Evidence map›Paper›PMID 24121499›Full record

ArticleThe Journal of biological chemistry2013

Apolipoproteins C-I and C-III inhibit lipoprotein lipase activity by displacement of the enzyme from lipid droplets.

Mikael Larsson, Evelina Vorrsjö, Philippa Talmud, Aivar Lookene, Gunilla Olivecrona

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in The Journal of biological chemistry, 2013. 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
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

87 citing papers in PubMed, 2 syntheses or guidelines pooled it, 163 citations in OpenAlex.

  1. Pooled it
  2. Pooled it
  3. Trial
  4. Article
  5. Atherogenic apolipoprotein C-III may not be as bad as we thought.Journal of thrombosis and haemostasis : JTH · 2026
    Article
  6. Article
  7. Review
  8. Article
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  14. Hypertriglyceridemia: Molecular and Genetic Landscapes.International journal of molecular sciences · 2024
    Review
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  20. The Impact of Acute Nutritional Interventions on the Plasma Proteome.The Journal of clinical endocrinology and metabolism · 2023
    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

5 authors at 3 institutions in 3 countries.

Mikael LarssonDepartment of Medical Biosciences/Physiological Chemistry, Umeå University, SE-901 87 Umeå, Sweden.
Evelina VorrsjöDepartment of Medical Biosciences/Physiological Chemistry, Umeå University, SE-901 87 Umeå, Sweden.
Philippa TalmudCentre for Cardiovascular Genetics, Institute of Cardiovascular Science, University College London, 5 University Street, London WC1E 6JF, United Kingdom.
Aivar LookeneDepartment of Chemistry, Tallinn University of Technology, Tallinn 12618, Estonia.
Gunilla OlivecronaDepartment of Medical Biosciences/Physiological Chemistry, Umeå University, SE-901 87 Umeå, Sweden. Electronic address: gunilla.olivecrona@medbio.umu.se.
Umeå University · SETallinn University of Technology · EEUniversity College London · GB

Funding

British Heart Foundation RG08/014
6 · The paper itself

Abstract

Apolipoproteins (apo) C-I and C-III are known to inhibit lipoprotein lipase (LPL) activity, but the molecular mechanisms for this remain obscure. We present evidence that either apoC-I or apoC-III, when bound to triglyceride-rich lipoproteins, prevent binding of LPL to the lipid/water interface. This results in decreased lipolytic activity of the enzyme. Site-directed mutagenesis revealed that hydrophobic amino acid residues centrally located in the apoC-III molecule are critical for attachment to lipid emulsion particles and consequently inhibition of LPL activity. Triglyceride-rich lipoproteins stabilize LPL and protect the enzyme from inactivating factors such as angiopoietin-like protein 4 (angptl4). The addition of either apoC-I or apoC-III to triglyceride-rich particles severely diminished their protective effect on LPL and rendered the enzyme more susceptible to inactivation by angptl4. These observations were seen using chylomicrons as well as the synthetic lipid emulsion Intralipid. In the presence of the LPL activator protein apoC-II, more of apoC-I or apoC-III was needed for displacement of LPL from the lipid/water interface. In conclusion, we show that apoC-I and apoC-III inhibit lipolysis by displacing LPL from lipid emulsion particles. We also propose a role for these apolipoproteins in the irreversible inactivation of LPL by factors such as angptl4.

Indexed as

Angiopoietin-Like Protein 4AngiopoietinsAnimalsApolipoprotein C-IApolipoprotein C-IIICattleEmulsionsHumansLipolysisLipoprotein LipaseMutagenesis, Site-DirectedTriglyceridesAngiopoietin-Like Protein 4AngiopoietinsANGPTL4 protein, humanAPOC1 protein, humanApolipoprotein C-IApolipoprotein C-IIIEmulsionsLipoprotein LipaseLPL protein, humanTriglyceridesApolipoprotein C-IApolipoprotein C-IIIApolipoproteinsDyslipidemiaLipolysisLipoproteinLipoprotein LipaseLipoprotein MetabolismTriglyceride

Identifiers

PMID24121499
PMCPMC3837139
OpenAlexW2037407219

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.