메뉴 건너뛰기




Volumn 51, Issue 3, 1998, Pages 371-381

Transport of proteolipid protein to the plasma membrane does not depend on glycosphingolipid cotransport in oligodendrocyte cultures

Author keywords

Galactosyl ceramide; Myelin proteolipid protein; Myelination; Protein lipid transport; Sulfatide

Indexed keywords

GALACTOSYLCERAMIDE; GLYCOSPHINGOLIPID; PROTEOLIPID PROTEIN; SODIUM CHLORATE; SULFATIDE;

EID: 0032006132     PISSN: 03604012     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-4547(19980201)51:3<371::AID-JNR10>3.0.CO;2-A     Document Type: Article
Times cited : (15)

References (45)
  • 1
    • 0018424467 scopus 로고
    • The characterization of sphingolipids of oligodendroglia from calf brain
    • Abe T, Norton WT (1979): The characterization of sphingolipids of oligodendroglia from calf brain. J Neurochem 32:823-832.
    • (1979) J Neurochem , vol.32 , pp. 823-832
    • Abe, T.1    Norton, W.T.2
  • 2
    • 0028295710 scopus 로고
    • Inhibition of protein and lipid sulfation in oligodendrocytes blocks biological responses to FGF-2 and retards cytoarchitectural maturation, but not developmental lineage progression
    • Bansal R, Pfeiffer SE (1994): Inhibition of protein and lipid sulfation in oligodendrocytes blocks biological responses to FGF-2 and retards cytoarchitectural maturation, but not developmental lineage progression. Dev Biol 162:511-524.
    • (1994) Dev Biol , vol.162 , pp. 511-524
    • Bansal, R.1    Pfeiffer, S.E.2
  • 3
    • 0020084329 scopus 로고
    • Cerebroside sulfotransferase in Golgi-enriched fractions from rat brain
    • Benjamins JA, Hadden T, Skoff RP (1982): Cerebroside sulfotransferase in Golgi-enriched fractions from rat brain. J Neurochem 38:233-241.
    • (1982) J Neurochem , vol.38 , pp. 233-241
    • Benjamins, J.A.1    Hadden, T.2    Skoff, R.P.3
  • 4
    • 33845261493 scopus 로고
    • A rapid method of total lipid extraction and purification
    • Bligh EG, Dyer WJ (1959): A rapid method of total lipid extraction and purification. Can J Biochem Physiol 37:911-917.
    • (1959) Can J Biochem Physiol , vol.37 , pp. 911-917
    • Bligh, E.G.1    Dyer, W.J.2
  • 5
    • 0026512314 scopus 로고
    • Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface
    • Brown DA, Rose JK (1992): Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface. Cell 68:533-544.
    • (1992) Cell , vol.68 , pp. 533-544
    • Brown, D.A.1    Rose, J.K.2
  • 7
    • 0020372097 scopus 로고
    • Synthesis and incorporation of myelin polypeptides into CNS myelin
    • Colman DR, Kreibich G, Frey AB, Sabatini DD (1982): Synthesis and incorporation of myelin polypeptides into CNS myelin. J Cell Biol 95:598-608.
    • (1982) J Cell Biol , vol.95 , pp. 598-608
    • Colman, D.R.1    Kreibich, G.2    Frey, A.B.3    Sabatini, D.D.4
  • 8
    • 0028955507 scopus 로고
    • Involvement of detergent-insoluble complexes in the intracellular transport of intestinal brush border enzymes
    • Danielsen EM (1995): Involvement of detergent-insoluble complexes in the intracellular transport of intestinal brush border enzymes. Biochemistry 34:1596-1605.
    • (1995) Biochemistry , vol.34 , pp. 1596-1605
    • Danielsen, E.M.1
  • 10
    • 0017877124 scopus 로고
    • Adenosine triphosphate sulfurylase from Penicillium chrysogenum: Equilibrium binding, substrate hydrolysis, and isotope exchange studies
    • Farly JR, Nakayama G, Cryns D, Segel IH (1978): Adenosine triphosphate sulfurylase from Penicillium chrysogenum: Equilibrium binding, substrate hydrolysis, and isotope exchange studies. Arch Biochem Biophys 185:376-390.
    • (1978) Arch Biochem Biophys , vol.185 , pp. 376-390
    • Farly, J.R.1    Nakayama, G.2    Cryns, D.3    Segel, I.H.4
  • 11
    • 0029094537 scopus 로고
    • Effects of brefeldin A on galactosphingolipid synthesis in an immortalized Schwann cell line: Evidence for different intracellular locations of galactosylceramide sulfotransferase and ceramide galactosyltransferase activities
    • Farrer RG, Warden MP, Quarles RH (1995): Effects of brefeldin A on galactosphingolipid synthesis in an immortalized Schwann cell line: Evidence for different intracellular locations of galactosylceramide sulfotransferase and ceramide galactosyltransferase activities. J Neurochem 65:1865-1873.
    • (1995) J Neurochem , vol.65 , pp. 1865-1873
    • Farrer, R.G.1    Warden, M.P.2    Quarles, R.H.3
  • 12
    • 0023183159 scopus 로고
    • Myelin-specific domain on the plasmalemma of oligodendroglia: Differential expression in the rat and hypomyelinating mouse mutants jimpy and quaking
    • Gard AL, Dutton GR (1987): Myelin-specific domain on the plasmalemma of oligodendroglia: Differential expression in the rat and hypomyelinating mouse mutants jimpy and quaking. J Neurosci Res 17:329-343.
    • (1987) J Neurosci Res , vol.17 , pp. 329-343
    • Gard, A.L.1    Dutton, G.R.2
  • 13
    • 0028287054 scopus 로고
    • Intracellular transport and sorting of the oligodendrocyte transmembrane proteolipid protein
    • Gow A, Friedrich VL, Lazzarini RA (1994): Intracellular transport and sorting of the oligodendrocyte transmembrane proteolipid protein. J Neurosci Res 37:563-573.
    • (1994) J Neurosci Res , vol.37 , pp. 563-573
    • Gow, A.1    Friedrich, V.L.2    Lazzarini, R.A.3
  • 14
    • 0031025729 scopus 로고    scopus 로고
    • Conservation of topology, but not conformation, of the proteolipid proteins of the myelin sheath
    • Gow A, Gragerov A, Gard A, Colman DR, Lazzarini RA (1997): Conservation of topology, but not conformation, of the proteolipid proteins of the myelin sheath. J Neurosci 17:181-189.
    • (1997) J Neurosci , vol.17 , pp. 181-189
    • Gow, A.1    Gragerov, A.2    Gard, A.3    Colman, D.R.4    Lazzarini, R.A.5
  • 15
    • 0028414481 scopus 로고
    • Mechanisms of myelin basic protein and proteolipid protein targeting in oligodendrocytes
    • Kalwy SA, Smith R (1994): Mechanisms of myelin basic protein and proteolipid protein targeting in oligodendrocytes. Mol Membrane Biol 11:67-78.
    • (1994) Mol Membrane Biol , vol.11 , pp. 67-78
    • Kalwy, S.A.1    Smith, R.2
  • 16
    • 0028875824 scopus 로고
    • Cloning and characterization of MVP17: A developmentally regulated myelin protein in oligodendrocytes
    • Kim T, Fiedler K, Madison DL, Krueger WH, Pfeiffer SE (1995): Cloning and characterization of MVP17: A developmentally regulated myelin protein in oligodendrocytes. J Neurosci Res 42:413-422.
    • (1995) J Neurosci Res , vol.42 , pp. 413-422
    • Kim, T.1    Fiedler, K.2    Madison, D.L.3    Krueger, W.H.4    Pfeiffer, S.E.5
  • 18
    • 0025187179 scopus 로고
    • A non-exchangeable fluorescent phospholipid analog as a membrane traffic marker of the endocytic pathway
    • Kok JW, Ter Beest MBA, Scherphof G, Hoekstra D (1990): A non-exchangeable fluorescent phospholipid analog as a membrane traffic marker of the endocytic pathway. Eur J Cell Biol 53:173-184.
    • (1990) Eur J Cell Biol , vol.53 , pp. 173-184
    • Kok, J.W.1    Ter Beest, M.B.A.2    Scherphof, G.3    Hoekstra, D.4
  • 19
    • 0025886954 scopus 로고
    • Sorting of sphingolipids in the endocytic pathway in HT29 cells
    • Kok JW, Babia T, Hoekstra D (1991): Sorting of sphingolipids in the endocytic pathway in HT29 cells. J Cell Biol 114:231-239.
    • (1991) J Cell Biol , vol.114 , pp. 231-239
    • Kok, J.W.1    Babia, T.2    Hoekstra, D.3
  • 20
    • 0000029565 scopus 로고
    • Proteins of myelin
    • Morell P (ed): New York: Plenum
    • Lees MB, Brostoff SW (1984): Proteins of myelin. In Morell P (ed): "Myelin." New York: Plenum, pp 197-224.
    • (1984) Myelin , pp. 197-224
    • Lees, M.B.1    Brostoff, S.W.2
  • 22
    • 0019313317 scopus 로고
    • Preparation of separate astroglial and oligodendroglial cell cultures from rat cerebral tissue
    • McCarthy KD, DeVellis J (1980): Preparation of separate astroglial and oligodendroglial cell cultures from rat cerebral tissue. J Cell Biol 85:890-902.
    • (1980) J Cell Biol , vol.85 , pp. 890-902
    • McCarthy, K.D.1    DeVellis, J.2
  • 23
    • 0031023458 scopus 로고    scopus 로고
    • The MAL proteolipid is a component of the detergent-insoluble membrane subdomains of human T-lymphocytes
    • Millan J, Puertollano R, Fan L, Rancano C, Alonso MA (1997): The MAL proteolipid is a component of the detergent-insoluble membrane subdomains of human T-lymphocytes. Biochem J 321:247-52.
    • (1997) Biochem J , vol.321 , pp. 247-252
    • Millan, J.1    Puertollano, R.2    Fan, L.3    Rancano, C.4    Alonso, M.A.5
  • 24
    • 0022133330 scopus 로고
    • Nucleotide sequences of two mRNAs for rat brain myelin proteolipid protein
    • Milner RJ, Lai C, Nave KA, Lenoir D, Ogata J, Sutcliffe JG (1985): Nucleotide sequences of two mRNAs for rat brain myelin proteolipid protein. Cell 42:931-939.
    • (1985) Cell , vol.42 , pp. 931-939
    • Milner, R.J.1    Lai, C.2    Nave, K.A.3    Lenoir, D.4    Ogata, J.5    Sutcliffe, J.G.6
  • 25
    • 0000072448 scopus 로고
    • Isolation and characterization of myelin
    • Morell P (ed): New York: Plenum
    • Norton WT, Cammer W (1984): Isolation and characterization of myelin. In Morell P (ed): "Myelin." New York: Plenum, pp 147-195.
    • (1984) Myelin , pp. 147-195
    • Norton, W.T.1    Cammer, W.2
  • 26
    • 0021088280 scopus 로고
    • Immunocytochemical demonstration of the transport of myelin proteolipids through the Golgi apparatus
    • Nussbaum JL, Roussel G (1983): Immunocytochemical demonstration of the transport of myelin proteolipids through the Golgi apparatus. Cell Tissue Res 234:547-559.
    • (1983) Cell Tissue Res , vol.234 , pp. 547-559
    • Nussbaum, J.L.1    Roussel, G.2
  • 27
    • 0024518799 scopus 로고
    • Inhibition of the synthesis of glycosphingolipids affects the translocation of proteolipid protein to the myelin membrane
    • Pasquini JM, Guarna MM, Besio-Moreno MA, Iturregui MT, Oteiza PI, Soto EF (1989): Inhibition of the synthesis of glycosphingolipids affects the translocation of proteolipid protein to the myelin membrane. J Neurosci Res 22:289-296.
    • (1989) J Neurosci Res , vol.22 , pp. 289-296
    • Pasquini, J.M.1    Guarna, M.M.2    Besio-Moreno, M.A.3    Iturregui, M.T.4    Oteiza, P.I.5    Soto, E.F.6
  • 28
    • 0029111982 scopus 로고
    • Characterization of a rat gene, rMAL, encoding a protein with four hydrophobic domains in central and peripheral myelin
    • Schaeren-Wiemers N, Valenzuela DM, Frank M, Schuab ME (1995a): Characterization of a rat gene, rMAL, encoding a protein with four hydrophobic domains in central and peripheral myelin. J Neurosci 15:5753-5764.
    • (1995) J Neurosci , vol.15 , pp. 5753-5764
    • Schaeren-Wiemers, N.1    Valenzuela, D.M.2    Frank, M.3    Schuab, M.E.4
  • 29
    • 0028882458 scopus 로고
    • The UDP-galactose:ceramide galactosyltransferase: Expression pattern in oligodendrocytes and schwann cells during myelination and substrate preference for hydroxyceramide
    • Schaeren-Wiemers N, Van der Bijl P, Schuab ME (1995b): The UDP-galactose:ceramide galactosyltransferase: Expression pattern in oligodendrocytes and schwann cells during myelination and substrate preference for hydroxyceramide. J Neurochem 65:2267-2278.
    • (1995) J Neurochem , vol.65 , pp. 2267-2278
    • Schaeren-Wiemers, N.1    Van Der Bijl, P.2    Schuab, M.E.3
  • 30
    • 0027440258 scopus 로고
    • Ceramide UDP-galactosyltransferase from myelinating rat brain: Purification, cloning, and expression
    • Schulte S, Stoffel W (1993): Ceramide UDP-galactosyltransferase from myelinating rat brain: Purification, cloning, and expression. Proc Natl Acad Sci USA 90:10265-10269.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 10265-10269
    • Schulte, S.1    Stoffel, W.2
  • 31
    • 0022391252 scopus 로고
    • Electron microscopic immunocytochemical localization of myelin proteolipid protein and myelin basic protein to oligodendrocytes in rat brain during myelination
    • Schwob VS, Clark HB, Agrawal D, Agrawal HC (1985): Electron microscopic immunocytochemical localization of myelin proteolipid protein and myelin basic protein to oligodendrocytes in rat brain during myelination. J Neurochem 45:559-571.
    • (1985) J Neurochem , vol.45 , pp. 559-571
    • Schwob, V.S.1    Clark, H.B.2    Agrawal, D.3    Agrawal, H.C.4
  • 32
    • 0025341760 scopus 로고
    • Polarized sorting in epithelia
    • Simons K, Wandinger-Ness A (1990): Polarized sorting in epithelia. Cell 62:207-210.
    • (1990) Cell , vol.62 , pp. 207-210
    • Simons, K.1    Wandinger-Ness, A.2
  • 33
    • 0028316886 scopus 로고
    • Proteolipid protein interactions in transfectants: Implications for myelin assembly
    • Sinoway MP, Kitagawa K, Timsit S, Hashim GA, Colman DR (1994): Proteolipid protein interactions in transfectants: Implications for myelin assembly. J Neurosci Res 37:551-562.
    • (1994) J Neurosci Res , vol.37 , pp. 551-562
    • Sinoway, M.P.1    Kitagawa, K.2    Timsit, S.3    Hashim, G.A.4    Colman, D.R.5
  • 34
    • 0024547523 scopus 로고
    • Differential extractability of influenza virus hemagglutinin during intracellular transport in polarized epithelial cells and nonpolar fibroblasts
    • Skibbens JE, Roth MG, Matlin KS (1989): Differential extractability of influenza virus hemagglutinin during intracellular transport in polarized epithelial cells and nonpolar fibroblasts. J Cell Biol 108:821-832.
    • (1989) J Cell Biol , vol.108 , pp. 821-832
    • Skibbens, J.E.1    Roth, M.G.2    Matlin, K.S.3
  • 35
    • 0021349321 scopus 로고
    • Inhibition of sphingolipid synthesis by cycloserine in vitro and in vivo
    • Soma Sundaram K, Lev M (1984): Inhibition of sphingolipid synthesis by cycloserine in vitro and in vivo. J Neurochem 42:577-581.
    • (1984) J Neurochem , vol.42 , pp. 577-581
    • Soma Sundaram, K.1    Lev, M.2
  • 36
    • 0028362977 scopus 로고
    • Isolation, characterization, and expression of cDNA clones that encode rat UDP-galactose: Ceramide galactosyltransferase
    • Stahl N, Jurevics H, Morell P, Suzuki K, Popko B (1994): Isolation, characterization, and expression of cDNA clones that encode rat UDP-galactose: Ceramide galactosyltransferase. J Neurosci Res 38:234-242.
    • (1994) J Neurosci Res , vol.38 , pp. 234-242
    • Stahl, N.1    Jurevics, H.2    Morell, P.3    Suzuki, K.4    Popko, B.5
  • 37
    • 0020636109 scopus 로고
    • Topography of cerebroside sulfotransferase in Golgi-enriched vesicles from rat brain
    • Tennekoon G, Zaruba M. Wolinsky J (1983): Topography of cerebroside sulfotransferase in Golgi-enriched vesicles from rat brain. J Cell Biol 97:1107-1112.
    • (1983) J Cell Biol , vol.97 , pp. 1107-1112
    • Tennekoon, G.1    Zaruba, M.2    Wolinsky, J.3
  • 38
    • 0028338896 scopus 로고
    • Reconstitution of proteolipid protein: Some properties and its role in interlamellar attachment
    • Ter Beest MBA, Hoekstra K, Sein A, Hoekstra D (1994): Reconstitution of proteolipid protein: Some properties and its role in interlamellar attachment. Biochem J 300:545-552.
    • (1994) Biochem J , vol.300 , pp. 545-552
    • Ter Beest, M.B.A.1    Hoekstra, K.2    Sein, A.3    Hoekstra, D.4
  • 39
    • 0020533125 scopus 로고
    • Effects of monensin on posttranslational processing of myelin proteins
    • Townsend LE, Benjamins JA (1983): Effects of monensin on posttranslational processing of myelin proteins. J Neurochem 40:1333-1339.
    • (1983) J Neurochem , vol.40 , pp. 1333-1339
    • Townsend, L.E.1    Benjamins, J.A.2
  • 40
    • 0021240414 scopus 로고
    • Effects of monensin and colchicine on myelin galactolipids
    • Townsend LE, Benjamins JA, Skoff RP (1984): Effects of monensin and colchicine on myelin galactolipids. J Neurochem 43:139-145.
    • (1984) J Neurochem , vol.43 , pp. 139-145
    • Townsend, L.E.1    Benjamins, J.A.2    Skoff, R.P.3
  • 41
    • 0030035439 scopus 로고    scopus 로고
    • Synthesis of non-hydroxy-galactosylceramides and galactosyldiglycerides by hydroxy-ceramide galactosyltransferase
    • Van der Bijl P, Strous GJ, Lopes-Cardozo M, Thomas-Oates J, Van Meer G (1996): Synthesis of non-hydroxy-galactosylceramides and galactosyldiglycerides by hydroxy-ceramide galactosyltransferase. Biochem J 317:589-597.
    • (1996) Biochem J , vol.317 , pp. 589-597
    • Van Der Bijl, P.1    Strous, G.J.2    Lopes-Cardozo, M.3    Thomas-Oates, J.4    Van Meer, G.5
  • 42
    • 0025091980 scopus 로고
    • A rapid procedure for the preparation of oligodendrocyteenriched cultures from rat spinal cord
    • Van der Pal RHM, Vos JP, Van Golde LMG, Lopes-Cardozo M (1990): A rapid procedure for the preparation of oligodendrocyteenriched cultures from rat spinal cord. Biochim Biophys Acta 1051:159-165.
    • (1990) Biochim Biophys Acta , vol.1051 , pp. 159-165
    • Van Der Pal, R.H.M.1    Vos, J.P.2    Van Golde, L.M.G.3    Lopes-Cardozo, M.4
  • 44
    • 0030870321 scopus 로고    scopus 로고
    • Aggregation reroutes molecules from a recycling to a vesicle-mediated secretory pathway during reticulocyte maturation
    • in press
    • Vidali M, Mangeat P, Hoekstra D (1997): Aggregation reroutes molecules from a recycling to a vesicle-mediated secretory pathway during reticulocyte maturation. J Cell Sci, in press.
    • (1997) J Cell Sci
    • Vidali, M.1    Mangeat, P.2    Hoekstra, D.3
  • 45
    • 0026002861 scopus 로고
    • Monoclonal antibodies against myelin proteolipid protein: Identification and characterization of two major determinants
    • Yamamura T, Konola JT, Werkele H, Lees MB (1991): Monoclonal antibodies against myelin proteolipid protein: Identification and characterization of two major determinants. J Neurochem 57:1671-1680.
    • (1991) J Neurochem , vol.57 , pp. 1671-1680
    • Yamamura, T.1    Konola, J.T.2    Werkele, H.3    Lees, M.B.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.