Evidence map›Paper›PMID 28694484›Full record

ArticleScientific reports2017

Self-assembled α-Tocopherol Transfer Protein Nanoparticles Promote Vitamin E Delivery Across an Endothelial Barrier.

Walter Aeschimann, Stefanie Staats, Stephan Kammer, Natacha Olieric, Jean-Marc Jeckelmann, Dimitrios Fotiadis, Thomas Netscher, Gerald Rimbach, Michele Cascella, Achim Stocker

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. 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
1.5field-weighted citation impact, top 20% 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, 27 citations in OpenAlex.

  1. The neuropathobiology of multiple sclerosis.Nature reviews. Neuroscience · 2024
    Review
  2. Review
  3. Article
  4. Vitamin E Biosynthesis and Its Regulation in Plants.Antioxidants (Basel, Switzerland) · 2017
    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

10 authors at 3 institutions in 3 countries.

Walter AeschimannUniversity of Bern, Department of Chemistry and Biochemistry, Bern, Switzerland.
Stefanie StaatsUniversity of Kiel, Institute of Human Nutrition and Food Science, Kiel, Germany.
Stephan KammerUniversity of Bern, Department of Chemistry and Biochemistry, Bern, Switzerland.
Natacha OliericPaul Scherrer Institut, Villigen, Switzerland.
Jean-Marc JeckelmannUniversity of Bern, Institute of Biochemistry and Molecular Medicine, Bern, Switzerland.
Dimitrios FotiadisUniversity of Bern, Institute of Biochemistry and Molecular Medicine, Bern, Switzerland.
Thomas NetscherDSM Nutritional Products Ltd., Basel, Switzerland.ORCID 0000-0002-9362-3244
Gerald RimbachUniversity of Kiel, Institute of Human Nutrition and Food Science, Kiel, Germany.
Michele CascellaUniversity of Oslo, Department of Chemistry and Centre for Theoretical and Computational Chemistry (CTCC), Oslo, Norway. michele.cascella@kjemi.uio.no.
Achim StockerUniversity of Bern, Department of Chemistry and Biochemistry, Bern, Switzerland. achim.stocker@dcb.unibe.ch.ORCID 0000-0001-6862-7887
University of Bern · CHPaul Scherrer Institute · CHUniversity of Oslo · NO

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Vitamin E is one of the most important natural antioxidants, protecting polyunsaturated fatty acids in the membranes of cells. Among different chemical isoforms assimilated from dietary regimes, RRR-α-tocopherol is the only one retained in higher animals. This is possible thanks to α-Tocopherol Transfer Protein (α-TTP), which extracts α-tocopherol from endosomal compartments in liver cells, facilitating its distribution into the body. Here we show that, upon binding to its substrate, α-TTP acquires tendency to aggregation into thermodynamically stable high molecular weight oligomers. Determination of the structure of such aggregates by X-ray crystallography revealed a spheroidal particle formed by 24 protein monomers. Oligomerization is triggered by refolding of the N-terminus. Experiments with cultured cell monolayers demonstrate that the same oligomers are efficiently transported through an endothelial barrier (HUVEC) and not through an epithelial one (Caco-2). Discovery of a human endogenous transport protein with intrinsic capability of crossing endothelial tissues opens to new ways of drug delivery into the brain or other tissues protected by endothelial barriers.

Indexed as

alpha-TocopherolCaco-2 CellsCarrier ProteinsCrystallography, X-RayEndosomesEndothelial CellsEpithelial CellsHumansHuman Umbilical Vein Endothelial CellsModels, MolecularNanoparticlesProtein AggregatesProtein ConformationProtein FoldingProtein MultimerizationProtein Stabilityalpha-Tocopherolalpha-tocopherol transfer proteinCarrier ProteinsProtein Aggregates

Identifiers

PMID28694484
PMCPMC5504013
OpenAlexW2728853753

What OpenQuestion holds

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LicenceCC BY
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.