Journal article
Effect of apolipoprotein C-I peptides on the apolipoprotein E content and receptor-binding properties of beta-migrating very low density lipoproteins
Journal of lipid research, v 35(1), pp 134-142
01 Jan 1994
PMID: 8138714
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
To evaluate the role of apolipoprotein (apo) C-I in inhibiting lipoprotein binding to the low density lipoprotein receptor-related protein (LRP), a putative lipoprotein remnant receptor, apoC-peptide fragments were prepared by chemical synthesis or by cyanogen bromide cleavage of intact apoC-I. In ligand-blotting assays, peptides corresponding to residues 1-38, 10-57, 20-57, 30-57, and 40-57 proved ineffective, but intact apoC-I was very effective, at inhibiting the binding of apoE-enriched beta-migrating very low density lipoproteins (beta-VLDL) to the LRP. Studies of the displacement of 125I-labeled apoE from apoE-enriched beta-VLDL showed that the largest peptide (residues 10-57) was two-thirds as effective as intact apoC-I; the other peptides were highly ineffective (residues 40-57, 1-38) or only partly effective (residues 20-57, 30-57). Changes in the intrinsic tryptophan fluorescence and helix content indicated that the largest peptide was similar to apoC-I in lipid binding affinity, while the other peptide fragments showed little or no affinity for either unilamellar or multilamellar vesicles of dimyristoyl-phosphatidylcholine. These findings suggest that the ability of apoC-I fragments to displace apoE from beta-VLDL is largely, but perhaps not exclusively, a reflection of their ability to bind to membranous bilayers and that apoC-I blocking of the interaction between apoE-rich beta-VLDL and the LRP probably involves displacement of a critical amount of the apoE from the surface of this lipoprotein.
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Details
- Title
- Effect of apolipoprotein C-I peptides on the apolipoprotein E content and receptor-binding properties of beta-migrating very low density lipoproteins
- Creators
- John B Swaney
- Publication Details
- Journal of lipid research, v 35(1), pp 134-142
- Publisher
- Elsevier
- Resource Type
- Journal article
- Language
- English
- Web of Science ID
- WOS:A1994MQ38700015
- Scopus ID
- 2-s2.0-0028010952
- Other Identifier
- 991019350685104721
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- Collaboration types
- Domestic collaboration
- Web of Science research areas
- Biochemistry & Molecular Biology