Evidence map›Paper›PMID 33996741›Full record

ArticleFrontiers in chemistry2021

ApoE and ApoE Nascent-Like HDL Particles at Model Cellular Membranes: Effect of Protein Isoform and Membrane Composition.

Sarah Waldie, Federica Sebastiani, Martine Moulin, Rita Del Giudice, Nicolò Paracini, Felix Roosen-Runge, Yuri Gerelli, Sylvain Prevost, John C Voss, Tamim A Darwish and 6 more

Open access · goldAbstract read
In one paragraph

Article in Frontiers in chemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.6field-weighted citation impact, top 36% 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

4 citing papers in PubMed, 11 citations in OpenAlex.

  1. Article
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  4. Review
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

16 authors at 8 institutions in 7 countries.

Sarah WaldieDepartment of Biomedical Science and Biofilms-Research Center for Biointerfaces, Malmö University, Malmö, Sweden.
Federica SebastianiDepartment of Biomedical Science and Biofilms-Research Center for Biointerfaces, Malmö University, Malmö, Sweden.
Martine MoulinInstitut Laue-Langevin, Grenoble, France.
Rita Del GiudiceDepartment of Biomedical Science and Biofilms-Research Center for Biointerfaces, Malmö University, Malmö, Sweden.
Nicolò ParaciniDepartment of Biomedical Science and Biofilms-Research Center for Biointerfaces, Malmö University, Malmö, Sweden.
Felix Roosen-RungeDepartment of Biomedical Science and Biofilms-Research Center for Biointerfaces, Malmö University, Malmö, Sweden.
Yuri GerelliInstitut Laue-Langevin, Grenoble, France.
Sylvain PrevostInstitut Laue-Langevin, Grenoble, France.
John C VossDepartment of Biochemistry and Molecular Medicine, University of California, Davis, Davis, CA, United States.
Tamim A DarwishNational Deuteration Facility, Australian Nuclear Science and Technology Organisation, Lucas Heights, NSW, Australia.
Nageshwar YepuriNational Deuteration Facility, Australian Nuclear Science and Technology Organisation, Lucas Heights, NSW, Australia.
Harald PichlerAustrian Centre of Industrial Biotechnology, Graz, Austria.
Selma MaricMAX IV Laboratory, Lund, Sweden.
V Trevor ForsythInstitut Laue-Langevin, Grenoble, France.
Michael HaertleinInstitut Laue-Langevin, Grenoble, France.
Marité CárdenasDepartment of Biomedical Science and Biofilms-Research Center for Biointerfaces, Malmö University, Malmö, Sweden.
Malmö University · SEInstitut Laue-Langevin · FRAustralian Nuclear Science and Technology Organisation · AUInstitute of Molecular Biotechnology · ATKeele University · GBMarche Polytechnic University · ITMAX IV Laboratory · SEUniversity of California, Davis · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Apolipoprotein E (ApoE), an important mediator of lipid transportation in plasma and the nervous system, plays a large role in diseases such as atherosclerosis and Alzheimer's. The major allele variants ApoE3 and ApoE4 differ only by one amino acid. However, this difference has major consequences for the physiological behaviour of each variant. In this paper, we follow (i) the initial interaction of lipid-free ApoE variants with model membranes as a function of lipid saturation, (ii) the formation of reconstituted High-Density Lipoprotein-like particles (rHDL) and their structural characterisation, and (iii) the rHDL ability to exchange lipids with model membranes made of saturated lipids in the presence and absence of cholesterol [1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC) or 1-palmitoyl-2-oleoyl-glycero-3-phosphocholine (POPC) with and without 20 mol% cholesterol]. Our neutron reflection results demonstrate that the protein variants interact differently with the model membranes, adopting different protein conformations. Moreover, the ApoE3 structure at the model membrane is sensitive to the level of lipid unsaturation. Small-angle neutron scattering shows that the ApoE containing lipid particles form elliptical disc-like structures, similar in shape but larger than nascent or discoidal HDL based on Apolipoprotein A1 (ApoA1). Neutron reflection shows that ApoE-rHDL do not remove cholesterol but rather exchange saturated lipids, as occurs in the brain. In contrast, ApoA1-containing particles remove and exchange lipids to a greater extent as occurs elsewhere in the body.

Indexed as

ApoE isoformslipid exchangemodel membranesneutron reflectionreconstituted HDLsmall-angle neutron scattering

Identifiers

PMID33996741
PMCPMC8117676
OpenAlexW3157934002

What OpenQuestion holds

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Registered trials

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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.