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Journal of Lipid Research, Vol 31, 701-708, Copyright © 1990 by Lipid Research, Inc.
M Kinoshita, ES Krul and G Schonfeld
The conformation of the apolipoprotein B-100 associated with low density
lipoproteins (LDL) is not fixed. Rather, the conformations of several
regions are subject to alteration by a variety of metabolic and therapeutic
perturbations that change either the lipid compositions and/or sizes of LDL
particles. However, because these perturbations simultaneously alter
several structural-compositional features of the particles it has been
difficult to relate structural-compositional features of LDL to apoB-100
conformations. Furthermore, in in vivo studies several days pass between
samplings, thus different sets of particles are studied before and after
experimental perturbation. In the present experiments more discrete
perturbations of LDL were obtained in vitro by incubating LDL with very low
density lipoproteins (VLDL) in the presence of partially purified human
plasma lipid transfer proteins. The conformations of apoB on the LDL
particles then were examined a) by probing epitope expression and b) by
examining interactions between LDL and LDL-receptors in cultured human
fibroblasts. During incubations with VLDL and lipid transfer proteins, the
diameters of LDL particles decreased; the percentage composition of LDL
triglycerides increased three-to fivefold; concomitantly, cholesteryl
esters decreased. Lipid transfer protein was required for the transfer to
occur and the magnitude of the increase in LDL- triglycerides depended upon
the duration of incubation, the ratio of VLDL/LDL, and unknown properties
specific to the various LDL preparations. The fact that the triglyceride
contents of all LDL preparations were not identically affected suggests
that initial packaging of the core region may affect capacity for lipid
exchange.(ABSTRACT TRUNCATED AT 250 WORDS)
ARTICLES
Modification of the core lipids of low density lipoproteins produces selective alterations in the expression of apoB-100 epitopes
Department of Internal Medicine, Washington University School of Medicine, St. Louis, MO 63110.
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