NDLI: Functional analysis of the missense APOC3 mutation Ala23Thr associated with human hypotriglyceridemia.

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Functional analysis of the missense APOC3 mutation Ala23Thr associated with human hypotriglyceridemia.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Sundaram, Meenakshi Zhong, Shumei Bou Khalil, Maroun Zhou, Hu Jiang, Zhenghui G. Zhao, Yang Iqbal, Jahangir Hussain, M. Mahmood Figeys, Daniel Wang, Yuwei Yao, Zemin
Description	Country affiliation: Canada Author Affiliation: Sundaram M ( Department of Biochemistry, Ottawa Institute of Systems Biology, University of Ottawa, Canada.)
Abstract	We have shown that expression of apolipoprotein (apo) C-III promotes VLDL secretion from transfected McA-RH7777 cells under lipid-rich conditions. To determine structural elements within apoC-III that confer to this function, we contrasted wild-type apoC-III with a mutant Ala23Thr originally identified in hypotriglyceridemia subjects. Although synthesis of [(3)H]glycerol-labeled TAG was comparable between cells expressing wild-type apoC-III (C3wt cells) or Ala23Thr mutant (C3AT cells), secretion of [(3)H]TAG from C3AT cells was markedly decreased. The lowered [(3)H]TAG secretion was associated with an inability of C3AT cells to assemble VLDL(1). Moreover, [(3)H]TAG within the microsomal lumen in C3AT cells was 60% higher than that in C3wt cells, yet the activity of microsomal triglyceride-transfer protein in C3AT cells was not elevated. The accumulated [(3)H]TAG in C3AT microsomal lumen was mainly associated with lumenal IDL/LDL-like lipoproteins. Phenotypically, this [(3)H]TAG fractionation profiling resembled what was observed in cells treated with brefeldin A, which at low dose specifically blocked the second-step VLDL(1) maturation. Furthermore, lumenal [(35)S]Ala23Thr protein accumulated in IDL/LDL fractions and was absent in VLDL fractions in C3AT cells. These results suggest that the presence of Ala23Thr protein in lumenal IDL/LDL particles might prevent effective fusion between lipid droplets and VLDL precursors. Thus, the current study reveals an important structural element residing within the N-terminal region of apoC-III that governs the second step VLDL(1) maturation.
File Format	HTM / HTML
ISSN	00222275
e-ISSN	15397262
DOI	10.1194/jlr.M005108
Journal	The Journal of Lipid Research
Issue Number	6
Volume Number	51
Language	English
Publisher	American Society for Biochemistry and Molecular Biology
Publisher Date	2010-06-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Discipline Biochemistry Apolipoproteins C Genetics Metabolism Lipid Metabolism Disorders Mutation, Missense Triglycerides Alanine Chemistry Brefeldin A Pharmacology Carrier Proteins Cell Line Gene Expression Regulation Lipoproteins, Idl Lipoproteins, Ldl Lipoproteins, Vldl Microsomes Models, Molecular Protein Binding Drug Effects Protein Structure, Secondary Threonine Research Support, Non-u.s. Gov't
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Endocrinology

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Functional analysis of the missense APOC3 mutation Ala23Thr associated with human hypotriglyceridemia

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Functional analysis of the missense APOC3 mutation Ala23Thr associated with human hypotriglyceridemia.

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Functional analysis of the missense APOC3 mutation Ala23Thr associated with human hypotriglyceridemia.