Fate of fatty acids taken up as cholesteryl ester by rat hepatocytes in primary culture from high-density lipoprotein.

Primary cultures of rat hepatocytes were incubated in the presence of high-density lipoproteins (HDL) labelled with [1-14C]oleyl or [1-14C]linoleyl cholesteryl ester. Labelled HDL were prepared by selective delipidation with heptane, relipidation and sequential ultracentrifugations. Hepatocytes took up cholesteryl esters and cholesteryl ether their non-hydrolizable analog, at the same rate. The uptake increased with time, the cholesteryl ester/protein ratio and the amount of added HDL. It was not dependent on the nature of acyl chain or on the nature of the bond. The uptake did not depend on a specific interaction between HDL and cell membranes, since cholesteryl ester was taken up from HDL to the same extent as from albumin complexes. Linoleic and oleic acids released from cholesteryl esters taken up by hepatocytes were mainly reesterified into phosphatidylcholine and triacylglycerols. Linoleic acid was preferentially channelled into PC. A portion of these lipids were secreted by hepatocytes during a 24-h reincubation in a medium devoid of lipoprotein. Nearly the same amount of radioactivity was recovered in secreted phospholipids as in secreted triacylglycerols, in contrast with hepatocytes labelled with free fatty acids which secreted very little radioactivity as phospholipids. From these results and the high content in polyunsaturated fatty acids of cholesteryl esters, one can hypothesize that hepatic cholesteryl ester uptake may contribute to biliary phosphatidylcholine production, and therefore to polyunsaturated fatty acid sparing.