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The Molecular Architecture of Myelin: Identification of the External Surface Membrane Components

  • Joseph F. Poduslo
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 100)

Summary

Basic information concerning the molecular organization of the myelin membrane is an intrinsic requirement for understanding the neurochemical events leading to myelination, as well as the potential mechanism of demyelination that might exist at the molecular level for a variety of neurological diseases. The application of chemical, enzymatic, fluorescent, and immunological membrane probes has contributed significantly to this end, although the diverse structural complexity of the myelin sheath has permitted only a rudimentary understanding of its molecular organization. Nevertheless, compelling evidence is accumulating which suggests that components of myelin are asymmetrically distributed in the membrane. Such membrane asymmetry should not only provide important clues to the mechanisms of membrane assembly in the process of myelination, but should also serve as a paradigm for potential functional asymmetry of the individual components at the molecular level. One particularly useful membrane probe is galactose oxidase which has the capacity for identifying surface galactose residues in both glycoproteins and glycolipids on the external surface of the myelin sheath. The identification of these surface components on the myelin sheath is of primary importance since such components might be more readily susceptible to immunological damage or act as a viral receptor which ultimately might lead to demyelination.

Keywords

Myelin Sheath High Molecular Weight Protein Proteolipid Protein Purple Membrane Myelin Membrane 
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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References

  1. 1.
    Abramson, M.B., Norton, W.T. and Kutzman, R., Study of ionic structures in phospholipids by infrared spectra, J. Biol. Chem. 240 (1965) 2389–2395.PubMedGoogle Scholar
  2. 2.
    Blaurock, A.E. and King, G.I., Asymmetric structure of the purple membrane, Science 196 (1977) 1101–1104.PubMedCrossRefGoogle Scholar
  3. 3.
    Boggs, J.M., Wood, D.D., Moscarello, M.A. and Papahadjopoulos, D., Lipid phase separation induced by a hydrophobic protein in phosphatidyserine-phosphatidylcholine vesicles, Biochemistry 16 (1977) 2325–2329.PubMedCrossRefGoogle Scholar
  4. 4.
    Curatolo, W., Sakura, J.D., Small, D.M. and Shipley, G.G., Protein-lipid interactions: Recombinants of the proteolipid apoprotein of myelin with dimyristoyllecithin, Biochemistry 16 (1977) 2313–2319.PubMedCrossRefGoogle Scholar
  5. 5.
    Dea, P., Chan, S.I. and Dea, F.J., High-resolution proton magnetic resonance spectra of a rabbit sciatic nerve, Science 175 (1972) 206–209.PubMedCrossRefGoogle Scholar
  6. 6.
    Feinstein, M.B. and Felsenfeld, H., Reactions of fluorescent probes with normal and chemically modified myelin, Biochemistry 14 (1975) 3041–3048.PubMedCrossRefGoogle Scholar
  7. 7.
    Feinstein, M.B. and Felsenfeld, H., Reactions of fluorescent probes with normal and chemically modified myelin basic protein and proteolipid. Comparisons with myelin, Biochemistry 14 (1975) 3049–3056.PubMedCrossRefGoogle Scholar
  8. 8.
    Fisher, K.A., Analysis of membrane halves: Cholesterol, Proc. Nat. Acad. Sci. USA 73 (1976) 173–177.PubMedCrossRefGoogle Scholar
  9. 9.
    Gahmberg, C.G. and Hakomori, S., External labelling of cell surface galactose and galactosamine in glycolipid and glycoprotein of human erythrocytes, J. Biol. Chem. 248 (1973) 4311–4317.PubMedGoogle Scholar
  10. 10.
    Gottlieb, M.H., The reactivity of human erythrocyte membrane cholesterol with a cholesterol oxidase, Biochim. Biophys.Acta 466 (1977) 422–428.PubMedCrossRefGoogle Scholar
  11. 11.
    Henderson, R. and Unwin, P.N.T., Three-dimensional model of purple membrane obtained by electron microscopy, Nature 257 (1975) 28–32.PubMedCrossRefGoogle Scholar
  12. 12.
    Herndon, R.M., Rauch, H.C. and Einstein, E.R., Immuno-electron microscopic localization of the encephalitogenic basic protein in myelin, Immunol. Comm. 2 (1973) 163–172.Google Scholar
  13. 13.
    Higgins, J.A., Florendo, N.T. and Barrnett, R.J., Localization of cholesterol in membranes of erythrocyte ghosts, J. Ultrastruct. Res. 42 (1973) 66–81.PubMedCrossRefGoogle Scholar
  14. 14.
    Lenard, J. and Rothmun, J.E., Transbilayer distribution and movement of cholesterol and phospholipid in the membrane of influenza virus, Proc. Nat. Acad. Sci. USA 73 (1976) 391–395.PubMedCrossRefGoogle Scholar
  15. 15.
    Norton, W.T. and Poduslo, S.E., Myelination in rat brain. Method of myelin isolation, J. Neurochem. 21 (1973) 749–757.PubMedCrossRefGoogle Scholar
  16. 16.
    Pieringer, R.A., Deshmukh, D.S. and Flynn, T.J., The association of the galactosyl diglycerides of nerve tissue with myelination, Progress in Brain Res. 40 (1973) 397–405.CrossRefGoogle Scholar
  17. 17.
    Poduslo, J.F., J. Biol. Chem.(1977), submitted for publication.Google Scholar
  18. 18.
    Poduslo, J.F. and Braun, P.E., Topographical arrangement of membrane proteins in the intact myelin sheath, J. Biol. Chem. 250 (1975) 1099–1105.PubMedGoogle Scholar
  19. 19.
    Poduslo, J.F., Quarles, R.H. and Brady, R.O., External labeling of galactose in surface membrane glycoproteins of the intact myelin sheath, J. Biol. Chem. 251 (1976) 153–158.PubMedGoogle Scholar
  20. 20.
    Poduslo, J.F., Everly, J.L. and Quarles, R.H., A low molecular weight glycoprotein associated with isolated myelin: Distinction from myelin proteolipid protein, J. Neurochem. 28 (1977) 977–986.PubMedCrossRefGoogle Scholar
  21. 21.
    Singer, S.J. and Nicolson, G.L., The fluid mosaic model of the structure of cell membranes, Science 175 (1972) 720–731.PubMedCrossRefGoogle Scholar
  22. 22.
    Steck, T.L., The organization of proteins in human erythrocyte membranes, in Membrane Research ( C.F. Fox, ed.) Academic Press, New York (1972) pp. 71–93.Google Scholar
  23. 23.
    Steck, T.L. and Dawson, G., Topographical distribution of complex carbohydrates in the erythrocyte membrane, J. Biol. Chem. 249 (1974) 2135–2142.PubMedGoogle Scholar
  24. 24.
    Vanderkooi, G. and Green, D.E., Biological membrane structure, I. The protein crystal model for membranes, Proc. Nat. Acad. Sci. 66 (1970) 615–621.PubMedCrossRefGoogle Scholar
  25. 25.
    Wallach, D.F.H. and Zahler, P.H., Protein conformations in cellular membranes, Proc. Nat. Acad. Sci. 56 (1966) 1552–1559.PubMedCrossRefGoogle Scholar
  26. 26.
    Williams, E.C. and Cordes, E.H., Natural abundance carbon-13 nuclear magnetic resonance studies of bovine white matter and myelin, Biochemists 15 (1976) 5792–5799.CrossRefGoogle Scholar
  27. 27.
    Wood, D.D., Epand, R.M. and Moscarello, M.A., Localization of the basic protein and lipophilin in the myelin membrane with a non-penetrating reagent, Biochim. Biophys. Acta 467 (1977) 120–129.CrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1978

Authors and Affiliations

  • Joseph F. Poduslo
    • 1
  1. 1.Neuroimmunology Branch, National Institute of Neurological and Communicative Disorders and StrokeNational Institutes of HealthBethesdaUSA

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