Evidence map›Paper›PMID 26658423›Full record

ArticleJournal of lipid research2016

Fatty acid binding proteins have the potential to channel dietary fatty acids into enterocyte nuclei.

Adriana Esteves, Anja Knoll-Gellida, Lucia Canclini, Maria Cecilia Silvarrey, Michèle André, Patrick J Babin

Open access · hybridAbstract read
In one paragraph

Article in Journal of lipid research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

16 citing papers in PubMed, 45 citations in OpenAlex.

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  8. The Many Faces of Lipids in Genome Stability (and How to Unmask Them).International journal of molecular sciences · 2021
    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

6 authors at 2 institutions in 2 countries.

Adriana EstevesFacultad de Ciencias, Universidad de la República, 11400 Montevideo, Uruguay.
Anja Knoll-GellidaUniversity Bordeaux, Maladies Rares: Génétique et Métabolisme (MRGM), F-33615 Pessac, France INSERM, U1211, F-33076, Bordeaux, France.
Lucia CancliniFacultad de Ciencias, Universidad de la República, 11400 Montevideo, Uruguay.
Maria Cecilia SilvarreyFacultad de Ciencias, Universidad de la República, 11400 Montevideo, Uruguay.
Michèle AndréUniversity Bordeaux, Maladies Rares: Génétique et Métabolisme (MRGM), F-33615 Pessac, France INSERM, U1211, F-33076, Bordeaux, France.
Patrick J BabinUniversity Bordeaux, Maladies Rares: Génétique et Métabolisme (MRGM), F-33615 Pessac, France INSERM, U1211, F-33076, Bordeaux, France p.babin@gpp.u-bordeaux1.fr.
Maladies Rares: Génétique et MétabolismeUniversidad de la República · UY

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Intracellular lipid binding proteins, including fatty acid binding proteins (FABPs) 1 and 2, are highly expressed in tissues involved in the active lipid metabolism. A zebrafish model was used to demonstrate differential expression levels of fabp1b.1, fabp1b.2, and fabp2 transcripts in liver, anterior intestine, and brain. Transcription levels of fabp1b.1 and fabp2 in the anterior intestine were upregulated after feeding and modulated according to diet formulation. Immunofluorescence and electron microscopy immunodetection with gold particles localized these FABPs in the microvilli, cytosol, and nuclei of most enterocytes in the anterior intestinal mucosa. Nuclear localization was mostly in the interchromatin space outside the condensed chromatin clusters. Native PAGE binding assay of BODIPY-FL-labeled FAs demonstrated binding of BODIPY-FLC(12) but not BODIPY-FLC(5) to recombinant Fabp1b.1 and Fabp2. The binding of BODIPY-FLC(12) to Fabp1b.1 was fully displaced by oleic acid. In vivo experiments demonstrated, for the first time, that intestinal absorption of dietary BODIPY-FLC(12) was followed by colocalization of the labeled FA with Fabp1b and Fabp2 in the nuclei. These data suggest that dietary FAs complexed with FABPs are able to reach the enterocyte nucleus with the potential to modulate nuclear activity.

Indexed as

AnimalsCell NucleusCytosolEnterocytesFatty Acid-Binding ProteinsFatty AcidsGene Expression RegulationHumansIntestinal MucosaLipid MetabolismZebrafishZebrafish ProteinsFABP2 protein, zebrafishfatty acid-binding protein 1b, zebrafishFatty Acid-Binding ProteinsFatty AcidsZebrafish ProteinsBODIPY-labeled fatty acidsDanio reriodiet and dietary lipidselectron microscopyfatty acid binding protein 1fatty acid binding protein 2fluorescence microscopygene expressionintestinenucleuszebrafish

Identifiers

PMID26658423
PMCPMC4727418
OpenAlexW2250890460

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.