Evidence map›Paper›PMID 32046769›Full record

ArticleFluids and barriers of the CNS2020

Choroid plexus LAT2 and SNAT3 as partners in CSF amino acid homeostasis maintenance.

Elena Dolgodilina, Simone M Camargo, Eva Roth, Brigitte Herzog, Virginia Nunes, Manuel Palacín, Francois Verrey

Open access · goldAbstract read
In one paragraph

Article in Fluids and barriers of the CNS, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.7field-weighted citation impact, top 19% 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

13 citing papers in PubMed, 20 citations in OpenAlex.

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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

7 authors at 4 institutions in 2 countries.

Elena DolgodilinaInstitute of Physiology, University of Zurich, Winterthurerstrasse 190, 8057, Zurich, Switzerland.
Simone M CamargoInstitute of Physiology, University of Zurich, Winterthurerstrasse 190, 8057, Zurich, Switzerland.
Eva RothInstitute of Physiology, University of Zurich, Winterthurerstrasse 190, 8057, Zurich, Switzerland.
Brigitte HerzogInstitute of Physiology, University of Zurich, Winterthurerstrasse 190, 8057, Zurich, Switzerland.
Virginia NunesGenes, Disease and Therapy Program, Molecular Genetics Laboratory-IDIBELL, Barcelona, Spain.
Manuel PalacínU730 and U731, Centro de investigacion Biomédica en Red de Enfermedades Raras, Barcelona, Spain.
Francois VerreyInstitute of Physiology, University of Zurich, Winterthurerstrasse 190, 8057, Zurich, Switzerland. francois.verrey@uzh.ch.ORCID http://orcid.org/0000-0003-3250-9824
University of Zurich · CHCentro de Investigación Biomédica en Red · ESInstitut d'Investigació Biomédica de Bellvitge · ESZHAW Zurich University of Applied Sciences · CH

Funding

Instituto de Salud Carlos III PI16/00217-R-FEDERInstituto de Salud Carlos III RTI2018-094211-B-100-FEDERSchweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung 31_166430/1
6 · The paper itself

Abstract

backgroundCerebrospinal fluid (CSF) is mainly produced by the choroid plexus (CP) located in brain ventricles. Although derived from blood plasma, it is nearly protein-free (~ 250-fold less) and contains about 2-20-fold less free amino acids, with the exception of glutamine (Gln) which is nearly equal. The aim of this study was to determine which amino acid transporters are expressed in mouse CP epithelium in order to gain understanding about how this barrier maintains the observed amino acid concentration gradient.

methodsExpression of amino acid transporters was assessed in isolated choroid plexuses (CPs) by qRT-PCR followed by localization studies using immunofluorescence with specific antibodies. The impact of LAT2 (Slc7a8) antiporter deletion on CSF amino acids was determined.

resultsThe purity of isolated choroid plexuses was tested on the mRNA level using specific markers, in particular transthyretin (Ttr) that was enriched 330-fold in CP compared to cerebral tissue. In a first experimental round, 14 out of 32 Slc amino acid transporters tested on the mRNA level by qPCR were selected for further investigation. Out of these, five were considered highly expressed, SNAT1 (Slc38a1), SNAT3 (Slc38a3), LAT2 (Slc7a8), ASC1 (Slc7a10) and SIT1 (Slc6a20b). Three of them were visualized by immunofluorescence: SNAT1 (Slc38a1), a neutral amino acid-Na

conclusionThese results suggest that Gln is actively transported by SNAT1 from the blood into CP epithelial cells and then released luminally into CSF via SNAT3 and LAT2. Its efflux via LAT2 may drive the reuptake from the CSF of essential amino acid substrates of this antiporter and thereby participates to maintaining the amino acid gradient between plasma and CSF.

Indexed as

HomeostasisAmino AcidsAmino Acid Transport Systems, NeutralAmino Acid Transport System y+AnimalsBiological TransportCells, CulturedChoroid PlexusEpithelial CellsFemaleFusion Regulatory Protein 1, Light ChainsGlutamic AcidMaleMice, KnockoutPrealbuminAmino AcidsAmino Acid Transport Systems, NeutralAmino Acid Transport System y+Fusion Regulatory Protein 1, Light ChainsGlutamic AcidPrealbuminSLC7A8 protein, mousesystem N protein 1Amino acid transportersBlood–cerebrospinal fluid barrierCSFHomeostasisLocalization

Identifiers

PMID32046769
PMCPMC7014681
OpenAlexW3005540314

What OpenQuestion holds

Textmetadata
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.