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Journal of Lipid Research, Vol 28, 798-809, Copyright © 1987 by Lipid Research, Inc.
B Oswald and S Quarfordt
The uptake and internalization of a triglyceride emulsion by rat
hepatocytes in culture less than 24 hr was either inhibited or uninfluenced
by apoE. ApoE significantly increased the uptake of these emulsions in
later cultures. Specific low density lipoprotein (LDL) binding was similar
for hepatocyte monolayers prior to and after 24 hr. Rat hepatocytes in
culture for 2 days, which were treated with collagenase, detached and then
replated within 1 hr and were apoE- responsive in 2 hr. Heparin inhibited
the apoE stimulation in both hepatocytes and hepatoma monolayers. Heparin
wash of hepatocytes or hepatoma cells incubated with apoE-[14C]triolein
emulsions at 4 degrees C resulted in a considerable loss in radiolabeled
cell lipid. A similar wash after 37 degrees C incubations produced little
loss suggesting internalization. Hepatocytes had lower affinity but similar
apoE- emulsion binding capacity compared to hepatoma cells. Triolein
emulsions with apoE were significantly more rapidly metabolized by the
hepatocyte than unsupplemented emulsions. The apoE-mediated hepatocyte
lipid uptake was inhibited by apoC proteins. High molar ratios of free
fatty acid/albumin also suppressed hepatocyte apoE-mediated lipid uptake.
Both rat high density lipoprotein (HDL) and LDL inhibited with a potency
directly related to their content of apoE. Human LDL and HDL without apoE
also inhibited the interaction with less potency than the rat lipoproteins.
Human HDL inhibition was diminished after removal of apoC proteins.
ARTICLES
Effect of apoE on triglyceride emulsion interaction with hepatocyte and hepatoma G2 cells
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