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Lipids

, 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
Article

Abstract

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 2.7.8.1), 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.

Keywords

Ethanolamine Diglyceride Soybean Lecithin Rabbit Brain Thin Layer Chro 
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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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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