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A more recent version of this article appeared on January 1, 2005

Papers In Press, published online ahead of print November 1, 2004
J. Lipid Res., doi:10.1194/jlr.M400296-JLR200
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Submitted on August 3, 2004
Revised on October 20, 2004
Accepted on October 21, 2004

Relation of the size and intracellular sorting of apoB to the formation of VLDL 1 and 2

Pia Stillemark-Billton, Caroline Beck, Jan Borén, and Sven-Olof Olofsson

The Wallenberg Laboratory, University of Göteborg, Göteborg SE-413 45

Corresponding Author: Sven-Olof.Olofsson{at}wlab.gu.se

In this study, we tested the hypothesis that two separate pathways—the two-step process and an apoB size-dependent lipidation process—give rise to different lipoproteins. Expression of apoB-100 and C-terminally truncated forms of apoB-100 in McA-RH7777 cells demonstrated that VLDL particles can be assembled by apoB size-dependent linear lipidation, resulting in particles whose density is inversely related to the size of apoB. This lipidation results in a LDL-VLDL 2 particle containing apoB-100. VLDL 1 is assembled by the two-step process by apoB-48 and larger forms of apoB but not to any significant amount by apoB-41. The major amount of intracellular apoB-80 and apoB-100 banded with a mean density of 1.10 g/ml. Its formation was dependent on the sequence between apoB-72 and apoB-90. This dense particle, which is retained in the cell, possibly by chaperons or association with the microsomal membrane, is a precursor of secreted VLDL 1. The intracellular LDL-VLDL 2 particles formed during size-dependent lipidation appear to be the precursors of intracellular VLDL 1. We propose that the dense apoB-100 intracellular particle is converted to LDL-VLDL 2 by size-dependent lipidation. LDL-VLDL 2 is secreted or converted to VLDL 1 by the uptake of the major amount of triglycerides.


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