Advertisement

Enzymic Studies on Glial and Neuronal Cells during Myelination

  • Helmut Woelk
  • Rosemarie Jahrreiss
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 100)

Summary

The formation of ethanolamine plasmalogen from labelled 1-alkyl-2-acyl-sn-glycero-3-phosphorylethanolamine was studied in neurons and glial cells of the developing rat brain. It was found that the conversion of the ether to the enol-ether bond of the 1-alkyl moiety by the neuronal and glial desaturase system requires unsaturated fatty acids at the 2 position of the substrate. There is almost no difference between the activity of the neuronal and glial desaturase during the period of active niyelination, whereas the neuronal cell fraction of the adult rats displays a threefold higher enzyme activity as compared to the glial cells.

Evidence for the involvement of a microsomal electrion transport system in the enzymic conversion of alkylacyl-glycero-3-phosphorylethanolamine to ethanolamine plasmalogen was obtained by using specific antibodies against NADH-cytochrome b5 reductase. Cytochrome b5 stimulated the biosynthesis of ethanolamine plasmalogen.

Keywords

Glial Cell Neuronal Cell Body Pyridine Nucleotide Rabbit Brain Label Fatty Acid 
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.

Abbreviations used

GPC

sn-glycero-3-phosphorylcholine

GPE

sn-glycero-3-phosphoryl­ethanolamine

GPS

sn-glycero-3-phosphorylserine.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. 1.
    Blank, M.L., Wykle, R.L. and Snyder, F., Enzymic synthesis of ethanolamine plasmalogens from an O-alkyl glycerolipid, FEBS Lett. 18 (1971) 92–94.PubMedCrossRefGoogle Scholar
  2. 2.
    Blomstrand, C. and Hamberger, A., Protein turnover in cell-enriched fractions from rabbit brain, J. Neurochem. 16 (1969) 1401–1407.PubMedCrossRefGoogle Scholar
  3. 3.
    Blomstrand, C. and Hamberger, A., Amino acid incorporation in vitro into protein of neuronal and glial cell-enriched fractions, J. Neurochem. 17 (1970) 1187–1195.PubMedCrossRefGoogle Scholar
  4. 4.
    Dawson, R.M.C., A hydrolytic procedure for the identification and estimation of individual phospholipids in biological samples, Biochem. J. 75 (1960) 45–53.PubMedGoogle Scholar
  5. 5.
    Freysz, L., Bieth, R. and Mandel, P., Kinetics of the biosynthesis of phospholipids in neurons and glial-cells isolated from rat brain cortex, J. Neurochem. 16 (1969) 1417–1424.PubMedCrossRefGoogle Scholar
  6. 6.
    Goracci, G., Blomstrand, C., Arienti, G., Bamberger, A. and Porcellati, G., Base-exchange enzymic system for the synthesis of phospholipids in neuronal and glial cells and their sub-fractions: a possible marker for neuronal membranes, J. Neurochem. 20 (1973) 1167–1180.PubMedCrossRefGoogle Scholar
  7. 7.
    Oshino, N. and Omura, T., Immunochemical evidence for the participation of cytochrome b5 in microsomal stearoyl-CoA desaturation reaction, Arch. Biochem. Biophys. 157 (1973) 395–404.CrossRefGoogle Scholar
  8. 8.
    Paltauf, F., Prough, R.A., Masters, B.S.S. and Johnston, J.M., Evidence for the participation of cytochrome b5 in plasmalogen biosynthesis, J. Biol. Chem. 249 (1974) 2661–2662.Google Scholar
  9. 9.
    Poduslo, S.E. and Norton, W.T., Isolation and some chemical properties of oligodendroglia from calf brain, J. Neurochem. 19 (1972) 727–736.PubMedCrossRefGoogle Scholar
  10. 10.
    Snyder, F., Blank, M.L. and Wykle, R.L., The enzymic synthesis of ethanolamine plasmalogens, J. Biol. Chem. 246 (1971) 3639–3645.PubMedGoogle Scholar
  11. 11.
    Woelk, H., Goracci, G., Gaiti, A., Porcellati, G., Phospholipase Al and A activities of neuronal and glial cells of the rabbit brain, Hoppe Seyler’s Z. Physiol. Chem. 354 (1973) 729–736.CrossRefGoogle Scholar
  12. 12.
    Woelk, H., Kanig, K., Peiler-Ichikawa, K., Phospholipid metabolism in experimental allergic encephalomyelitis: Activity of mitochondrial phospholipase A2 of rat brain towards specifically labelled 1,2-diacyl-, 1-alk-1’-enyl-2-acyl-and 1-alkyl2-acyl-sn-glycero-3-phosphorylcholine, J. Neurochem. 23 (1974) 745–750.PubMedCrossRefGoogle Scholar
  13. 13.
    Woelk, H., Porcellati, G., Subcellular distribution and kinetic properties of rat brain phospholipases A and A2. Hoppe Seyler’s Z. Physiol. Chem. 354 (1973) 90–100.CrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1978

Authors and Affiliations

  • Helmut Woelk
    • 1
    • 2
  • Rosemarie Jahrreiss
    • 1
    • 2
  1. 1.Einheit für NeurobiochemieUniversitäts-Nervenklinik Erlangen852 ErlangenGermany
  2. 2.Universitäts-NervenklinikUniversität des Saarlandes665 HomburgGermany

Personalised recommendations