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A deazaadenosine‐insensitive methylation of phosphatidylethanolamine is involved in lipoprotein secretion
Author(s) -
Vance Jean E.,
Vance Dennis E.
Publication year - 1986
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(86)80820-1
Subject(s) - phosphatidylethanolamine , phosphatidylcholine , methylation , serine , secretion , ethanolamine , biochemistry , choline , chemistry , moiety , lipoprotein , biology , phospholipid , stereochemistry , phosphorylation , cholesterol , gene , membrane
We have examined the effect of inhibitors of methylation of phosphatidylethanolamine on lipoprotein secretion from cultured rat hepatocytes. The incorporation of [1‐ 3 H]ethanolamine into phosphatidylcholine of hepatocytes and secreted lipoproteins was inhibited by greater than 90% by the methylation inhibitors 3‐deazaadenosine and Neplanocin. In addition, these compounds strongly inhibited the incorporation of [3‐ 3 H]serine into the choline moiety of phosphatidylcholine of the hepatocytes, but had no effect on incorporation of [3‐ 3 H]serine into secreted phosphatidylcholine. The results suggest that a pool of phosphatidylcholine targeted for lipoprotein secretion originates from phosphatidylethanolamine made from serine and this methylation reaction has the unique property of being insensitive to 3‐deazaadenosine.