Inhibition of protein N-glycosylation has no effect on the binding of acetyl LDL to J774 cells.

Acetyl-LDL (Ac-LDL) bound to transformed mouse macrophage J774 cells in a high affinity, saturable and specific manner. When cells were cultured for 24h in the presence of tunicamycin such that incorporation of N-linked sugars into protein but not protein synthesis itself was inhibited significantly, the binding characteristics of Ac-LDL to the cells were unaltered. In this respect the Ac-LDL receptor of J774 cells is similar to the asialoglycoprotein receptor of HepG2 cells.