Lipoprotein binding to canine hepatic membranes. Metabolically distinct apo-E and apo-B,E receptors.
Open accessAbstract
Hepatic membranes from adult dog livers have receptors which bind to lipoproteins containing the E apoprotein (the apo-E HDLc) but lack specific receptors for the apo-B-containing low density lipoproteins (LDL). Scatchard analysis of direct binding data for 125I-apo-E-HDLc revealed nonlinearity of the binding which could be resolved into two components, suggesting the presence of two separate binding sites. The binding site for apo-E HDLc that possessed the highest affinity (Kd = 0.23 x 10(-9) M) was calcium-dependent and was sensitive to proteolytic digestion with pronase. The lower affinity (Kd = 20 x 10(-9) M) binding site for apo-E HDLc did not require calcium and was resistant to pronase digestion. Chemical modification of the arginyl or lysyl residues of the apo-E HDLc prevented the HDLc from binding to the higher affinity receptor but had no effect on their binding to the lower affinity site. Adult canine liver membranes also bound canine 125I-HDL. However, the binding of HDL was of lower affinity (Kd = 8.2 x 10(-8) M), did not require calcium, was not blocked by modification of the lysyl or arginyl residues, and may not be of physiologic significance. Although the liver membranes from normal chow-fed adult dogs did not bind canine LDL, it was possible to demonstrate specific high affinity binding of LDL under certain metabolic conditions in dogs. When adult dogs were treated with the hypocholesterolemic agent cholestyramine, the liver membranes from these animals read…
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The apo E or remnant receptor is found only in hepatic tissues and recognizes particles containing apo E but not apo B.
“The second is the apo E or remnant receptor, which is found in hepatic tissues only and is able to recognize particles containing apo E but not apo B (18).”
From Apolipoprotein E2-Christchurch (136 Arg----Ser). New variant of human apolipoprotein E in a patient with type III hyperlipoproteinemia. (1987) · cites this paper as [18]
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- Authors
- Hui, D. Y., Innerarity, T. L., & Mahley, R. W.
- Affiliations
- University of California System (US)
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1981-06
- Volume
- 256
- Issue
- 11
- Pages
- 5646-5655
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1488147530
- Cited by
- 383
- References
- 2
- Citations by year
- 2020: 1 · 2019: 1 · 2018: 2 · 2015: 2 · 2014: 1 · 2013: 3 · 2012: 1
- FWCI
- 85.81
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- 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 › Cardiology and Cardiovascular Medicine › Lipid metabolism and disorders
- Keywords
- lipoprotein receptors, canine liver, HDL cholesterol, low-density lipoprotein, receptor binding sites, calcium-dependent binding, cholestyramine, hypocholesterolemia, receptor binding affinity, Scatchard analysis
- MeSH terms
- Animals, Apolipoproteins, Apolipoproteins B, Apolipoproteins E, Calcium, Cell Membrane, Cholestyramine Resin, Dogs, Edetic Acid, Female, Hydrogen-Ion Concentration, Kinetics, Lipoproteins, HDL, Lipoproteins, VLDL, Liver, Male, Receptors, Cell Surface, Low Density Lipoprotein Receptor-Related Protein-1
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