Apolipoprotein E isoforms and lipoprotein metabolism
Abstract
Apolipoprotein (apo) E is a 299‐residue protein which functions as a key regulator of plasma lipid levels. Human apoE exists as three common isoforms and the parent form, apoE3, operates optimally in promoting clearance of triglyceride (TG)‐rich lipoproteins and is associated with normal plasma lipid levels. This result occurs because apoE3 possesses both the requisite lipid‐binding ability and affinity for the low density lipoprotein receptor (LDLR) to mediate appropriate lipolytic processing and endocytosis of TG‐rich lipoprotein remnant particles. ApoE2 which differs from apoE3 by the single amino acid substitution Arg158Cys located near the LDLR recognition site exhibits impaired binding to the receptor and an inability to promote clearance of TG‐rich lipoprotein remnant particles; this isoform is associated with Type‐III hyperlipoproteinemia. ApoE4 which differs from apoE3 by the single amino acid substitution Cys112Arg is also associated with dyslipidemia although binding of this isoform to the LDLR is unaffected. The amino acid substitution affects the organization and stability of both the N‐terminal helix bundle domain and separately folded C‐terminal domain so that apoE4 has enhanced lipid binding ability. As a consequence, apoE4 binds better than apoE3 to the surface of very low density lipoprotein (VLDL) particles and impairs their lipolytic processing in the circulation so that apoE4 is associated with a more pro‐atherogenic lipoprotein‐cholesterol distribution (higher VLDL‐cholesterol/high density lipoprotein‐cholesterol ratio). This review summarizes current understanding of the structural differences between apoE2, apoE3, and apoE4, and the molecular mechanisms responsible for the alterations in lipoprotein metabolism resulting from this polymorphism of apoE. Detailed knowledge of how expression of structurally distinct apoE variants modifies lipoprotein metabolism provides a basis for developing ways to manipulate the functionality of apoE in vivo. © 2014 IUBMB Life, 66(9):616–623, 2014
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The cysteine change at position 158 in APOE2, near the LDLR binding region, hinders APOE2 binding to the LDLR.
“This is attributed to the fact that the cysteine change at position 158 in APOE2, near the LDLR binding region, hinders APOE2 binding to the LDLR [30, 40].”
ApoE4 binds better and is more abundant on the surface of VLDL and chylomicron particles than apoE3 or apoE2.
“As a result, apoE4 binds better and is more abundant on the surface of VLDL and chylomicron particles than apoE3 or apoE2 19).”
From Impact of Apolipoprotein E Variants: A Review of Naturally Occurring Variants and Clinical Features (2025) · cites this paper as [19]
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- Authors
- Phillips, M. C.
- Affiliations
- University of Pennsylvania (US)
- Corresponding author
- Phillips, Michael C.
- ORCID
- Phillips, Michael C.
- Venue
- IUBMB Life
- Publisher
- Wiley
- Published
- 2014-09
- Volume
- 66
- Issue
- 9
- Pages
- 616-623
- ISSN
- 1521-6543 (ISSN-L)
- 1521-6551
- OpenAlex
- W1841798962
- Cited by
- 328
- References
- 59
- Citations by year
- 2026: 20 · 2025: 25 · 2024: 41 · 2023: 35 · 2022: 36 · 2021: 38 · 2020: 27 · 2019: 27 · 2018: 24 · 2017: 23 · 2016: 22 · 2015: 8
- FWCI
- 2.85
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- IUBMB Life (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Lipid metabolism and disorders
- Health Sciences › Medicine › Surgery › Lipoproteins and Cardiovascular Health
- Health Sciences › Medicine › Surgery › Cholesterol and Lipid Metabolism
- Keywords
- apolipoprotein E, apolipoprotein E isoforms, apolipoprotein E2, apolipoprotein E3, APOE ε4, lipoprotein metabolism, LDL receptor binding, type III hyperlipoproteinemia, dyslipidemia, VLDL cholesterol, protein structure, lipid binding, genetic polymorphism
- MeSH terms
- Apolipoproteins E, Humans, Lipoproteins, Models, Molecular, Protein Binding, Amino Acid Substitution, Protein Isoforms, Lipid Metabolism Disorders
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