, Volume 9, Issue 10, pp 738–747 | Cite as

Enzymic synthesis of ethanolamine plasmalogens through ethanolaminephosphotransferase activity in neurons and glial cells of rabbit in vitro

  • L. Binaglia
  • R. Roberti
  • G. Goracci
  • E. Francescangeli
  • G. Porcellati


The de novo synthesis of ethanolamine plasmalogen in isolated neuronal and glial cells from adult rabbit brain cortex was investigated in vitro, using labeled cytidine-5′-diphosphate ethanolamine as lipid precursor. The neuronal cell enriched fraction was found to possess a twofold ethanolaminephosphotransferase activity (EC, as compared to the glial fraction. The neuronal/glial ratio was similar both in the absence and in the presence of saturating alkenylacyl glycerol. Under the most favorable conditions, rates of 31 nmoles and 16 nmoles ethanolamine plasmalogen/mg protein/30 min were obtained for neurons and glia, respectively. Several kinetic properties of the phosphotransferase were found to be similar both in neurons and glia, e.g., Km of cytidine-5′-diphosphate ethanolamine, pH optimum, need for divalent cations; the Km value for alkenylacyl glycerol was twofold higher in glia (4 mM) than in neurons (2 mM). The neuronal/glial ratio for the phosphatidylethanolamine synthesizing activity was 2, 4.5, and 6 on using diacyl glycerols prepared from ox heart, ox brain, and soybean, respectively. It is concluded that the cytidine-dependent system for ethanolamine plasmalogen and phosphatidylethanolamine synthesis is concentrated prevalently in the neuronal cells, as compared to glia.


Ethanolamine Diglyceride Soybean Lecithin Rabbit Brain Thin Layer Chro 
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Copyright information

© American Oil Chemists’ Society 1974

Authors and Affiliations

  • L. Binaglia
    • 1
  • R. Roberti
    • 1
  • G. Goracci
    • 1
  • E. Francescangeli
    • 1
  • G. Porcellati
    • 1
  1. 1.Department of Biochemistry, The Medical SchoolUniversity of PerugiaPerugiaItaly

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