A lecithin:retinol acyltransferase activity in human and rat liver.

This report demonstrates that exogenous phosphatidylcholine will serve as an acyl donor for the esterification of retinol complexed to cellular retinol-binding protein (CRBP) by human and rat liver microsomal preparations. The retinyl ester synthases utilized phosphatidylcholine but had little or no ability to transfer acyl groups from lysophosphatidylcholine, phosphatidyl-ethanolamine, or phosphatidic acid to retinol-CRBP. The human and rat activities also demonstrated positional selectivity as only the fatty acyl group at the sn-1 position of phosphatidylcholine was transferred. This in vitro activity may have considerable physiological importance since the fatty acyl composition at the sn-1 position of phosphatidylcholine is remarkably similar to the hepatic retinyl esters observed in vivo.