The DOI matches its Crossref record; 29 of the 29 references it cites were found in a registry or an index.
Structural and metabolic heterogeneity of beta-very low density lipoproteins from cholesterol-fed dogs and from humans with type III hyperlipoproteinemia.
Open accessAbstract
Cholesteryl ester-rich beta-very low density lipoproteins (beta-VLDL) are beta-migrating lipoproteins that accumulate in the d < 1.006 g/ml fraction of plasma from cholesterol-fed animals and from patients with Type III hyperlipoproteinemia. They can be separated from pre-beta-migrating very low density lipoproteins in the d 1.006 g/ml fraction by Geon-Pevikon block electrophoresis. The beta-VLDL have a general property of stimulating cholesteryl ester synthesis and accumulation in macrophages. In the present study, we demonstrated that beta-VLDL obtained from cholesterol-fed dogs fasted for 16 hr were heterogeneous and that two subpopulations of particles, referred to as Fractions I and II, could be isolated from the whole beta-VLDL fraction using gel filtration chromatography. These fractions of beta-VLDL were similar in that both were cholesteryl ester rich, had beta-electrophoretic mobility on Geon-Pevikon electrophoresis, and possessed the B and E apoproteins as major constituents. However, Fractions I and II differed in size, shape, electrophoretic mobility, chemical composition, and apoprotein B type. (Fraction I vs. Fraction II: size: 90 to 300 nm vs. 20 to 70 nm; shape: irregular with redundant surface vs. spherical; electrophoretic mobility on paper: origin vs. beta; chemical composition: rich in phospholipid and poor in protein vs. rich in protein and poor in triglycerides; apoprotein B types: equal amounts of the high and low molecular weight forms vs. predominant…
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“This defective binding causes impaired clearance of chylomicron and very low density lipoprotein remnants (β-VLDL) (5, 6), which accumulate in the plasma and cause both hypercholesterolemia and hypertriglyceridemia.”
From Apolipoprotein E3-Leiden contains a seven-amino acid insertion that is a tandem repeat of residues 121–127 (1989) · cites this paper as [5]
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Plasma lipoproteins: apolipoprotein structure and function.
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Self-citationAstrocytes synthesize apolipoprotein E and metabolize apolipoprotein E-containing lipoproteins
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Metadata
- Authors
- Fainaru, M., Mahley, R. W., Hamilton, R. L., & Innerarity, T. L.
- Affiliations
- Gladstone Institutes (US)
- Venue
- Journal of Lipid Research
- Publisher
- Elsevier BV
- Published
- 1982-07
- Volume
- 23
- Issue
- 5
- Pages
- 702-714
- ISSN
- 0022-2275 (ISSN-L)
- OpenAlex
- W2336112818
- Cited by
- 156
- References
- 29
- Citations by year
- 2023: 1 · 2020: 1
- FWCI
- 34.22
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Lipid Research (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Cholesterol and Lipid Metabolism
- Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Lipoproteins and Cardiovascular Health
- Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Lipid metabolism and disorders
- Keywords
- beta-VLDL, chylomicron remnants, type III hyperlipoproteinemia, apolipoprotein B, lipoprotein heterogeneity, cholesteryl ester synthesis, macrophages, retinol transport, lipoprotein clearance, fasting, lipoprotein metabolism, size exclusion chromatography
- MeSH terms
- Animals, Cells, Cultured, Cholesterol, Dietary, Chromatography, Gel, Dogs, Electrophoresis, Polyacrylamide Gel, Fasting, Female, Humans, Hyperlipoproteinemia Type III, Lipoproteins, VLDL, Male, Microscopy, Electron, Vitamin A, Mice
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