Evidence map›Paper›PMID 29100061›Full record

ReviewAtherosclerosis2017

Apolipoprotein C-II: New findings related to genetics, biochemistry, and role in triglyceride metabolism.

Anna Wolska, Richard L Dunbar, Lita A Freeman, Masako Ueda, Marcelo J Amar, Denis O Sviridov, Alan T Remaley

Abstract readReview
In one paragraph

Review in Atherosclerosis, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 123 papers.

0numbers the graph read from it
0cells of the map it votes in
123citing papers in PubMed
9.5field-weighted citation impact, top 1% 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

123 citing papers in PubMed, 218 citations in OpenAlex.

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  16. An overview of persistent chylomicronemia: much more than meets the eye.Current opinion in endocrinology, diabetes, and obesity · 2025
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63 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

7 authors at 3 institutions in 1 country.

Anna WolskaLipoprotein Metabolism Section, Cardio-Pulmonary Branch, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD, USA. Electronic address: anna.wolska@nih.gov.
Richard L DunbarDivision of Translational Medicine and Human Genetics, Department of Medicine, Perelman School of Medicine at the University of Pennsylvania, Philadelphia, PA, USA; ICON plc, North Wales, PA, USA; Cardiometabolic and Lipid Clinic, Corporal Michael J. Crescenz VA Medical Center, Philadelphia, PA, USA.
Lita A FreemanLipoprotein Metabolism Section, Cardio-Pulmonary Branch, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD, USA.
Masako UedaDivision of Translational Medicine and Human Genetics, Department of Medicine, Perelman School of Medicine at the University of Pennsylvania, Philadelphia, PA, USA.
Marcelo J AmarLipoprotein Metabolism Section, Cardio-Pulmonary Branch, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD, USA.
Denis O SviridovLipoprotein Metabolism Section, Cardio-Pulmonary Branch, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD, USA.
Alan T RemaleyLipoprotein Metabolism Section, Cardio-Pulmonary Branch, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD, USA.
National Institutes of Health · USPhiladelphia VA Medical Center · USUniversity of Pennsylvania · US

Funding

Development of Apo Mimetic Peptides for the Treatment Cardiovascular DiseaseZIAHL006095 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI REMALEY, ALAN THOMAS · 2010 to 2025
$20.3M
Intramural NIH HHS ZIA HL006095
6 · The paper itself

Abstract

Apolipoprotein C-II (apoC-II) is a small exchangeable apolipoprotein found on triglyceride-rich lipoproteins (TRL), such as chylomicrons (CM) and very low-density lipoproteins (VLDL), and on high-density lipoproteins (HDL), particularly during fasting. ApoC-II plays a critical role in TRL metabolism by acting as a cofactor of lipoprotein lipase (LPL), the main enzyme that hydrolyses plasma triglycerides (TG) on TRL. Here, we present an overview of the role of apoC-II in TG metabolism, emphasizing recent novel findings regarding its transcriptional regulation and biochemistry. We also review the 24 genetic mutations in the APOC2 gene reported to date that cause hypertriglyceridemia (HTG). Finally, we describe the clinical presentation of apoC-II deficiency and assess the current therapeutic approaches, as well as potential novel emerging therapies.

Indexed as

AnimalsApolipoprotein C-IIChylomicronsGene Expression RegulationHumansHydrolysisIntestinal MucosaLipolysisLipoprotein LipaseLipoproteinsLipoproteins, HDLLipoproteins, VLDLLiverMacrophagesMiceMultigene FamilyApolipoprotein C-IIChylomicronsLipoprotein LipaseLipoproteinsLipoproteins, HDLLipoproteins, VLDLTriglyceridesApoC-IIApoC-II deficiencyApoC-II mutationsHypertriglyceridemiaLipoprotein lipaseTriglyceride-rich lipoproteinsTriglycerides

Identifiers

PMID29100061
PMCPMC5705268
OpenAlexW2767128978

What OpenQuestion holds

Textmetadata
LicenceTDM
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.