A change in apolipoprotein B expression is required for the binding of apolipoprotein E to very low density lipoprotein.

Abstract

Factors affecting the association of apolipoprotein E (apoE) with human plasma very low density lipoprotein (VLDL) were investigated in experiments in which the lipid content of the lipoprotein was modified either by lipid transfer in the absence of lipolysis or through the action of lipoprotein lipase. In both cases, lipoprotein particles initially containing no apoE (VLDL-E), isolated by heparin affinity chromatography, were modified until they had the same lipid composition as native apoE-containing VLDL (VLDL+E) from the same plasma. Transfer-modified lipoproteins, unlike native VLDL+E, did not bind apoE or interact with heparin. In contrast, VLDL-E, whose lipid composition was modified to the same extent by lipase, bound apoE and bound to heparin under the same conditions as native VLDL+E. A structural protein (apolipoprotein B) epitope characteristic of VLDL+E was expressed during lipolysis prior to ApoE or heparin binding. The data suggest that the reaction of apoE with VLDL-E is a two-step reaction. The appearance of apoB is modified during lipolysis, with expression of a major heparin-binding site. The modified VLDL then becomes competent to bind apoE. The lipid composition of VLDL appears not to be a major factor in the ability of VLDL to bind apoE or to bind to heparin.