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Volumn 21, Issue 3-4, 2004, Pages 97-110

A glycosynapse in myelin?

Author keywords

galactosylceramide; lipid rafts; oligodendrocytes; signaling; sulfatide

Indexed keywords

ALBUMIN; ANTIBODY; GALACTOSE; GALACTOSYLCERAMIDE; GALACTOSYLCERAMIDE SULFATE; LIPOSOME; MEMBRANE PROTEIN; MYELIN; PHOSPHOTRANSFERASE; UNCLASSIFIED DRUG;

EID: 6044233339     PISSN: 02820080     EISSN: None     Source Type: Journal    
DOI: 10.1023/B:GLYC.0000044842.34958.f8     Document Type: Review
Times cited : (42)

References (145)
  • 1
    • 0001918961 scopus 로고
    • Ultrastructural study of remyelination in an experimental lesion in adult cat spinal cord
    • Bunge MB, Bunge RP, Ris H, Ultrastructural study of remyelination in an experimental lesion in adult cat spinal cord, J Biophys Biochem Cytol 10, 67-94 (1961).
    • (1961) J Biophys Biochem Cytol , vol.10 , pp. 67-94
    • Bunge, M.B.1    Bunge, R.P.2    Ris, H.3
  • 2
    • 0002279596 scopus 로고
    • Isolation and characterization of myelin
    • edited by Morell P (Plenum Press, New York)
    • Norton WT, Isolation and characterization of myelin. In Myelin, edited by Morell P (Plenum Press, New York, 1977), pp. 161-99.
    • (1977) Myelin , pp. 161-199
    • Norton, W.T.1
  • 3
    • 0023840428 scopus 로고
    • Membrane interactions in nerve myelin: II. Determination of surface charge from biochemical data
    • Inouye H, Kirschner DA, Membrane interactions in nerve myelin: II. Determination of surface charge from biochemical data, Biophys J 53, 247-60 (1988).
    • (1988) Biophys J , vol.53 , pp. 247-260
    • Inouye, H.1    Kirschner, D.A.2
  • 4
    • 0018398036 scopus 로고
    • Sulphated glycoglycerolipids in rat brain: Decrease and disappearance after developmental age
    • Ishizuka I, Inomata M, Sulphated glycoglycerolipids in rat brain: Decrease and disappearance after developmental age, J Neurochem 33, 387-8 (1979).
    • (1979) J Neurochem , vol.33 , pp. 387-388
    • Ishizuka, I.1    Inomata, M.2
  • 5
    • 0023761355 scopus 로고
    • Lipid synthesis by oligodendrocytes from adult pig brain maintained in long-term culture
    • Burgisser P, Althaus H-H, Rohmann A, Neuhoff V, Lipid synthesis by oligodendrocytes from adult pig brain maintained in long-term culture, Neurochem Int 13, 111-8 (1988).
    • (1988) Neurochem Int , vol.13 , pp. 111-118
    • Burgisser, P.1    Althaus, H.-H.2    Rohmann, A.3    Neuhoff, V.4
  • 6
    • 0021270684 scopus 로고
    • Changes in monogalactosyl diacylglycerols, alkylgalactolipids, and cerebroside fatty acid esters in maturing brain measured by high-performance liquid chromatography
    • Shimomura K, Kishimoto Y, Changes in monogalactosyl diacylglycerols, alkylgalactolipids, and cerebroside fatty acid esters in maturing brain measured by high-performance liquid chromatography, Biochim Biophys Acta 794, 162-4 (1984).
    • (1984) Biochim Biophys Acta , vol.794 , pp. 162-164
    • Shimomura, K.1    Kishimoto, Y.2
  • 7
    • 0017746927 scopus 로고
    • The association of the sulphogalactosylglycerolipid of rat brain with myelination
    • Pieringer J, Rao GS, Mandel P, Pieringer RA, The association of the sulphogalactosylglycerolipid of rat brain with myelination, Biochem J 166, 421-8 (1977).
    • (1977) Biochem J , vol.166 , pp. 421-428
    • Pieringer, J.1    Rao, G.S.2    Mandel, P.3    Pieringer, R.A.4
  • 8
    • 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, Suzuki K, Popko B, Myelination in the absence of galactocerebroside and sulfatide: Normal structure with abnormal function and regional instability, Cell 86, 209-19 (1996).
    • (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    Suzuki, K.7    Popko, B.8
  • 9
    • 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, 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, 13280-5 (1996).
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 13280-13285
    • Bosio, A.1    Binczek, E.2    Stoffel, W.3
  • 10
    • 0033552610 scopus 로고    scopus 로고
    • Axo-glial interactions regulate the localization of axonal paranodal proteins
    • Dupree JL, Girault J-A, Popko B. Axo-glial interactions regulate the localization of axonal paranodal proteins, J Cell Biol 147, 1145-51 (1999).
    • (1999) J Cell Biol , vol.147 , pp. 1145-1151
    • Dupree, J.L.1    Girault, J.-A.2    Popko, B.3
  • 11
    • 0027986675 scopus 로고
    • Disruption of the compacted myelin sheath of axons of the central nervous system in proteolipid protein-deficient mice
    • Boison D, Stoffel W, Disruption of the compacted myelin sheath of axons of the central nervous system in proteolipid protein-deficient mice, Proc Nad Acad Sci USA 91, 11709-13 (1994).
    • (1994) Proc Nad Acad Sci USA , vol.91 , pp. 11709-11713
    • Boison, D.1    Stoffel, W.2
  • 14
    • 0036703477 scopus 로고    scopus 로고
    • A myelin galactolipid, sulfatide, is essential for maintenance of ion channels on myelinated axon but not essential for initial cluster formation
    • Ishibashi T, Dupree JL, Ikenaka K, Hirahara Y, Honke K, Peles E, Popko B, Suzuki K, Nishino H, Baba H, A myelin galactolipid, sulfatide, is essential for maintenance of ion channels on myelinated axon but not essential for initial cluster formation, J Neurosci 22, 6507-14 (2002).
    • (2002) J Neurosci , vol.22 , pp. 6507-6514
    • Ishibashi, T.1    Dupree, J.L.2    Ikenaka, K.3    Hirahara, Y.4    Honke, K.5    Peles, E.6    Popko, B.7    Suzuki, K.8    Nishino, H.9    Baba, H.10
  • 15
    • 0035478027 scopus 로고    scopus 로고
    • Localization of Caspr2 in myelinated nerves depends on axon-glia interactions and the generation of barriers along the axon
    • Poliak S, Gollan L, Salomon D, Berglund EO, Ohara R, Ranscht B, Peles E, Localization of Caspr2 in myelinated nerves depends on axon-glia interactions and the generation of barriers along the axon, J Neurosci 21, 7568-75 (2001).
    • (2001) J Neurosci , vol.21 , pp. 7568-7575
    • Poliak, S.1    Gollan, L.2    Salomon, D.3    Berglund, E.O.4    Ohara, R.5    Ranscht, B.6    Peles, E.7
  • 16
    • 0037017404 scopus 로고    scopus 로고
    • Myelin-associated glycoprotein and myelin galactolipids stabilize developing axo-glial interactions
    • Marcus J, Dupree JE, Popko B, Myelin-associated glycoprotein and myelin galactolipids stabilize developing axo-glial interactions, J Cell Biol 156, 567-77 (2002).
    • (2002) J Cell Biol , vol.156 , pp. 567-577
    • Marcus, J.1    Dupree, J.E.2    Popko, B.3
  • 17
    • 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, Sulfatide is a negative regulator of oligodendrocyte differentiation: Development in sulfatide-null mice, Glia 45, 269-77 (2004).
    • (2004) Glia , vol.45 , pp. 269-277
    • Hirahara, Y.1    Bansal, R.2    Honke, K.3    Ikenaka, K.4    Wada, Y.5
  • 18
    • 0022349073 scopus 로고
    • Lipid composition of the nervous system of earthworms (Lumbricus terrestris)
    • Okamura N, Stoskopf M, Yamaguchi H, Kishimoto Y, Lipid composition of the nervous system of earthworms (Lumbricus terrestris), J Neurochem 45, 1875-9 (1985).
    • (1985) J Neurochem , vol.45 , pp. 1875-1879
    • Okamura, N.1    Stoskopf, M.2    Yamaguchi, H.3    Kishimoto, Y.4
  • 19
    • 0023050990 scopus 로고
    • Phylogenetic development of myelin glycosphingolipids
    • Kishimoto Y, Phylogenetic development of myelin glycosphingolipids, Chem Phys Lipids 42, 117-28 (1986).
    • (1986) Chem Phys Lipids , vol.42 , pp. 117-128
    • Kishimoto, Y.1
  • 21
    • 6044232819 scopus 로고
    • Phylogenetic aspects of myelin structure
    • edited by Jeserich G, Althaus HH, Waehneldt TV (Springer-Verlag, Berlin)
    • Inouye H, Kirschner DA, Phylogenetic aspects of myelin structure. In Cellular and Molecular Biology of Myelination, edited by Jeserich G, Althaus HH, Waehneldt TV (Springer-Verlag, Berlin, 1990), pp. 376-87.
    • (1990) Cellular and Molecular Biology of Myelination , pp. 376-387
    • Inouye, H.1    Kirschner, D.A.2
  • 22
    • 0017123934 scopus 로고
    • Variation in myelin lipid composition induced by change in environmental temperature of goldfish (Carassius aurattus L.)
    • Selivonchick DP, Roots BI, Variation in myelin lipid composition induced by change in environmental temperature of goldfish (Carassius aurattus L.), J Thermal Biol 1, 131-5 (1976).
    • (1976) J Thermal Biol , vol.1 , pp. 131-135
    • Selivonchick, D.P.1    Roots, B.I.2
  • 24
    • 0026782306 scopus 로고
    • Characteristic distribution of glycolipids in gadoid fish nerve tissues and its bearing on phylogeny
    • Tamai Y, Kojima H, Saito S, Takayama-Abe K, Horichi H, Characteristic distribution of glycolipids in gadoid fish nerve tissues and its bearing on phylogeny, J Lipid Res 33, 1351-9 (1992).
    • (1992) J Lipid Res , vol.33 , pp. 1351-1359
    • Tamai, Y.1    Kojima, H.2    Saito, S.3    Takayama-Abe, K.4    Horichi, H.5
  • 25
    • 0027639941 scopus 로고
    • Caveolae: Where incoming and outgoing messengers meet
    • Anderson RG, Caveolae: Where incoming and outgoing messengers meet, Curr Opin Cell Biol 5, 647-52 (1993).
    • (1993) Curr Opin Cell Biol , vol.5 , pp. 647-652
    • Anderson, R.G.1
  • 27
    • 0034531102 scopus 로고    scopus 로고
    • Functional roles of glycosphingolipids in signal transduction via lipid rafts
    • Kasahara K, Sanai Y, Functional roles of glycosphingolipids in signal transduction via lipid rafts, Glycoconj J 17, 153-62 (2000).
    • (2000) Glycoconj J , vol.17 , pp. 153-162
    • Kasahara, K.1    Sanai, Y.2
  • 28
    • 0034531095 scopus 로고    scopus 로고
    • Signaling through sphingolipid microdomains of the plasma membrane: The concept of signaling platform
    • Hoessli DC, Ilangumaran S, Soltermann A, Robinson PJ, Borisch B, and Ud-Din N, Signaling through sphingolipid microdomains of the plasma membrane: The concept of signaling platform, Glycoconj J 17, 191-7 (2000).
    • (2000) Glycoconj J , vol.17 , pp. 191-197
    • Hoessli, D.C.1    Ilangumaran, S.2    Soltermann, A.3    Robinson, P.J.4    Borisch, B.5    Ud-Din, N.6
  • 29
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons K, Ikonen E, Functional rafts in cell membranes, Nature 387, 569-72 (1997).
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 30
    • 0345255951 scopus 로고    scopus 로고
    • The myelin-axolemmal complex: Biochemical dissection and the role of galactosphingolipids
    • Menon K, Rasband MN, Taylor CM, Brophy P, Bansal R, Pfeiffer SE, The myelin-axolemmal complex: Biochemical dissection and the role of galactosphingolipids, J Neurochem 87, 995-1009 (2003).
    • (2003) J Neurochem , vol.87 , pp. 995-1009
    • Menon, K.1    Rasband, M.N.2    Taylor, C.M.3    Brophy, P.4    Bansal, R.5    Pfeiffer, S.E.6
  • 32
    • 0035920114 scopus 로고    scopus 로고
    • Suppression of integrin expression and tumorigenicity by sulfation of lactosylceramide in 3LL Lewis lung carcinoma cells
    • Kabayama K, Ito N, Honke K, Igarashi Y, Inokuchi J-I, Suppression of integrin expression and tumorigenicity by sulfation of lactosylceramide in 3LL Lewis lung carcinoma cells, J Biol Chem 276, 26777-83 (2001).
    • (2001) J Biol Chem , vol.276 , pp. 26777-26783
    • Kabayama, K.1    Ito, N.2    Honke, K.3    Igarashi, Y.4    Inokuchi, J.-I.5
  • 33
    • 0033842398 scopus 로고    scopus 로고
    • Kidney lipids in galactosylceramide synthase-deficient mice: Absence of galactosylsulfatide and compensatory increase in more polar sulfoglycolipids
    • Tadano-Aritomi K, Hikita T, Fujimoto H, Suzuki K, Motegi K, Ishizuka I, Kidney lipids in galactosylceramide synthase-deficient mice: Absence of galactosylsulfatide and compensatory increase in more polar sulfoglycolipids, J Lip Res 41, 1237-43 (2000).
    • (2000) J Lip Res , vol.41 , pp. 1237-1243
    • Tadano-Aritomi, K.1    Hikita, T.2    Fujimoto, H.3    Suzuki, K.4    Motegi, K.5    Ishizuka, I.6
  • 34
    • 0027933127 scopus 로고
    • Sulfatides trigger increase of cytosolic free calcium and enhanced expression of TNF-i and IL-8 mRNA in human neutrophils. Evidence for a role of L-selectin as a signaling molecule
    • Laudana C, Constantin G, Baron P, Scarpini E, Scarlato G, Cabrini G, Dechecchi C, Rossi F, Cassatella MA, Berton G, Sulfatides trigger increase of cytosolic free calcium and enhanced expression of TNF-i and IL-8 mRNA in human neutrophils. Evidence for a role of L-selectin as a signaling molecule, J Biol Chem 269, 4021-6 (1994).
    • (1994) J Biol Chem , vol.269 , pp. 4021-4026
    • Laudana, C.1    Constantin, G.2    Baron, P.3    Scarpini, E.4    Scarlato, G.5    Cabrini, G.6    Dechecchi, C.7    Rossi, F.8    Cassatella, M.A.9    Berton, G.10
  • 36
    • 0023161223 scopus 로고
    • Sulfatide-binding proteins
    • Roberts DD, Sulfatide-binding proteins, Methods Enzymol 138, 473-83 (1987).
    • (1987) Methods Enzymol , vol.138 , pp. 473-483
    • Roberts, D.D.1
  • 37
    • 0030919911 scopus 로고    scopus 로고
    • Tenascin-R is an intrinsic autocrine factor for oligodendrocyte differentiation and promotes cell adhesion by a sulfatide-mediated mechanism
    • Pesheva P, Gloor S, Schachner M, Probstmeier R, Tenascin-R is an intrinsic autocrine factor for oligodendrocyte differentiation and promotes cell adhesion by a sulfatide-mediated mechanism, J Neurosci 17, 4642-51 (1997).
    • (1997) J Neurosci , vol.17 , pp. 4642-4651
    • Pesheva, P.1    Gloor, S.2    Schachner, M.3    Probstmeier, R.4
  • 38
    • 0026487041 scopus 로고
    • Specific binding of cytotactin to sulfated glycolipids
    • Crossin KL, Edelman GM, Specific binding of cytotactin to sulfated glycolipids, J Neurosci Res 33, 631-8 (1992).
    • (1992) J Neurosci Res , vol.33 , pp. 631-638
    • Crossin, K.L.1    Edelman, G.M.2
  • 39
    • 0035957230 scopus 로고    scopus 로고
    • Hsp70s contain a specific sulfogalactolipid binding site. Differential aglycone influence on sulfogalactosyl ceramide binding by recombinant prokaryotic and eukaryotic hsp70 family members
    • Mamelak D, Mylvaganam M, Whetstone H, Hartmann E, Lennarz W, Wyrick PB, Raulston J, Han H, Hoffman P, Lingwood CA, Hsp70s contain a specific sulfogalactolipid binding site. Differential aglycone influence on sulfogalactosyl ceramide binding by recombinant prokaryotic and eukaryotic hsp70 family members, Biochemistry 40, 3572-82 (2001).
    • (2001) Biochemistry , vol.40 , pp. 3572-3582
    • Mamelak, D.1    Mylvaganam, M.2    Whetstone, H.3    Hartmann, E.4    Lennarz, W.5    Wyrick, P.B.6    Raulston, J.7    Han, H.8    Hoffman, P.9    Lingwood, C.A.10
  • 40
    • 0000823149 scopus 로고
    • Salt-mediated interactions between vesicles of the thylakoid lipid digalactosyldiacylglycerol
    • Webb MS, Tilcock CPS, Green BR, Salt-mediated interactions between vesicles of the thylakoid lipid digalactosyldiacylglycerol, Biochim Biophys Acta 938, 323-33 (1988).
    • (1988) Biochim Biophys Acta , vol.938 , pp. 323-333
    • Webb, M.S.1    Tilcock, C.P.S.2    Green, B.R.3
  • 41
    • 0024378959 scopus 로고
    • Specific interaction between gangliotriaosylceramide (Gg3) and sialosyllactosylceramide (GM3) as a basis for specific cellular recognition between lymphoma and melanoma cells
    • Kojima N, Hakomori SJ, Specific interaction between gangliotriaosylceramide (Gg3) and sialosyllactosylceramide (GM3) as a basis for specific cellular recognition between lymphoma and melanoma cells, J Biol Chem 264, 20159-62 (1989).
    • (1989) J Biol Chem , vol.264 , pp. 20159-20162
    • Kojima, N.1    Hakomori, S.J.2
  • 42
    • 0024474715 scopus 로고
    • x determinants. A possible basis for cell recognition in preimplantation embryos and in embryonal carcinoma cells
    • x determinants. A possible basis for cell recognition in preimplantation embryos and in embryonal carcinoma cells, J Biol Chem 264, 9467-84 (1989).
    • (1989) J Biol Chem , vol.264 , pp. 9467-9484
    • Eggens, I.1    Fenderson, B.2    Toyokuni, T.3    Dean, B.4    Stroud, M.5    Hakomori, S.6
  • 43
    • 0025945830 scopus 로고
    • Cell adhesion, spreading, and motility of GM3-expressing cells based on glycolipid-glycolipid interaction
    • Kojima N, Hakomori S, Cell adhesion, spreading, and motility of GM3-expressing cells based on glycolipid-glycolipid interaction, J Biol Chem 266, 17552-8 (1991).
    • (1991) J Biol Chem , vol.266 , pp. 17552-17558
    • Kojima, N.1    Hakomori, S.2
  • 44
    • 0026788506 scopus 로고
    • Cell adhesion in a dynamic flow system as compared to static system. Glycosphingolipid-glycosphingolipid interaction in the dynamic system predominate over lectin- or integrin-based mechanisms in adhesion of B16 melanoma cells to non-activated endothelial cells
    • Kojima N, Shiota M, Sadahira Y, Handa K, Hakomori S, Cell adhesion in a dynamic flow system as compared to static system. Glycosphingolipid- glycosphingolipid interaction in the dynamic system predominate over lectin- or integrin-based mechanisms in adhesion of B16 melanoma cells to non-activated endothelial cells, J Biol Chem 267, 17264-70 (1992).
    • (1992) J Biol Chem , vol.267 , pp. 17264-17270
    • Kojima, N.1    Shiota, M.2    Sadahira, Y.3    Handa, K.4    Hakomori, S.5
  • 45
    • 0000147431 scopus 로고
    • Carbohydrate-carbohydrate interaction as an initial step in cell recognition
    • Hakomori S, Carbohydrate-carbohydrate interaction as an initial step in cell recognition, Pure Appl Chem 63, 473-82 (1991).
    • (1991) Pure Appl Chem , vol.63 , pp. 473-482
    • Hakomori, S.1
  • 46
    • 0028095587 scopus 로고
    • Carbohydrates in cellular recognition: From leucine-zipper to sugar-zipper?
    • Spillmann D, Carbohydrates in cellular recognition: From leucine-zipper to sugar-zipper? Glycoconj J 11, 169-71 (1994).
    • (1994) Glycoconj J , vol.11 , pp. 169-171
    • Spillmann, D.1
  • 47
    • 0002436277 scopus 로고    scopus 로고
    • Carbohydrate-carbohydrate interaction
    • edited by Gabius H-J, Gabius S (Chapman and Hall, Weinheim)
    • Bovin NV, Carbohydrate-carbohydrate interaction, in Glycosciences: Status and Perspectives, edited by Gabius H-J, Gabius S (Chapman and Hall, Weinheim, 1997) pp. 277-89.
    • (1997) Glycosciences: Status and Perspectives , pp. 277-289
    • Bovin, N.V.1
  • 48
    • 0016793191 scopus 로고
    • Calcium-carbohydrate bridges composed of uncharged sugars. Structure of a hydrated calcium bromide complex of α-fucose
    • Cook WJ, Bugg, CE, Calcium-carbohydrate bridges composed of uncharged sugars. Structure of a hydrated calcium bromide complex of α-fucose, Biochim Biophys Acta 389, 428-35 (1975).
    • (1975) Biochim Biophys Acta , vol.389 , pp. 428-435
    • Cook, W.J.1    Bugg, C.E.2
  • 49
    • 0032502032 scopus 로고    scopus 로고
    • Molecular forces between membranes displaying neutral glycosphingolipids: Evidence for carbohydrate attraction
    • Yu ZW, Calvert TL, Leckband D, Molecular forces between membranes displaying neutral glycosphingolipids: Evidence for carbohydrate attraction, Biochemistry 37, 1540-50 (1998).
    • (1998) Biochemistry , vol.37 , pp. 1540-1550
    • Yu, Z.W.1    Calvert, T.L.2    Leckband, D.3
  • 52
    • 0028949325 scopus 로고
    • Binding strength between cell adhesion proteoglycans measured by atomic force microscopy
    • Dammer U, Popescu O, Wagner P, Anselmetti D, Guntherodt H-J, Misevic GN, Binding strength between cell adhesion proteoglycans measured by atomic force microscopy, Science 267, 1173-5 (1995).
    • (1995) Science , vol.267 , pp. 1173-1175
    • Dammer, U.1    Popescu, O.2    Wagner, P.3    Anselmetti, D.4    Guntherodt, H.-J.5    Misevic, G.N.6
  • 53
    • 0034596320 scopus 로고    scopus 로고
    • A quantitative estimation of carbohydrate-carbohydrate interaction using clustered oligosaccharides of glycolipid monolayers and of artificial glycoconjugate polymers by surface plasmon resonance
    • Matsuura K, Kitakouji H, Sawada N, Ishida H, Kiso M, Kitajima K, Kobayashi K, A quantitative estimation of carbohydrate-carbohydrate interaction using clustered oligosaccharides of glycolipid monolayers and of artificial glycoconjugate polymers by surface plasmon resonance, J Am Chem Soc 122, 7406-7 (2000).
    • (2000) J Am Chem Soc , vol.122 , pp. 7406-7407
    • Matsuura, K.1    Kitakouji, H.2    Sawada, N.3    Ishida, H.4    Kiso, M.5    Kitajima, K.6    Kobayashi, K.7
  • 55
    • 0037414924 scopus 로고    scopus 로고
    • Probing specificity in carbohydrate-carbohydrate interactions with micelles and Langmuir monolayers
    • Santacroce PV, Basu A, Probing specificity in carbohydrate-carbohydrate interactions with micelles and Langmuir monolayers, Angew Chem Int Ed 42, 95-8 (2003).
    • (2003) Angew Chem Int Ed , vol.42 , pp. 95-98
    • Santacroce, P.V.1    Basu, A.2
  • 56
    • 0032579279 scopus 로고    scopus 로고
    • Globoside-dependent adhesion of human embryonal carcinoma cells, based on carbohydrate-carbohydrate interaction, initiates signal transduction and induces enhanced activity of transcription factors AP1 and CREB
    • Song Y, Withers DA, Hakomori S, Globoside-dependent adhesion of human embryonal carcinoma cells, based on carbohydrate-carbohydrate interaction, initiates signal transduction and induces enhanced activity of transcription factors AP1 and CREB, J Biol Chem 273, 2517-25 (1998).
    • (1998) J Biol Chem , vol.273 , pp. 2517-2525
    • Song, Y.1    Withers, D.A.2    Hakomori, S.3
  • 57
    • 0027368866 scopus 로고
    • The carbohydrate-carbohydrate interaction between galactosylceramide- containing liposomes and cerebroside sulfate-containing liposomes: Dependence on the glycolipid ceramide composition
    • Stewart RJ, Boggs, JM, The carbohydrate-carbohydrate interaction between galactosylceramide-containing liposomes and cerebroside sulfate-containing liposomes: Dependence on the glycolipid ceramide composition, Biochemistry 32, 10666-74 (1993).
    • (1993) Biochemistry , vol.32 , pp. 10666-10674
    • Stewart, R.J.1    Boggs, J.M.2
  • 58
    • 0034038067 scopus 로고    scopus 로고
    • Trans interaction between galactosylceramide and cerebroside sulfate across apposed bilayers
    • Boggs JM, Menikh A, Rangaraj G, Trans interaction between galactosylceramide and cerebroside sulfate across apposed bilayers, Biophys J 78, 874-85 (2000).
    • (2000) Biophys J , vol.78 , pp. 874-885
    • Boggs, J.M.1    Menikh, A.2    Rangaraj, G.3
  • 59
    • 0030058606 scopus 로고    scopus 로고
    • 3 sulfate by electrospray ionization mass spectrometry
    • 3 sulfate by electrospray ionization mass spectrometry, J Biol Chem 271, 3496-9 (1996).
    • (1996) J Biol Chem , vol.271 , pp. 3496-3499
    • Koshy, I.C.A.1    Boggs, J.M.2
  • 60
    • 0032975041 scopus 로고    scopus 로고
    • Divalent-cation mediated interaction between cerebroside sulfate and cerebrosides: An investigation of the effect of structural variations of lipids by electrospray ionization mass spectrometry
    • Koshy KM, Wang J, Boggs JM, Divalent-cation mediated interaction between cerebroside sulfate and cerebrosides: An investigation of the effect of structural variations of lipids by electrospray ionization mass spectrometry, Biophys J 77, 306-18 (1999).
    • (1999) Biophys J , vol.77 , pp. 306-318
    • Koshy, K.M.1    Wang, J.2    Boggs, J.M.3
  • 61
    • 0032975218 scopus 로고    scopus 로고
    • Modulation of nanotube formation by structural modifications of sphingolipids
    • Kulkarni VS, Boggs JM, RE Brown, Modulation of nanotube formation by structural modifications of sphingolipids, Biophys J 77, 319-30 (1999).
    • (1999) Biophys J , vol.77 , pp. 319-330
    • Kulkarni, V.S.1    Boggs, J.M.2    Brown, R.E.3
  • 63
    • 0027568112 scopus 로고
    • Novel oligodendrocyte transmembrane signaling systems
    • Dyer CA, Novel oligodendrocyte transmembrane signaling systems, Mol Neurobiol 7, 1-22 (1993).
    • (1993) Mol Neurobiol , vol.7 , pp. 1-22
    • Dyer, C.A.1
  • 65
    • 0026352248 scopus 로고
    • GPI-anchored cell-surface molecules complexed to protein tyrosine kinases
    • Stefanova I, Horejsi V, Ansotegui IJ, Knapp W, Stockinger H, GPI-anchored cell-surface molecules complexed to protein tyrosine kinases, Science 254, 1016-9 (1991).
    • (1991) Science , vol.254 , pp. 1016-1019
    • Stefanova, I.1    Horejsi, V.2    Ansotegui, I.J.3    Knapp, W.4    Stockinger, H.5
  • 67
    • 0029798012 scopus 로고    scopus 로고
    • R24 anti-GD3 ganglioside antibody can induce costimulation and prevent the induction of alloantigen-specific T cell clonal anergy
    • Boussiotis VA, Pardo NA, Collins H, Houghton A, Ritz J, Nadler LM, Soiffer RJ, R24 anti-GD3 ganglioside antibody can induce costimulation and prevent the induction of alloantigen-specific T cell clonal anergy, Eur J Immunol 26, 2149-54 (1996).
    • (1996) Eur J Immunol , vol.26 , pp. 2149-2154
    • Boussiotis, V.A.1    Pardo, N.A.2    Collins, H.3    Houghton, A.4    Ritz, J.5    Nadler, L.M.6    Soiffer, R.J.7
  • 68
    • 0030664824 scopus 로고    scopus 로고
    • Association of Src family tyrosine kinase Lyn with ganglioside GD3 in rat brain
    • Kasahara K, Watanabe Y, Yamamoto T, Sanai Y, Association of Src family tyrosine kinase Lyn with ganglioside GD3 in rat brain, J Biol Chem 272, 29947-53 (1997).
    • (1997) J Biol Chem , vol.272 , pp. 29947-29953
    • Kasahara, K.1    Watanabe, Y.2    Yamamoto, T.3    Sanai, Y.4
  • 69
    • 0032502722 scopus 로고    scopus 로고
    • GMS-enriched microdomain involved in cell adhesion and signal transduction through carbohydrate-carbohydrate interaction in mouse melanoma B16 cells
    • Iwabuchi K, Yamamura S, Prinetti A, Handa K, Hakomori, S, GMS-enriched microdomain involved in cell adhesion and signal transduction through carbohydrate-carbohydrate interaction in mouse melanoma B16 cells, J Biol Chem 273, 9130-8 (1998).
    • (1998) J Biol Chem , vol.273 , pp. 9130-9138
    • Iwabuchi, K.1    Yamamura, S.2    Prinetti, A.3    Handa, K.4    Hakomori, S.5
  • 70
    • 0032509356 scopus 로고    scopus 로고
    • Separation of "glycosphingolipid signaling domain" from caveolin-containing membrane fraction in mouse melanoma B16 cells and its role in cell adhesion coupled with signaling
    • Iwabuchi K, Handa K, Hakomori S, Separation of "glycosphingolipid signaling domain" from caveolin-containing membrane fraction in mouse melanoma B16 cells and its role in cell adhesion coupled with signaling, J Biol Chem 273, 33766-73 (1998).
    • (1998) J Biol Chem , vol.273 , pp. 33766-33773
    • Iwabuchi, K.1    Handa, K.2    Hakomori, S.3
  • 71
    • 0033597907 scopus 로고    scopus 로고
    • Glycosphingolipid-enriched signaling domain in mouse neuroblastoma neuro2a cells
    • Prinetti A, Iwabuchi K, Hakomori S, Glycosphingolipid-enriched signaling domain in mouse neuroblastoma neuro2a cells, J Biol Chem 274, 20916-24 (1999).
    • (1999) J Biol Chem , vol.274 , pp. 20916-20924
    • Prinetti, A.1    Iwabuchi, K.2    Hakomori, S.3
  • 72
    • 0034528032 scopus 로고    scopus 로고
    • Cell adhesion/recognition and signal transduction through glycosphingolipid microdomain
    • Hakomori S, Cell adhesion/recognition and signal transduction through glycosphingolipid microdomain, Glycoconj J 17, 143-51 (2000).
    • (2000) Glycoconj J , vol.17 , pp. 143-151
    • Hakomori, S.1
  • 74
    • 0037201965 scopus 로고    scopus 로고
    • Glycosphingolipid-dependent cross-talk between glycosynapses interfacing tumor cells with their host cells: Essential basis to define tumor malignancy
    • Hakomoi S, Handa K, Glycosphingolipid-dependent cross-talk between glycosynapses interfacing tumor cells with their host cells: Essential basis to define tumor malignancy, FEBS Lett 531, 88-92 (2002).
    • (2002) FEBS Lett , vol.531 , pp. 88-92
    • Hakomoi, S.1    Handa, K.2
  • 75
    • 0024458998 scopus 로고
    • Myelin membrane structure and composition correlated: A phylogenetic study
    • Kirschner DA, Inouye H, Ganser AL, Mann V, Myelin membrane structure and composition correlated: a phylogenetic study, J Neurochem 53, 1599-609 (1989).
    • (1989) J Neurochem , vol.53 , pp. 1599-1609
    • Kirschner, D.A.1    Inouye, H.2    Ganser, A.L.3    Mann, V.4
  • 76
    • 0346422375 scopus 로고    scopus 로고
    • Lipid bilayers: Thermodynamics, structure, fluctuations, and interactions
    • Tristram-Nagle S, Nagle JF, Lipid bilayers: Thermodynamics, structure, fluctuations, and interactions, Chem Phys Lipids 127, 3-14 (2004).
    • (2004) Chem Phys Lipids , vol.127 , pp. 3-14
    • Tristram-Nagle, S.1    Nagle, J.F.2
  • 77
    • 0344053287 scopus 로고    scopus 로고
    • Oligodendrocytes direct glycosyl phosphatidylinositol-anchored proteins to the myelin sheath in glycosphingolipid-rich complexes
    • Kramer E-M, Koch T, Niehaus A, Trotter J, Oligodendrocytes direct glycosyl phosphatidylinositol-anchored proteins to the myelin sheath in glycosphingolipid-rich complexes, J Biol Chem 272, 8937-45 (1997).
    • (1997) J Biol Chem , vol.272 , pp. 8937-8945
    • Kramer, E.-M.1    Koch, T.2    Niehaus, A.3    Trotter, J.4
  • 78
    • 0038933866 scopus 로고    scopus 로고
    • Compartmentation of fyn kinase with glycosylphosphatidylinositolanchored molecules in oligodendrocytes facilitates kinase activation during myelination
    • Kramer E-M, Klein C, Koch T, Boytinck M, Trotter J, Compartmentation of fyn kinase with glycosylphosphatidylinositolanchored molecules in oligodendrocytes facilitates kinase activation during myelination, J Biol Chem 274, 29042-9 (1999).
    • (1999) J Biol Chem , vol.274 , pp. 29042-29049
    • Kramer, E.-M.1    Klein, C.2    Koch, T.3    Boytinck, M.4    Trotter, J.5
  • 79
    • 0034597142 scopus 로고    scopus 로고
    • Assembly of myelin by association of proteolipid protein with cholesteroland galactosylceramide-rich membrane domains
    • Simons M, Kramer EM, Thiele C, Stoffel W, Trotter J, Assembly of myelin by association of proteolipid protein with cholesteroland galactosylceramide- rich membrane domains, J Cell Biol 151, 143-54 (2000).
    • (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
  • 80
    • 1442274918 scopus 로고    scopus 로고
    • Membrane-associated estrogen receptor and caveolin-1 are present in central nervous system myelin and oligodendrocyte plasma membranes
    • Arvanitis DN, Wang H, Bagshaw RD, Callahan JW, Boggs JM, Membrane-associated estrogen receptor and caveolin-1 are present in central nervous system myelin and oligodendrocyte plasma membranes, J Neurosci Res 75, 603-13 (2004).
    • (2004) J Neurosci Res , vol.75 , pp. 603-613
    • Arvanitis, D.N.1    Wang, H.2    Bagshaw, R.D.3    Callahan, J.W.4    Boggs, J.M.5
  • 81
    • 0025601960 scopus 로고
    • Glycolipids and transmembrane signaling in oligodendroglia
    • Benjamins JA, Dyer CA, Glycolipids and transmembrane signaling in oligodendroglia, Annals NY Acad Sci 605, 90-100 (1990).
    • (1990) Annals NY Acad Sci , vol.605 , pp. 90-100
    • Benjamins, J.A.1    Dyer, C.A.2
  • 82
    • 0024231989 scopus 로고
    • Stimulation of oligodendrocyte differentiation in culture by growth in the presence of a monoclonal antibody to sulfated glycolipid
    • Bansal R, Gard AL, Pfeiffer SE, Stimulation of oligodendrocyte differentiation in culture by growth in the presence of a monoclonal antibody to sulfated glycolipid, J Neurosci Res 21, 260-7 (1988).
    • (1988) J Neurosci Res , vol.21 , pp. 260-267
    • Bansal, R.1    Gard, A.L.2    Pfeiffer, S.E.3
  • 83
    • 0005830431 scopus 로고
    • Reversible inhibition of oligodendrocyte progenitor differentiation by a monoclonal antibody against surface galactolipids
    • Bansal R, Pfeiffer SE, Reversible inhibition of oligodendrocyte progenitor differentiation by a monoclonal antibody against surface galactolipids, Proc Natl Acad Sci USA 86, 6181-5 (1989).
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 6181-6185
    • Bansal, R.1    Pfeiffer, S.E.2
  • 84
    • 0028545219 scopus 로고
    • Regulation of gene expression in mature oligodendrocytes by the specialized myelin-like membrane environment: Antibody perturbation in culture with the monoclonal antibody R-mAb
    • Bansal R, Pfeiffer SE, Regulation of gene expression in mature oligodendrocytes by the specialized myelin-like membrane environment: Antibody perturbation in culture with the monoclonal antibody R-mAb, Glia 12, 173-9 (1994).
    • (1994) Glia , vol.12 , pp. 173-179
    • Bansal, R.1    Pfeiffer, S.E.2
  • 85
    • 0026350796 scopus 로고
    • Galactocerebroside and sulfatide independently mediate Ca responses in oligodendrocytes
    • Dyer CA, Benjamins JA, Galactocerebroside and sulfatide independently mediate Ca responses in oligodendrocytes, J Neurosci Res 30, 699-711 (1991).
    • (1991) J Neurosci Res , vol.30 , pp. 699-711
    • Dyer, C.A.1    Benjamins, J.A.2
  • 86
    • 0028129521 scopus 로고
    • Billings-Gagliardi S, MBP mediates extracellular signals that regulate microtubule stability in oligodendrocyte membrane sheets
    • Dyer CA, Philibotte TM, Wolf MK, Billings-Gagliardi S, MBP mediates extracellular signals that regulate microtubule stability in oligodendrocyte membrane sheets, J Neurosci Res 39, 97-107 (1994).
    • (1994) J Neurosci Res , vol.39 , pp. 97-107
    • Dyer, C.A.1    Philibotte, T.M.2    Wolf, M.K.3
  • 87
    • 0030861428 scopus 로고    scopus 로고
    • Regulation of cytoskeleton by myelin components: Studies on Shiverer oligodendrocytes carrying an MBP transgene
    • Dyer CA, Philibotte T, Wolf MK, Billings-Gagliardi S, Regulation of cytoskeleton by myelin components: Studies on Shiverer oligodendrocytes carrying an MBP transgene, Dev Neurosci 19, 395-409 (1997).
    • (1997) Dev Neurosci , vol.19 , pp. 395-409
    • Dyer, C.A.1    Philibotte, T.2    Wolf, M.K.3    Billings-Gagliardi, S.4
  • 88
    • 0024841022 scopus 로고
    • Multiple and novel specificities of monoclonal Abs 01, 04, and R-mAb used in the analysis of oligodendrocyte development
    • Bansal R, Warrington AE, Gard AE, Ranscht B, Pfeiffer SE, Multiple and novel specificities of monoclonal Abs 01, 04, and R-mAb used in the analysis of oligodendrocyte development, J Neurosci Res 24, 548-57 (1989).
    • (1989) J Neurosci Res , vol.24 , pp. 548-557
    • Bansal, R.1    Warrington, A.E.2    Gard, A.E.3    Ranscht, B.4    Pfeiffer, S.E.5
  • 89
    • 0033568843 scopus 로고    scopus 로고
    • Negative regulation of oligodendrocyte differentiation by galactosphingolipids
    • Bansal R, Winkler S, Bheddah S, Negative regulation of oligodendrocyte differentiation by galactosphingolipids, J Neurosci 19, 7913-24 (1999).
    • (1999) J Neurosci , vol.19 , pp. 7913-7924
    • Bansal, R.1    Winkler, S.2    Bheddah, S.3
  • 90
    • 0023410731 scopus 로고
    • Inhibition of in vitro peripheral myelin formation by monoclonal anti-galactocerebroside
    • Ranscht B, Wood PM, Bunge RP, Inhibition of in vitro peripheral myelin formation by monoclonal anti-galactocerebroside, J Neurosci 7, 2936-47 (1987).
    • (1987) J Neurosci , vol.7 , pp. 2936-2947
    • Ranscht, B.1    Wood, P.M.2    Bunge, R.P.3
  • 91
    • 0035888265 scopus 로고    scopus 로고
    • Effect of liposomes containing cerebroside and cerebroside sulfate on cytoskeleton of cultured oligodendro-cytes
    • Boggs JM, Wang H, Effect of liposomes containing cerebroside and cerebroside sulfate on cytoskeleton of cultured oligodendro-cytes, J Neurosci Res 66, 242-53 (2001).
    • (2001) J Neurosci Res , vol.66 , pp. 242-253
    • Boggs, J.M.1    Wang, H.2
  • 92
    • 2342446570 scopus 로고    scopus 로고
    • Co-clustering of galactosylceramide and membrane proteins in oligodendrocyte membranes on interaction with polyvalent carbohydrate and prevention by an intact cytoskeleton
    • Boggs JM, Wang H, Co-clustering of galactosylceramide and membrane proteins in oligodendrocyte membranes on interaction with polyvalent carbohydrate and prevention by an intact cytoskeleton, J Neurosci Res 76, 342-55 (2004).
    • (2004) J Neurosci Res , vol.76 , pp. 342-355
    • Boggs, J.M.1    Wang, H.2
  • 93
    • 0017744736 scopus 로고
    • Immune reactivities of antibodies against glycolipids. I. Properties of anti-galactocerebroside antibodies purified by a novel technique of affinity binding to liposomes
    • Alving CR, Richards RE, Immune reactivities of antibodies against glycolipids. I. Properties of anti-galactocerebroside antibodies purified by a novel technique of affinity binding to liposomes, Immunochemistry 14, 373-81 (1977).
    • (1977) Immunochemistry , vol.14 , pp. 373-381
    • Alving, C.R.1    Richards, R.E.2
  • 94
    • 0020028647 scopus 로고
    • Chemical synthesis of α-fucopyranosylceramide and its analogues and preparation of antibodies directed to this glycolipid
    • Yoshino T, Watanabe K, Hakomori S, Chemical synthesis of α-fucopyranosylceramide and its analogues and preparation of antibodies directed to this glycolipid, Biochemistry 21, 928-34 (1982).
    • (1982) Biochemistry , vol.21 , pp. 928-934
    • Yoshino, T.1    Watanabe, K.2    Hakomori, S.3
  • 95
    • 0021215577 scopus 로고
    • Haptenic activity of galactosyl ceramide and its topographical distribution in liposomal membranes, Effects of temperature and phospholipid composition
    • Utsumi H, Suzuki T, Inoue K, Nojima S, Haptenic activity of galactosyl ceramide and its topographical distribution in liposomal membranes, Effects of temperature and phospholipid composition, J Biochem 96, 97-105 (1984).
    • (1984) J Biochem , vol.96 , pp. 97-105
    • Utsumi, H.1    Suzuki, T.2    Inoue, K.3    Nojima, S.4
  • 96
    • 0022838662 scopus 로고
    • Factors affecting surface expression of glycolipids: Influence of lipid environment and ceramide composition on antibody recognition of cerebroside sulfate in liposomes
    • Crook SJ, Boggs JM, Vistnes AI, Koshy KM, Factors affecting surface expression of glycolipids: Influence of lipid environment and ceramide composition on antibody recognition of cerebroside sulfate in liposomes, Biochemistry 25, 7488-94 (1986).
    • (1986) Biochemistry , vol.25 , pp. 7488-7494
    • Crook, S.J.1    Boggs, J.M.2    Vistnes, A.I.3    Koshy, K.M.4
  • 97
    • 0027207472 scopus 로고
    • Exposure of galactosylceramide to galactose oxidase in liposomes: Dependence on lipid environment and ceramide composition
    • Stewart RJ, Boggs JM, Exposure of galactosylceramide to galactose oxidase in liposomes: Dependence on lipid environment and ceramide composition, Biochemistry 32, 5605-14 (1993).
    • (1993) Biochemistry , vol.32 , pp. 5605-5614
    • Stewart, R.J.1    Boggs, J.M.2
  • 98
    • 0019898557 scopus 로고
    • Possible role of ceramide in defining structure and function of membrane glycolipids
    • Kannagi R, Nudelman E, Hakomori S, Possible role of ceramide in defining structure and function of membrane glycolipids, Proc Natl Acad Sci USA 79, 3470-4 (1982).
    • (1982) Proc Natl Acad Sci USA , vol.79 , pp. 3470-3474
    • Kannagi, R.1    Nudelman, E.2    Hakomori, S.3
  • 100
    • 0042845804 scopus 로고    scopus 로고
    • Fluorescence energy transfer reveals microdomain formation at physiological temperatures in lipid mixtures modeling the outer leaflet of the plasma membrane
    • Silvius JR, Fluorescence energy transfer reveals microdomain formation at physiological temperatures in lipid mixtures modeling the outer leaflet of the plasma membrane, Biophys J 85, 1034-45 (2003).
    • (2003) Biophys J , vol.85 , pp. 1034-1045
    • Silvius, J.R.1
  • 101
    • 0024343586 scopus 로고
    • Intermixing of dipalmitoylphosphatidylcholine with phospho- and sphingolipids bearing highly asymmetric hydrocarbon chains
    • Gardam M, Silvius JR, Intermixing of dipalmitoylphosphatidylcholine with phospho- and sphingolipids bearing highly asymmetric hydrocarbon chains, Biochim Biophys Acta 980, 319-25 (1989).
    • (1989) Biochim Biophys Acta , vol.980 , pp. 319-325
    • Gardam, M.1    Silvius, J.R.2
  • 102
    • 0023239664 scopus 로고
    • Lipid intermolecular hydrogen bonding: Influence on structural organization and membrane function
    • Boggs JM, Lipid intermolecular hydrogen bonding: Influence on structural organization and membrane function, Biochim Biophys Acta 906, 353-404 (1987).
    • (1987) Biochim Biophys Acta , vol.906 , pp. 353-404
    • Boggs, J.M.1
  • 104
    • 0028009878 scopus 로고
    • Do the long fatty acid chains of sphingolipids interdigitate across the center of abilayer of shorter chain symmetric phospholipids?
    • Boggs JM, Koshy, KM, Do the long fatty acid chains of sphingolipids interdigitate across the center of abilayer of shorter chain symmetric phospholipids? Biochim Biophys Acta 1189, 233-41 (1994).
    • (1994) Biochim Biophys Acta , vol.1189 , pp. 233-241
    • Boggs, J.M.1    Koshy, K.M.2
  • 106
    • 0029829384 scopus 로고    scopus 로고
    • Noncovalent associations of T lymphocyte surface proteins
    • Cerny J, Stockinger H, Horejsi V, Noncovalent associations of T lymphocyte surface proteins, Eur J Immunol 26, 2335-43 (1996).
    • (1996) Eur J Immunol , vol.26 , pp. 2335-2343
    • Cerny, J.1    Stockinger, H.2    Horejsi, V.3
  • 107
    • 0033573083 scopus 로고    scopus 로고
    • Functionally different GPI proteins are organized in different domains on the neuronal surface
    • Madore N, Smith KL, Graham CH, Jen A, Brady K, Hall S, Morris R, Functionally different GPI proteins are organized in different domains on the neuronal surface, EMBO J 18, 6917-22 (1999).
    • (1999) EMBO J , vol.18 , pp. 6917-6922
    • Madore, N.1    Smith, K.L.2    Graham, C.H.3    Jen, A.4    Brady, K.5    Hall, S.6    Morris, R.7
  • 108
    • 0034282003 scopus 로고    scopus 로고
    • Retention of prominin in microvilli reveals distinct cholesterol-based lipid micro-domains in the apical plasma membrane
    • Roper K, Corbeil D, Huttner WB, Retention of prominin in microvilli reveals distinct cholesterol-based lipid micro-domains in the apical plasma membrane, Nat Cell Biol 2, 582-92 (2000).
    • (2000) Nat Cell Biol , vol.2 , pp. 582-592
    • Roper, K.1    Corbeil, D.2    Huttner, W.B.3
  • 109
    • 0035896648 scopus 로고    scopus 로고
    • Evaluation of prototype transmembrane 4 superfamily protein complexes and their relation to lipid rafts
    • Claas C, Stipp CS, Hemler ME, Evaluation of prototype transmembrane 4 superfamily protein complexes and their relation to lipid rafts, J Biol Chem 276, 7974-84 (2001).
    • (2001) J Biol Chem , vol.276 , pp. 7974-7984
    • Claas, C.1    Stipp, C.S.2    Hemler, M.E.3
  • 110
    • 0036319382 scopus 로고    scopus 로고
    • Detergent-insoluble glycosphingolipid/cholesterol microdomains of the myelin membrane
    • Taylor CM, Coetzee T, Pfeiffer SE, Detergent-insoluble glycosphingolipid/cholesterol microdomains of the myelin membrane, J Neurochem 81, 993-1004 (2002).
    • (2002) J Neurochem , vol.81 , pp. 993-1004
    • Taylor, C.M.1    Coetzee, T.2    Pfeiffer, S.E.3
  • 111
    • 0023898127 scopus 로고
    • Triton X-100 extractions of central nervous system myelin indicate a possible role for the minor myelin proteins in the stability in lamellae
    • Pereyra PM, Horvath E, Braun PE, Triton X-100 extractions of central nervous system myelin indicate a possible role for the minor myelin proteins in the stability in lamellae, Neurochem Res 13, 583-95 (1988).
    • (1988) Neurochem Res , vol.13 , pp. 583-595
    • Pereyra, P.M.1    Horvath, E.2    Braun, P.E.3
  • 112
    • 0036785238 scopus 로고    scopus 로고
    • Myelin proteolipid protein, basic protein, the small isoform of myelin-associated glycoprotein, and p42MAPK are associated in the TX-100 extract of central nervous system myelin
    • Arvanitis DN, Yang W, Boggs JM, Myelin proteolipid protein, basic protein, the small isoform of myelin-associated glycoprotein, and p42MAPK are associated in the TX-100 extract of central nervous system myelin, J Neurosci Res 70, 8-23 (2002).
    • (2002) J Neurosci Res , vol.70 , pp. 8-23
    • Arvanitis, D.N.1    Yang, W.2    Boggs, J.M.3
  • 113
    • 0033497984 scopus 로고    scopus 로고
    • Myelin glycosphingolipid/cholesterol-enriched microdomains selectively sequester the non-compact myelin proteins CNP and MOG
    • Kim T, Pfeiffer SE, Myelin glycosphingolipid/cholesterol-enriched microdomains selectively sequester the non-compact myelin proteins CNP and MOG, J Neurocytol 28, 281-93 (1999).
    • (1999) J Neurocytol , vol.28 , pp. 281-293
    • Kim, T.1    Pfeiffer, S.E.2
  • 114
    • 0038722226 scopus 로고    scopus 로고
    • Antibody cross-linking of myelin oligodendrocyte glycoprotein leads to its rapid repartitioning into detergent-insoluble fractions, and altered protein phosphorylation and cell morphology
    • Marta CB, Taylor CM, Coetzee T, Kim T, Winkler S, Bansal R, Pfeiffer SE, Antibody cross-linking of myelin oligodendrocyte glycoprotein leads to its rapid repartitioning into detergent-insoluble fractions, and altered protein phosphorylation and cell morphology, J Neurosci 23, 5461-71 (2003).
    • (2003) J Neurosci , vol.23 , pp. 5461-5471
    • Marta, C.B.1    Taylor, C.M.2    Coetzee, T.3    Kim, T.4    Winkler, S.5    Bansal, R.6    Pfeiffer, S.E.7
  • 116
  • 118
    • 0036702299 scopus 로고    scopus 로고
    • Plasma membrane microdomains
    • Maxfield FR, Plasma membrane microdomains, Curr Opin Cell Biol 14, 483-7 (2002).
    • (2002) Curr Opin Cell Biol , vol.14 , pp. 483-487
    • Maxfield, F.R.1
  • 120
    • 0033936363 scopus 로고    scopus 로고
    • Evidence that ganglioside enriched domains are distinct from caveolae in MDCK II and human fibroblast cells in culture
    • Chigorno V, Palestini P, Sciannamblo M, Dolo V, Pavan A, Tettamanti G, Sonnino S, Evidence that ganglioside enriched domains are distinct from caveolae in MDCK II and human fibroblast cells in culture, Eur J Biochem 267, 4187-97 (2000).
    • (2000) Eur J Biochem , vol.267 , pp. 4187-4197
    • Chigorno, V.1    Palestini, P.2    Sciannamblo, M.3    Dolo, V.4    Pavan, A.5    Tettamanti, G.6    Sonnino, S.7
  • 121
    • 0035082123 scopus 로고    scopus 로고
    • Segregation of gangliosides GM1 and GD3 on cell membranes, isolated membrane rafts, and defined supported lipid monolayers
    • Vyas KA, Patel HV, Vyas AA, Schnaar RL, Segregation of gangliosides GM1 and GD3 on cell membranes, isolated membrane rafts, and defined supported lipid monolayers, Biol Chem 382, 241-50 (2001).
    • (2001) Biol Chem , vol.382 , pp. 241-250
    • Vyas, K.A.1    Patel, H.V.2    Vyas, A.A.3    Schnaar, R.L.4
  • 122
    • 0032169870 scopus 로고    scopus 로고
    • Determination of the non-ionic detergent insolubility and phosphoprotein associations of glycosylphosphatidylinositol-anchored proteins expressed on T cells
    • Solomon KR, Mallory MA, Finberg RW, Determination of the non-ionic detergent insolubility and phosphoprotein associations of glycosylphosphatidylinositol-anchored proteins expressed on T cells, Biochem J 334(pt 2), 325-33 (1998).
    • (1998) Biochem J , vol.334 , Issue.2 PART , pp. 325-333
    • Solomon, K.R.1    Mallory, M.A.2    Finberg, R.W.3
  • 123
    • 0036727004 scopus 로고    scopus 로고
    • Evidence for segregation of heterologous GPI-anchored proteins into separate lipid rafts within the plasma membrane
    • Wang J, Gunning W, Kelley KMM, Ratnam M, Evidence for segregation of heterologous GPI-anchored proteins into separate lipid rafts within the plasma membrane, J Membr Biol 189, 35-43 (2002).
    • (2002) J Membr Biol , vol.189 , pp. 35-43
    • Wang, J.1    Gunning, W.2    Kelley, K.M.M.3    Ratnam, M.4
  • 124
    • 0027976632 scopus 로고
    • Initial events of myelination involve Fyn tyrosine kinase signalling
    • Umemori H, Sato S, Yagi T, Alzawa S, Yamamoto T, Initial events of myelination involve Fyn tyrosine kinase signalling, Nature 367, 572-6 (1994).
    • (1994) Nature , vol.367 , pp. 572-576
    • Umemori, H.1    Sato, S.2    Yagi, T.3    Alzawa, S.4    Yamamoto, T.5
  • 125
    • 0024442564 scopus 로고
    • Organization of oligodendroglial membrane sheets. I: Association of MBP and CNPase with cytoskeleton
    • Dyer CA, Benjamins JA, Organization of oligodendroglial membrane sheets. I: Association of MBP and CNPase with cytoskeleton, J Neurosci Res 24, 201-11 (1989).
    • (1989) J Neurosci Res , vol.24 , pp. 201-211
    • Dyer, C.A.1    Benjamins, J.A.2
  • 127
    • 0030222116 scopus 로고    scopus 로고
    • Cell surface organization by the membrane skeleton
    • Kusumi A, Sako Y, Cell surface organization by the membrane skeleton, Curr Opin Cell Biol 8, 566-74 (1996).
    • (1996) Curr Opin Cell Biol , vol.8 , pp. 566-574
    • Kusumi, A.1    Sako, Y.2
  • 128
    • 0032820709 scopus 로고    scopus 로고
    • Mobility and cytoskeletal interactions of cell adhesion receptors
    • Kusumi A, Suzuki K, Koyasako K, Mobility and cytoskeletal interactions of cell adhesion receptors, Curr Opin Cell Biol 11, 582-90 (1999).
    • (1999) Curr Opin Cell Biol , vol.11 , pp. 582-590
    • Kusumi, A.1    Suzuki, K.2    Koyasako, K.3
  • 129
    • 0032563615 scopus 로고    scopus 로고
    • Regulation mechanism of the lateral diffusion of band 3 in erythrocyte membranes by the membrane skeleton
    • Tomishige M, Sako Y, Kusumi A, Regulation mechanism of the lateral diffusion of band 3 in erythrocyte membranes by the membrane skeleton, J Cell Biol 142, 989-1000 (1998).
    • (1998) J Cell Biol , vol.142 , pp. 989-1000
    • Tomishige, M.1    Sako, Y.2    Kusumi, A.3
  • 130
    • 0037054546 scopus 로고    scopus 로고
    • Phospholipids undergo hop diffusion in compartmentalized cell membrane
    • Fujiwara T, Ritchie K, Murakoshi H, Jacobson K, Kusumi A, Phospholipids undergo hop diffusion in compartmentalized cell membrane, J Cell Biol 157, 1071-81 (2002).
    • (2002) J Cell Biol , vol.157 , pp. 1071-1081
    • Fujiwara, T.1    Ritchie, K.2    Murakoshi, H.3    Jacobson, K.4    Kusumi, A.5
  • 131
    • 0025358961 scopus 로고
    • A membrane receptor for gangliosides is associated with CNS myelin
    • Tiemeyer M, Swank-Hill P, Schnaar RL, A membrane receptor for gangliosides is associated with CNS myelin, J Biol Chem 265, 11990-9 (1990).
    • (1990) J Biol Chem , vol.265 , pp. 11990-11999
    • Tiemeyer, M.1    Swank-Hill, P.2    Schnaar, R.L.3
  • 132
    • 0026967530 scopus 로고
    • Carbohydrate moieties of myelin-associated glycoprotein, major glycoprotein of the peripheral nervous system myelin and other myelin glycoproteins potentially involved in cell adhesion
    • Badache A, Burger D, Villarroya H, Robert Y, Kuchler S, Steck AJ, Zanetta J-P, Carbohydrate moieties of myelin-associated glycoprotein, major glycoprotein of the peripheral nervous system myelin and other myelin glycoproteins potentially involved in cell adhesion, Develop Neurosci 14, 342-50 (1992).
    • (1992) Develop Neurosci , vol.14 , pp. 342-350
    • Badache, A.1    Burger, D.2    Villarroya, H.3    Robert, Y.4    Kuchler, S.5    Steck, A.J.6    Zanetta, J.-P.7
  • 133
    • 0028230423 scopus 로고
    • MGDG, a marker for myelination, activates oligodendroglial protein kinase C
    • Schmidt-Schultz T, Althaus HH, MGDG, a marker for myelination, activates oligodendroglial protein kinase C, J Neurochem 62, 1578-85 (1994).
    • (1994) J Neurochem , vol.62 , pp. 1578-1585
    • Schmidt-Schultz, T.1    Althaus, H.H.2
  • 134
    • 0033962213 scopus 로고    scopus 로고
    • The oligodendroglia cytoskeleton in health and disease
    • Richter-Landsberg C, The oligodendroglia cytoskeleton in health and disease, J Neurosci Res 59, 11-8 (2000).
    • (2000) J Neurosci Res , vol.59 , pp. 11-18
    • Richter-Landsberg, C.1
  • 135
    • 0028390644 scopus 로고
    • Contact with myelin evokes a release of calcium from internal stores in neonatal rat oligodendrocytes in vitro
    • Moorman SJ, Hume RL, Contact with myelin evokes a release of calcium from internal stores in neonatal rat oligodendrocytes in vitro, Glia 10, 202-10 (1994).
    • (1994) Glia , vol.10 , pp. 202-210
    • Moorman, S.J.1    Hume, R.L.2
  • 136
    • 0030106239 scopus 로고    scopus 로고
    • The inhibition of motility that results from contact between two oligodendrocytes in vitro can be blocked by pertussis toxin
    • Moorman SJ, The inhibition of motility that results from contact between two oligodendrocytes in vitro can be blocked by pertussis toxin, Glia 16, 257-65 (1996).
    • (1996) Glia , vol.16 , pp. 257-265
    • Moorman, S.J.1
  • 137
    • 0034650970 scopus 로고    scopus 로고
    • Unwrapping new layers of complexity in axon/glial relationships
    • Witt A, Brady ST, Unwrapping new layers of complexity in axon/glial relationships, Glia 29, 112-7 (2000).
    • (2000) Glia , vol.29 , pp. 112-117
    • Witt, A.1    Brady, S.T.2
  • 138
    • 0034212602 scopus 로고    scopus 로고
    • The evolution of lipophilin genes from invertebrates to tetrapods: DM-20 cannot replace PLP in CNS myelin
    • Stecca B, Southwood CM, Gragerov A, Kelley KA, Friedrich VL, Jr., Gow A, The evolution of lipophilin genes from invertebrates to tetrapods: DM-20 cannot replace PLP in CNS myelin, J Neurosci 20, 4002-10 (2000).
    • (2000) J Neurosci , vol.20 , pp. 4002-4010
    • Stecca, B.1    Southwood, C.M.2    Gragerov, A.3    Kelley, K.A.4    Friedrich Jr., V.L.5    Gow, A.6
  • 139
    • 0033573229 scopus 로고    scopus 로고
    • Completion of myelin compaction, but not the attachment of oligodendroglial processes triggers K channel clustering
    • Baba H, Akita H, Ishibashi T, Inoue Y, Nakahira K, Ikenaka K, Completion of myelin compaction, but not the attachment of oligodendroglial processes triggers K channel clustering, J Neurosci Res 58, 752-64 (1999).
    • (1999) J Neurosci Res , vol.58 , pp. 752-764
    • Baba, H.1    Akita, H.2    Ishibashi, T.3    Inoue, Y.4    Nakahira, K.5    Ikenaka, K.6
  • 140
    • 0021277652 scopus 로고
    • Impulse conduction regulates myelin basic protein phosphorylation in rat optic nerve
    • Murray N and Steck AJ, Impulse conduction regulates myelin basic protein phosphorylation in rat optic nerve, J Neurochem 43, 243-8 (1984).
    • (1984) J Neurochem , vol.43 , pp. 243-248
    • Murray, N.1    Steck, A.J.2
  • 141
    • 0033198188 scopus 로고    scopus 로고
    • Reactive oxygen species mediate activity-dependent neuron-glia signaling in output fibers of the hippocampus
    • Atkins CM, Sweatt JD, Reactive oxygen species mediate activity-dependent neuron-glia signaling in output fibers of the hippocampus, J Neurosci 19, 7241-8 (1999).
    • (1999) J Neurosci , vol.19 , pp. 7241-7248
    • Atkins, C.M.1    Sweatt, J.D.2
  • 142
    • 0032927454 scopus 로고    scopus 로고
    • The phosphoinositide signaling cycle in myelin requires cooperative interaction with the axon
    • Chakraborty G, Drivas A, Ledeen R, The phosphoinositide signaling cycle in myelin requires cooperative interaction with the axon, Neurochem Res 24, 249-54 (1999).
    • (1999) Neurochem Res , vol.24 , pp. 249-254
    • Chakraborty, G.1    Drivas, A.2    Ledeen, R.3
  • 143
    • 0034890751 scopus 로고    scopus 로고
    • Intraneuronal N-acetylaspartate supplies acetyl groups for myelin lipid synthesis: Evidence for myelin-associated aspartoacylase
    • Chakraborty G, Mekala P, Yahya D, Wu G, Ledeen RW, Intraneuronal N-acetylaspartate supplies acetyl groups for myelin lipid synthesis: Evidence for myelin-associated aspartoacylase, J Neurochem 78, 736-45 (2001).
    • (2001) J Neurochem , vol.78 , pp. 736-745
    • Chakraborty, G.1    Mekala, P.2    Yahya, D.3    Wu, G.4    Ledeen, R.W.5
  • 144
    • 0020566047 scopus 로고
    • Axon-myelin transfer of glycerol-labeled lipids and inorganic phosphate during axonal transport
    • Ledeen RW, Golly F, Haley JE, Axon-myelin transfer of glycerol-labeled lipids and inorganic phosphate during axonal transport, Brain Res 269, 267-75 (1992).
    • (1992) Brain Res , vol.269 , pp. 267-275
    • Ledeen, R.W.1    Golly, F.2    Haley, J.E.3
  • 145
    • 0017753626 scopus 로고
    • Distribution of Schwann cell cytoplasm and plasmalemmal vesicles (caveolae) in peripheral myelin sheaths. An electron microscopic study with thin sections and freeze-fracturing
    • Mugnaini E, Osen KK, Schnapp B, Friedrich, Jr., VL, Distribution of Schwann cell cytoplasm and plasmalemmal vesicles (caveolae) in peripheral myelin sheaths. An electron microscopic study with thin sections and freeze-fracturing, J Neurocytol 6, 647-68 (1977).
    • (1977) J Neurocytol , vol.6 , pp. 647-668
    • Mugnaini, E.1    Osen, K.K.2    Schnapp, B.3    Friedrich Jr., V.L.4


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