Enhanced binding by cultured human fibroblasts of apo-E-containing lipoproteins as compared with low density lipoproteins
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ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTEnhanced binding by cultured human fibroblasts of apo-E-containing lipoproteins as compared with low density lipoproteinsThomas L. Innerarity and Robert W. MahleyCite this: Biochemistry 1978, 17, 8, 1440–1447Publication Date (Print):April 18, 1978Publication History Published online1 May 2002Published inissue 18 April 1978https://pubs.acs.org/doi/10.1021/bi00601a013https://doi.org/10.1021/bi00601a013research-articleACS PublicationsRequest reuse permissionsArticle Views191Altmetric-Citations323LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked…
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The apo B,E or LDL receptor is present in most tissues, and apo E has much higher affinity than apo B for it because apo E-containing particles can form multiple interactions with several sites on the receptor.
“The first of these, apo B,E or low-density lipoprotein (LDL) receptor, is present in most tissues.Apo E has a much higher affinity than apolipoprotein B for this receptor because of the potential of apo E-containing particles to form multiple interactions with several sites on the receptor (15)(16)(17).”
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 [16]
Lipidation of apoE significantly alters its propensity to bind to LDLR, with increased lipid levels leading to enhanced binding.
“The lipidation of apoE also significantly alters its propensity to bind to LDLR, with increased lipid levels leading to enhanced binding [46].”
From Measurement of apolipoprotein E and amyloid β clearance rates in the mouse brain using bolus stable isotope labeling (2012) · cites this paper as [46]
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- Authors
- Innerarity, T. L., & Mahley, R. W.
- ORCID
- Mahley, Robert W.
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 1978-04-18
- Volume
- 17
- Issue
- 8
- Pages
- 1440-1447
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W2008099488
- Cited by
- 433
- References
- 0
- Citations by year
- 2026: 1 · 2025: 2 · 2024: 2 · 2023: 1 · 2022: 2 · 2021: 4 · 2020: 1 · 2019: 4 · 2018: 1 · 2017: 1 · 2016: 5 · 2015: 3 · 2014: 8 · 2013: 3 · 2012: 4
- FWCI
- 47.85
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biochemistry (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Surgery › Cholesterol and Lipid Metabolism
- Health Sciences › Medicine › Surgery › Lipoproteins and Cardiovascular Health
- Life Sciences › Immunology and Microbiology › Immunology › Atherosclerosis and Cardiovascular Diseases
- Keywords
- apolipoprotein E, lipoprotein binding, human fibroblasts, low-density lipoprotein, lipoprotein uptake, cultured fibroblasts, cell surface receptors
- MeSH terms
- Animals, Apoproteins, Arginine, Cells, Cultured, Cholesterol, Dietary, Dogs, Fibroblasts, Humans, Lipoproteins, HDL, Lipoproteins, LDL, Protein Binding, Receptors, Drug, Species Specificity, Swine
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