Lipid emulsions used in parenteral nutrition interact with lipoproteins leading to exchanges of lipids and acquisition of several apolipoproteins (apo). It has been previously observed that, during in vitro incubation of emulsions with purified LDL, a variable fraction of LDL binds to TG-rich emulsion particles. The purpose of this study was to better characterize such an interaction. Two emulsions containing 20% soybean oil (Endolipid(R), B. Braun AG, Melsungen, Germany) or fish oil were incubated with LDL, either alone or in the presence of various plasma subfractions, for different durations and at different temperatures. The fraction named M-LE (containing TG-rich particles modified after incubation) was separated by ultracentrifugation or gel filtration chromatography, and the apoB content was measured as an index of LDL binding to TG-rich emulsion particles. The formation of such complexes was visualized by freeze-fracture electron microscopy. LDL binding was not influenced by the method used for M-LE isolation. Binding occurred quickly, did not increase with prolonged incubation, was inversely related to increasing incubation or ultracentrifugation temperature, and withstood 40 h of ultracentrifugation at 163,000 x g. The presence of glycerol or excess phospholipids in the emulsion did not markedly affect the formation of the complexes. In contrast, adding very small amounts of lipoprotein-poor plasma (d > 1.210 g/mL) or HDL markedly reduced the process, and albumin had no effect. The TG composition of the emulsion influenced the binding of LDL to TG-rich particles, since more apoB was found in M-LE from fish oil than from soybean oil emulsion.
