Evidence map›Paper›PMID 23255610›Full record

ArticleThe Journal of biological chemistry2013

Impaired monoamine and organic cation uptake in choroid plexus in mice with targeted disruption of the plasma membrane monoamine transporter (Slc29a4) gene.

Haichuan Duan, Joanne Wang

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

45 citing papers in PubMed, 63 citations in OpenAlex.

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  3. Metabolite transport across central nervous system barriers.Journal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism · 2024
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  15. Science advances · 2022
    Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Drug metabolism and disposition: the biological fate of chemicals · 2022
    Article
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

2 authors at 1 institution in 1 country.

Haichuan DuanDepartment of Pharmaceutics, University of Washington, Seattle, Washington 98195, USA.
Joanne Wang
University of Washington · US

Funding

TISSUE DISTRIBUTION FOR RARE DISEASE RESEARCHU42RR006042 · NCRR · NATIONAL DISEASE RESEARCH INTERCHANGE · PI LONSDALE, JOHN T · 1991 to 2011
$16.5M
The plasma membrane monoamine transporter (PMAT): expression and role in mIBG disposition in neuroblastomaR01GM066233 · NIGMS · UNIVERSITY OF WASHINGTON · PI WANG, JOANNE · 2002 to 2020
$5.1M
NCRR NIH HHS 5 U42 RR006042NCRR NIH HHS U42 RR006042NIGMS NIH HHS GM066233NIGMS NIH HHS GM066233-07S1NIGMS NIH HHS R01 GM066233
6 · The paper itself

Abstract

The choroid plexus (CP) forms the blood-cerebrospinal fluid (CSF) barrier and protects the brain from circulating metabolites, drugs, and toxins. The plasma membrane monoamine transporter (PMAT, SLC29A4) is a new polyspecific organic cation transporter that transports a wide variety of organic cations including biogenic amines, cationic drugs, and neurotoxins. PMAT is known to be expressed in the CP, but its specific role in CP transport of organic cations has not been clearly defined. Here we showed that PMAT transcript is highly expressed in human and mouse CPs, whereas transcripts of other functionally related transporters are minimally expressed in the CPs. Immunofluorescence staining further revealed that PMAT protein is localized to the apical (CSF-facing) membrane of the CP epithelium, consistent with a role of transporting organic cations from the CSF into CP epithelial cells. To further evaluate the role of PMAT in the CP, mice with targeted deletion of the Slc29a4 gene were generated and validated. Although Pmat(-/-) mice showed no overt abnormalities, the uptake of monoamines and the neurotoxin 1-methyl-4-phenylpyridinium was significantly reduced in CP tissues isolated from the knock-out mice. Together, our data demonstrated that PMAT is a major transporter for CP uptake of bioactive amines and xenobiotic cations. By removing its substrates from the CSF, PMAT may play an important role in protecting the brain from cationic neurotoxins and other potentially toxic organic cations.

Indexed as

Gene TargetingAnimalsBiogenic MonoaminesCationsCell MembraneCell PolarityChoroid PlexusEpithelial CellsEquilibrative Nucleoside Transport ProteinsGene DeletionGene Expression RegulationHEK293 CellsHumansInhibitory Concentration 50MiceMice, Inbred C57BLBiogenic MonoaminesCationsEquilibrative Nucleoside Transport ProteinsOrganic Cation Transport ProteinsRNA, MessengerSLC29A4 protein, humanVesicular Monoamine Transport Proteins

Identifiers

PMID23255610
PMCPMC3561572
OpenAlexW1992940294

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.