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J. Biol. Chem., Vol. 255, Issue 5, 1839-1848, Mar, 1980
JL Goldstein, YK Ho, MS Brown, TL Innerarity and RW Mahley
The synthesis and accumulation of cholesteryl esters by monolayers of mouse
peritoneal macrophages was stimulated 20- to 160-fold by incubation with
beta-migrating very low density lipoproteins (beta- VLDL, density less than
1.006 g/ml) isolated from the plasma of cholesterol-fed dogs. Three other
cholesterol-rich lipoprotein fractions obtained from the plasma of the same
hypercholesterolemic dogs, including low density lipoprotein (LDL),
cholesterol-induced high density lipoprotein (HDLc), and apo-E HDLc, had
little to no stimulatory effect. Plasma VLDL (density less than 1.006 g/ml)
from normal dogs did not increase cholesteryl ester formation in
macrophages. The enhancement in cholesteryl ester synthesis and
accumulation by hypercholesterolemic canine beta-VLDL was due to the
presence of a high affinity binding site on the macrophage cell surface
that mediated the uptake and lysosomal degradation of the beta-VLDL.
Competition studies with fucoidin and dextran sulfate indicated that the
receptor for canine beta-VLDL was different from that previously described
for human acetylated low density lipoprotein (acetyl-LDL). Prior incubation
of macrophage monolayers with either unlabeled canine beta-VLDL or human
acetyl-LDL, both of which raised the cellular content of cholesteryl
esters, reduced the ability of the cells to degrade 125I-labeled beta-VLDL,
suggesting that the receptor for beta- VLDL is subject to regulation. The
current findings indicate: 1) that macrophages possess a high affinity
receptor that recognizes one of the four cholesterol-rich lipoproteins
present in the plasma of cholesterol- fed dogs, beta-VLDL, and 2) that the
receptor-mediated ingestion of beta-VLDL leads to cholesteryl ester
deposition in these cells.
Cholesteryl ester accumulation in macrophages resulting from receptor- mediated uptake and degradation of hypercholesterolemic canine beta- very low density lipoproteins
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