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  • Title: Scavenger function of sinusoidal liver cells. Acetylated low-density lipoprotein is endocytosed via a route distinct from formaldehyde-treated serum albumin.
    Author: Horiuchi S, Takata K, Maeda H, Morino Y.
    Journal: J Biol Chem; 1985 Jan 10; 260(1):53-6. PubMed ID: 2981216.
    Abstract:
    Chemically modified proteins such as acetylated low-density lipoprotein (acetyl-LDL) and formaldehyde-treated serum albumin (f-Alb) infused intravenously are known to undergo receptor-mediated endocytosis by sinusoidal liver cells, major intravascular scavenger cells in vivo. The aim of the present study was to elucidate whether the endocytic uptake of acetyl-LDL and f-Alb is mediated by the same receptor or not. Experiments on the binding of 125I-acetyl-LDL to isolated rat liver sinusoidal cells revealed the presence of a specific, high-affinity, saturable, membrane-associated receptor with an apparent Kd = 7 micrograms of the ligand at 0 degrees C. Unlabeled acetyl-LDL effectively inhibited 125I-f-Alb binding to the cells. By contrast, the binding of 125I-acetyl-LDL to the cells was affected neither by unlabeled f-Alb nor by the antibody raised against the f-Alb receptor. These results indicate that the scavenger receptors for these two ligands are distinct from each other but similarly sensitive to polyanionic compounds.
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