Cited by 277Cholesterol and Lipid MetabolismLipoproteins and Cardiovascular HealthAlzheimer's disease research and treatments

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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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Mahley, R. W., and Angelin, B. (1983) Adv. Intern. Med., in press

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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: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 13542 d)
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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The receptor-binding domain of human apolipoprotein E. Binding of apolipoprotein E fragments.

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