Binding of rat chylomicrons and their remnants to the hepatic low-density-lipoprotein receptor and its role in remnant removal

Windler, E E T; Greeve, J; Daerr, W H; Greten, H

doi:10.1042/bj2520553

Cited by 67Cholesterol and Lipid MetabolismLipid metabolism and disordersLipoproteins and Cardiovascular Health

Binding of rat chylomicrons and their remnants to the hepatic low-density-lipoprotein receptor and its role in remnant removal

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Windler, E E T, Greeve, J, Daerr, W H, Greten, H·1988·Biochemical Journal

DOI 10.1042/bj2520553PMC PMC1149179

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Abstract

Binding and uptake of rat chylomicrons of different metabolic stages by the hepatic low-density-lipoprotein (LDL) receptor were studied. Pure chylomicrons, characterized by apolipoprotein B-48 devoid of contaminating B-100, were labelled in their cholesteryl esters. Lymph chylomicrons and serum chylomicrons, enriched in apolipoprotein E and the C-apolipoproteins, bound poorly to rat hepatic membranes. In contrast, chylomicron remnants, containing the apolipoproteins B-48 and E, bound with high affinity. Specific binding of remnants was virtually completely competed for by LDL free of apolipoprotein E. In addition, in ligand blots both remnants and LDL associated with the same protein with an Mr characteristic of the LDL receptor. Uptake of remnants during a single pass through isolated perfused rat livers was decreased to about 50% by an excess of LDL. It is concluded that rat chylomicron remnants are a ligand of the hepatic LDL receptor. The much higher affinity as compared with LDL is mediated by apolipoprotein E but not B-48, and is inhibited by the C-apolipoproteins. This explains why serum chylomicrons are not taken up by the liver, whereas remnants are rapidly removed from the circulation. Results from experiments in vivo suggest that the LDL receptor makes an important contribution to the hepatic uptake of remnants and may be the principal binding site of the liver responsible for remnant removal.

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Increased circulating chylomicron-remnant particles are preferentially taken up by the liver by a receptor-mediated process, resulting in nonalcoholic fatty liver disease and hepatic insulin resistance.
“Increased concentrations of circulating chylomicron-remnant particles are then preferentially taken up by the liver by means of a receptor-mediated process,18–22 resulting in non-alcoholic fatty liver disease and hepatic insulin resistance.”
From Apolipoprotein C3 gene variants in nonalcoholic fatty liver disease (2010) · cites this paper as [19]

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Authors: Windler, E. E. T., Greeve, J., Daerr, W. H., & Greten, H.
Affiliations: University Medical Center Hamburg-Eppendorf (DE)
ORCID: Windler, E E T
Venue: Biochemical Journal
Publisher: Portland Press Ltd.
Published: 1988-06-01
Volume: 252
Issue: 2
Pages: 553-561
ISSN: 0264-6021 (ISSN-L)
1470-8728
DOI: 10.1042/bj2520553
PMC: PMC1149179
OpenAlex: W1457207713
Cited by: 67
References: 46
Citations by year: 2023: 1 · 2020: 1 · 2018: 1 · 2016: 1 · 2014: 2
FWCI: 8.54
Type: journal article
Language: en
Open access: bronze
doi.org
Locations: Biochemical Journal (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: Deutsche Forschungsgemeinschaft
Universität Innsbruck
Topics: Health Sciences › Medicine › Surgery › Cholesterol and Lipid Metabolism
Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Lipid metabolism and disorders
Health Sciences › Medicine › Surgery › Lipoproteins and Cardiovascular Health
Keywords: chylomicron remnants, LDL receptor, apolipoprotein E, apolipoprotein B-48, apolipoprotein C, ligand competition, isolated perfused liver, rats
MeSH terms: Animals, Apolipoproteins, Binding Sites, Binding, Competitive, Cell Membrane, Cholesterol, Chylomicrons, Electrophoresis, Polyacrylamide Gel, Isoelectric Focusing, Liver, Rats, Inbred Strains, Receptors, LDL, Triglycerides, Rats

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Binding of rat chylomicrons and their remnants to the hepatic low-density-lipoprotein receptor and its role in remnant removal

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