 로고    scopus 로고
    • Myelin-associated glycoprotein and its axonal receptors
    • Schnaar RL, Lopez PH (2009) Myelin-associated glycoprotein and its axonal receptors. J Neurosci Res 87:3267-3276
    • (2009) J Neurosci Res , vol.87 , pp. 3267-3276
    • Schnaar, R.L.1    Lopez, P.H.2
  • 171
    • 0025651203 scopus 로고
    • Myelin-associated glycoprotein Location and potential functions
    • Trapp BD (1990) Myelin-associated glycoprotein. Location and potential functions. Ann N Y Acad Sci 605:29-43
    • (1990) Ann N y Acad Sci , vol.605 , pp. 29-43
    • Trapp, B.D.1
  • 172
    • 0034651036 scopus 로고    scopus 로고
    • Multiple functions of the myelin-associated glycoprotein MAG (siglec-4a) in formation and maintenance of myelin
    • Schachner M, Bartsch U (2000) Multiple functions of the myelin-associated glycoprotein MAG (siglec-4a) in formation and maintenance of myelin. Glia 29:154-165
    • (2000) Glia , vol.29 , pp. 154-165
    • Schachner, M.1    Bartsch, U.2
  • 173
    • 33847718359 scopus 로고    scopus 로고
    • Myelin-associated glycoprotein (MAG): Past, present and beyond
    • Quarles RH (2007) Myelin-associated glycoprotein (MAG): past, present and beyond. J Neurochem 100:1431-1448
    • (2007) J Neurochem , vol.100 , pp. 1431-1448
    • Quarles, R.H.1
  • 174
    • 0031439129 scopus 로고    scopus 로고
    • Neural cell adhesion molecules of the immunoglobulin superfamily: Role in axon growth and guidance
    • Walsh FS, Doherty P (1997) Neural cell adhesion molecules of the immunoglobulin superfamily: role in axon growth and guidance. Annu Rev Cell Dev Biol 13:425-456
    • (1997) Annu Rev Cell Dev Biol , vol.13 , pp. 425-456
    • Walsh, F.S.1    Doherty, P.2
  • 175
    • 33645347979 scopus 로고    scopus 로고
    • Unraveling the differential expression of the two isoforms of myelin-associated glycoprotein in a mouse expressing GFP-tagged S-MAG specifically regulated and targeted into the different myelin compartments
    • Erb M, Flueck B, Kern F, Erne B, Steck AJ, Schaeren-Wiemers N (2006) Unraveling the differential expression of the two isoforms of myelin-associated glycoprotein in a mouse expressing GFP-tagged S-MAG specifically regulated and targeted into the different myelin compartments. Mol Cell Neurosci 31:613-627
    • (2006) Mol Cell Neurosci , vol.31 , pp. 613-627
    • Erb, M.1    Flueck, B.2    Kern, F.3    Erne, B.4    Steck, A.J.5    Schaeren-Wiemers, N.6
  • 176
    • 0031574066 scopus 로고    scopus 로고
    • Reciprocal expression of myelin-associated glycoprotein splice variants in the adult human peripheral and central nervous systems
    • Miescher GC, Lutzelschwab R, Erne B, Ferracin F, Huber S, Steck AJ (1997) Reciprocal expression of myelin-associated glycoprotein splice variants in the adult human peripheral and central nervous systems. Brain Res Mol Brain Res 52:299-306
    • (1997) Brain Res Mol Brain Res , vol.52 , pp. 299-306
    • Miescher, G.C.1    Lutzelschwab, R.2    Erne, B.3    Ferracin, F.4    Huber, S.5    Steck, A.J.6
  • 177
    • 0027730463 scopus 로고
    • Identification of the glycosylated sequons of human myelin-associated glycoprotein
    • Burger D, Pidoux L, Steck AJ (1993) Identification of the glycosylated sequons of human myelin-associated glycoprotein. Biochem Biophys Res Commun 197:457-464
    • (1993) Biochem Biophys Res Commun , vol.197 , pp. 457-464
    • Burger, D.1    Pidoux, L.2    Steck, A.J.3
  • 178
    • 0029809869 scopus 로고    scopus 로고
    • Structure of the HNK-1 carbohydrate epitope on bovine peripheral myelin glycoprotein P0
    • Voshol H, van Zuylen CW, Orberger G, Vliegenthart JF, Schachner M (1996) Structure of the HNK-1 carbohydrate epitope on bovine peripheral myelin glycoprotein P0. J Biol Chem 271:22957-22960
    • (1996) J Biol Chem , vol.271 , pp. 22957-22960
    • Voshol, H.1    Van Zuylen, C.W.2    Orberger, G.3    Vliegenthart, J.F.4    Schachner, M.5
  • 179
  • 180
    • 0028540931 scopus 로고
    • Sialoadhesin, myelin-associated glycoprotein and CD22 define a new family of sialic acid-dependent adhesion molecules of the immunoglobulin superfamily
    • Kelm S, Pelz A, Schauer R, Filbin MT, Tang S, de Bellard ME, Schnaar RL, Mahoney JA, Hartnell A, Bradfield P et al (1994) Sialoadhesin, myelin-associated glycoprotein and CD22 define a new family of sialic acid-dependent adhesion molecules of the immunoglobulin superfamily. Curr Biol 4:965-972
    • (1994) Curr Biol , vol.4 , pp. 965-972
    • Kelm, S.1    Pelz, A.2    Schauer, R.3    Filbin, M.T.4    Tang, S.5    De Bellard, M.E.6    Schnaar, R.L.7    Mahoney, J.A.8    Hartnell, A.9    Bradfield, P.10
  • 182
    • 0034855317 scopus 로고    scopus 로고
    • Brain gangliosides: Functional ligands for myelin stability and the control of nerve regeneration
    • Vyas AA, Schnaar RL (2001) Brain gangliosides: functional ligands for myelin stability and the control of nerve regeneration. Biochimie 83:677-682
    • (2001) Biochimie , vol.83 , pp. 677-682
    • Vyas, A.A.1    Schnaar, R.L.2
  • 184
    • 14444268726 scopus 로고    scopus 로고
    • Myelin-associated glyco-protein interacts with neurons via a sialic acid binding site at ARG118 and a distinct neurite inhibition site
    • Tang S, Shen YJ, DeBellard ME, Mukhopadhyay G, Salzer JL, Crocker PR, Filbin MT (1997) Myelin-associated glyco-protein interacts with neurons via a sialic acid binding site at ARG118 and a distinct neurite inhibition site. J Cell Biol 138:1355-1366
    • (1997) J Cell Biol , vol.138 , pp. 1355-1366
    • Tang, S.1    Shen, Y.J.2    Debellard, M.E.3    Mukhopadhyay, G.4    Salzer, J.L.5    Crocker, P.R.6    Filbin, M.T.7
  • 185
    • 0027943833 scopus 로고
    • Identification of tyrosine 620 as the major phosphorylation site of myelin-associated glycoprotein and its implication in interacting with signaling molecules
    • Jaramillo ML, Afar DE, Almazan G, Bell JC (1994) Identification of tyrosine 620 as the major phosphorylation site of myelin-associated glycoprotein and its implication in interacting with signaling molecules. J Biol Chem 269:27240-27245
    • (1994) J Biol Chem , vol.269 , pp. 27240-27245
    • Jaramillo, M.L.1    Afar, D.E.2    Almazan, G.3    Bell, J.C.4
  • 186
    • 0032822035 scopus 로고    scopus 로고
    • Calcium-dependent interaction between the large myelin-associated glycoprotein and S100beta
    • Kursula P, Tikkanen G, Lehto VP, Nishikimi M, Heape AM (1999) Calcium-dependent interaction between the large myelin-associated glycoprotein and S100beta. J Neurochem 73:1724-1732
    • (1999) J Neurochem , vol.73 , pp. 1724-1732
    • Kursula, P.1    Tikkanen, G.2    Lehto, V.P.3    Nishikimi, M.4    Heape, A.M.5
  • 188
    • 0027976632 scopus 로고
    • Initial events of myelination involve Fyn tyrosine kinase signalling
    • Umemori H, Sato S, Yagi T, Aizawa S, Yamamoto T (1994) Initial events of myelination involve Fyn tyrosine kinase signalling. Nature 367:572-576
    • (1994) Nature , vol.367 , pp. 572-576
    • Umemori, H.1    Sato, S.2    Yagi, T.3    Aizawa, S.4    Yamamoto, T.5
  • 189
    • 0032521096 scopus 로고    scopus 로고
    • The cytoplasmic domain of the large myelin-associated glycoprotein isoform is needed for proper CNS but not peripheral nervous system myelination
    • Fujita N, Kemper A, Dupree J, Nakayasu H, Bartsch U, Schachner M, Maeda N, Suzuki K, Popko B (1998) The cytoplasmic domain of the large myelin-associated glycoprotein isoform is needed for proper CNS but not peripheral nervous system myelination. J Neurosci 18:1970-1978
    • (1998) J Neurosci , vol.18 , pp. 1970-1978
    • Fujita, N.1    Kemper, A.2    Dupree, J.3    Nakayasu, H.4    Bartsch, U.5    Schachner, M.6    Maeda, N.7    Suzuki, K.8    Popko, B.9
  • 190
    • 0035910940 scopus 로고    scopus 로고
    • The small myelin-associated glycoprotein binds to tubulin and microtubules
    • Kursula P, Lehto VP, Heape AM (2001) The small myelin-associated glycoprotein binds to tubulin and microtubules. Brain Res Mol Brain Res 87:22-30
    • (2001) Brain Res Mol Brain Res , vol.87 , pp. 22-30
    • Kursula, P.1    Lehto, V.P.2    Heape, A.M.3
  • 191
    • 0034597142 scopus 로고    scopus 로고
    • Assembly of myelin by association of proteolipid protein with cholesterol-and galactosylceramide-rich membrane domains
    • Simons M, Kramer EM, Thiele C, Stoffel W, Trotter J (2000) Assembly of myelin by association of proteolipid protein with cholesterol-and galactosylceramide-rich membrane domains. J Cell Biol 151:143-154
    • (2000) J Cell Biol , vol.151 , pp. 143-154
    • Simons, M.1    Kramer, E.M.2    Thiele, C.3    Stoffel, W.4    Trotter, J.5
  • 192
    • 15744381624 scopus 로고    scopus 로고
    • Myelin associated glycoprotein cross-linking triggers its partitioning into lipid rafts, specific signaling events and cytoskeletal rearrangements in oligodendrocytes
    • Marta CB, Taylor CM, Cheng S, Quarles RH, Bansal R, Pfeiffer SE (2004) Myelin associated glycoprotein cross-linking triggers its partitioning into lipid rafts, specific signaling events and cytoskeletal rearrangements in oligodendrocytes. Neuron Glia Biol 1:35-46
    • (2004) Neuron Glia Biol , vol.1 , pp. 35-46
    • Marta, C.B.1    Taylor, C.M.2    Cheng, S.3    Quarles, R.H.4    Bansal, R.5    Pfeiffer, S.E.6
  • 193
    • 0036983427 scopus 로고    scopus 로고
    • Immunocytological studies of L-MAG expression regulation during myelination of embryonic brain cell cocultures
    • Keita M, Magy L, Heape A, Richard L, Piaser M, Vallat JM (2002) Immunocytological studies of L-MAG expression regulation during myelination of embryonic brain cell cocultures. Dev Neurosci 24:495-503
    • (2002) Dev Neurosci , vol.24 , pp. 495-503
    • Keita, M.1    Magy, L.2    Heape, A.3    Richard, L.4    Piaser, M.5    Vallat, J.M.6
  • 194
    • 0013150219 scopus 로고    scopus 로고
    • Neural CAMS and their role in the development and organization of myelin sheaths
    • Bartsch U (2003) Neural CAMS and their role in the development and organization of myelin sheaths. Front Biosci 8:d477-d490
    • (2003) Front Biosci , vol.8
    • Bartsch, U.1
  • 197
    • 0031081587 scopus 로고    scopus 로고
    • Dying-back oligodendrogliopathy: A late sequel of myelin-associated glycoprotein deficiency
    • Lassmann H, Bartsch U, Montag D, Schachner M (1997) Dying-back oligodendrogliopathy: a late sequel of myelin-associated glycoprotein deficiency. Glia 19:104-110
    • (1997) Glia , vol.19 , pp. 104-110
    • Lassmann, H.1    Bartsch, U.2    Montag, D.3    Schachner, M.4
  • 198
    • 0028923245 scopus 로고
    • Crucial role for the myelin-associated glycoprotein in the maintenance of axon-myelin integrity
    • Fruttiger M, Montag D, Schachner M, Martini R (1995) Crucial role for the myelin-associated glycoprotein in the maintenance of axon-myelin integrity. Eur J NeuroSci 7:511-515
    • (1995) Eur J NeuroSci , vol.7 , pp. 511-515
    • Fruttiger, M.1    Montag, D.2    Schachner, M.3    Martini, R.4
  • 199
    • 5644259586 scopus 로고    scopus 로고
    • Comparison of myelin, axon, lipid, and immunopathology in the central nervous system of differentially myelin-compromised mutant mice: A morphological and biochemical study
    • Loers G, Aboul-Enein F, Bartsch U, Lassmann H, Schachner M (2004) Comparison of myelin, axon, lipid, and immunopathology in the central nervous system of differentially myelin-compromised mutant mice: a morphological and biochemical study. Mol Cell Neurosci 27:175-189
    • (2004) Mol Cell Neurosci , vol.27 , pp. 175-189
    • Loers, G.1    Aboul-Enein, F.2    Bartsch, U.3    Lassmann, H.4    Schachner, M.5
  • 200
    • 2442693021 scopus 로고    scopus 로고
    • Myelin-, reactive glia-, and scar-derived CNS axon growth inhibitors: Expression, receptor signaling, and correlation with axon regeneration
    • Sandvig A, Berry M, Barrett LB, Butt A, Logan A (2004) Myelin-, reactive glia-, and scar-derived CNS axon growth inhibitors: expression, receptor signaling, and correlation with axon regeneration. Glia 46:225-251
    • (2004) Glia , vol.46 , pp. 225-251
    • Sandvig, A.1    Berry, M.2    Barrett, L.B.3    Butt, A.4    Logan, A.5
  • 201
    • 0028075680 scopus 로고
    • Identification of myelin-associated glycoprotein as a major myelin-derived inhibitor of neurite growth
    • McKerracher L, David S, Jackson DL, Kottis V, Dunn RJ, Braun PE (1994) Identification of myelin-associated glycoprotein as a major myelin-derived inhibitor of neurite growth. Neuron 13:805-811
    • (1994) Neuron , vol.13 , pp. 805-811
    • McKerracher, L.1    David, S.2    Jackson, D.L.3    Kottis, V.4    Dunn, R.J.5    Braun, P.E.6
  • 202
    • 0028060651 scopus 로고
    • A novel role for myelin-associated glycoprotein as an inhibitor of axonal regeneration
    • Mukhopadhyay G, Doherty P, Walsh FS, Crocker PR, Filbin MT (1994) A novel role for myelin-associated glycoprotein as an inhibitor of axonal regeneration. Neuron 13:757-767
    • (1994) Neuron , vol.13 , pp. 757-767
    • Mukhopadhyay, G.1    Doherty, P.2    Walsh, F.S.3    Crocker, P.R.4    Filbin, M.T.5
  • 203
    • 33746308062 scopus 로고    scopus 로고
    • Glial inhibition of CNS axon regeneration
    • Yiu G, He Z (2006) Glial inhibition of CNS axon regeneration. Nat Rev Neurosci 7:617-627
    • (2006) Nat Rev Neurosci , vol.7 , pp. 617-627
    • Yiu, G.1    He, Z.2
  • 204
    • 0035827606 scopus 로고    scopus 로고
    • Myelin-associated glycoprotein interacts with ganglioside GT1b. A mechanism for neurite outgrowth inhibition
    • Vinson M, Strijbos PJ, Rowles A, Facci L, Moore SE, Simmons DL, Walsh FS (2001) Myelin-associated glycoprotein interacts with ganglioside GT1b. A mechanism for neurite outgrowth inhibition. J Biol Chem 276:20280-20285
    • (2001) J Biol Chem , vol.276 , pp. 20280-20285
    • Vinson, M.1    Strijbos, P.J.2    Rowles, A.3    Facci, L.4    Moore, S.E.5    Simmons, D.L.6    Walsh, F.S.7
  • 207
    • 0037119581 scopus 로고    scopus 로고
    • Myelin-associated glycoprotein as a functional ligand for the Nogo-66 receptor
    • Liu BP, Fournier A, GrandPre T, Strittmatter SM (2002) Myelin-associated glycoprotein as a functional ligand for the Nogo-66 receptor. Science 297:1190-1193
    • (2002) Science , vol.297 , pp. 1190-1193
    • Liu, B.P.1    Fournier, A.2    Grandpre, T.3    Strittmatter, S.M.4
  • 210
    • 34548190855 scopus 로고    scopus 로고
    • The inhibition site on myelin-associated glycoprotein is within Ig-domain 5 and is distinct from the sialic acid binding site
    • Cao Z, Qiu J, Domeniconi M, Hou J, Bryson JB, Mellado W, Filbin MT (2007) The inhibition site on myelin-associated glycoprotein is within Ig-domain 5 and is distinct from the sialic acid binding site. J Neurosci 27:9146-9154
    • (2007) J Neurosci , vol.27 , pp. 9146-9154
    • Cao, Z.1    Qiu, J.2    Domeniconi, M.3    Hou, J.4    Bryson, J.B.5    Mellado, W.6    Filbin, M.T.7
  • 211
    • 34948855519 scopus 로고    scopus 로고
    • Gangliosides and Nogo receptors independently mediate myelin-associated glycoprotein inhibition of neurite outgrowth in different nerve cells
    • Mehta NR, Lopez PH, Vyas AA, Schnaar RL (2007) Gangliosides and Nogo receptors independently mediate myelin-associated glycoprotein inhibition of neurite outgrowth in different nerve cells. J Biol Chem 282:27875-27886
    • (2007) J Biol Chem , vol.282 , pp. 27875-27886
    • Mehta, N.R.1    Lopez, P.H.2    Vyas, A.A.3    Schnaar, R.L.4
  • 212
    • 34248218509 scopus 로고    scopus 로고
    • Molecular dissection of the myelin-associated glycoprotein receptor complex reveals cell type-specific mechanisms for neurite outgrowth inhibition
    • Venkatesh K, Chivatakarn O, Sheu SS, Giger RJ (2007) Molecular dissection of the myelin-associated glycoprotein receptor complex reveals cell type-specific mechanisms for neurite outgrowth inhibition. J Cell Biol 177:393-399
    • (2007) J Cell Biol , vol.177 , pp. 393-399
    • Venkatesh, K.1    Chivatakarn, O.2    Sheu, S.S.3    Giger, R.J.4
  • 213
    • 18044377435 scopus 로고    scopus 로고
    • Roles of proteolysis and lipid rafts in the processing of the amyloid precursor protein and prion protein
    • Hooper NM (2005) Roles of proteolysis and lipid rafts in the processing of the amyloid precursor protein and prion protein. Biochem Soc Trans 33:335-338
    • (2005) Biochem Soc Trans , vol.33 , pp. 335-338
    • Hooper, N.M.1
  • 214
    • 15544379325 scopus 로고    scopus 로고
    • Aggregation and fibrillization of prions in lipid membranes
    • Kazlauskaite J, Pinheiro TJ (2005) Aggregation and fibrillization of prions in lipid membranes. Biochem Soc Symp 211-222
    • (2005) Biochem Soc Symp , pp. 211-222
    • Kazlauskaite, J.1    Pinheiro, T.J.2
  • 216
    • 2942687937 scopus 로고    scopus 로고
    • The cell biology of lysosomal storage disorders
    • Futerman AH, van Meer G (2004) The cell biology of lysosomal storage disorders. Nat Rev Mol Cell Biol 5:554-565
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 554-565
    • Futerman, A.H.1    Van Meer, G.2
  • 217
    • 33845343984 scopus 로고    scopus 로고
    • Sphingolipid metabolism diseases
    • Kolter T, Sandhoff K (2006) Sphingolipid metabolism diseases. Biochim Biophys Acta 1758:2057-2079
    • (2006) Biochim Biophys Acta , vol.1758 , pp. 2057-2079
    • Kolter, T.1    Sandhoff, K.2
  • 218
    • 51449114507 scopus 로고    scopus 로고
    • Lipid composition of microdomains is altered in a cell model of Gaucher disease
    • Hein LK, Duplock S, Hopwood JJ, Fuller M (2008) Lipid composition of microdomains is altered in a cell model of Gaucher disease. J Lipid Res 49:1725-1734
    • (2008) J Lipid Res , vol.49 , pp. 1725-1734
    • Hein, L.K.1    Duplock, S.2    Hopwood, J.J.3    Fuller, M.4
  • 222
    • 35248814255 scopus 로고    scopus 로고
    • The pathogenesis and treatment of acid sphingomyelinase-deficient Niemann-Pick disease
    • Schuchman EH (2007) The pathogenesis and treatment of acid sphingomyelinase-deficient Niemann-Pick disease. J Inherit Metab Dis 30:654-663
    • (2007) J Inherit Metab Dis , vol.30 , pp. 654-663
    • Schuchman, E.H.1
  • 225
    • 48549100652 scopus 로고    scopus 로고
    • Role of ganglioside metabolism in the pathogenesis of Alzheimer's disease\a review
    • Ariga T, McDonald MP, Yu RK (2008) Role of ganglioside metabolism in the pathogenesis of Alzheimer's disease\a review. J Lipid Res 49:1157-1175
    • (2008) J Lipid Res , vol.49 , pp. 1157-1175
    • Ariga, T.1    McDonald, M.P.2    Yu, R.K.3
  • 226
    • 0024794215 scopus 로고
    • Gangliosides in the brain in adult Down's syndrome and Alzheimer's disease
    • Brooksbank BW, McGovern J (1989) Gangliosides in the brain in adult Down's syndrome and Alzheimer's disease. Mol Chem Neuropathol 11:143-156
    • (1989) Mol Chem Neuropathol , vol.11 , pp. 143-156
    • Brooksbank, B.W.1    McGovern, J.2
  • 228
    • 0026279740 scopus 로고
    • Regional distribution of brain gangliosides in Alzheimer's disease
    • Kalanj S, Kracun I, Rosner H, Cosovic C (1991) Regional distribution of brain gangliosides in Alzheimer's disease. Neurol Croat 40:269-281
    • (1991) Neurol Croat , vol.40 , pp. 269-281
    • Kalanj, S.1    Kracun, I.2    Rosner, H.3    Cosovic, C.4
  • 231
    • 2542579484 scopus 로고    scopus 로고
    • Specificity and potential mechanism of sulfatide deficiency in Alzheimer's disease: An electrospray ionization mass spectrometric study
    • Cheng H, Xu J, McKeel DW Jr, Han X (2003) Specificity and potential mechanism of sulfatide deficiency in Alzheimer's disease: an electrospray ionization mass spectrometric study. Cell Mol Biol (Noisy-le-grand) 49:809-818
    • (2003) Cell Mol Biol (Noisy-le-grand) , vol.49 , pp. 809-818
    • Cheng, H.1    Xu, J.2    McKeel Jr., D.W.3    Han, X.4
  • 232
    • 0042526080 scopus 로고    scopus 로고
    • Gene therapy progress and prospects: Gene therapy of lysosomal storage disorders
    • Cheng SH, Smith AE (2003) Gene therapy progress and prospects: gene therapy of lysosomal storage disorders. Gene Ther 10:1275-1281
    • (2003) Gene Ther , vol.10 , pp. 1275-1281
    • Cheng, S.H.1    Smith, A.E.2
  • 234
    • 13244272410 scopus 로고    scopus 로고
    • Structural membrane alterations in Alzheimer brains found to be associated with regional disease development; Increased density of gangliosides GM1 and GM2 and loss of cholesterol in detergent-resistant membrane domains
    • Molander-Melin M, Blennow K, Bogdanovic N, Dellheden B, Mansson JE, Fredman P (2005) Structural membrane alterations in Alzheimer brains found to be associated with regional disease development; increased density of gangliosides GM1 and GM2 and loss of cholesterol in detergent-resistant membrane domains. J Neurochem 92:171-182
    • (2005) J Neurochem , vol.92 , pp. 171-182
    • Molander-Melin, M.1    Blennow, K.2    Bogdanovic, N.3    Dellheden, B.4    Mansson, J.E.5    Fredman, P.6
  • 235
    • 0023818883 scopus 로고
    • Antibodies to ganglioside GM1 in patients with Alzheimer's disease
    • Chapman J, Sela BA, Wertman E, Michaelson DM (1988) Antibodies to ganglioside GM1 in patients with Alzheimer's disease. Neurosci Lett 86:235-240
    • (1988) Neurosci Lett , vol.86 , pp. 235-240
    • Chapman, J.1    Sela, B.A.2    Wertman, E.3    Michaelson, D.M.4
  • 236
    • 33947577504 scopus 로고    scopus 로고
    • Gene expression alterations in the sphingolipid metabolism pathways during progression of dementia and Alzheimer's disease: A shift toward ceramide accumulation at the earliest recognizable stages of Alzheimer's diseasé
    • Katsel P, Li C, Haroutunian V (2007) Gene expression alterations in the sphingolipid metabolism pathways during progression of dementia and Alzheimer's disease: a shift toward ceramide accumulation at the earliest recognizable stages of Alzheimer's diseasé Neurochem Res 32:845-856
    • (2007) Neurochem Res , vol.32 , pp. 845-856
    • Katsel, P.1    Li, C.2    Haroutunian, V.3
  • 237
    • 0028176153 scopus 로고
    • Role of the beta-amyloid precursor protein in Alzheimer's disease
    • Ashall F, Goate AM (1994) Role of the beta-amyloid precursor protein in Alzheimer's disease. Trends Biochem Sci 19:42-46
    • (1994) Trends Biochem Sci , vol.19 , pp. 42-46
    • Ashall, F.1    Goate, A.M.2
  • 239
    • 0033103343 scopus 로고    scopus 로고
    • The amyloid precursor protein interacts with Go heterotrimeric protein within a cell compartment specialized in signal transduction
    • Brouillet E, Trembleau A, Galanaud D, Volovitch M, Bouillot C, Valenza C, Prochiantz A, Allinquant B (1999) The amyloid precursor protein interacts with Go heterotrimeric protein within a cell compartment specialized in signal transduction. J Neurosci 19:1717-1727
    • (1999) J Neurosci , vol.19 , pp. 1717-1727
    • Brouillet, E.1    Trembleau, A.2    Galanaud, D.3    Volovitch, M.4    Bouillot, C.5    Valenza, C.6    Prochiantz, A.7    Allinquant, B.8
  • 240
    • 0032562615 scopus 로고    scopus 로고
    • Caveolae, plasma membrane microdo-mains for alpha-secretase-mediated processing of the amyloid precursor protein
    • Ikezu T, Trapp BD, Song KS, Schlegel A, Lisanti MP, Okamoto T (1998) Caveolae, plasma membrane microdo-mains for alpha-secretase-mediated processing of the amyloid precursor protein. J Biol Chem 273:10485-10495
    • (1998) J Biol Chem , vol.273 , pp. 10485-10495
    • Ikezu, T.1    Trapp, B.D.2    Song, K.S.3    Schlegel, A.4    Lisanti, M.P.5    Okamoto, T.6
  • 243
    • 33645299023 scopus 로고    scopus 로고
    • The involvement of lipid rafts in Alzheimer's disease
    • Cordy JM, Hooper NM, Turner AJ (2006) The involvement of lipid rafts in Alzheimer's disease. Mol Membr Biol 23:111-122
    • (2006) Mol Membr Biol , vol.23 , pp. 111-122
    • Cordy, J.M.1    Hooper, N.M.2    Turner, A.J.3
  • 244
    • 15944371915 scopus 로고    scopus 로고
    • Cholesterol and Alzheimer's disease: Statins, cholesterol depletion in APP processing and Abeta generation
    • Hartman T (2005) Cholesterol and Alzheimer's disease: statins, cholesterol depletion in APP processing and Abeta generation. Subcell Biochem 38:365-380
    • (2005) Subcell Biochem , vol.38 , pp. 365-380
    • Hartman, T.1
  • 245
    • 6044221306 scopus 로고    scopus 로고
    • GM1 ganglioside regulates the proteolysis of amyloid precursor protein
    • Zha Q, Ruan Y, Hartmann T, Beyreuther K, Zhang D (2004) GM1 ganglioside regulates the proteolysis of amyloid precursor protein. Mol Psychiatry 9:946-952
    • (2004) Mol Psychiatry , vol.9 , pp. 946-952
    • Zha, Q.1    Ruan, Y.2    Hartmann, T.3    Beyreuther, K.4    Zhang, D.5
  • 246
    • 23044510465 scopus 로고    scopus 로고
    • Inhibition of glycosphingolipid biosynthesis reduces secretion of the beta-amyloid precursor protein and amyloid beta-peptide
    • Tamboli IY, Prager K, Barth E, Heneka M, Sandhoff K, Walter J (2005) Inhibition of glycosphingolipid biosynthesis reduces secretion of the beta-amyloid precursor protein and amyloid beta-peptide. J Biol Chem 280:28110-28117
    • (2005) J Biol Chem , vol.280 , pp. 28110-28117
    • Tamboli, I.Y.1    Prager, K.2    Barth, E.3    Heneka, M.4    Sandhoff, K.5    Walter, J.6
  • 248
    • 0037490159 scopus 로고    scopus 로고
    • Ceramide stabilizes beta-site amyloid precursor protein-cleaving enzyme 1 and promotes amyloid beta-peptide biogenesis
    • Puglielli L, Ellis BC, Saunders AJ, Kovacs DM (2003) Ceramide stabilizes beta-site amyloid precursor protein-cleaving enzyme 1 and promotes amyloid beta-peptide biogenesis. J Biol Chem 278:19777-19783
    • (2003) J Biol Chem , vol.278 , pp. 19777-19783
    • Puglielli, L.1    Ellis, B.C.2    Saunders, A.J.3    Kovacs, D.M.4
  • 249
    • 0037421206 scopus 로고    scopus 로고
    • Amyloidogenic processing of the Alzheimer beta-amyloid precursor protein depends on lipid rafts
    • Ehehalt R, Keller P, Haass C, Thiele C, Simons K (2003) Amyloidogenic processing of the Alzheimer beta-amyloid precursor protein depends on lipid rafts. J Cell Biol 160:113-123
    • (2003) J Cell Biol , vol.160 , pp. 113-123
    • Ehehalt, R.1    Keller, P.2    Haass, C.3    Thiele, C.4    Simons, K.5
  • 250
    • 33749467048 scopus 로고    scopus 로고
    • Amyloid beta oligomerization is induced by brain lipid rafts
    • Kim SI, Yi JS, Ko YG (2006) Amyloid beta oligomerization is induced by brain lipid rafts. J Cell Biochem 99:878-889
    • (2006) J Cell Biochem , vol.99 , pp. 878-889
    • Kim, S.I.1    Yi, J.S.2    Ko, Y.G.3
  • 252
    • 34547350809 scopus 로고    scopus 로고
    • Physicochemical interactions of amyloid beta-peptide with lipid bilayers
    • Matsuzaki K (2007) Physicochemical interactions of amyloid beta-peptide with lipid bilayers. Biochim Biophys Acta 1768:1935-1942
    • (2007) Biochim Biophys Acta , vol.1768 , pp. 1935-1942
    • Matsuzaki, K.1
  • 253
    • 0028982292 scopus 로고
    • Self-association of beta-amyloid peptide (1-40) in solution and binding to lipid membranes
    • Terzi E, Holzemann G, Seelig J (1995) Self-association of beta-amyloid peptide (1-40) in solution and binding to lipid membranes. J Mol Biol 252:633-642
    • (1995) J Mol Biol , vol.252 , pp. 633-642
    • Terzi, E.1    Holzemann, G.2    Seelig, J.3
  • 254
    • 0028885854 scopus 로고
    • GM1 ganglioside-bound amyloid beta-protein (A beta): A possible form of preamyloid in Alzheimer's disease
    • Yanagisawa K, Odaka A, Suzuki N, Ihara Y (1995) GM1 ganglioside-bound amyloid beta-protein (A beta): a possible form of preamyloid in Alzheimer's disease. Nat Med 1:1062-1066
    • (1995) Nat Med , vol.1 , pp. 1062-1066
    • Yanagisawa, K.1    Odaka, A.2    Suzuki, N.3    Ihara, Y.4
  • 255
    • 0031957080 scopus 로고    scopus 로고
    • GM1 ganglioside-bound amyloid beta-protein in Alzheimer's disease brain
    • Yanagisawa K, Ihara Y (1998) GM1 ganglioside-bound amyloid beta-protein in Alzheimer's disease brain. Neurobiol Aging 19: S65-S67
    • (1998) Neurobiol Aging , vol.19
    • Yanagisawa, K.1    Ihara, Y.2
  • 256
    • 0037062582 scopus 로고    scopus 로고
    • Interactions of amyloid beta-protein with various gangliosides in raft-like membranes: Importance of GM1 ganglioside-bound form as an endogenous seed for Alzheimer amyloid
    • Kakio A, Nishimoto S, Yanagisawa K, Kozutsumi Y, Matsuzaki K (2002) Interactions of amyloid beta-protein with various gangliosides in raft-like membranes: importance of GM1 ganglioside-bound form as an endogenous seed for Alzheimer amyloid. Biochemistry 41:7385-7390
    • (2002) Biochemistry , vol.41 , pp. 7385-7390
    • Kakio, A.1    Nishimoto, S.2    Yanagisawa, K.3    Kozutsumi, Y.4    Matsuzaki, K.5
  • 257
    • 72649096531 scopus 로고    scopus 로고
    • Up-and-down topological mode of amyloid beta-peptide lying on hydrophilic/hydrophobic interface of ganglioside clusters
    • Utsumi M, Yamaguchi Y, Sasakawa H, Yamamoto N, Yanagisawa K, Kato K (2008) Up-and-down topological mode of amyloid beta-peptide lying on hydrophilic/hydrophobic interface of ganglioside clusters. Glycoconj J 26:999-1006
    • (2008) Glycoconj J , vol.26 , pp. 999-1006
    • Utsumi, M.1    Yamaguchi, Y.2    Sasakawa, H.3    Yamamoto, N.4    Yanagisawa, K.5    Kato, K.6
  • 258
    • 13744255467 scopus 로고    scopus 로고
    • GM1 ganglioside-mediated accumulation of amyloid beta-protein on cell membranes
    • Wakabayashi M,Okada T, Kozutsumi Y, Matsuzaki K (2005) GM1 ganglioside-mediated accumulation of amyloid beta-protein on cell membranes. Biochem Biophys Res Commun 328:1019-1023
    • (2005) Biochem Biophys Res Commun , vol.328 , pp. 1019-1023
    • Wakabayashi Mokada, T.1    Kozutsumi, Y.2    Matsuzaki, K.3
  • 259
    • 34547152918 scopus 로고    scopus 로고
    • Role of gangliosides in Alzheimer's disease
    • Yanagisawa K (2007) Role of gangliosides in Alzheimer's disease. Biochim Biophys Acta 1768:1943-1951
    • (2007) Biochim Biophys Acta , vol.1768 , pp. 1943-1951
    • Yanagisawa, K.1
  • 261
    • 55749095544 scopus 로고    scopus 로고
    • Age-dependent high-density clustering of GM1 ganglioside at presynaptic neuritic terminals promotes amyloid beta-protein fibrillogenesis
    • Yamamoto N, Matsubara T, Sato T, Yanagisawa K (2008) Age-dependent high-density clustering of GM1 ganglioside at presynaptic neuritic terminals promotes amyloid beta-protein fibrillogenesis. Biochim Biophys Acta 1778:2717-2726
    • (2008) Biochim Biophys Acta , vol.1778 , pp. 2717-2726
    • Yamamoto, N.1    Matsubara, T.2    Sato, T.3    Yanagisawa, K.4
  • 263
    • 0030823756 scopus 로고    scopus 로고
    • Acceleration of amyloid fibril formation by specific binding of Abeta-(1-40) peptide to ganglioside-containing membrane vesicles
    • Choo-Smith LP, Garzon-Rodriguez W, Glabe CG, Surewicz WK (1997) Acceleration of amyloid fibril formation by specific binding of Abeta-(1-40) peptide to ganglioside-containing membrane vesicles. J Biol Chem 272:22987-22990
    • (1997) J Biol Chem , vol.272 , pp. 22987-22990
    • Choo-Smith, L.P.1    Garzon-Rodriguez, W.2    Glabe, C.G.3    Surewicz, W.K.4
  • 264
    • 0034968340 scopus 로고    scopus 로고
    • Neuropeptides interact with glycolipid receptors: A surface plasmon resonance study
    • Valdes-Gonzalez T, Inagawa J, Ido T (2001) Neuropeptides interact with glycolipid receptors: a surface plasmon resonance study. Peptides 22:1099-1106
    • (2001) Peptides , vol.22 , pp. 1099-1106
    • Valdes-Gonzalez, T.1    Inagawa, J.2    Ido, T.3
  • 265
    • 0035816709 scopus 로고    scopus 로고
    • Cholesterol-dependent formation of GM1 ganglioside-bound amyloid beta-protein, an endogenous seed for Alzheimer amyloid
    • Kakio A, Nishimoto SI, Yanagisawa K, Kozutsumi Y, Matsuzaki K (2001) Cholesterol-dependent formation of GM1 ganglioside-bound amyloid beta-protein, an endogenous seed for Alzheimer amyloid. J Biol Chem 276:24985-24990
    • (2001) J Biol Chem , vol.276 , pp. 24985-24990
    • Kakio, A.1    Nishimoto, S.I.2    Yanagisawa, K.3    Kozutsumi, Y.4    Matsuzaki, K.5
  • 267
    • 0037418767 scopus 로고    scopus 로고
    • Formation of a membrane-active form of amyloid beta-protein in raft-like model membranes
    • Kakio A, Nishimoto S, Kozutsumi Y, Matsuzaki K (2003) Formation of a membrane-active form of amyloid beta-protein in raft-like model membranes. Biochem Biophys Res Commun 303:514-518
    • (2003) Biochem Biophys Res Commun , vol.303 , pp. 514-518
    • Kakio, A.1    Nishimoto, S.2    Kozutsumi, Y.3    Matsuzaki, K.4
  • 268
    • 3042770433 scopus 로고    scopus 로고
    • Environment-and mutation-dependent aggregation behavior of Alzheimer amyloid beta-protein
    • Yamamoto N, Hasegawa K, Matsuzaki K, Naiki H, Yanagisawa K (2004) Environment-and mutation-dependent aggregation behavior of Alzheimer amyloid beta-protein. J Neurochem 90:62-69
    • (2004) J Neurochem , vol.90 , pp. 62-69
    • Yamamoto, N.1    Hasegawa, K.2    Matsuzaki, K.3    Naiki, H.4    Yanagisawa, K.5
  • 270
    • 28244452110 scopus 로고    scopus 로고
    • Cross-seeding of wild-type and hereditary variant-type amyloid beta-proteins in the presence of gangliosides
    • Yamamoto N, Matsuzaki K, Yanagisawa K (2005) Cross-seeding of wild-type and hereditary variant-type amyloid beta-proteins in the presence of gangliosides. J Neurochem 95:1167-1176
    • (2005) J Neurochem , vol.95 , pp. 1167-1176
    • Yamamoto, N.1    Matsuzaki, K.2    Yanagisawa, K.3
  • 271
    • 25144505865 scopus 로고    scopus 로고
    • Suppression of Abeta deposition in brain by peripheral administration of Fab fragments of anti-seed antibody
    • Yamamoto N, Yokoseki T, Shibata M, Yamaguchi H, Yanagisawa K (2005) Suppression of Abeta deposition in brain by peripheral administration of Fab fragments of anti-seed antibody. Biochem Biophys Res Commun 335:45-47
    • (2005) Biochem Biophys Res Commun , vol.335 , pp. 45-47
    • Yamamoto, N.1    Yokoseki, T.2    Shibata, M.3    Yamaguchi, H.4    Yanagisawa, K.5
  • 273
    • 35148816608 scopus 로고    scopus 로고
    • Endosomal accumulation of GM1 ganglioside-bound amyloid beta-protein in neurons of aged monkey brains
    • Kimura N, Yanagisawa K (2007) Endosomal accumulation of GM1 ganglioside-bound amyloid beta-protein in neurons of aged monkey brains. NeuroReport 18:1669-1673
    • (2007) NeuroReport , vol.18 , pp. 1669-1673
    • Kimura, N.1    Yanagisawa, K.2
  • 275
    • 33745543727 scopus 로고    scopus 로고
    • Neurotrophic enhancers as therapy for behavioral deficits in rodent models of Huntington's disease: Use of gangliosides, substituted pyrimidines, and mesenchymal stem cells
    • Dunbar GL, Sandstrom MI, Rossignol J, Lescaudron L (2006) Neurotrophic enhancers as therapy for behavioral deficits in rodent models of Huntington's disease: use of gangliosides, substituted pyrimidines, and mesenchymal stem cells. Behav Cogn Neurosci Rev 5:63-79
    • (2006) Behav Cogn Neurosci Rev , vol.5 , pp. 63-79
    • Dunbar, G.L.1    Sandstrom, M.I.2    Rossignol, J.3    Lescaudron, L.4
  • 276
    • 0017839485 scopus 로고
    • Juvenile Huntington chorea: Clinical, ultrastructural, and biochemical studies
    • Goebel HH, Heipertz R, Scholz W, Iqbal K, Tellez-Nagel I (1978) Juvenile Huntington chorea: clinical, ultrastructural, and biochemical studies. Neurology 28:23-31
    • (1978) Neurology , vol.28 , pp. 23-31
    • Goebel, H.H.1    Heipertz, R.2    Scholz, W.3    Iqbal, K.4    Tellez-Nagel, I.5
  • 277
    • 0017714497 scopus 로고
    • The fatty acid composition of sphingomyelin from adult human cerebral white matter and changes in childhood, senium and unspecific brain damage
    • Heipertz R, Pilz H, Scholz W (1977) The fatty acid composition of sphingomyelin from adult human cerebral white matter and changes in childhood, senium and unspecific brain damage. J Neurol 216:57-65
    • (1977) J Neurol , vol.216 , pp. 57-65
    • Heipertz, R.1    Pilz, H.2    Scholz, W.3
  • 278
    • 0014518683 scopus 로고
    • Erythrocyte glycolipids in Huntington's chorea
    • Wherrett JR, Brown BL (1969) Erythrocyte glycolipids in Huntington's chorea. Neurology 19:489-493
    • (1969) Neurology , vol.19 , pp. 489-493
    • Wherrett, J.R.1    Brown, B.L.2
  • 279
    • 0019410942 scopus 로고
    • Striatal ganglioside levels in the rat following kainic acid lesions: Comparison with Huntington's disease
    • Higatsberger MR, Sperk G, Bernheimer H, Shannak KS, Hornykiewicz O (1981) Striatal ganglioside levels in the rat following kainic acid lesions: comparison with Huntington's disease. Exp Brain Res 44:93-96
    • (1981) Exp Brain Res , vol.44 , pp. 93-96
    • Higatsberger, M.R.1    Sperk, G.2    Bernheimer, H.3    Shannak, K.S.4    Hornykiewicz, O.5
  • 282
  • 286
    • 33847022701 scopus 로고    scopus 로고
    • GM1 specifically interacts with alpha-synuclein and inhibits fibrillation
    • Martinez Z, Zhu M, Han S, Fink AL (2007) GM1 specifically interacts with alpha-synuclein and inhibits fibrillation. Biochemistry 46:1868-1877
    • (2007) Biochemistry , vol.46 , pp. 1868-1877
    • Martinez, Z.1    Zhu, M.2    Han, S.3    Fink, A.L.4
  • 287
    • 67449123312 scopus 로고    scopus 로고
    • On the mechanism of internalization of alpha-synuclein into microglia: Roles of ganglioside GM1 and lipid raft
    • Park JY, Kim KS, Lee SB, Ryu JS, Chung KC, Choo YK, Jou I, Kim J, Park SM (2009) On the mechanism of internalization of alpha-synuclein into microglia: roles of ganglioside GM1 and lipid raft. J Neurochem 110:400-411
    • (2009) J Neurochem , vol.110 , pp. 400-411
    • Park, J.Y.1    Kim, K.S.2    Lee, S.B.3    Ryu, J.S.4    Chung, K.C.5    Choo, Y.K.6    Jou, I.7    Kim, J.8    Park, S.M.9
  • 288
    • 0036544646 scopus 로고    scopus 로고
    • Trisialoganglioside GT1b induces in vivo degeneration of nigral dopaminergic neurons: Role of microglia
    • Ryu JK, Shin WH, Kim J, Joe EH, Lee YB, Cho KG, Oh YJ, Kim SU, Jin BK (2002) Trisialoganglioside GT1b induces in vivo degeneration of nigral dopaminergic neurons: role of microglia. Glia 38:15-23
    • (2002) Glia , vol.38 , pp. 15-23
    • Ryu, J.K.1    Shin, W.H.2    Kim, J.3    Joe, E.H.4    Lee, Y.B.5    Cho, K.G.6    Oh, Y.J.7    Kim, S.U.8    Jin, B.K.9
  • 289
    • 0030822582 scopus 로고    scopus 로고
    • Prion diseases and the BSE crisis
    • Prusiner SB (1997) Prion diseases and the BSE crisis. Science 278:245-251
    • (1997) Science , vol.278 , pp. 245-251
    • Prusiner, S.B.1
  • 290
    • 0031843985 scopus 로고    scopus 로고
    • Prion rods contain small amounts of two host sphingolipids as revealed by thin-layer chromatography and mass spectrometry
    • Klein TR, Kirsch D, Kaufmann R, Riesner D (1998) Prion rods contain small amounts of two host sphingolipids as revealed by thin-layer chromatography and mass spectrometry. Biol Chem 379:655-666
    • (1998) Biol Chem , vol.379 , pp. 655-666
    • Klein, T.R.1    Kirsch, D.2    Kaufmann, R.3    Riesner, D.4
  • 292
    • 0036306046 scopus 로고    scopus 로고
    • Binding of prion protein to lipid membranes and implications for prion conversion
    • Sanghera N, Pinheiro TJ (2002) Binding of prion protein to lipid membranes and implications for prion conversion. J Mol Biol 315:1241-1256
    • (2002) J Mol Biol , vol.315 , pp. 1241-1256
    • Sanghera, N.1    Pinheiro, T.J.2
  • 293
    • 68949114443 scopus 로고    scopus 로고
    • Effects of lipid composition and phase on the membrane interaction of the prion peptide 106-126 amide
    • Zhong J, Yang C, Zheng W, Huang L, Hong Y, Wang L, Sha Y (2009) Effects of lipid composition and phase on the membrane interaction of the prion peptide 106-126 amide. Biophys J 96:4610-4621
    • (2009) Biophys J , vol.96 , pp. 4610-4621
    • Zhong, J.1    Yang, C.2    Zheng, W.3    Huang, L.4    Hong, Y.5    Wang, L.6    Sha, Y.7
  • 294
    • 33847738814 scopus 로고    scopus 로고
    • Lipid rafts: Structure, function and role in HIV, Alzheimer's and prion diseases
    • Fantini J, Garmy N, Mahfoud R, Yahi N (2002) Lipid rafts: structure, function and role in HIV, Alzheimer's and prion diseases. Expert Rev Mol Med 4:1-22
    • (2002) Expert Rev Mol Med , vol.4 , pp. 1-22
    • Fantini, J.1    Garmy, N.2    Mahfoud, R.3    Yahi, N.4
  • 295
    • 0030964917 scopus 로고    scopus 로고
    • COOH-terminal sequence of the cellular prion protein directs subcellular trafficking and controls conversion into the scrapie isoform
    • Kaneko K, Vey M, Scott M, Pilkuhn S, Cohen FE, Prusiner SB (1997) COOH-terminal sequence of the cellular prion protein directs subcellular trafficking and controls conversion into the scrapie isoform. Proc Natl Acad Sci USA 94:2333-2338
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 2333-2338
    • Kaneko, K.1    Vey, M.2    Scott, M.3    Pilkuhn, S.4    Cohen, F.E.5    Prusiner, S.B.6
  • 296
    • 0026780714 scopus 로고
    • Glycosylinositol phospholipid anchors of the scrapie and cellular prion proteins contain sialic acid
    • Stahl N, Baldwin MA, Hecker R, Pan KM, Burlingame AL, Prusiner SB (1992) Glycosylinositol phospholipid anchors of the scrapie and cellular prion proteins contain sialic acid. Biochemistry 31:5043-5053
    • (1992) Biochemistry , vol.31 , pp. 5043-5053
    • Stahl, N.1    Baldwin, M.A.2    Hecker, R.3    Pan, K.M.4    Burlingame, A.L.5    Prusiner, S.B.6
  • 297
    • 0028966735 scopus 로고
    • Cholesterol depletion and modification of COOH-terminal targeting sequence of the prion protein inhibit formation of the scrapie isoform
    • Taraboulos A, Scott M, Semenov A, Avrahami D, Laszlo L, Prusiner SB (1995) Cholesterol depletion and modification of COOH-terminal targeting sequence of the prion protein inhibit formation of the scrapie isoform. J Cell Biol 129:121-132
    • (1995) J Cell Biol , vol.129 , pp. 121-132
    • Taraboulos, A.1    Scott, M.2    Semenov, A.3    Avrahami, D.4    Laszlo, L.5    Prusiner, S.B.6
  • 298
    • 0036500554 scopus 로고    scopus 로고
    • Conversion of raft associated prion protein to the protease-resistant state requires insertion of PrP-res (PrP(Sc)) into contiguous membranes
    • Baron GS, Wehrly K, Dorward DW, Chesebro B, Caughey B (2002) Conversion of raft associated prion protein to the protease-resistant state requires insertion of PrP-res (PrP(Sc)) into contiguous membranes. Embo J 21:1031-1040
    • (2002) Embo J , vol.21 , pp. 1031-1040
    • Baron, G.S.1    Wehrly, K.2    Dorward, D.W.3    Chesebro, B.4    Caughey, B.5
  • 299
    • 0033793094 scopus 로고    scopus 로고
    • The cellular prion protein colocalizes with the dystroglycan complex in the brain
    • Keshet GI, Bar-Peled O, Yaffe D, Nudel U, Gabizon R (2000) The cellular prion protein colocalizes with the dystroglycan complex in the brain. J Neurochem 75:1889-1897
    • (2000) J Neurochem , vol.75 , pp. 1889-1897
    • Keshet, G.I.1    Bar-Peled, O.2    Yaffe, D.3    Nudel, U.4    Gabizon, R.5
  • 300
    • 27644593331 scopus 로고    scopus 로고
    • The membrane environment of endogenous cellular prion protein in primary rat cerebellar neurons
    • Loberto N, Prioni S, Bettiga A, Chigorno V, Prinetti A, Sonnino S (2005) The membrane environment of endogenous cellular prion protein in primary rat cerebellar neurons. J Neurochem 95:771-783
    • (2005) J Neurochem , vol.95 , pp. 771-783
    • Loberto, N.1    Prioni, S.2    Bettiga, A.3    Chigorno, V.4    Prinetti, A.5    Sonnino, S.6
  • 301
    • 36248945111 scopus 로고    scopus 로고
    • Reorganization of prion protein membrane environment during low potassium-induced apoptosis in primary rat cerebellar neurons
    • Rivaroli A, Prioni S, Loberto N, Bettiga A, Chigorno V, Prinetti A, Sonnino S (2007) Reorganization of prion protein membrane environment during low potassium-induced apoptosis in primary rat cerebellar neurons. J Neurochem 103:1954-1967
    • (2007) J Neurochem , vol.103 , pp. 1954-1967
    • Rivaroli, A.1    Prioni, S.2    Loberto, N.3    Bettiga, A.4    Chigorno, V.5    Prinetti, A.6    Sonnino, S.7
  • 302
    • 0021712039 scopus 로고
    • Alterations in brain gangliosides and other lipids of patients with Creutzfeldt-Jakob disease and subacute sclerosing panencephalitis (SSPE
    • Ando S, Toyoda Y, Nagai Y, Ikuta F (1984) Alterations in brain gangliosides and other lipids of patients with Creutzfeldt-Jakob disease and subacute sclerosing panencephalitis (SSPE). Jpn J Exp Med 54:229-234
    • (1984) Jpn J Exp Med , vol.54 , pp. 229-234
    • Ando, S.1    Toyoda, Y.2    Nagai, Y.3    Ikuta, F.4
  • 303
    • 0030512374 scopus 로고    scopus 로고
    • Ganglioside alterations in the central and peripheral nervous systems of patients with Creutzfeldt-Jakob disease
    • Ohtani Y, Tamai Y, Ohnuki Y, Miura S (1996) Ganglioside alterations in the central and peripheral nervous systems of patients with Creutzfeldt-Jakob disease. Neurodegeneration 5:331-338
    • (1996) Neurodegeneration , vol.5 , pp. 331-338
    • Ohtani, Y.1    Tamai, Y.2    Ohnuki, Y.3    Miura, S.4
  • 304
    • 0018305226 scopus 로고
    • Creutzfeldt-Jakob disease\alteration in ganglioside sphingosine in the brain of a patient
    • Tamai Y, Ohtani Y, Miura S, Narita Y, Iwata T, Kaiya H, Namba M (1979) Creutzfeldt-Jakob disease\alteration in ganglioside sphingosine in the brain of a patient. Neurosci Lett 11:81-86
    • (1979) Neurosci Lett , vol.11 , pp. 81-86
    • Tamai, Y.1    Ohtani, Y.2    Miura, S.3    Narita, Y.4    Iwata, T.5    Kaiya, H.6    Namba, M.7
  • 305
    • 0015978662 scopus 로고
    • Ganglioside changes in slow virus diseases: Analyses of chimpanzee brains infected with kuru and Creutzfeldt-Jakob agents
    • Yu RK, Ledeen RW, Gajdusek DC, Gibbs CJ (1974) Ganglioside changes in slow virus diseases: analyses of chimpanzee brains infected with kuru and Creutzfeldt-Jakob agents. Brain Res 70:103-112
    • (1974) Brain Res , vol.70 , pp. 103-112
    • Yu, R.K.1    Ledeen, R.W.2    Gajdusek, D.C.3    Gibbs, C.J.4
  • 306
    • 0017927888 scopus 로고
    • Ganglioside alterations in guinea pig brains at end stages of experimental Creutzfeldt-Jakob disease
    • Yu RK, Manuelidis EE (1978) Ganglioside alterations in guinea pig brains at end stages of experimental Creutzfeldt-Jakob disease. J Neurol Sci 35:15-23
    • (1978) J Neurol Sci , vol.35 , pp. 15-23
    • Yu, R.K.1    Manuelidis, E.E.2
  • 307
    • 0027194795 scopus 로고
    • Ganglioside composition changes in spongiform encephalopathies: Analyses of 263K scrapie-infected hamster brains
    • Di Martino A, Safar J, Callegaro L, Salem N Jr, Gibbs CJ Jr (1993) Ganglioside composition changes in spongiform encephalopathies: analyses of 263K scrapie-infected hamster brains. Neurochem Res 18:907-913
    • (1993) Neurochem Res , vol.18 , pp. 907-913
    • Di Martino, A.1    Safar, J.2    Callegaro, L.3    Salem Jr., N.4    Gibbs Jr., G.J.5
  • 310
    • 0027296130 scopus 로고
    • Low levels of CSF gangliotetraose-series gangliosides in West syndrome: Implication of brain maturation disturbance
    • Izumi T, Ogawa T, Koizumi H, Fukuyama Y (1993) Low levels of CSF gangliotetraose-series gangliosides in West syndrome: implication of brain maturation disturbance. Pediatr Neurol 9:293-296
    • (1993) Pediatr Neurol , vol.9 , pp. 293-296
    • Izumi, T.1    Ogawa, T.2    Koizumi, H.3    Fukuyama, Y.4
  • 311
    • 0016779388 scopus 로고
    • Possible role of gangliosides in epilepsy: Effects of epileptic seizures on cerebral gangliosides
    • Yu RK, Glaser GH (1975) Possible role of gangliosides in epilepsy: effects of epileptic seizures on cerebral gangliosides. Trans Am Neurol Assoc 100:261-263
    • (1975) Trans Am Neurol Assoc , vol.100 , pp. 261-263
    • Yu, R.K.1    Glaser, G.H.2
  • 312
    • 0023104860 scopus 로고
    • Ganglioside changes associated with temporal lobe epilepsy in the human hippocampus
    • Yu RK, Holley JA, Macala LJ, Spencer DD (1987) Ganglioside changes associated with temporal lobe epilepsy in the human hippocampus. Yale J Biol Med 60:107-117
    • (1987) Yale J Biol Med , vol.60 , pp. 107-117
    • Yu, R.K.1    Holley, J.A.2    MacAla, L.J.3    Spencer, D.D.4
  • 314
    • 27144547245 scopus 로고    scopus 로고
    • Exogenous gangliosides, neuronal plasticity and repair, and the neurotrophins
    • Mocchetti I (2005) Exogenous gangliosides, neuronal plasticity and repair, and the neurotrophins. Cell Mol Life Sci 62:2283-2294
    • (2005) Cell Mol Life Sci , vol.62 , pp. 2283-2294
    • Mocchetti, I.1
  • 315
    • 33746099710 scopus 로고    scopus 로고
    • The synthetic ceramide analog L-PDMP partially protects striatal dopamine levels but does not promote dopamine neuron survival in murine models of parkinsonism
    • Schneider JS, Bradbury KA, Anada Y, Inokuchi J, Anderson DW (2006) The synthetic ceramide analog L-PDMP partially protects striatal dopamine levels but does not promote dopamine neuron survival in murine models of parkinsonism. Brain Res 1099:199-205
    • (2006) Brain Res , vol.1099 , pp. 199-205
    • Schneider, J.S.1    Bradbury, K.A.2    Anada, Y.3    Inokuchi, J.4    Anderson, D.W.5
  • 316
    • 67650088127 scopus 로고    scopus 로고
    • Neurotrophic and neuroprotective actions of an enhancer of ganglioside biosynthesis
    • Inokuchi J (2009) Neurotrophic and neuroprotective actions of an enhancer of ganglioside biosynthesis. Int Rev Neurobiol 85:319-336
    • (2009) Int Rev Neurobiol , vol.85 , pp. 319-336
    • Inokuchi, J.1
  • 317
    • 0242270777 scopus 로고    scopus 로고
    • Gene transfer strategies for correction of lysosomal storage disorders
    • D'Azzo A (2003) Gene transfer strategies for correction of lysosomal storage disorders. Acta Haematol 110:71-85
    • (2003) Acta Haematol , vol.110 , pp. 71-85
    • D'Azzo, A.1
  • 319
    • 0037097043 scopus 로고    scopus 로고
    • Correction of mucopolysaccharidosis type IIIb fibroblasts by lentiviral vector-mediated gene transfer
    • Villani GR, Follenzi A, Vanacore B, Di Domenico C, Naldini L, Di Natale P (2002) Correction of mucopolysaccharidosis type IIIb fibroblasts by lentiviral vector-mediated gene transfer. Biochem J 364:747-753
    • (2002) Biochem J , vol.364 , pp. 747-753
    • Villani, G.R.1    Follenzi, A.2    Vanacore, B.3    Di Domenico, C.4    Naldini, L.5    Di Natale, P.6
  • 320
    • 0036895451 scopus 로고    scopus 로고
    • Enzyme replacement and enhancement therapies: Lessons from lysosomal disorders
    • Desnick RJ, Schuchman EH (2002) Enzyme replacement and enhancement therapies: lessons from lysosomal disorders. Nat Rev Genet 3:954-966
    • (2002) Nat Rev Genet , vol.3 , pp. 954-966
    • Desnick, R.J.1    Schuchman, E.H.2
  • 322
    • 0242524418 scopus 로고    scopus 로고
    • Enzyme therapy for lysosomal storage disease: Principles, practice, and prospects
    • Grabowski GA, Hopkin RJ (2003) Enzyme therapy for lysosomal storage disease: principles, practice, and prospects. Annu Rev Genomics Hum Genet 4:403-436
    • (2003) Annu Rev Genomics Hum Genet , vol.4 , pp. 403-436
    • Grabowski, G.A.1    Hopkin, R.J.2
  • 323
    • 0347093304 scopus 로고    scopus 로고
    • Mannose 6-phosphate receptor-mediated uptake is defective in acid sphingomyelinase-deficient macrophages: Implications for Niemann-Pick disease enzyme replacement therapy
    • Dhami R, Schuchman EH (2004) Mannose 6-phosphate receptor-mediated uptake is defective in acid sphingomyelinase-deficient macrophages: implications for Niemann-Pick disease enzyme replacement therapy. J Biol Chem 279:1526-1532
    • (2004) J Biol Chem , vol.279 , pp. 1526-1532
    • Dhami, R.1    Schuchman, E.H.2
  • 324
    • 0037180511 scopus 로고    scopus 로고
    • Chemical chaperones increase the cellular activity of N370S beta-glucosidase: A therapeutic strategy for Gaucher disease
    • Sawkar AR, Cheng WC, Beutler E, Wong CH, Balch WE, Kelly JW (2002) Chemical chaperones increase the cellular activity of N370S beta-glucosidase: a therapeutic strategy for Gaucher disease. Proc Natl Acad Sci USA 99:15428-15433
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 15428-15433
    • Sawkar, A.R.1    Cheng, W.C.2    Beutler, E.3    Wong, C.H.4    Balch, W.E.5    Kelly, J.W.6
  • 325
    • 0038206527 scopus 로고    scopus 로고
    • Miglustat Oxford glycosciences/actelion
    • Lachmann RH (2003) Miglustat. Oxford glycosciences/actelion. Curr Opin Investig Drugs 4:472-479
    • (2003) Curr Opin Investig Drugs , vol.4 , pp. 472-479
    • Lachmann, R.H.1
  • 328
    • 34547753513 scopus 로고    scopus 로고
    • Miglustat for treatment of Niemann-Pick C disease: A randomised controlled study
    • Patterson MC, Vecchio D, Prady H, Abel L, Wraith JE (2007) Miglustat for treatment of Niemann-Pick C disease: a randomised controlled study. Lancet Neurol 6:765-772
    • (2007) Lancet Neurol , vol.6 , pp. 765-772
    • Patterson, M.C.1    Vecchio, D.2    Prady, H.3    Abel, L.4    Wraith, J.E.5


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