Apolipoprotein E Effectively Inhibits Lipoprotein Lipase-mediated Lipolysis of Chylomicron-like Triglyceride-rich Lipid Emulsions and

Rensen, Patrick C.N.; van Berkel, Theo J.C.

doi:10.1074/jbc.271.25.14791

Cited by 144Lipid metabolism and disordersLipid metabolism and biosynthesisCholesterol and Lipid Metabolism

Apolipoprotein E Effectively Inhibits Lipoprotein Lipase-mediated Lipolysis of Chylomicron-like Triglyceride-rich Lipid Emulsions and

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Rensen, Patrick C.N., van Berkel, Theo J.C.·1996·Journal of Biological Chemistry

DOI 10.1074/jbc.271.25.14791

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Abstract

Apolipoprotein E (apoE) is an important determinant for the liver uptake of triglyceride-rich lipoproteins and emulsions by the remnant receptor. In the current study, we assessed an additional role of apoE as modulator of the metabolism of triglyceride-rich lipoproteins in vitro and in vivo. Glycerol tri[3H]oleate [14C]cholesteryl oleate double-labeled triglyceride-rich emulsions were injected into fasted rats. The serum half-life of glycerol tri[3H]oleate was 3-fold faster (5.4 min) than that of [14C]cholesteryl oleate (16.7 min), confirming lipoprotein lipase (LPL)-mediated processing. To establish a specific effect of apoE on emulsion lipolysis rather than liver uptake, rats were functionally hepatectomized, and hypo(apo)lipoproteinemia was induced by 17alpha-ethinyl estradiol treatment. An apoE concentration-dependent inhibition of emulsion-triglyceride hydrolysis was observed, reaching a 14.8-fold increased half-life of glycerol tri[3H]oleate as compared with that in the absence of exogenous apoE. The mechanism and specificity of the effect of apoE on emulsion lipolysis by purified LPL was assessed in vitro. Addition of apoE to glycerol tri[3H]oleate-labeled emulsions led to a concentration-dependent inhibition of [3H]oleate release (9.5% residual LPL activity at 60 microg/ml apoE), while apoA-I was ineffective. The inhibitory effect of apoE was not abolished by reductive methylation of lysine residues, whereas selective modification of arginine residues by 1,2-cyclohexadione completely cancelled the inhibitory effect of apoE. It is concluded that apoE can specifically inhibit the LPL-mediated hydrolysis of emulsion triglycerides both in vitro and in vivo, and that arginine residues in apoE are essential for this effect. We suggest that in addition to its role in receptor recognition, apoE also modulates the LPL-mediated processing of triglyceride-rich lipoproteins.

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An excess of APOE on VLDL particles can hinder their lipolysis, resulting in elevated plasma triglyceride levels.
“Additionally, an excess of APOE on VLDL particles can hinder their lipolysis [34], resulting in elevated plasma triglyceride levels.”
From Analysis of early effects of human APOE isoforms on Alzheimer’s disease and type III hyperlipoproteinemia pathways using knock-in rat models with humanized APP and APOE (2024) · cites this paper as [34]
The paper reports that apoE content was inversely correlated with the lipolysis rate of VLDL in vitro (background passage labeled Abstract; page unavailable). Its own in-vivo experiments found inhibited lipolysis of apoE-enriched chylomicron-like emulsions, not VLDL. The paper suggests a role in regulating plasma triglycerides but does not establish that excess apoE on VLDL elevates plasma triglyceride levels. (LLM, conf=0.83)
Experimental — accuracy not yet measured
In vessels, apoE on VLDL and chylomicron particles competitively inhibits triglyceride degradation processing by lipoprotein lipase (LPL) promoted by apoC-II and apoA-V.
“Meanwhile, in vessels, apoE on VLDL and chylomicron particles competitively inhibits triglyceride degradation processing by lipoprotein lipase (LPL) promoted by apoC-II and apoA-V20).”
From Impact of Apolipoprotein E Variants: A Review of Naturally Occurring Variants and Clinical Features (2025) · cites this paper as [20]
The ‘Effect of ApoE on LPL Activity in Vitro’ section (page unavailable) reports that apoE inhibited LPL-mediated triglyceride hydrolysis in chylomicron-like emulsions even when apoC-II was present. The Discussion (page unavailable) describes supporting experiments in rats, but the paper does not establish competitive inhibition by apoE on native VLDL and chylomicrons, or address apoA-V’s role in promoting lipolysis. (LLM, conf=0.88)
Experimental — accuracy not yet measured
The insufficiency of LPL appears to result from inhibition of this enzyme by apoE, which accumulates in VLDL/IDL/LDL-size lipoprotein particles.
“As reported previously ( 36,37 ), the insuffi ciency of LPL appears to result from inhibition of this enzyme by apoE, which accumulates in VLDL/IDL/LDL-size lipoprotein particles.”
From Molecular etiology of a dominant form of type III hyperlipoproteinemia caused by R142C substitution in apoE4 (2011) · cites this paper as [37]
The paper concludes that apoE inhibits LPL-mediated hydrolysis of chylomicron-like emulsion triglycerides in vitro and in vivo. It also says VLDL and chylomicrons become enriched in apoE during lipolysis, but the cited passages do not establish that apoE accumulation in VLDL/IDL/LDL-size particles causes the particular LPL insufficiency described here. Page numbers are unavailable in our copy. (LLM, conf=0.85)
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Self-citation
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Self-citation
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Background
apoE3[K146N/R147W] acts as a dominant negative apoE form that prevents remnant clearance and inhibits the biogenesis of HDL
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Authors: Rensen, P. C. N., & van Berkel, T. J. C.
Affiliations: Leiden University (NL)
Corresponding author: Rensen, Patrick C.N.
ORCID: Rensen, Patrick C.N.
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 1996-06
Volume: 271
Issue: 25
Pages: 14791-14799
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1074/jbc.271.25.14791
OpenAlex: W2134193555
Cited by: 144
References: 77
Citations by year: 2025: 3 · 2024: 2 · 2023: 2 · 2022: 3 · 2021: 4 · 2020: 3 · 2019: 8 · 2018: 3 · 2017: 1 · 2016: 2 · 2015: 3 · 2014: 7 · 2013: 4 · 2012: 4
FWCI: 9.58
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 8902 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
PubMed (publishedVersion)
Topics: Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Lipid metabolism and disorders
Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Lipid metabolism and biosynthesis
Health Sciences › Medicine › Surgery › Cholesterol and Lipid Metabolism
Keywords: apolipoprotein E, lipoprotein lipase, triglyceride-rich lipoproteins, lipolysis, lipolysis inhibition, arginine residues, hepatectomy, apolipoprotein A-I, lysine methylation, serum half-life
MeSH terms: Animals, Apolipoproteins E, Cholesterol Esters, Chylomicrons, Emulsions, Fasting, Half-Life, Hepatectomy, Humans, Kinetics, Lipolysis, Lipoprotein Lipase, Liver, Male, Recombinant Proteins, Time Factors, Triglycerides, Triolein, Tritium, Mutagenesis, Site-Directed, Rats, Wistar, Point Mutation, Rats

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Apolipoprotein E Effectively Inhibits Lipoprotein Lipase-mediated Lipolysis of Chylomicron-like Triglyceride-rich Lipid Emulsions and

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