Evidence map›Paper›PMID 19622837›Full record

ArticleJournal of lipid research2010

Expression of apolipoprotein C-III in McA-RH7777 cells enhances VLDL assembly and secretion under lipid-rich conditions.

Meenakshi Sundaram, Shumei Zhong, Maroun Bou Khalil, Philip H Links, Yang Zhao, Jahangir Iqbal, M Mahmood Hussain, Robin J Parks, Yuwei Wang, Zemin Yao

Open access · greenAbstract read
In one paragraph

Article in Journal of lipid research, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 87 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
87citing papers in PubMed, 2 pooled it
5.4field-weighted citation impact, top 4% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

87 citing papers in PubMed, 2 syntheses or guidelines pooled it, 150 citations in OpenAlex.

  1. Pooled it
  2. Pooled it
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  14. New approaches to triglyceride reduction: Is there any hope left?American journal of preventive cardiology · 2024
    Article
  15. Apolipoprotein C3: form begets function.Journal of lipid research · 2024
    Review
  16. Review
  17. Apo CIII Proteoforms, Plasma Lipids, and Cardiovascular Risk in MESA.Arteriosclerosis, thrombosis, and vascular biology · 2023
    Observational
  18. Review
  19. Article
  20. Article

27 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

10 authors at 4 institutions in 2 countries.

Meenakshi SundaramDepartment of Biochemistry, Microbiology and Immunology, Department of Pathology and Laboratory Medicine, Ottawa Institute of Systems Biology, University of Ottawa Canada K1H 8M5.
Shumei Zhong
Maroun Bou Khalil
Philip H Links
Yang Zhao
Jahangir Iqbal
M Mahmood Hussain
Robin J Parks
Yuwei Wang
Zemin Yao
University of Ottawa · CASUNY Downstate Health Sciences University · USCanadian VIGOUR Centre · CAHealth Canada · CA

Funding

Canadian Institutes of Health Research MT-15486
6 · The paper itself

Abstract

Apolipoprotein (apo) C-III plays a regulatory role in VLDL lipolysis and clearance. In this study, we determined a potential intracellular role of apoC-III in hepatic VLDL assembly and secretion. Stable expression of recombinant apoC-III in McA-RH7777 cells resulted in increased secretion efficiency of VLDL-associated triacylglycerol (TAG) and apoB-100 in a gene-dosage-dependent manner. The stimulatory effect of apoC-III on TAG secretion was manifested only when cells were cultured under lipid-rich (i.e., media supplemented with exogenous oleate) but not lipid-poor conditions. The stimulated TAG secretion was accompanied by increased secretion of apoB-100 and apoB-48 as VLDL(1). Expression of apoC-III also increased mRNA and activity of microsomal triglyceride transfer protein (MTP). Pulse-chase experiments showed that apoC-III expression promoted VLDL(1) secretion even under conditions where the MTP activity was inhibited immediately after the formation of lipid-poor apoB-100 particles, suggesting an involvement of apoC-III in the second-step VLDL assembly process. Consistent with this notion, the newly synthesized apoC-III was predominantly associated with TAG within the microsomal lumen that resembled lipid precursors of VLDL. Introducing an Ala23-to-Thr mutation into apoC-III, a naturally occurring mutation originally identified in two Mayan Indian subjects with hypotriglyceridemia, abolished the ability of apoC-III to stimulate VLDL secretion from transfected cells. Thus, expression of apoC-III in McA-RH7777 cells enhances hepatic TAG-rich VLDL assembly and secretion under lipid-rich conditions.

Indexed as

AnimalsApolipoprotein B-100Apolipoprotein B-48Apolipoprotein C-IIICarrier ProteinsCell Line, TumorCholesterol, VLDLGene DosageGene Knockdown TechniquesHumansRatsRNA, Small InterferingTransfectionTriglyceridesApolipoprotein B-100Apolipoprotein B-48Apolipoprotein C-IIICarrier ProteinsCholesterol, VLDLmicrosomal triglyceride transfer proteinRNA, Small InterferingTriglycerides

Identifiers

PMID19622837
PMCPMC2789775
OpenAlexW2128293328

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.