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Human umbilical vein endothelial cells, when plated on plastic dishes, induced the release of large amounts of alpha-tocopherol-transfer protein when exposed to oxidized low density lipoprotein (LDL) and apolipoprotein E (apoE)-enriched very low density lipoprotein (VLDL). Tocopherol-transfer protein was identified in the medium by enzymatic and immunochemical methods. The time course of tocopherol-transfer protein secretion correlated with the accumulation of oxidized lipids in cells and their ability to bind and internalize LDL. Prolonged treatment with LDL led to the appearance of esterified cholesterol in cells and the hydrolysis of oxidized lipids in the medium. In contrast, cells incubated with alpha-tocopherol-transfer protein-free VLDL did not accumulate oxidized lipids. Thus, the active lipoprotein did not appear to interfere with the uptake of oxidized lipids. The ability of cells to oxidize LDL cholesterol and the ability to bind and degrade VLDL were equally dependent on a class of high-affinity scavenger receptors. In contrast, cells cultured on type I collagen required alpha-tocopherol-transfer protein to oxidize LDL cholesterol but not to degrade oxidized lipids in the medium. The results suggest that VLDL can directly interact with cells via scavenger receptors and that these receptors can simultaneously degrade oxidized lipids in the medium. In contrast, tocopherol-transfer protein-mediated oxidation of LDL led to the accumulation of oxidized lipids in the medium. Thus, oxidized lipids may become sequestered in cells and lead to cellular damage.Q:
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