Evidence map›Paper›PMID 30333618›Full record

ArticleScientific reports2018

Identification and characterization of two zebrafish Twik related potassium channels, Kcnk2a and Kcnk2b.

Nathalie Nasr, Adèle Faucherre, Marc Borsotto, Catherine Heurteaux, Jean Mazella, Chris Jopling, Hamid Moha Ou Maati

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2018. 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
0.4field-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

4 citing papers in PubMed, 11 citations in OpenAlex.

  1. Article
  2. Article
  3. Evolution of two-pore domain potassium channels and their gene expression in zebrafish embryos.Developmental dynamics : an official publication of the American Association of Anatomists · 2024
    Article
  4. International journal of molecular sciences · 2019
    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

7 authors at 3 institutions in 1 country.

Nathalie NasrIGF, CNRS, INSERM, Université de Montpellier, Labex ICST, F-34094, Montpellier, France.
Adèle FaucherreIGF, CNRS, INSERM, Université de Montpellier, Labex ICST, F-34094, Montpellier, France.
Marc BorsottoIPMC, CNRS, INSERM, Université de Nice Sophia Antipolis, Labex ICST, F-06560, Valbonne, France.
Catherine HeurteauxIPMC, CNRS, INSERM, Université de Nice Sophia Antipolis, Labex ICST, F-06560, Valbonne, France.
Jean MazellaIPMC, CNRS, INSERM, Université de Nice Sophia Antipolis, Labex ICST, F-06560, Valbonne, France.
Chris JoplingIGF, CNRS, INSERM, Université de Montpellier, Labex ICST, F-34094, Montpellier, France. chris.jopling@igf.cnrs.fr.
Hamid Moha Ou MaatiIGF, CNRS, INSERM, Université de Montpellier, Labex ICST, F-34094, Montpellier, France. hamid.moha@igf.cnrs.fr.
Centre National de la Recherche Scientifique · FRInserm · FRInstitut de Génomique Fonctionnelle · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

KCNK2 is a 2 pore domain potassium channel involved in maintaining cellular membrane resting potentials. Although KCNK2 is regarded as a mechanosensitive ion channel, it can also be gated chemically. Previous research indicates that KCNK2 expression is particularly enriched in neuronal and cardiac tissues. In this respect, KCNK2 plays an important role in neuroprotection and has also been linked to cardiac arrhythmias. KCNK2 has subsequently become an attractive pharmacologic target for developing preventative/curative strategies for neuro/cardio pathophysiological conditions. Zebrafish represent an important in vivo model for rapidly analysing pharmacological compounds. We therefore sought to identify and characterise zebrafish kcnk2 to allow this model system to be incorporated into therapeutic research. Our data indicates that zebrafish possess two kcnk2 orthologs, kcnk2a and kcnk2b. Electrophysiological analysis of both zebrafish Kcnk2 orthologs shows that, like their human counterparts, they are activated by different physiological stimuli such as mechanical stretch, polyunsaturated fatty acids and intracellular acidification. Furthermore, both zebrafish Kcnk2 channels are inhibited by the human KCNK2 inhibitory peptide spadin. Taken together, our results demonstrate that both Kcnk2a and Kcnk2b share similar biophysiological and pharmacological properties to human KCNK2 and indicate that the zebrafish will be a useful model for developing KCNK2 targeting strategies.

Indexed as

AnimalsAntidepressive Agents, Second-GenerationCells, CulturedFluoxetineHEK293 CellsHumansIon Channel GatingMembrane PotentialsNeuroprotective AgentsPeptidesPotassium Channels, Tandem Pore DomainProtein IsoformsRiluzoleZebrafishZebrafish ProteinsAntidepressive Agents, Second-GenerationFluoxetineNeuroprotective AgentsPeptidespotassium channel protein TREK-1Potassium Channels, Tandem Pore DomainProtein IsoformsRiluzolespadin peptideZebrafish Proteins

Identifiers

PMID30333618
PMCPMC6192994
OpenAlexW2897040343

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.