Evidence map›Paper›PMID 33557294›Full record

ArticleInternational journal of molecular sciences2021

Multiple Na,K-ATPase Subunits Colocalize in the Brush Border of Mouse Choroid Plexus Epithelial Cells.

Inga Baasch Christensen, Lei Cheng, Jonathan R Brewer, Udo Bartsch, Robert A Fenton, Helle H Damkier, Jeppe Praetorius

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.5field-weighted citation impact, top 39% 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

3 citing papers in PubMed, 10 citations in OpenAlex.

  1. Aberrant adenosine ANature communications · 2025
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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 3 institutions in 2 countries.

Inga Baasch ChristensenDepartment of Biomedicine, Faculty of Health Science, Aarhus University, 8000 Aarhus, Denmark.
Lei ChengDepartment of Biomedicine, Faculty of Health Science, Aarhus University, 8000 Aarhus, Denmark.
Jonathan R BrewerDepartment of Biochemistry and Molecular Biology, Faculty of Science, University of Southern Denmark, 5230 Odense, Denmark.
Udo BartschDepartment of Ophthalmology, Experimental Ophthalmology, University Medical Center Hamburg-Eppendorf, 20246 Hamburg, Germany.
Robert A FentonDepartment of Biomedicine, Faculty of Health Science, Aarhus University, 8000 Aarhus, Denmark.ORCID 0000-0003-1623-199X
Helle H DamkierDepartment of Biomedicine, Faculty of Health Science, Aarhus University, 8000 Aarhus, Denmark.
Jeppe PraetoriusDepartment of Biomedicine, Faculty of Health Science, Aarhus University, 8000 Aarhus, Denmark.ORCID 0000-0001-6109-247X
Aarhus University · DKUniversität Hamburg · DEUniversity of Southern Denmark · DK

Funding

Lundbeckfonden R54-A5378Novo Nordisk Fonden NNF17OC0028584Sundhed og Sygdom, Det Frie Forskningsråd 0602-02404BUniversity Research Foundation N/A
6 · The paper itself

Abstract

(1) Background: The unusual accumulation of Na,K-ATPase complexes in the brush border membrane of choroid plexus epithelial cells have intrigued researchers for decades. However, the full range of the expressed Na,K-ATPase subunits and their relation to the microvillus cytoskeleton remains unknown. (2) Methods: RT-PCR analysis, co-immunoprecipitation, native PAGE, mass spectrometry, and differential centrifugation were combined with high-resolution immunofluorescence histochemistry, proximity ligase assays, and stimulated emission depletion (STED) microscopy on mouse choroid plexus cells or tissues in order to resolve these issues. (3) Results: The choroid plexus epithelium expresses Na,K-ATPase subunits α1, α2, β1, β2, β3, and phospholemman. The α1, α2, β1, and β2, subunits are all localized to the brush border membrane, where they appear to form a complex. The ATPase complexes may stabilize in the brush border membrane via anchoring to microvillar actin indirectly through ankyrin-3 or directly via other co-precipitated proteins. Aquaporin 1 (AQP1) may form part of the proposed multi-protein complexes in contrast to another membrane protein, the Na-K-2Cl cotransporter 1 (NKCC1). NKCC1 expression seems necessary for full brush border membrane accumulation of the Na,K-ATPase in the choroid plexus. (4) Conclusion: A multitude of Na,K-ATPase subunits form molecular complexes in the choroid plexus brush border, which may bind to the cytoskeleton by various alternative actin binding proteins.

Indexed as

ActinsAnimalsAquaporin 1Cell MembraneChoroid PlexusCytoskeletonEpithelial CellsMaleMiceMice, Inbred C57BLMice, KnockoutMicrovilliSolute Carrier Family 12, Member 2ActinsAqp1 protein, mouseAquaporin 1Slc12a2 protein, mouseSolute Carrier Family 12, Member 2actinankyrinchoroid plexuscytoskeletonmembrane stabilizationmembrane targetingNa,K-ATPasespectrin

Identifiers

PMID33557294
PMCPMC7915972
OpenAlexW3127894044

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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.