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J Biol Chem, Vol. 274, Issue 12, 8247-8253, March 19, 1999
§,**,
From the Departments of Following the internalization of
low density lipoprotein (LDL) by the LDL receptor within cells, both
the lipid and the protein components of LDL are completely degraded
within the lysosomes. Remnant lipoproteins are also internalized by
cells via the LDL receptor as well as other receptors, but the events
following the internalization of these complexes, which use
apolipoprotein E (apoE) as their ligand for receptor capture, have not
been defined. There is evidence that apoE-containing Medicine,
§ Pathology, and ** Pharmacology, Vanderbilt University
School of Medicine, Nashville, Tennessee 37232
-very low
density lipoproteins follow differential intracellular routing
depending on their size and apoE content and that apoE internalized
with lipoproteins can be resecreted by cultured hepatocytes and
fibroblasts. In the present studies, we addressed the question of apoE
sparing or recycling as a physiologic phenomenon. Remnant lipoproteins (d < 1.019 g/ml) from normal mouse plasma were
iodinated and injected into normal C57BL/6 mice. Livers were collected
at 10, 30, 60, and 120 min after injection, and hepatic Golgi fractions
were prepared for gel electrophoresis analysis. Golgi preparations were
analyzed for galactosyltransferase enrichment (>40-fold above cell
homogenate) and by appearance of the Golgi stacks and vesicles on
electron microscopy. Iodinated apoE was consistently found in the
Golgi fractions peaking at 10 min and disappearing by 2 h after
injection. Although traces of apoB48 were present in the Golgi
fractions, the apoE/apoB ratio in the Golgi was 50-fold higher compared
with serum. Quantitatively similar results were obtained when the very
low density lipoprotein remnants were injected into mice deficient in
either apoE or the LDL receptor, indicating that the phenomenon of apoE
recycling is not influenced by the production of endogenous apoE and is
not dependent on the presence of LDL receptors. In addition,
radioactive apoE in the Golgi fractions was part of d = 1.019-1.21 g/ml complexes, indicating an association of recycled
apoE with either newly formed lipoproteins or the internalized
complexes. These studies show that apoE recycling is a physiologic
phenomenon in vivo and establish the presence of a unique
pathway of intracellular processing of apoE-containing remnant lipoproteins.
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