Molecular Organisation in Central Nerve Myelin

  • A. J. Crang
  • M. G. Rumsby
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 100)


Pertinent data from the literature and in press is summarised and used to construct a model for the molecular arrangement of lipid and protein in the lamellae of compact central nerve myelin. For the lipid phase of myelin the available data is best interpreted in terms of a bilayer arrangement while physical studies suggest that the lipids are in an intermediate fluid state maintained by the presence of cholesterol and water in the system. Lipids will interact to maintain this condition. The proteins of myelin differ in their membrane locations. The high molecular weight proteins are considered to be intrinsic components with at least part of their polypeptide chains in the lipid phase. The proteolipid protein is also intrinsic and may be completely buried in the lipid phase. The basic protein of myelin is an extrinsic component and must be localised at the surface of the lipid phase at either the external or cytoplasmic face of the lamellae. Present results suggest an elusive location at the cytoplasmic apposition region. The lipid-interacting properties of the basic protein are segregated on the polypeptide chain of the molecule and this may be important for the possible role of the basic protein in bridging adjacent lamellae at the cytoplasmic apposition. It is speculated that association of the proteolipid protein with the basic protein in a 1:1 molar ratio would form an effective lipid-complexing nucleus in the lipid rich myelin lamellae but experimental data to support this idea is lacking at present.


Myelin Basic Protein Basic Protein Myelin Sheath Lipid Phase High Molecular Weight Protein 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


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  1. 1.
    Braun, P.E. and Radin, N.S., Interactions of lipids with a membrane structural protein from myelin, Biochem. 8 (1969)4310–4313.Google Scholar
  2. Brostoff, S. and Eylar, E.H., Localisation of methylated arginine in the Al protein from myelin, Proc. Natl. Acad. Sci. U.S. 68 (1971) 765–769.Google Scholar
  3. 3.
    Carnegie, P.R. and Dunkley, P.R., Basic proteins of central and peripheral nervous system myelin, in: Advances in Neurochemistry (B.W. Agranoff and M.H. Aprison, eds.) Vol. 1, Plenum Press, New York (1975) pp. 95–126.Google Scholar
  4. Chapman, B.E. and Moore, W.J., Conformation of the myelin basic protein in aqueous solution from nuclear magnetic resonance spectroscopy, Biochem. Biophys. Res. Comm. 73 (1976) 758–766.Google Scholar
  5. Clowes, A.W., Cherry, R.J. and Chapman, D., Physical properties of lecithin-cerebroside films, Biochim. Biophys. Acta 249 (1971) 301–307.Google Scholar
  6. 6.
    Crang, A.J., Grainger, J.M. and Rumsby, M.G., Covalent probe investigations with central nerve myelin, in: Myelination and Demyelination, Recent Chemical Advances, Satellite Symposium of the ISN, Helsinki, August 1977.Google Scholar
  7. Crang, A.J. and Rumsby, M.G., The labelling of lipid and protein components in isolated central nervous system myelin with dansyl chloride, Biochem. Soc. Trans. 5 (1977) 110–112.Google Scholar
  8. 8.
    Epand, R.M., Moscarello, M.A., Zierenberg, B. and Vail, W.J., The folded conformation of the encephalitogenic protein of the human brain, Biochem. 13 (197L) 1264–1267.Google Scholar
  9. 9.
    Eylar, E.H., Amino acid sequence of the basic protein of the myelin membrane, Proc. Nat_. Acad. Sci. U.S. 67 (1970) 14251431.Google Scholar
  10. 10.
    Finean, J.B., Phospholipid-cholesterol complex in the structure of myelin, Experientia 9 (1953) 17.Google Scholar
  11. Finean, J.B. and Burge, R.E., The determination of the Fourier transform of the myelin layer from a study of swelling phenomena, J. Mol. Biol. 1 (1963)Google Scholar
  12. 12.
    Golds, E.E. and Braun, P.E., Organisation of membrane proteins in the intact myelin sheath, J. Biol. Chem. (1976) 4729-4735.Google Scholar
  13. 13.
    Green, D.E., Membrane proteins, Science 174 (1971) 863–867.Google Scholar
  14. 14.
    Guidotti, G., Membrane proteins, Ann. Rev. Biochem. 41 (1972) 731-752.Google Scholar
  15. 15.
    Henn, F.A. and Thompson, T.E., Properties of lipid bilayer membranes separating two aqueous phases: composition studies J. Mol. Biol. 31 (1968) 227-235.Google Scholar
  16. 16.
    Jones, A.J.S. and Rumsby, M.G., Intrinsic fluorescence properties of the myelin basic protein, J. Neurochem. 25 (1975) 565-572.Google Scholar
  17. 17.
    Jones, A.J.S. and Rumsby, M.G., Localisation of sites for ionic interaction with lipid in the C-terminal third of the bovine myelin basic protein, Biochem. J. (1977) in press.Google Scholar
  18. de Kruyff, B., VanDijek, P.W.M., Demel, R.A., Schnijff, A., Brants, F. and van Deenen, L.L.M., Non-randon distribution of cholesterol in phosphatidyl choline bilayers, Biochim. Biophys. Acta 350 (1974) 1–7.Google Scholar
  19. Ladbrooke, B.D., Jenkinson, T.J., Kamat, V.B. and Chapman, D., Physical studies on myelin, Biochim. Biophys. Acta 164 (1968) 101–109.Google Scholar
  20. 20.
    Liebes, L.F., Zand, R. and Phillips, W.D., Solution behaviour, circular dichroism and 220 MHz PMR studies on the bovine myelin basic protein, Biochim. Biophys. Acta (1975) 27-39.Google Scholar
  21. 21.
    Linington, C. and Rumsby, M.G., On the accessibility and localisation of cerebrosides in central nervous system myelin, in: Myelination and Demyelination, Recent Chemical Advances, Satellite symposium of the ISN, Helsinki, August 1977.Google Scholar
  22. London, Y., Demel, R.A., Beurts van Kessel, W.S.M., Vossenberg, F.G.A. and van Deenen, L.L.M., The protection of Al myelin basic protein against the action of proteolytic enzymes after interaction of the protein with lipids at the air-water interface, Biochim. Biophys. Acta 311 (1973) 520–530.Google Scholar
  23. London, Y. and Vossenberg, F.G.A., Specific interaction of central nervous system myelin basic protein with lipids, Biochim. Biophys. Acts, 307 (1973) 478–490.Google Scholar
  24. McIntosh, T.J. and Robertson, J.D., Observations on the effect of hypotonic solutions on the myelin sheath in the central nervous system, J. Mol. Biol. 100 (1975) 213–217.Google Scholar
  25. 25.
    Mokrasch, L.C., Bear, R.S. and Schmitt, F.O., Myelin, Neurosciences Research Bulletin 9 (1971) 440–598.Google Scholar
  26. 26.
    Norton, W.T., Myelin: Structure and biochemistry, in: The Nervous System (D.B. Tower, ed.) Vol. 1, Raven Press, New York (1975) pp. 467–481.Google Scholar
  27. Nussbaum, J.L., Rouayrenc, J.L., Mandel, P., Jolles, J. and Jolles, P., Isolation and terminal sequence determination of the major rat brain myelin proteolipid P7 apoprotein, Biochem. Biophys. Res. Comm. 57 (1974) 1240–1247.Google Scholar
  28. 28.
    Olive, J., Cryo-ultramicrotomy and freeze-etching of lipid-water phases, in: Freeze Etching Techniques and Applications ( E.L. Benedetti and P. Favard, eds.) S.F.M.E., Paris (1973) pp. 187–198.Google Scholar
  29. Palmer, F. and Dawson, R.M.C., The isolation and properties of experimental allergic encephalitogenic protein, Biochem. J. 111 (1969) 629–636.Google Scholar
  30. 30.
    Papahadjopoulos, D., Moscarello, M., Eyler, E.H. and Isac, T., Effects of proteins on thermotropic phase transitions of phospholipid membranes, Biochim. Biophys. Acta 401 (1975) 317-335.Google Scholar
  31. 31.
    Papahadjopoulos, D., Vail, W.J. and Moscarello, M., Interaction of a purified hydrophobic protein from myelin with phospholipid membranes, J. Membrane Biol. 22 (1975) 143–164.Google Scholar
  32. Pascher, J. Molecular arrangements in sphingolipids: Conformation and hydrogen bonding of ceramide and their implication in membrane stability and permeability, Biochim. Biophys. Acta 455 (1976) 431–451.Google Scholar
  33. 33.
    Poduslo, J.F., Distribution of galactose residues in surface membrane glycoproteins and glycolipids of the intact myelin sheath, Fifth ISN Conference, Barcelona (1975) Abstract No. 319Google Scholar
  34. Poduslo, J.F. and Braun, P.E., Topographical arrangement of membrane proteins in the intact myelin sheath, J. Biol. Chem. 250 (1975) 1099–1105.Google Scholar
  35. Reynolds, J.A. and Green, H.O., Polypeptide chains from porcine cerebral myelin, J. Biol. Chem. 248 (1973) 1207–1210.Google Scholar
  36. 36.
    Rumsby, M.G. and Crang, A.J., The myelin sheath - a structural examination, in: Cell Surface Reviews (G. Poste and G.L. Nicholson, eds.) Vol. 4, North Holland, New York (1977) in press.Google Scholar
  37. 37.
    Rumsby, M.G. and Grainger, J.M., Reaction of the covalentlybinding probes trinitrobenzene sulphonic acid and dinitrofluorobenzene with isolated myelin sheath preparations, Biochem. Soc. Trans. 5 (1977) in press.Google Scholar
  38. 38.
    daSilva, ±.P. and Miller, R.G., Membrane particles on fracture faces of frozen myelin, Proc. Natl. Acad. Sci. U.S. 72 (1975)404–406.Google Scholar
  39. 39.
    Vandenheuvel, F.A., Biological structure at the molecular level with stereomodel projections, J. Am. Oil Chem. Soc. 40 (1963) 455–472.Google Scholar

Copyright information

© Plenum Press, New York 1978

Authors and Affiliations

  • A. J. Crang
    • 1
  • M. G. Rumsby
    • 1
  1. 1.Department of BiologyUniversity of York HeslingtonYorkUK

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