Skip to main content
Log in

Distribution of lipid synthesizing enzymes, 2′,3′-cyclic nucleotide 3′-phosphodiesterase, and myelin proteins in rat forebrain subfractions during development

  • Original Articles
  • Published:
Neurochemical Research Aims and scope Submit manuscript

Abstract

The distribution of UDP-galactose: ceramide galactosyltransferase (CGalT) was studied in subcellular fractions of rat forebrain during development using zonal centrifugation on linear gradients. Specialized subfractions: SN 1, a microsomal fraction, SN 4, a myelin-related fraction, and purified myelin were also used for this study. For comparison, two microsomal lipid synthesizing enzymes, a myelin-specific enzyme, 2′,3′-cyclic nucleotide 3′-phosphodiesterase and myelin proteins were measured in the same subfractions. UDP-glucose: ceramide glucosyltransferase and cerebroside sulfotransferase were confined to microsomes. CGalT was ferase and cerebroside sulfotransferase were confined to microsomes. CGalT was localized in microsomes, but also in myelin and myelin-related fractions. The developmental change in distribution of CGalT in adult animals toward myelin containing fractions could indicate that the replacement of galactosylceramide in compact myelin could be carried out in close proximity to compact myelin (mesaxon, paranodal loops) rather than in the distant oligodendrocyte perikaryon.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Similar content being viewed by others

References

  1. Burkart, T., Siegrist, H. P., Herschkowitz, N. N., andWiesmann, U. N. 1977. 3′-Phosphoadenylsulfate: galactosylceramide 3′-sulfotransferase. An optimized assay in homogenates of developing brain. Biochim. Biophys. Acta 483:303–311.

    Google Scholar 

  2. Cestelli, A., White, F. V., andCostantino-Ceccarini, E. 1979. The use of liposomes as acceptors for the assay of lipid glycosyltransferases from rat brain. Biochim. Biophys. Acta 572:283–292.

    Google Scholar 

  3. Costantino-Ceccarini, E., andSuzuki, K. 1975. Evidence for the presence of UDP-galactose: ceramide galactosyltransferase in rat myelin. Brain Res. 93:358–362.

    Google Scholar 

  4. Costantino-Ceccarini, E., Cestelli, A., andDeVries, G. H. 1979. Characterization and developmental changes of UDP-galactose: ceramide galactosyltransferase in a rat CNS axolemma-enriched fraction. Differences and similarities of the enzyme associated with the microsomal and myelin fractions. J. Neurochem. 32:1175–1182.

    Google Scholar 

  5. Jungalwala, F. B. 1974. Synthesis and turnover of cerebroside sulfate of myelin in adult and developing rat brain. J. Lipid Res. 15:114–123.

    Google Scholar 

  6. Koul, O., Chou, K.-H., andJungalwala, F. B. 1980. UDP-galactose: ceramide galactosyltransferase in rat brain myelin subfractions during development. Biochem. J. 186:959–969.

    Google Scholar 

  7. Kurihara, T. andTsukada, Y. 1967. The regional and subcellular distribution of 2′,3′-cyclic nucleotide 3′-phosphohydrolase in the central nervous system. J. Neurochem. 14:1167–1174.

    Google Scholar 

  8. Lowry, O. H., Rosebrough, N. J., Farr, A. L., andRandall, R. J. 1951. Protein measurement with the Folin phenol reagent. J. Biol. Chem. 193:265–275.

    Google Scholar 

  9. Matthieu, J.-M., Honegger, P., Favrod, P., Gautier, E., andDolivo, M. 1979. Biochemical characterization of a myelin fraction isolated from rat brain aggregating cell cultures. J. Neurochem. 32:869–881.

    Google Scholar 

  10. Nescovic, N. M., Sarlieve, L. L., andMandel, P. 1973. Subcellular and submicrosomal distribution of glycolipidsynthesizing transferases in young rat brain. J. Neurochem. 20:1419–1430.

    Google Scholar 

  11. Norton, W. T. 1980. Myelin enzymes: indicators of non-insulating functions. Pages 64–75.in Boese, A. (ed.), Search for the cause of multiple sclerosis and other chronic diseases of the central nervous system, Verlag Chemie, Weinheim, FRG.

    Google Scholar 

  12. Sims, N. R., andCarnegie, P. R. 1978. 2′,3′-Cyclic nucleotide 3′-phosphodiesterase. Adv. Neurochem. 3:1–41.

    Google Scholar 

  13. Suzuki, K. 1980. Myelin-associated enzymes. Pages 333–347,in Baumann, N. (ed.), Elsevier/North-Holland Biomedical Press, Amsterdam, Neurological Mutations Affecting Myelination INSERM Symposium No. 14.

    Google Scholar 

  14. Waehneldt, T. V. 1975. Ontogenetic study of a myelin-derived fraction with 2′,3′-cyclic nucleotide 3′-phosphohydrolase activity higher than that of myelin. Biochem. J. 151:435–437.

    Google Scholar 

  15. Waehneldt, T. V. 1978. Density and protein profiles of myelin from two regions of young and adult rat CNS. Brain Res. Bull. 3:37–44.

    Google Scholar 

  16. Waehneldt, T. V., andLane, J. D. 1980. Dissociation of myelin from its “enzyme markers” during ontogeny. J. Neurochem. 35:566–573.

    Google Scholar 

  17. Waehneldt, T. V., Matthieu, J.-M., andNeuhoff, V. 1977. Characterization of a myelin-related fraction (SN 4) isolated from rat forebrain at two developmental stages. Brain Res. 138:29–43.

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

Costantino-Ceccarini, E., Waehneldt, T.V., Ginalski, H. et al. Distribution of lipid synthesizing enzymes, 2′,3′-cyclic nucleotide 3′-phosphodiesterase, and myelin proteins in rat forebrain subfractions during development. Neurochem Res 7, 1–12 (1982). https://doi.org/10.1007/BF00965064

Download citation

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00965064

Keywords

Navigation