AbstractThe effect of tunicamycin (TM) on the metabolism of acetylated low‐density lipoprotein (AcLDL) was examined to determine whetherN‐linked glycosylation is required for the proper function of the AcLDL pathway. Proteolytic degradation of [125I]‐AcLDL was increased twofold in the presence of TM. This did not occur via an increase in total lysosomal enzyme activity or extracellular proteolysis; rather, the rate of uptake of [125I]‐AcLDL was increased. The enhanced degradation of AcLDL did not lead to a commensurate increase in the rate of synthesis of cholesteryl oleate. Conversely, the rate of cholesterol esterification was reduced in the presence of TM. The uptake of [125I]‐AcLDL was more sensitive to inhibition by chloroquine in TM‐treated cells. However, the presence of TM did not affect the ability of chloroquine to inhibit constitutive recycling of AcLDL binding sites. These results suggest thatN‐linked glycosylation may be involved in the regulation of AcLDL metabolism