A Monomeric, Biologically Active, Full-Length Human Apolipoprotein E
Abstract
Apolipoprotein E (apoE) is an exchangeable apolipoprotein that plays an important role in lipid/lipoprotein metabolism and cardiovascular diseases. Recent evidence indicates that apoE is also critical in several other important biological processes, including Alzheimer's disease, cognitive function, immunoregulation, cell signaling, and infectious diseases. Although the X-ray crystal structure of the apoE N-terminal domain was solved in 1991, the structural study of full-length apoE is hindered by apoE's oligomerization property. Using protein-engineering techniques, we generated a monomeric, biologically active, full-length apoE. Cross-linking experiments indicate that this mutant is nearly 95-100% monomeric even at 20 mg/mL. CD spectroscopy and guanidine hydrochloride denaturation demonstrate that the structure and stability of the monomeric mutant are identical to wild-type apoE. Monomeric and wild-type apoE display similar lipid-binding activities in dimyristoylphosphatidylcholine clearance assays and formation of reconstituted high-density lipoproteins. Furthermore, the monomeric and wild-type apoE proteins display an identical LDL receptor binding activity. Availability of this monomeric, biologically active, full-length apoE allows us to collect high quality NMR data for structural determination. Our initial NMR data of lipid-free apoE demonstrates that the N-terminal domain in the full-length apoE adopts a nearly identical structure as the isolated N-terminal domain, whereas the C-terminal domain appears to become more structured than the isolated C-terminal domain fragment, suggesting a weak domain-domain interaction. This interaction is confirmed by NMR examination of a segmental labeled apoE, in which the N-terminal domain is deuterated and the C-terminal domain is double-labeled. NMR titration experiments further suggest that the hinge region (residues 192-215) that connects apoE's N- and C-terminal domains may play an important role in mediating this domain-domain interaction.
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APOE itself has been shown to form aggregates, particularly in its non-lipidated state.
“however, APOE itself has also been shown to form aggregates, particularly in its non-lipidated state99,134,135 (Fig. 2).”
From Multifaceted roles of APOE in Alzheimer disease (2024) · cites this paper as [135]
ApoE self-associates through the C-terminal domain, and the C-terminal α-helical regions are responsible for the self-association.
“ApoE is known to self-associate through the C-terminal domain in solution and the C-terminal α-helical regions are responsible for the self-association (21, 45–47).”
From Role of the N- and C-Terminal Domains in Binding of Apolipoprotein E Isoforms to Heparan Sulfate and Dermatan Sulfate: A Surface Plasmon Resonance Study (2008) · cites this paper as [46]
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- Authors
- Zhang, Y., Vasudevan, S., Sojitrawala, R., Zhao, W., Cui, C., Xu, C., Fan, D., Newhouse, Y., Balestra, R., Jerome, W. G., Weisgraber, K., Li, Q., & Wang, J.
- Affiliations
- Southern Illinois University Carbondale (US)
- Corresponding author
- Wang, Jianjun
- ORCID
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 2007-08-23
- Volume
- 46
- Issue
- 37
- Pages
- 10722-10732
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W2067976699
- Cited by
- 79
- References
- 4
- Citations by year
- 2026: 3 · 2025: 3 · 2024: 2 · 2023: 5 · 2022: 2 · 2021: 2 · 2020: 3 · 2019: 6 · 2018: 3 · 2017: 5 · 2016: 1 · 2015: 2 · 2014: 5 · 2013: 2 · 2012: 5
- FWCI
- 2.62
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biochemistry (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute on Aging (R01AG020235)
- National Heart, Lung, and Blood Institute (R01HL049148, R01HL074365)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Health Sciences › Medicine › Surgery › Cholesterol and Lipid Metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
- Keywords
- apolipoprotein E, oligomerization, domain-domain interactions, N-terminal domain, C-terminal domain, hinge region, lipid binding, LDL receptor binding, protein structure, protein stability
- MeSH terms
- Circular Dichroism, Dimyristoylphosphatidylcholine, Humans, Lipoproteins, HDL, Magnetic Resonance Spectroscopy, Protein Binding, Receptors, LDL, Structure-Activity Relationship, Thermodynamics, Protein Engineering, Protein Structure, Tertiary, Lipid Metabolism, Mutant Proteins, Apolipoprotein E3
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