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The receptor-binding domain of human apolipoprotein E. Binding of apolipoprotein E fragments.
Open accessAbstract
To identify the domain of apolipoprotein E (apo-E) involved in binding to low density lipoprotein (LDL) receptors on cultured human fibroblasts, apo-E was cleaved and the fragments were tested for receptor binding activity. Two large thrombolytic peptides (residues 1-191 and 216-299) of normal apo-E3 were combined with the phospholipid dimyristoylphosphatidylcholine (DMPC) and tested for their ability to compete with 125I-LDL for binding to the LDL (apo-B,E) receptors on human fibroblasts. The NH2-terminal two-thirds (residues 1-191) of apo-E3 was as active as intact apo-E3 . DMPC, while the smaller peptide (residues 216-299) was devoid of receptor-binding activity. When apo-E3 was digested with cyanogen bromide (CNBr) and the four largest CNBr fragments were combined with DMPC and tested, only one fragment competed with 125I-LDL for binding to cultured human fibroblasts (CNBr II, residues 126-218). This fragment possessed binding activity similar to that of human LDL. The 125I-labeled CNBr II . DMPC complex also demonstrated high affinity, calcium-dependent saturable binding to solubilized bovine adrenal membranes. The binding of CNBr II . DMPC was inhibited by 1,2-cyclohexanedione modification of arginyl residues or diketene modification of lysyl residues. In addition, the CNBr II had to be combined with DMPC before it demonstrated any receptor-binding activity. Pronase treatment of the membranes abolished the ability of this fragment to bind to the apo-B,E receptors. This…
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“In contrast, when the 22-kDa thrombolytic fragment of apoE3Leiden was complexed with DMPC, its receptor binding activity was nearly identical to normal apoE3·DMPC (Fig. 6) and the normal apoE3 22-kDa thrombolytic fragment (24).”
From Apolipoprotein E3-Leiden contains a seven-amino acid insertion that is a tandem repeat of residues 121–127 (1989) · cites this paper as [24]
In the citing paper
“While numerous lipoprotein receptors have been shown to interact with apoE in the brain, the LDLR is the only receptor in its class of receptors to show varying binding affinities for the three apoE isoforms (E4 > E3 >> E2) (Innerarity et al., 1983, Yamamoto et al., 2008).”
From Apolipoprotein E–low density lipoprotein receptor interaction affects spatial memory retention and brain ApoE levels in an isoform-dependent manner (2014) · cites this paper as Innerarity et al., 1983
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Metadata
- Authors
- Innerarity, T. L., Friedlander, E. J., Rall, S. C., Weisgraber, K. H., & Mahley, R. W.
- Affiliations
- University of California, San Francisco (US)
- ORCID
- Mahley, R W
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1983-10
- Volume
- 258
- Issue
- 20
- Pages
- 12341-12347
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W134453782
- Cited by
- 276
- References
- 33
- Citations by year
- 2026: 4 · 2024: 3 · 2023: 2 · 2022: 1 · 2021: 1 · 2020: 5 · 2019: 1 · 2017: 4 · 2016: 2 · 2015: 3 · 2014: 7 · 2013: 3 · 2012: 1
- FWCI
- 28.66
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Cholesterol and Lipid Metabolism
- Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Lipoproteins and Cardiovascular Health
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Keywords
- apolipoprotein E, receptor binding domain, LDL receptor, apolipoprotein E3, CNBr fragments, dimyristoylphosphatidylcholine, calcium-dependent binding, fibroblasts
- MeSH terms
- Adrenal Cortex, Amino Acids, Animals, Apolipoproteins, Apolipoproteins E, Cattle, Cell Membrane, Cells, Cultured, Fibroblasts, Humans, Infant, Newborn, Kinetics, Lipoproteins, LDL, Male, Peptide Fragments, Receptors, Cell Surface, Receptors, LDL, Skin, Thrombin
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