The DOI matches its Crossref record; 35 of the 35 references it cites were found in a registry or an index.
Discrete carboxyl-terminal segments of apolipoprotein E mediate lipoprotein association and protein oligomerization
Open accessAbstract
The carboxyl terminus of apolipoprotein (apo) E is required for lipoprotein association and for tetramer formation. To correlate these roles with specific regions within the carboxyl terminus, a series of apoE3 variants with carboxyl-terminal truncations at residues 266, 244, 223, and 191 were expressed in Escherichia coli. As determined by gel permeation and sedimentation equilibrium centrifugation, the four truncated variants were monomeric in solution. Compared to native apoE3 (299 residues), all had reduced affinity for lipoproteins, as assessed by incubation of 125I-labeled proteins with plasma followed by fractionation of lipoprotein classes by gel filtration. The 266-residue variant associated with very low density lipoproteins and high density lipoproteins, but was partly non-lipoprotein-bound (25% of total). Shorter variants, with 244 or fewer residues, did not associate with very low density lipoproteins and only associated slightly (approximately 20%) with high density lipoproteins, with the major portion non-lipoprotein-bound (65-73%). After these proteins were injected into rabbits, the clearance rate was proportional to the plasma level of non-lipoprotein-bound protein. These results indicate lipoprotein association modulates the clearance of apoE, residues within the segment 267-299 are critical for apoE tetramerization and facilitate lipoprotein association, and residues within the segment 245-266 also contribute to lipoprotein association.
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In the citing paper
“APOE has two domains separated by a short hinge region.”
From APOE traffics to astrocyte lipid droplets and modulates triglyceride saturation and droplet size (2024) · cites this paper as Westerlund and Weisgraber, 1993
In the citing paper
“Its N-terminal domain forms a soluble four-helix bundle and contains a patch of basic residues required for APOE binding to lipoprotein receptors; the C-terminal domain is an amphipathic alpha-helix that mediates binding of APOE to the surface of lipoproteins (Westerlund and Weisgraber, 1993).”
From APOE traffics to astrocyte lipid droplets and modulates triglyceride saturation and droplet size (2024) · cites this paper as Westerlund and Weisgraber, 1993
In the citing paper
“Its N-terminal domain forms a soluble four-helix bundle and contains a patch of basic residues required for APOE binding to lipoprotein receptors; the C-terminal domain is an amphipathic alpha-helix that mediates binding of APOE to the surface of lipoproteins (Westerlund and Weisgraber, 1993).”
From APOE traffics to astrocyte lipid droplets and modulates triglyceride saturation and droplet size (2024) · cites this paper as Westerlund and Weisgraber, 1993
In the citing paper
“whereas the C-terminal domain contains amphipathic α-helices that are involved in binding to lipoproteins with high affinity (21, 22).”
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 [21]
In the citing paper
“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 [21]
Citations
Cites
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Self-citationSegrest, J., Jones, M., Loof, H. D., Brouillette, C. G., Venkatachalapathi, Y. V., & Anantharamaiah, G. M. (1992) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)41536-6 · Cited by 868
Three-Dimensional Structure of the LDL Receptor-Binding Domain of Human Apolipoprotein E
Wilson, C., Wardell, M. R., Weisgraber, K. H., Mahley, R. W., & Agard, D. A. (1991) · Science · doi:10.1126/science.2063194 · Cited by 678
Self-citationAmphipathic helix motif: Classes and properties
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Self-citationHuman apolipoprotein E3 in aqueous solution. I. Evidence for two structural domains.
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Self-citationThe receptor-binding domain of human apolipoprotein E. Binding of apolipoprotein E fragments.
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Self-citation
Research works printed but not linked: 1
- Kraft, 1988, Biotech niques, 6, 544
Cited by
Sorted by citations
Apolipoprotein E: Structure-Function Relationships
Weisgraber, K. H. (1994) · Advances in Protein Chemistry · doi:10.1016/s0065-3233(08)60642-7 · Cited by 830
Self-citationStrittmatter, W. J., Saunders, A. M., Goedert, M., Weisgraber, K. H., Dong, L. M., Jakes, R., Huang, D. Y., Pericak-Vance, M., Schmechel, D., & Roses, A. D. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.23.11183 · Cited by 474
Self-citationApolipoprotein E: an important gene and protein to follow in laboratory medicine
Siest, G., Pillot, T., Régis-Bailly, A., Leininger-Muller, B., Steinmetz, J., Galteau, M. M., & Visvikis, S. (1995) · Clinical Chemistry · doi:10.1093/clinchem/41.8.1068 · Cited by 347
“Studies to determine the carboxy-terminal region of apo E were mainly performed with truncated variants and synthetic peptide fragments (23).”
BackgroundApolipoprotein E isoforms and lipoprotein metabolism
Phillips, M. C. (2014) · IUBMB Life · doi:10.1002/iub.1314 · Cited by 328
Dong, L. M., Wilson, C., Wardell, M. R., Simmons, T., Mahley, R. W., Weisgraber, K. H., & Agard, D. A. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)31797-0 · Cited by 320
Self-citation
Metadata
- Authors
- Westerlund, J. A., & Weisgraber, K. H.
- Affiliations
- University of California, San Francisco (US)
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1993-07
- Volume
- 268
- Issue
- 21
- Pages
- 15745-15750
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1659662945
- Cited by
- 164
- References
- 35
- Citations by year
- 2026: 2 · 2025: 1 · 2024: 4 · 2023: 1 · 2022: 4 · 2021: 2 · 2020: 3 · 2019: 6 · 2018: 3 · 2017: 4 · 2016: 4 · 2015: 5 · 2014: 7 · 2013: 3 · 2012: 4
- FWCI
- 4.44
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- National Heart, Lung, and Blood Institute (HL-41633, P01HL041633)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Lipoproteins and Cardiovascular Health
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Cholesterol and Lipid Metabolism
- Keywords
- apolipoprotein E, carboxyl-terminal truncation, protein oligomerization, tetramer formation, VLDL, high-density lipoprotein, plasma clearance, protein-lipid interactions
- MeSH terms
- Animals, Apolipoproteins E, Humans, Iodine Radioisotopes, Lipoproteins, HDL, Lipoproteins, VLDL, Male, Metabolic Clearance Rate, Mutation, Peptide Fragments, Polymers, Protein Binding, Rabbits
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