Evidence map›Paper›PMID 28701354›Full record

ArticleJournal of lipid research2017

Pleiotropic effects of apolipoprotein C3 on HDL functionality and adipose tissue metabolic activity.

Evangelia Zvintzou, Marie Lhomme, Stella Chasapi, Serafoula Filou, Vassilis Theodoropoulos, Eva Xapapadaki, Anatol Kontush, George Spyroulias, Constantinos C Tellis, Alexandros D Tselepis and 2 more

Open access · hybridAbstract read
In one paragraph

Article in Journal of lipid research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed, 1 pooled it
1.2field-weighted citation impact, top 23% 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

22 citing papers in PubMed, 1 synthesis or guideline pooled it, 45 citations in OpenAlex.

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  8. HDL, heart disease, and the lung.Journal of lipid research · 2022
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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

12 authors at 4 institutions in 2 countries.

Evangelia ZvintzouPharmacology Department, University of Patras Medical School, Rio Achaias TK 26500, Greece.
Marie LhommeICANalytics and INSERM UMR_S 1166, ICAN, 75013 Paris, France.
Stella ChasapiDepartment of Pharmacy, University of Patras, 26504 Patras, Greece.
Serafoula FilouPharmacology Department, University of Patras Medical School, Rio Achaias TK 26500, Greece.
Vassilis TheodoropoulosPharmacology Department, University of Patras Medical School, Rio Achaias TK 26500, Greece.
Eva XapapadakiPharmacology Department, University of Patras Medical School, Rio Achaias TK 26500, Greece.
Anatol KontushFaculté de Médecine Pitié-Salpêtrière, ICAN, 75013 Paris, France.
George SpyrouliasDepartment of Pharmacy, University of Patras, 26504 Patras, Greece.
Constantinos C TellisLaboratory of Biochemistry, Department of Chemistry, University of Ioannina, 45110 Ioannina, Greece.
Alexandros D TselepisLaboratory of Biochemistry, Department of Chemistry, University of Ioannina, 45110 Ioannina, Greece.
Caterina ConstantinouPharmacology Department, University of Patras Medical School, Rio Achaias TK 26500, Greece.
Kyriakos E KypreosPharmacology Department, University of Patras Medical School, Rio Achaias TK 26500, Greece. Electronic address: kkypreos@med.upatras.gr.
University of Patras · GRUniversity of Ioannina · GRFondation pour l’innovation en Cadiométabolisme et Nutrition · FRInserm · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

APOC3 is produced mainly by the liver and intestine and approximately half of plasma APOC3 associates with HDL. Though it was believed that APOC3 associates with HDL by simple binding to preexisting particles, recent data support that biogenesis of APOC3-containing HDL (APOC3-HDL) requires Abca1. Moreover, APOC3-HDL contributes to plasma triglyceride homeostasis by preventing APOC3 association with triglyceride-rich lipoproteins. Interestingly, APOC3-HDL also shows positive correlation with the morbidly obese phenotype. However, the roles of APOC3 in HDL functionality and adipose tissue metabolic activity remain unknown. Therefore, here we investigated the direct effects of APOC3 expression on HDL structure and function, as well as white adipose tissue (WAT) and brown adipose tissue (BAT) metabolic activity. C57BL/6 mice were infected with an adenovirus expressing human APOC3 or a recombinant attenuated control adenovirus expressing green fluorescent protein and blood and tissue samples were collected at 5 days postinfection. HDL was then analyzed for its apolipoprotein and lipid composition and particle functionality. Additionally, purified mitochondria from BAT and WAT were analyzed for uncoupling protein 1, cytochrome c (Cytc), and Cytc oxidase subunit 4 protein levels as an indirect measure of their metabolic activity. Serum metabolomic analysis was performed by NMR. Combined, our data show that APOC3 modulates HDL structure and function, while it selectively promotes BAT metabolic activation.

Indexed as

Genetic PleiotropyAdenosine TriphosphateAdenoviridaeAdipose Tissue, BrownAdipose Tissue, WhiteAnimalsAntioxidantsApolipoprotein C-IIIBiological TransportCholesterolEnergy MetabolismGene Transfer TechniquesHEK293 CellsHumansLipoproteins, HDLMiceAdenosine TriphosphateAntioxidantsApolipoprotein C-IIICholesterolLipoproteins, HDLTumor Necrosis Factor-alphabrown adipose tissuecholesterol effluxhigh density lipoproteinlipidomicsmetabolomicswhite adipose tissue

Identifiers

PMID28701354
PMCPMC5580900
OpenAlexW2736020675

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.