Hydrolysis of retinyl esters in rat liver. Description of a lysosomal activity.

When incorporated into liposomes made of phospholipids, retinyl palmitate is an adequate substrate for an acidic REH (aREH). In rat liver, this activity is mainly localized in the lysosomal fraction. Kinetic parameters have been determined for retinyl palmitate (Km = 315 microM; maximal rate = 22.1 nmol retinol/h per mg protein). The aREH activity is different from the lysosomal acidic cholesteryl ester hydrolase (aCEH): cholesteryl oleate does not inhibit aREH activity, neither do some aCEH specific inhibitors, and aREH does not hydrolyse cholesteryl ester. Involvement of aREH in the hydrolysis of lipid droplets retinyl esters in fat storing cells is discussed.