Human very low density lipoprotein apolipoprotein E isoprotein polymorphism is explained by genetic variation and posttranslational modification
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ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTHuman very low density lipoprotein apolipoprotein E isoprotein polymorphism is explained by genetic variation and posttranslational modificationVassilis I. Zannis and Jan L. BreslowCite this: Biochemistry 1981, 20, 4, 1033–1041Publication Date (Print):February 17, 1981Publication History Published online1 May 2002Published inissue 17 February 1981https://doi.org/10.1021/bi00507a059Request reuse permissionsArticle Views373Altmetric-Citations400LEARN 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 InReddit PDF (4 MB) Get e-Alertsclose Get e-Alerts
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The complex isoelectric focusing pattern of apo E results from posttranslational desialylation superimposed on genetic polymorphism.
“The complex isoelectric focusing pattern exhibited by apo E results from posttranslational desialylation superimposed on genetic polymorphism (45,46).”
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 [45]
Apo E3 is the most common form in the population and is regarded as the parent or normal isoform.
“As apo E3 is the most common form in the population (28, 45, 47), it is regarded as the parent (24) or normal isoform (48).”
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 [45]
APOE2 homozygosity can lead to Hyperlipoproteinemia type III (HLP), characterized by mixed hypercholesterolemia and hypertriglyceridemia.
“The critical role of APOE in lipid metabolism is underscored by evidence showing that APOE2 homozygosity can lead to Hyperlipoproteinemia type III (HLP), characterized by mixed hypercholesterolemia and hypertriglyceridemia [35–39].”
APOE2hAβ rats are characterized as a model for type III HLP.
“This observation, coupled with evident mixed hypercholesterolemia and hypertriglyceridemia, supports the characterization of APOE2hAβ rats as a model for type III HLP”
There are three common APOE alleles (E2, E3, and E4), each encoding APOE isoforms expressed primarily in the liver and brain.
“There are three common APOE alleles (E2, E3, and E4), each encoding APOE isoforms expressed primarily in the liver and brain.7,8”
From AAVrh.10-Mediated APOE2 Central Nervous System Gene Therapy for APOE4-Associated Alzheimer's Disease (2018) · cites this paper as [8]
Human apoE has three isoforms, apoE2, apoE3, and apoE4, corresponding to three common alleles, ε2, ε3, and ε4, defined by two exonic SNPs, rs429358/ε4 and rs7412/ε2, in APOE.
“Human apoE has three isoforms: apoE2, apoE3, and apoE4.Genetically, these isoforms correspond to three common alleles, ε2, ε3, and ε4, defined by two exonic single nucleotide polymorphisms (SNPs; rs429358/ε4, rs7412/ε2) in APOE [13,29].”
From Plasma levels of apolipoprotein E, APOE genotype and risk of dementia and ischemic heart disease: A review (2016) · cites this paper as [29]
The introduction of additional basic residues in apoE ɛ3 and apoE ɛ4 results in a shift in the isoelectric point of the proteins and was the basis of their nomenclature.
“The introductionof the additional basic residues in apoE ɛ3 and apoE ɛ4 results in a shift in the isoelectric point of the proteins and was the basis of their nomenclature [4, 5].”
From Discovery of a Missense Mutation (Q222K) of the <i>APOE</i> Gene from the Australian Imaging, Biomarker and Lifestyle Study (2023) · cites this paper as [5]
The mutation to arginine in apoE ɛ3 and ɛ4 produces one or two additional positive charges relative to apoE ɛ2 at biological pH.
“The mutation to arginine produces one or two additional positive charges relative to apoE ɛ2, at biological pH.”
From Discovery of a Missense Mutation (Q222K) of the <i>APOE</i> Gene from the Australian Imaging, Biomarker and Lifestyle Study (2023) · cites this paper as [5]
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- Authors
- Zannis, V. I., & Breslow, J. L.
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 1981-02-17
- Volume
- 20
- Issue
- 4
- Pages
- 1033-1041
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W2029007538
- Cited by
- 563
- References
- 51
- Citations by year
- 2026: 1 · 2025: 6 · 2024: 2 · 2023: 10 · 2022: 2 · 2021: 6 · 2020: 2 · 2019: 4 · 2018: 7 · 2017: 3 · 2016: 7 · 2015: 4 · 2014: 8 · 2013: 4 · 2012: 3
- FWCI
- 59.48
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biochemistry (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Surgery › Lipoproteins and Cardiovascular Health
- Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Lipid metabolism and disorders
- Health Sciences › Medicine › Surgery › Cholesterol and Lipid Metabolism
- Keywords
- apolipoprotein E, VLDL, genetic variation, post-translational modification, protein isoforms
- MeSH terms
- Adult, Apolipoproteins, Apolipoproteins E, Child, Clostridium perfringens, Electrophoresis, Polyacrylamide Gel, Female, Humans, Hyperlipoproteinemias, Lipoproteins, VLDL, Male, Molecular Weight, Neuraminidase
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