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• W2159127160 abstract "The in vivo fate of beta-very low density lipoproteins (beta-VLDLs) was investigated after Cu(2+)-mediated oxidative modification (Ox-beta-VLDL). Ox-beta-VLDL may be physiologically relevant under conditions of defective VLDL removal by the liver (type III hyperlipoproteinemia) or overloading of the remnant receptor (high cholesterol feeding). On oxidation of beta-VLDL, the kinetics of its removal from the blood and uptake by the liver are unchanged. However, in contrast to beta-VLDL, which is recognized by the remnant receptor of parenchymal cells, liver uptake of Ox-beta-VLDL is mediated mainly by Kupffer cells (65% of liver-associated radioactivity). In vitro competition studies show that the cell association and degradation of iodine-125-labeled Ox-beta-VLDL by both liver endothelial and Kupffer cells are only marginally competed for by acetylated LDL (10-20%), while an efficient blockade is noted with Ox-beta-VLDL, oxidized low density lipoproteins, or polyinosinic acid (80-90%). The capacity of Kupffer cells to associate with and degrade 125I-Ox-beta-VLDL appears to be twofold higher than for endothelial cells. It is concluded that on oxidation of beta-VLDL, the recognition system responsible for the uptake of beta-VLDL from the blood circulation is shifted from the remnant receptor to a specific oxidized-lipoprotein receptor. The efficiency of the scavenger activity on Kupffer cells will then form the protection system against the prolonged circulation of these atherogenic lipoproteins in the blood." @default.
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• W2159127160 date "1992-01-01" @default.
• W2159127160 modified "2023-09-26" @default.
• W2159127160 title "Recognition sites on rat liver cells for oxidatively modified beta-very low density lipoproteins." @default.
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• W2159127160 doi "https://doi.org/10.1161/01.atv.12.1.41" @default.
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