Separate myocardial ethanolamine phosphotransferase activities responsible for plasmenylethanolamine and phosphatidylethanolamine synthesis Published, JLR Papers in Press, December 16, 2002. DOI 10.1194/jlr.M200426-JLR200

Ethanolamine phosphotransferase (EPT) is a key enzyme responsible for the synthesis of ethanolamine glycerophospholipids. Plasmenylethanolamine is a predominant molecular subclass of ethanolamine glycerophospholipids in the heart. The present study was designed to identify the selective use of 1-O-alk-1′-enyl-2-acyl-sn-glycerol as a substrate for EPT as a mechanism responsible for the predominance of plasmenylethanolamine in the rabbit heart. EPT activity in rabbit myocardial membranes using 1,2-diacyl-sn-glycerol as substrate is activated by Mn2+, inhibited by dithiobisnitrobenzoic acid (DTNB) and is unaffected by Ca2+. In contrast, ethanolamine phosphotransferase activity using 1-O-alk-1′-enyl-2-acyl-sn-glycerol as substrate is inhibited by Mn2+ and Ca2+, but is activated by DTNB. Additionally, ethanolamine phosphotransferase activity using 1-O-alk-1′-enyl-2-acyl-sn-glycerol substrate was more sensitive to thermal denaturation compared with that of 1,2-diacyl-sn-glycerol. Taken together, these results suggest that separate ethanolamine phosphotransferase activities are present in heart membranes that are responsible for the synthesis of phosphatidylethanolamine and plasmenylethanolamine.

• Publication year

  2003

• Venue

  Journal of Lipid Research

• Publication date

  2003-03-01

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1194/JLR.M200426-JLR200PMID 12562835
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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