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Volumn 8, Issue 4, 2005, Pages 468-475

High cholesterol level is essential for myelin membrane growth

Author keywords

[No Author keywords available]

Indexed keywords

CHOLESTEROL; MYELIN; 2',3' CYCLIC NUCLEOTIDE 3' PHOSPHODIESTERASE; APOLIPOPROTEIN E; CREATINE; LOW DENSITY LIPOPROTEIN RECEPTOR; PROTEOLIPID PROTEIN; RNA; SQUALENE SYNTHASE;

EID: 20044370505     PISSN: 10976256     EISSN: None     Source Type: Journal    
DOI: 10.1038/nn1426     Document Type: Article
Times cited : (548)

References (49)
  • 2
    • 0029942903 scopus 로고    scopus 로고
    • Origin of cholesterol in myelin
    • Morell, P. & Jurevics, H. Origin of cholesterol in myelin. Neurochem. Res. 21, 463-470 (1996).
    • (1996) Neurochem. Res. , vol.21 , pp. 463-470
    • Morell, P.1    Jurevics, H.2
  • 4
    • 0034969390 scopus 로고    scopus 로고
    • Do sterols reduce proton and sodium leaks through lipid bilayers?
    • Haines, T.H. Do sterols reduce proton and sodium leaks through lipid bilayers? Prog. Lipid Res. 40, 299-324 (2001).
    • (2001) Prog. Lipid Res. , vol.40 , pp. 299-324
    • Haines, T.H.1
  • 5
    • 0034625373 scopus 로고    scopus 로고
    • Structure and function of sphingolipid- and cholesterol-rich membrane rafts
    • Brown, D.A. & London, E. Structure and function of sphingolipid- and cholesterol-rich membrane rafts. J. Biol. Chem. 275, 17221-17224 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 17221-17224
    • Brown, D.A.1    London, E.2
  • 7
    • 0035869494 scopus 로고    scopus 로고
    • Membrane traffic in myelinating oligodendrocytes
    • Kramer, E.M., Schardt, A. & Nave, K.A. Membrane traffic in myelinating oligodendrocytes. Microsc. Res. Tech. 52, 656-671 (2001).
    • (2001) Microsc. Res. Tech. , vol.52 , pp. 656-671
    • Kramer, E.M.1    Schardt, A.2    Nave, K.A.3
  • 8
    • 0036865625 scopus 로고    scopus 로고
    • Myelin biogenesis: Vesicle transport in oligodendrocytes
    • Larocca, J.N. & Rodriguez-Gabin, A.G. Myelin biogenesis: vesicle transport in oligodendrocytes. Neurochem. Res. 27, 1313-1329 (2002).
    • (2002) Neurochem. Res. , vol.27 , pp. 1313-1329
    • Larocca, J.N.1    Rodriguez-Gabin, A.G.2
  • 9
    • 0034597142 scopus 로고    scopus 로고
    • Assembly of myelin by association of proteolipid protein with cholesterol- and galactosylceramide-rich membrane domains
    • Simons, M., Kramer, E.M., Thiele, C., Stoffel, W. & Trotter, J. Assembly of myelin by association of proteolipid protein with cholesterol- and galactosylceramide-rich membrane domains. J. Cell Biol. 151, 143-154 (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
  • 10
    • 0032973711 scopus 로고    scopus 로고
    • Inhibition of cholesterol production but not of nonsterol isoprenoid products induces neuronal cell death
    • Michikawa, M. & Yanagisawa, K. Inhibition of cholesterol production but not of nonsterol isoprenoid products induces neuronal cell death. J. Neurochem. 72, 2278-2285 (1999).
    • (1999) J. Neurochem. , vol.72 , pp. 2278-2285
    • Michikawa, M.1    Yanagisawa, K.2
  • 11
    • 0026702230 scopus 로고
    • Squalene synthase-deficient mutant of Chinese hamster ovary cells
    • Bradfute, D.L., Silva, C.J. & Simoni, R.D. Squalene synthase-deficient mutant of Chinese hamster ovary cells. J. Biol. Chem. 267, 18308-18314 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 18308-18314
    • Bradfute, D.L.1    Silva, C.J.2    Simoni, R.D.3
  • 12
    • 0242290361 scopus 로고    scopus 로고
    • Early embryonic lethality caused by targeted disruption of the HMG-CoA reductase gene
    • Ohashi, K. et al. Early embryonic lethality caused by targeted disruption of the HMG-CoA reductase gene. J. Biol. Chem. 278, 42936-42941 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 42936-42941
    • Ohashi, K.1
  • 13
    • 0032748583 scopus 로고    scopus 로고
    • Embryonic lethality and defective neural tube closure in mice lacking squalene synthase
    • Tozawa, R. et al. Embryonic lethality and defective neural tube closure in mice lacking squalene synthase. J. Biol. Chem. 274, 30843-30848 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 30843-30848
    • Tozawa, R.1
  • 14
    • 0032524330 scopus 로고    scopus 로고
    • Function-structure studies and identification of three enzyme domains involved in the catalytic activity in rat hepatic squalene synthase
    • Gu, P., Ishii, Y., Spencer, T.A. & Shechter, I. Function-structure studies and identification of three enzyme domains involved in the catalytic activity in rat hepatic squalene synthase. J. Biol. Chem. 273, 12515-12525 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 12515-12525
    • Gu, P.1    Ishii, Y.2    Spencer, T.A.3    Shechter, I.4
  • 15
    • 0037370361 scopus 로고    scopus 로고
    • Disruption of Cnp1 uncouples oligodendroglial functions in axonal support and myelination
    • Lappe-Siefke, C. et al. Disruption of Cnp1 uncouples oligodendroglial functions in axonal support and myelination. Nat. Genet. 33, 366-374 (2003).
    • (2003) Nat. Genet. , vol.33 , pp. 366-374
    • Lappe-Siefke, C.1
  • 16
    • 0037135989 scopus 로고    scopus 로고
    • Notch1 control of oligodendrocyte differentiation in the spinal cord
    • Genoud, S. et al. Notch1 control of oligodendrocyte differentiation in the spinal cord. J. Cell Biol. 158, 709-718 (2002).
    • (2002) J. Cell Biol. , vol.158 , pp. 709-718
    • Genoud, S.1
  • 17
    • 0035674255 scopus 로고    scopus 로고
    • Unraveling oligodendrocyte origin and function by cell-specific transgenesis
    • Belachew, S., Yuan, X. & Gallo, V. Unraveling oligodendrocyte origin and function by cell-specific transgenesis. Dev. Neurosci. 23, 287-298 (2001).
    • (2001) Dev. Neurosci. , vol.23 , pp. 287-298
    • Belachew, S.1    Yuan, X.2    Gallo, V.3
  • 18
    • 0018634293 scopus 로고
    • Silver staining of myelin by means of physical development
    • Gallyas, F. Silver staining of myelin by means of physical development. Neurol. Res. 1, 203-209 (1979).
    • (1979) Neurol. Res. , vol.1 , pp. 203-209
    • Gallyas, F.1
  • 19
    • 0141987863 scopus 로고    scopus 로고
    • Polarized domains of myelinated axons
    • Salzer, J.L. Polarized domains of myelinated axons. Neuron 40, 297-318 (2003).
    • (2003) Neuron , vol.40 , pp. 297-318
    • Salzer, J.L.1
  • 20
    • 0037137492 scopus 로고    scopus 로고
    • Galactolipidsare molecular determinants of myelin development and axo-glial organization
    • Marcus, J. & Popko, B. Galactolipidsare molecular determinants of myelin development and axo-glial organization. Biochim. Biophys. Acta 1573, 406-413 (2002).
    • (2002) Biochim. Biophys. Acta , vol.1573 , pp. 406-413
    • Marcus, J.1    Popko, B.2
  • 21
    • 0030808781 scopus 로고    scopus 로고
    • Myelin glycolipids and their functions
    • Stoffel, W. & Bosio, A. Myelin glycolipids and their functions. Curr. Opin. Neurobiol. 7, 654-661 (1997).
    • (1997) Curr. Opin. Neurobiol. , vol.7 , pp. 654-661
    • Stoffel, W.1    Bosio, A.2
  • 22
    • 84903112806 scopus 로고    scopus 로고
    • Models of Pelizaeus-Merzbacher disease
    • (ed. Lazzarini, R.A.) Academic, London
    • Nave, K.A. & Griffiths, I.R. Models of Pelizaeus-Merzbacher disease, in Myelin Biology and Disorders Vol. 2 (ed. Lazzarini, R.A.) 1125-1142 (Academic, London, 2003).
    • (2003) Myelin Biology and Disorders , vol.2 , pp. 1125-1142
    • Nave, K.A.1    Griffiths, I.R.2
  • 23
    • 0344196958 scopus 로고    scopus 로고
    • Determination of cholesterol at the low picomole level by nano-electrospray ionization tandem mass spectrometry
    • Sandhoff, R., Brügger, B., Jeckel, D., Lehmann, W.D. & Wieland, F.T. Determination of cholesterol at the low picomole level by nano-electrospray ionization tandem mass spectrometry. J. Lipid Res. 40, 126-132 (1999).
    • (1999) J. Lipid Res. , vol.40 , pp. 126-132
    • Sandhoff, R.1    Brügger, B.2    Jeckel, D.3    Lehmann, W.D.4    Wieland, F.T.5
  • 24
    • 0037092050 scopus 로고    scopus 로고
    • Overexpression of the myelin proteolipid protein leads to accumulation of cholesterol and proteolipid protein in endosomes/lysosomes: Implications for Pelizaeus-Merzbacher disease
    • Simons, M. et al. Overexpression of the myelin proteolipid protein leads to accumulation of cholesterol and proteolipid protein in endosomes/lysosomes: implications for Pelizaeus-Merzbacher disease. J. Cell Biol. 157, 327-336 (2002).
    • (2002) J. Cell Biol. , vol.157 , pp. 327-336
    • Simons, M.1
  • 25
    • 0023613854 scopus 로고
    • Expression of a myelin basic protein gene in transgenic shiverer mice: Correction of the dysmyelinating phenotype
    • Readhead, C. et al. Expression of a myelin basic protein gene in transgenic shiverer mice: correction of the dysmyelinating phenotype. Cell 48, 703-712 (1987).
    • (1987) Cell , vol.48 , pp. 703-712
    • Readhead, C.1
  • 26
    • 0037230328 scopus 로고    scopus 로고
    • Outsourcing in the brain: Do neurons depend on cholesterol delivery by astrocytes?
    • Pfrieger, F.W. Outsourcing in the brain: do neurons depend on cholesterol delivery by astrocytes? Bioessays 25, 72-78 (2003).
    • (2003) Bioessays , vol.25 , pp. 72-78
    • Pfrieger, F.W.1
  • 27
    • 0035997373 scopus 로고    scopus 로고
    • Lipoprotein receptors in the nervous system
    • Herz, J. & Bock, H.H. Lipoprotein receptors in the nervous system. Annu. Rev. Biochem. 71, 405-434 (2002).
    • (2002) Annu. Rev. Biochem. , vol.71 , pp. 405-434
    • Herz, J.1    Bock, H.H.2
  • 28
    • 0033767315 scopus 로고    scopus 로고
    • Sonic hedgehog-regulated oligodendrocyte lineage genes encoding bHLH proteins in the mammalian central nervous system
    • Lu, Q.R. et al. Sonic hedgehog-regulated oligodendrocyte lineage genes encoding bHLH proteins in the mammalian central nervous system. Neuron 25, 317-329 (2000).
    • (2000) Neuron , vol.25 , pp. 317-329
    • Lu, Q.R.1
  • 29
    • 0035169326 scopus 로고    scopus 로고
    • Sonic hedgehog is required during an early phase of oligodendrocyte development in mammalian brain
    • Alberta, J.A. et al. Sonic hedgehog is required during an early phase of oligodendrocyte development in mammalian brain. Mol. Cell. Neurosci. 18, 434-441 (2001).
    • (2001) Mol. Cell. Neurosci. , vol.18 , pp. 434-441
    • Alberta, J.A.1
  • 30
    • 0344953585 scopus 로고    scopus 로고
    • A defective response to Hedgehog signaling in disorders of cholesterol biosynthesis
    • Cooper, M.K. et al. A defective response to Hedgehog signaling in disorders of cholesterol biosynthesis. Nat. Genet. 33, 508-513 (2003).
    • (2003) Nat. Genet. , vol.33 , pp. 508-513
    • Cooper, M.K.1
  • 31
    • 0034793082 scopus 로고    scopus 로고
    • Genetic disorders of cholesterol biosynthesis in mice and humans
    • Nwokoro, N.A., Wassif, O.A. & Porter, F.D. Genetic disorders of cholesterol biosynthesis in mice and humans. Mol. Genet. Metab. 74, 105-119 (2001).
    • (2001) Mol. Genet. Metab. , vol.74 , pp. 105-119
    • Nwokoro, N.A.1    Wassif, O.A.2    Porter, F.D.3
  • 32
    • 0016821785 scopus 로고
    • Effects of the cholesterol biosynthesis inhibitor ay9944 on organotypic cultures of mouse spinal cord. Retarded myelinogenesis and induction of cytoplasmic inclusions
    • Kim, S.U. Effects of the cholesterol biosynthesis inhibitor ay9944 on organotypic cultures of mouse spinal cord. Retarded myelinogenesis and induction of cytoplasmic inclusions. Lab. Invest. 32, 720-728 (1975).
    • (1975) Lab. Invest. , vol.32 , pp. 720-728
    • Kim, S.U.1
  • 33
    • 0033613147 scopus 로고    scopus 로고
    • A proteolytic pathway that controls the cholesterol content of membranes, cells, and blood
    • Brown, M.S. & Goldstein, J.L. A proteolytic pathway that controls the cholesterol content of membranes, cells, and blood. Proc. Natl. Acad. Sci. USA 96, 11041-11048 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 11041-11048
    • Brown, M.S.1    Goldstein, J.L.2
  • 34
    • 0141594942 scopus 로고    scopus 로고
    • Local regulation of fat metabolism in peripheral nerves
    • Verheijen, M.H., Chrast, R., Burrola, P. & Lemke, G. Local regulation of fat metabolism in peripheral nerves. Genes Dev. 17, 2450-2464 (2003).
    • (2003) Genes Dev. , vol.17 , pp. 2450-2464
    • Verheijen, M.H.1    Chrast, R.2    Burrola, P.3    Lemke, G.4
  • 35
    • 0347185347 scopus 로고    scopus 로고
    • Therapeutic administration of progesterone antagonist in a model of Charcot-Marie-Tooth disease (CMT-1A)
    • Sereda, M.W., Meyer Zu, H.G., Suter, U., Uzma, N. & Nave, K.A. Therapeutic administration of progesterone antagonist in a model of Charcot-Marie-Tooth disease (CMT-1A). Nat. Med. 9, 1533-1537 (2003).
    • (2003) Nat. Med. , vol.9 , pp. 1533-1537
    • Sereda, M.W.1    Meyer Zu, H.G.2    Suter, U.3    Uzma, N.4    Nave, K.A.5
  • 37
    • 0023623847 scopus 로고
    • Myelin deficient mice: Expression of myelin basic protein and generation of mice with varying levels of myelin
    • Popko, B. et al. Myelin deficient mice: expression of myelin basic protein and generation of mice with varying levels of myelin. Cell 48, 713-721 (1987).
    • (1987) Cell , vol.48 , pp. 713-721
    • Popko, B.1
  • 38
    • 2442557294 scopus 로고    scopus 로고
    • Brain cholesterol: Long secret life behind a barrier
    • Bjorkhem, I. & Meaney, S. Brain cholesterol: long secret life behind a barrier. Arterioscler. Thromb. Vasc. Biol. 24, 806-815 (2004).
    • (2004) Arterioscler. Thromb. Vasc. Biol. , vol.24 , pp. 806-815
    • Bjorkhem, I.1    Meaney, S.2
  • 39
    • 0347623324 scopus 로고    scopus 로고
    • Generation of viable cholesterol-free mice
    • Wechsler, A. et al. Generation of viable cholesterol-free mice. Science 302, 2087 (2003).
    • (2003) Science , vol.302 , pp. 2087
    • Wechsler, A.1
  • 40
    • 0026264296 scopus 로고
    • Gene targeting and gene trap screens using embryonic stem cells: New approaches to mammalian development
    • Joyner, A.L. Gene targeting and gene trap screens using embryonic stem cells: new approaches to mammalian development. Bioessays 13, 649-656 (1991).
    • (1991) Bioessays , vol.13 , pp. 649-656
    • Joyner, A.L.1
  • 41
    • 0014241360 scopus 로고
    • A rotarod suitable for quantitative measurements of motor incoordination in naive mice
    • Jones, B.J. & Roberts, D.J. A rotarod suitable for quantitative measurements of motor incoordination in naive mice. Naunyn Schmiedebergs Arch. Exp. Pathol. Pharmakol. 259, 211 (1968).
    • (1968) Naunyn Schmiedebergs Arch. Exp. Pathol. Pharmakol. , vol.259 , pp. 211
    • Jones, B.J.1    Roberts, D.J.2
  • 42
    • 0027773169 scopus 로고
    • A single protocol to detect transcripts of various types and expression levels in neural tissue and cultured cells: In situ hybridization using digoxigenin-labelled cRNA probes
    • Schaeren-Wiemers, N. & Gerfin-Moser, A. A single protocol to detect transcripts of various types and expression levels in neural tissue and cultured cells: in situ hybridization using digoxigenin-labelled cRNA probes. Histochemistry 100, 431-440 (1993).
    • (1993) Histochemistry , vol.100 , pp. 431-440
    • Schaeren-Wiemers, N.1    Gerfin-Moser, A.2
  • 43
    • 0036582979 scopus 로고    scopus 로고
    • Patterns of Nogo mRNA and protein expression in the developing and adult rat and after CNS lesions
    • Huber, A.B., Weinmann, O., Brosamle, C., Oertle, T. & Schwab, M.E. Patterns of Nogo mRNA and protein expression in the developing and adult rat and after CNS lesions J. Neurosci. 22, 3553-3567 (2002).
    • (2002) J. Neurosci. , vol.22 , pp. 3553-3567
    • Huber, A.B.1    Weinmann, O.2    Brosamle, C.3    Oertle, T.4    Schwab, M.E.5
  • 44
    • 0029845073 scopus 로고    scopus 로고
    • Monoclonal antibody 010 defines & conformationally sensitive cell-surface epitope of proteohpid protein (PLP): Evidence that PLP misfolding underlies dysmyelination in mutant mice
    • Jung, M., Sommer, I., Schachner, M. & Nave, K.A. Monoclonal antibody 010 defines & conformationally sensitive cell-surface epitope of proteohpid protein (PLP): evidence that PLP misfolding underlies dysmyelination in mutant mice. J. Neurosci. 16, 7920-7929 (1996).
    • (1996) J. Neurosci. , vol.16 , pp. 7920-7929
    • Jung, M.1    Sommer, I.2    Schachner, M.3    Nave, K.A.4
  • 45
    • 0015857284 scopus 로고
    • Myelination in rat brain: Method of myelin isolation
    • Norton, W.T. & Poduslo, S.E. Myelination in rat brain: method of myelin isolation J. Neurochem. 21, 749-757 (1973).
    • (1973) J. Neurochem. , vol.21 , pp. 749-757
    • Norton, W.T.1    Poduslo, S.E.2
  • 46
    • 0026512314 scopus 로고
    • Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface
    • Brown, D.A. & Rose, J.K. Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface. Cell 68, 533-544 (1992).
    • (1992) Cell , vol.68 , pp. 533-544
    • Brown, D.A.1    Rose, J.K.2
  • 47
    • 0037443707 scopus 로고    scopus 로고
    • Normal metabolism but different physical properties of myelin from mice deficient in proteolipid protein
    • Jurevics, H. et al. Normal metabolism but different physical properties of myelin from mice deficient in proteolipid protein. J. Neurosci. Res. 71, 826-834 (2003).
    • (2003) J. Neurosci. Res. , vol.71 , pp. 826-834
    • Jurevics, H.1
  • 48
    • 0032762728 scopus 로고    scopus 로고
    • Separation of the intracellular secretory compartment of rat liver and isolated rat hepatocytes in a single step using self-generating gradients of lodixanol
    • Plonne, D. et al. Separation of the intracellular secretory compartment of rat liver and isolated rat hepatocytes in a single step using self-generating gradients of lodixanol Anal. Biochem. 276, 88-96 (1999).
    • (1999) Anal. Biochem. , vol.276 , pp. 88-96
    • Plonne, D.1
  • 49
    • 33845261493 scopus 로고
    • A rapid method of total lipid extraction and purification
    • Bligh, E.G. & Dyer, W.J. A rapid method of total lipid extraction and purification Can. J. Med. Sci. 37, 911-917 (1959).
    • (1959) Can. J. Med. Sci. , vol.37 , pp. 911-917
    • Bligh, E.G.1    Dyer, W.J.2


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