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.
Rapid Communication| February 01 1992
Inhibition of protein N-glycosylation has no effect on the binding of acetyl LDL to J774 cells
David P. Armstrong;
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David P. Armstrong, David A. White; Inhibition of protein N-glycosylation has no effect on the binding of acetyl LDL to J774 cells. Biosci Rep 1 February 1992; 12 (1): 37–46. doi: https://doi.org/10.1007/BF01125826
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