Plasma lipoproteins: apolipoprotein structure and function.
Open accessAbstract
Plasma lipoprotein metabolism is regulated and controlled by the specific apolipoprotein (apo-) constituents of the various lipoprotein classes. The major apolipoproteins include apoE, apoB, apoA-I, apoA-II, apoA-IV, apoC-I, apoC-II, and apoC-III. Specific apolipoproteins function in the regulation of lipoprotein metabolism through their involvement in the transport and redistribution of lipids among various cells and tissues, through their role as cofactors for enzymes of lipid metabolism, or through their maintenance of the structure of the lipoprotein particles. The primary structures of most of the apolipoproteins are now known, and various functional domains of these proteins are being mapped using selective chemical modification, synthetic peptides, and monoclonal antibodies. Furthermore, the establishment of structure-function relationships has been greatly advanced by the identification of genetically determined variants of specific apolipoproteins that are associated with a disorder of lipoprotein metabolism. Future studies will rely heavily on the use of recombinant DNA technology and site-specific mutagenesis to elucidate further the correlations between structure and function and the role of specific apolipoproteins in lipoprotein metabolism.
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The substitution of cysteine for arginine at position 158 is a common apoE2 mutation causing familial type III hyperlipoproteinemia.
“the substitution of cysteine for arginine at position 158 is recognized as a common apoE2 mutation causing familial type Ⅲ hyperlipoproteinemia 7)”
From Significance of a Novel Apolipoprotein E Variant, ApoE Osaka/Kurashiki, in Lipoprotein Glomerulopathy (2011) · cites this paper as [7]
Apolipoprotein E is an arginine-rich protein.
“ApoE is an arginine-rich protein”
From Significance of a Novel Apolipoprotein E Variant, ApoE Osaka/Kurashiki, in Lipoprotein Glomerulopathy (2011) · cites this paper as [7]
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- Authors
- Mahley, R. W., Innerarity, T. L., Rall, S. C., & Weisgraber, K. H.
- Affiliations
- University of California, San Francisco (US)
- ORCID
- Mahley, R W
- Venue
- Journal of Lipid Research
- Publisher
- Elsevier BV
- Published
- 1984-12
- Volume
- 25
- Issue
- 12
- Pages
- 1277-1294
- ISSN
- 0022-2275 (ISSN-L)
- OpenAlex
- W1920171370
- Cited by
- 1,155
- References
- 7
- Citations by year
- 2026: 17 · 2025: 30 · 2024: 35 · 2023: 41 · 2022: 47 · 2021: 47 · 2020: 31 · 2019: 34 · 2018: 17 · 2017: 20 · 2016: 21 · 2015: 29 · 2014: 28 · 2013: 26 · 2012: 35
- FWCI
- 37.22
- 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
- Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Lipid metabolism and disorders
- Health Sciences › Medicine › Surgery › Cholesterol and Lipid Metabolism
- Health Sciences › Medicine › Surgery › Lipoproteins and Cardiovascular Health
- Keywords
- apolipoproteins, serum lipoproteins, lipoprotein metabolism, apolipoprotein E, apolipoprotein B, apolipoprotein A-I, apolipoprotein A-II, apolipoprotein A-IV, apolipoprotein C, lipid transport, enzyme cofactors, site-directed mutagenesis
- MeSH terms
- Apolipoproteins, Apolipoproteins A, Apolipoproteins B, Apolipoproteins C, Apolipoproteins E, Cholesterol, Heparin, Humans, Lipolysis, Lipoproteins, Molecular Conformation, Receptors, Cell Surface, Apolipoprotein A-I, Apolipoprotein A-II, Receptors, Lipoprotein, Apolipoprotein C-I, Apolipoprotein C-II, Apolipoprotein C-III
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