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The crucial roles of apolipoproteins E and C-III in apoB lipoprotein metabolism in normolipidemia and hypertriglyceridemia.
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- Author(s): Sacks FM;Sacks FM
- Source:
Current opinion in lipidology [Curr Opin Lipidol] 2015 Feb; Vol. 26 (1), pp. 56-63.
- Publication Type:
Journal Article; Research Support, N.I.H., Extramural; Review
- Language:
English
- Additional Information
- Source:
Publisher: Lippincott Williams & Wilkins Country of Publication: England NLM ID: 9010000 Publication Model: Print Cited Medium: Internet ISSN: 1473-6535 (Electronic) Linking ISSN: 09579672 NLM ISO Abbreviation: Curr Opin Lipidol Subsets: MEDLINE
- Publication Information:
Publication: London : Lippincott Williams & Wilkins
Original Publication: London, UK : Current Science, c1990-
- Subject Terms:
- Abstract:
Purpose of Review: To describe the roles of apolipoprotein C-III (apoC-III) and apoE in VLDL and LDL metabolism
Recent Findings: ApoC-III can block clearance from the circulation of apolipoprotein B (apoB) lipoproteins, whereas apoE mediates their clearance. Normolipidemia is sustained by hepatic secretion of VLDL and IDL subspecies that contain both apoE and apoC-III (VLDL E+C-III+). Most of this VLDL E+C-III+ is speedily lipolyzed, reduced in apoC-III content, and cleared from the circulation as apoE containing dense VLDL, IDL, and light LDL. In contrast, in hypertriglyceridemia, most VLDL is secreted with apoC-III but without apoE, and so it is not cleared until it loses apoC-III during lipolysis to dense LDL. In normolipidemia, the liver also secretes IDL and large and medium-size LDL, whereas in hypertriglyceridemia, the liver secretes more dense LDL with and without apoC-III. These pathways establish the hypertriglyceridemic phenotype and link it metabolically to dense LDL. Dietary carbohydrate compared with unsaturated fat suppresses metabolic pathways mediated by apoE that are qualitatively similar to those suppressed in hypertriglyceridemia.
Summary: The opposing actions of apoC-III and apoE on subspecies of VLDL and LDL, and the direct secretion of LDL in several sizes, establish much of the basic structure of human apoB lipoprotein metabolism in normal and hypertriglyceridemic humans.
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- Grant Information:
R01 HL069376 United States HL NHLBI NIH HHS; R01 HL070159 United States HL NHLBI NIH HHS
- Accession Number:
0 (Apolipoprotein C-III)
0 (Apolipoproteins B)
0 (Apolipoproteins E)
EC 3.1.1.34 (Lipoprotein Lipase)
- Publication Date:
Date Created: 20150101 Date Completed: 20150831 Latest Revision: 20181113
- Publication Date:
20221213
- Accession Number:
PMC4371603
- Accession Number:
10.1097/MOL.0000000000000146
- Accession Number:
25551803
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