Abstract
The interaction of human myelin basic protein with lipophilin has been demonstrated by affinity chromatography. The interaction was specific since neither basic protein, nor albumin bound to an affinity column consisting of BP bound to agarose. Conversely an albumin affinity column failed to bind BP. The pH dependency of the interaction correlated with the known pK for histidine. By the use of large peptides formed by tryptophanyl cleavage by BNPS-skatole, peptide 1–117 bound to the BP affinity column while neither the smaller peptide, 118–170, nor the synthetic nonapeptide bound. The large fragment contains 9 of the 10 histidines in the molecule which may explain the binding of this fragment. The result of such protein-protein interactions makes available a large number of new antigenic sites and extends considerably the range of encephalitogens for disease induction.
Similar content being viewed by others
References
Boggs, J. M., Moscarello, M. A., andPapahadjopoulos, D. 1982.in Jost, P. andGriffith, O. H., (eds.), Lipid-Protein Interactions. Vol. II, Academic Press, New York.
Kies, M. W., andAlvord, E. C., Jr. 1959. Encephalitogenic activity in guinea pigs of water-soluble protein fractions of nervous tissue. Pages 293–299,in Kies, M. W., andAlvord, E. C. Jr., (eds.), “Allergic” Encephalomyelitis Thomas Springfield, Ill.
Roboz-Einstein, E., Robertson, D. M., DiCaprio, J. M., andMoore, W. 1962. The isolation from bovine spinal cord of a homogeneous protein with encephalitogenic activity. J. Neurochem. 9:353–361.
Waksman, B. H., Porter, H., Lees, M. B., Adams, R. D., andFolch, J. 1954. A study of the chemical nature of components of bovine white matter effective in producing allergic encephalomyelitis in the rabbit. J. Exptl. Med. 100:451–459.
Hashim, G. A., Wood, D. D., andMoscarello, M. A. 1980. Myelin lipophilin-induced demyelinating disease of the central nervous system. Neurochem. Res. 5:1137–1145.
Hashim, G. A. 1978. Myelin basic protein: Structure, Function and Antigenic Determinants. Immunol. Rev. 39:60–107.
Boggs, J. M., Samji, N., Moscarello, M. A., Hashim, G. A., andDay, E. 1983. Immune lysis of reconstituted myelin basic protein-lipid vesicles and myelin vesicles. J. Immunol. 130:1687–1694.
Stollery, J., Boggs, J. M., andMoscarello, M. A. 1980. The variable interaction of human myelin basic protein with different acidic lipids. Biochemistry 19:1219–1226.
Boggs, J. M., Stollery, J., andMoscarello, M. A. 1980. Effect of lipid environment on the motion of a spin-label covalently bound to myelin basic protein. Biochemistry 19:1226–1234.
Madrid, R. E., Wisniewski, H. M., Hashim, G. A., Fredane, L., Wood, D. D., andMoscarello, M. A. 1982. The potentiating effect of lipophilin upon myelin basic protein-induced EAE in guinea pigs. Trans. Amer. Soc. Neurochem. 13:211.
Crang, A. J., andRumsby, M. G. 1977. Molecular organization of lipid and protein in the myelin sheath. Biochem. Soc. Trans. 5:1431–1434.
Lowden, J. A., Moscarello, M. A., andMorecki, R. 1966. The isolation and characterization of an acid-soluble protein from myelin. Can. J. Biochem. 44:567–577.
Gagnon, J., Finch, P. R., Wood, D. D., andMoscarello, M. A. 1971. Isolation of a highly purified myelin protein. Biochemistry 10:4756–4762.
Markwell, M. A. K. 1982. A new solid-state reagent to iodinate proteins. I. Conditions for the efficient labelling of antiserum. Anal. Biochem. 125:427–432.
Martenson, R. E., Diebler, G. E., Kramer, A. J., andLevine, S. 1975. Comparative studies of guinea pig and bovine myelin basic proteins. Partial characterization of chemically derived fragments and their encephalitogenic activities in Lewis Rats. J. Neurochem. 24:173–182.
Cockle, S. A., Epand, R. M., andMoscarello, M. A. 1978. Resistance of lipophilin, a hydrophobic myelin protein, to denaturation by urea and guanidinium salts. J. Biol. Chem. 253:8019–8026.
Braun, P. E. 1977. Molecular architecture of myelin Pages 91–115,in P. Morell, (ed.), Myelin. Plenum Press, New York.
Smith, R. 1977. Non-covalent cross-linking of lipid bilayers by myelin basic protein. A possible role in myelin formation. Biochim. Biophys. Acta 470:170–184.
Smith, R. 1980. Sedimentation analysis of the self-association of bovine myelin basic protein. Biochemistry 19:1826–1831.
Burns, P. F., Campagnoni, C. W., Chalken, I. M., andCampagnoni, A. T. 1981. Interactions of free and immobilized myelin basic protein with anionic detergents. Biochemistry 20:2463–2469.
Author information
Authors and Affiliations
Additional information
Special Issue dedicated to Dr. Elizabeth Roboz-Einstein.
Rights and permissions
About this article
Cite this article
Wood, D.D., Vella, G.J. & Moscarello, M.A. Interaction between human myelin basic protein and lipophilin. Neurochem Res 9, 1523–1531 (1984). https://doi.org/10.1007/BF00964678
Accepted:
Issue Date:
DOI: https://doi.org/10.1007/BF00964678