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The receptor-binding domain of human apolipoprotein E. Binding of apolipoprotein E fragments.

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Innerarity, T L, Friedlander, E J, Rall, S C, Weisgraber, K H, Mahley, R W·1983·Journal of Biological Chemistry
DOI 10.1016/s0021-9258(17)44180-9
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Abstract

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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  • When the 22-kDa thrombolytic fragment of apoE3-Leiden was complexed with DMPC, its receptor binding activity was nearly identical to normal apoE3·DMPC and the normal apoE3 22-kDa thrombolytic fragment.

    “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]

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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)
DOI
10.1016/s0021-9258(17)44180-9
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
Licence
Locations
  • Journal of Biological Chemistry (publishedVersion, cc-by)
  • PubMed (publishedVersion)
Topics
  • Health Sciences › Medicine › Surgery › Cholesterol and Lipid Metabolism
  • Health Sciences › Medicine › Surgery › Lipoproteins and Cardiovascular Health
  • Health Sciences › Medicine › Physiology › 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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