Plasma homocysteine is regulated by phospholipid methylation

J Biol Chem. 2003 Feb 21;278(8):5952-5. doi: 10.1074/jbc.M212194200. Epub 2002 Dec 12.

Abstract

Mild hyperhomocysteinemia is an independent risk factor for cardiovascular disease. Homocysteine, a non-protein amino acid, is formed from S-adenosylhomocysteine and partially secreted into plasma. A potential source for homocysteine is methylation of the lipid phosphatidylethanolamine to phosphatidylcholine by phosphatidylethanolamine N-methyltransferase in the liver. We show that mice that lack phosphatidylethanolamine N-methyltransferase have plasma levels of homocysteine that are approximately 50% of those in wild-type mice. Hepatocytes isolated from methyltransferase-deficient mice secrete approximately 50% less homocysteine. Rat hepatoma cells transfected with phosphatidylethanolamine N-methyltransferase secrete more homocysteine than wild-type cells. Thus, phosphatidylethanolamine N-methyltransferase is an important source of plasma homocysteine and a potential therapeutic target for hyperhomocysteinemia.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Hepatocytes / metabolism*
  • Homocysteine / blood*
  • Homocysteine / deficiency
  • Liver Neoplasms, Experimental / metabolism
  • Male
  • Methylation
  • Methyltransferases / deficiency
  • Methyltransferases / metabolism*
  • Mice
  • Mice, Knockout
  • Phosphatidylethanolamine N-Methyltransferase
  • Phospholipids / metabolism*
  • Rats
  • Rats, Mutant Strains
  • Recombinant Proteins
  • Reference Values
  • Transfection

Substances

  • Phospholipids
  • Recombinant Proteins
  • Homocysteine
  • Methyltransferases
  • Phosphatidylethanolamine N-Methyltransferase