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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]
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Examination of Lipid-bound Conformation of Apolipoprotein E4 by Pyrene Excimer Fluorescence
Drury, J., & Narayanaswami, V. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m414019200 · Cited by 37
Wang, H., Eschweiler, J. D., Cui, W., Zhang, H., Frieden, C., Ruotolo, B. T., & Gross, M. L. (2019) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-019-02148-z · Cited by 37
Orientation and mode of lipid-binding interaction of human apolipoprotein E C-terminal domain
Raussens, V., Drury, J., Forte, T. M., Choy, N., Goormaghtigh, E., Ruysschaert, J., & Narayanaswami, V. (2005) · Biochemical Journal · doi:10.1042/bj20041536 · Cited by 35
Lins, L., Thomas‐Soumarmon, A., Pillot, T., Vandekerckhove, J. S., Rosseneu, M., & Brasseur, R. (1999) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1999.0730758.x · Cited by 36
Perugini, M. A., Schuck, P., & Howlett, G. J. (2002) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2002.03319.x · Cited by 35
The C Terminus of Apolipoprotein A-V Modulates Lipid-binding Activity
Beckstead, J. A., Mauldin, K., Gupta, V., Wan, C.-P. L., Cook, V. R., Weinberg, R. B., Weers, P. M. M., & Ryan, R. O. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m611797200 · Cited by 35
Pillot, T., Goethals, M., Vanloo, B., Lins, L., Brasseur, R., Vandekerckhove, J. S., & Rosseneu, M. (1997) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1997.00650.x · Cited by 35
Weers, P. M. M., Narayanaswami, V., Choy, N., Luty, R., Hicks, L. D., Kay, C. M., & Ryan, R. O. (2002) · Biophysical Chemistry · doi:10.1016/s0301-4622(02)00300-9 · Cited by 33
Mishra, V., Palgunachari, M. N., Lund‐Katz, S., Phillips, M. C., Segrest, J. P., & Anantharamaiah, G. M. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.4.1602 · Cited by 33
Hoffer, M. J. V., Niththyananthan, S., Naoumova, R. P., Kibirige, M. S., Frants, R. R., Havekes, L. M., & Thompson, G. R. (1996) · Atherosclerosis · doi:10.1016/0021-9150(96)05819-4 · Cited by 32
Sheng, Z., Prorok, M., Brown, B., & Castellino, F. (2008) · Neuropharmacology · doi:10.1016/j.neuropharm.2008.05.016 · Cited by 32
“…HSPGs (Mahley and Ji, 1999) The 10 kDa COOH-terminal domain facilitates the association of apoE with various lipoproteins (Weisgraber and Xi, 1990; Westerlund and Weisgraber, 1993), and is also responsible for the self-association of lipid-free apoE (Aggerbeck et al., 1988) This latter region…”
BackgroundThe HepG2 Extracellular Matrix Contains Separate Heparinase- and Lipid-releasable Pools of ApoE
Burgess, J. W., Gould, D. R., & Marcel, Y. L. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.10.5645 · Cited by 30
Apo E: The role of conserved residues in defining function
Frieden, C. (2015) · Protein Science · doi:10.1002/pro.2597 · Cited by 29
“2(D)] in agreement with earlier reports that the region spanning residues 250–299 was important for lipid binding.(22,23) On the other hand, the region of 230–243 is not conserved (Fig.”
MethodResultKypreos, K. E., Teusink, B., Dijk, K. O. W., Havekes, L. M., & Zannis, V. I. (2001) · The FASEB Journal · doi:10.1096/fj.00-0882fje · Cited by 29
Structural Basis for the Recognition and Cross-linking of Amyloid Fibrils by Human Apolipoprotein E
Gunzburg, M. J., Perugini, M. A., & Howlett, G. J. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m706425200 · Cited by 28
Garai, K., Baban, B. A., & Frieden, C. (2011) · Biochemistry · doi:10.1021/bi2006702 · Cited by 27
Dong, L., Innerarity, T. L., Arnold, K. S., Newhouse, Y. M., & Weisgraber, K. H. (1998) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)32541-4 · Cited by 26
Self-citationRole of Apolipoprotein E in Alzheimer’s Disease
Zannis, V. I., Zanni, E. E., Makrides, S. C., Kardassis, D., & Aleshkov, S. B. (1998) · Springer eBooks · doi:10.1007/978-1-4899-0133-0_13 · Cited by 26
Tran, T. N., Kim, S. H., Gallo, C., Amaya, M., Kyees, J., & Narayanaswami, V. (2012) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2012.10.007 · Cited by 26
NMR Structure and Dynamics of a Receptor-active Apolipoprotein E Peptide
Raussens, V., Slupsky, C. M., Ryan, R. O., & Sykes, B. D. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m204043200 · Cited by 26
Yamamura, T., Dong, L.-M., & Yamamoto, A. (1999) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)33364-2 · Cited by 25
Peelman, F., Goethals, M., Vanloo, B., Labeur, C., Brasseur, R., Vandekerckhove, J. S., & Rosseneu, M. (1997) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1997.t01-2-00708.x · Cited by 25
Muñoz, S. S., Li, H., Ruberu, K. R., Chu, Q., Saghatelian, A., Ooi, L., & Garner, B. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra117.001278 · Cited by 24
“regions in the C-terminal domain (such as permitting lipoprotein interaction (67, 70), promoting self-aggregation (67, 70), and”
BackgroundStructure-guided Protein Engineering Modulates Helix Bundle Exchangeable Apolipoprotein Properties
Kiss, R. S., Weers, P. M. M., Narayanaswami, V., Cohen, J. K., Kay, C. M., & Ryan, R. O. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m302676200 · Cited by 24
ApoE: In Vitro Studies of a Small Molecule Effector
Mondal, T., Wang, H., DeKoster, G. T., Baban, B. A., Gross, M. L., & Frieden, C. (2016) · Biochemistry · doi:10.1021/acs.biochem.6b00324 · Cited by 25
“Based on results using C-terminal truncated forms of apoE, Weisgraber and colleagues (31, 32) suggested that a region of the C-terminal domain 250–299 was critical for lipid binding.”
ResultExtracellular Interactions between Hepatitis C Virus and Secreted Apolipoprotein E
Li, Z., Li, Y., Bi, Y., Zhang, H., Yao, Y., Li, Q., Cun, W., & Dong, S. (2017) · Journal of Virology · doi:10.1128/jvi.02227-16 · Cited by 23
“phobic surface and that interact with residues in the N-terminal helix bundle domain through hydrogen bonds and salt bridges (26).”
BackgroundHsieh, Y.-H., & Chou, C. (2011) · Journal of Biomedical Science · doi:10.1186/1423-0127-18-4 · Cited by 23
“The residues between 140-150 in the fourth a-helix, comprising many basic amino acids, has been identified as the low-density lipoprotein receptor (LDLR) binding region [4], with the lipid binding region shown to be in the carboxyl-terminal (CT) domain [5,6].”
Background
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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