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Journal of Lipid Research, Vol 26, 556-565, Copyright © 1985 by Lipid Research, Inc.
E Windler and RJ Havel
Like rat C apolipoproteins, each of the C apolipoproteins from human blood
plasma (C-I, C-II, C-III-1, and C-III-2) bound to small chylomicrons from
mesenteric lymph of estradiol-treated rats and inhibited their uptake by
the isolated perfused rat liver. This inhibitory effect of the C
apolipoproteins was independent of apolipoprotein E, which is present only
in trace amounts in these chylomicrons. Addition of rat apolipoprotein E to
small chylomicrons from mesenteric lymph of normal rats did not displace C
apolipoproteins and had no effect on the uptake of these particles by the
perfused liver, indicating that an increased ratio of E apolipoproteins to
C apolipoproteins on chylomicron particles, unaccompanied by depletion of
the latter, may not promote recognition by the chylomicron remnant
receptor. The hepatic uptake of remnants of rat hepatic very low density
lipoproteins (VLDL) and small chylomicrons, which had been produced in
functionally eviscerated rats, was also inhibited by addition of C
apolipoproteins. These observations are consistent with the hypothesis that
the addition of all of the C apolipoproteins to newly secreted chylomicrons
and VLDL inhibits premature uptake of these particles by the liver and that
depletion of all of these apolipoproteins from remnant particles
facilitates their hepatic uptake. Remnants of chylomicrons and VLDL
incubated with rat C apolipoproteins efficiently took up C-III
apolipoproteins, but not apolipoprotein C-II (the activator protein for
lipoprotein lipase). Preferential loss of apolipoprotein C-II during
remnant formation may regulate the termination of triglyceride hydrolysis
prior to complete removal of triglycerides from chylomicrons and VLDL.
ARTICLES
Inhibitory effects of C apolipoproteins from rats and humans on the uptake of triglyceride-rich lipoproteins and their remnants by the perfused rat liver
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