Evidence mapPaperPMID 28159869Full record

ArticleJournal of lipid research2017

Aromatic residues in the C terminus of apolipoprotein C-III mediate lipid binding and LPL inhibition.

Nathan L Meyers, Mikael Larsson, Evelina Vorrsjö, Gunilla Olivecrona, Donald M Small

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 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.8field-weighted citation impact, top 14% 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

12 citing papers in PubMed, 26 citations in OpenAlex.

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  6. The Effect of the Feeding System on Fat Deposition in Yak Subcutaneous Fat.International journal of molecular sciences · 2023
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  7. A Tale of Two New Targets for Hypertriglyceridaemia: Which Choice of Therapy?BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2022
    Review
  8. Review
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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

5 authors at 3 institutions in 2 countries.

Nathan L MeyersDepartment of Physiology and Biophysics, Boston University School of Medicine, Boston, MA.
Mikael LarssonDepartment of Medicine, University of California, Los Angeles, Los Angeles, CA.
Evelina VorrsjöDepartment of Medical Biosciences/Physiological Chemistry, Umeå University, Umeå, Sweden.
Gunilla OlivecronaDepartment of Medical Biosciences/Physiological Chemistry, Umeå University, Umeå, Sweden.
Donald M SmallDepartment of Physiology and Biophysics, Boston University School of Medicine, Boston, MA dmsmall@bu.edu.
Boston University · USUmeå University · SEUniversity of California, Los Angeles · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Plasma apoC-III levels correlate with triglyceride (TG) levels and are a strong predictor of CVD outcomes. ApoC-III elevates TG in part by inhibiting LPL. ApoC-III likely inhibits LPL by competing for lipid binding. To probe this, we used oil-drop tensiometry to characterize binding of six apoC-III variants to lipid/water interfaces. This technique monitors the dependence of lipid binding on surface pressure, which increases during TG hydrolysis by LPL. ApoC-III adsorption increased surface pressure by upward of 18 mN/m at phospholipid/TG/water interfaces. ApoC-III was retained to high pressures at these interfaces, desorbing at 21-25 mN/m. Point mutants, which substituted alanine for aromatic residues, impaired the lipid binding of apoC-III. Adsorption and retention pressures decreased by 1-6 mN/m in point mutants, with the magnitude determined by the location of alanine substitutions. Trp42 was most critical to mediating lipid binding. These results strongly correlate with our previous results, linking apoC-III point mutants to increased LPL binding and activity at lipid surfaces. We propose that aromatic residues in the C-terminal half of apoC-III mediate binding to TG-rich lipoproteins. Increased apoC-III expression in the hypertriglyceridemic state allows apoC-III to accumulate on lipoproteins and inhibit LPL by preventing binding and/or access to substrate.

Indexed as

Lipid MetabolismAdsorptionAmino Acid SequenceApolipoprotein C-IIHumansLipoprotein LipaseMutationStructure-Activity RelationshipTriglyceridesApolipoprotein C-IILipoprotein LipaseTriglyceridesdrop tensiometryLDL/metabolismlipid and lipoprotein metabolismlipid/emulsionslipoprotein lipaseprotein-lipid interactionsurface pressure

Identifiers

PMID28159869
PMCPMC5408602
OpenAlexW2583749096

What Socratic 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 Socratic graph.