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Specific pools of phospholipids are used for lipoprotein secretion by cultured rat hepatocytes

Conference · · Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States)
OSTI ID:7171078
The role of phospholipid biosynthesis in lipoprotein secretion from cultured rat hepatocytes has been investigated. In liver, phosphatidylcholine (PC) is made both by the CDP-choline pathway and by the methylation of phosphatidyl-ethanolamine (PE), which in turn is derived from both serine (via phosphatidylserine) and ethanolamine (via CDP-ethanol-amine). Monolayer cultures of rat hepatocytes were incubated in the presence of (methyl-/sup 3/H)choline, (2-/sup 3/H)ethanolamine or (3-/sup 3/H)serine. The specific radioactivity of the phospholipids derived from each of these precursors was measured in the cells and in the secreted lipoproteins of the culture medium. The specific radioactivities of PC and PE derived from (1-/sup 3/H)ethanolamine were markedly lower (approximately 1/2 and less than 1/10, respectively) in the secreted phospholipids than in the cellular phospholipids. Thus, ethanolamine was not an effective precursor of the phospholipids in lipoproteins. On the contrary, the specific radioactivity of PC made from (methyl-/sup 3/H)choline was approximately equal in cells and lipoproteins. In addition, over the first 4 h of incubation with (3-/sup 3/H)serine, the specific radioactivities of PC and PE were significantly higher in the lipoproteins than in the cells. These data indicate that specific pools of phospholipids are selected on the basis of their routes of biosynthesis, for secretion into lipoproteins.
Research Organization:
Univ. of British Columbia, Vancouver
OSTI ID:
7171078
Report Number(s):
CONF-8606151-
Conference Information:
Journal Name: Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States) Journal Volume: 45:6
Country of Publication:
United States
Language:
English