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J. Biol. Chem., Vol. 262, Issue 6, 2443-2450, 02, 1987
RC Pittman, TP Knecht, MS Rosenbaum and CA Taylor Jr
We have previously described in rats the selective uptake of HDL-
associated cholesterol esters (traced by [3H]cholesteryl oleyl ether) in
excess of the uptake of HDL-associated apoA-I. In the present studies we
show that the mechanism also exists in cultured cells of human and mouse
origin as well. This selective uptake represents a net uptake of
cholesterol esters and not an isotope exchange, as shown by mass flux
studies in adrenal cells. Inhibitors of receptor recycling, chloroquine,
monensin, and colchicine, inhibited uptake of apoA-I from HDL by Hep G-2
human hepatoma cells to about the same extent as a reference protein,
asialofetuin, but inhibited uptake of the cholesteryl ether tracer much
less. Levels of NaN3 which effectively inhibited sucrose pinocytosis
inhibited uptake of apoA-I to about the same extent but did not inhibit
uptake of the cholesteryl ether at all. Thus, not only receptor recycling,
but endocytosis as well, appears not to be involved in selective uptake.
This conclusion was supported by studies in which synthetic HDL particles
were made to contain two neutral lipid core tracers; one of them, the
[3H]cholesteryl ether previously used, was selectively taken up, whereas
the other, [14C]sucrose octaoleate, was excluded from selective uptake.
Thus, selective uptake cannot involve endocytosis of the entire lipid core,
but may involve other specific transfer mechanisms.
A nonendocytotic mechanism for the selective uptake of high density lipoprotein-associated cholesterol esters
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