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.
Armstrong
D P
DP
Department of Biochemistry, University of Nottingham Medical School, Queen's Medical Centre, U.K.
White
D A
DA
D000818:Animals; D015815:Cell Adhesion Molecules; D002460:Cell Line; D006023:Glycoproteins / Q000187:drug effects* / Q000378:metabolism; D006031:Glycosylation / Q000187:drug effects; D006801:Humans; D008077:Lipoproteins, LDL / Q000187:drug effects* / Q000378:metabolism; D008264:Macrophages / Q000187:drug effects* / Q000378:metabolism; D051379:Mice; D011973:Receptors, LDL / Q000187:drug effects* / Q000378:metabolism; D051116:Receptors, Scavenger; D014415:Tunicamycin / Q000494:pharmacology*
D015815:Cell Adhesion Molecules; D006023:Glycoproteins; D008077:Lipoproteins, LDL; D011973:Receptors, LDL; D051116:Receptors, Scavenger; C032629:acetyl-LDL; D014415:Tunicamycin