Evidence map›Paper›PMID 15579540›Full record

ArticleThe Journal of physiology2004

Heteromeric KCNE2/KCNQ1 potassium channels in the luminal membrane of gastric parietal cells.

Dirk Heitzmann, Florian Grahammer, Thomas von Hahn, Annette Schmitt-Gräff, Elisa Romeo, Roland Nitschke, Uwe Gerlach, Hans Jochen Lang, François Verrey, Jacques Barhanin and 1 more

Open access · greenAbstract readComparative Study
In one paragraph

Article in The Journal of physiology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing papers in PubMed
4.2field-weighted citation impact, top 6% 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

59 citing papers in PubMed, 121 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Review
  6. Clinically RelevantInternational journal of molecular sciences · 2022
    Article
  7. Article
  8. Kv7 Channels and Excitability Disorders.Handbook of experimental pharmacology · 2021
    Article
  9. Review
  10. Review
  11. Review
  12. Analysis ofThe journal of histochemistry and cytochemistry : official journal of the Histochemistry Society · 2019
    Article
  13. The KCNE2 potassium channel β subunit is required for normal lung function and resilience to ischemia and reperfusion injury.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019
    Article
  14. Review
  15. Article
  16. A novel cancer syndrome caused byJournal of carcinogenesis · 2018
    Article
  17. Review
  18. Review
  19. Article
  20. Review
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

11 authors at 4 institutions in 3 countries.

Dirk HeitzmannInstitute of Physiology, Universitätsstrasse 31, 93053 Regensburg, Germany.
Florian Grahammer
Thomas von Hahn
Annette Schmitt-Gräff
Elisa Romeo
Roland Nitschke
Uwe Gerlach
Hans Jochen Lang
François Verrey
Jacques Barhanin
Richard Warth
Institut de Pharmacologie Moléculaire et Cellulaire · FRUniversity of Regensburg · DEUniversity of Zurich · CHUniversity of Tübingen · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Recently, we and others have shown that luminal K+ recycling via KCNQ1 K+ channels is required for gastric H+ secretion. Inhibition of KCNQ1 by the chromanol 293B strongly diminished H+ secretion. The present study aims at clarifying KCNQ1 subunit composition, subcellular localization, regulation and pharmacology in parietal cells. Using in situ hybridization and immunofluorescence techniques, we identified KCNE2 as the beta subunit of KCNQ1 in the luminal membrane compartment of parietal cells. Expressed in COS cells, hKCNE2/hKCNQ1 channels were activated by acidic pH, PIP2, cAMP and purinergic receptor stimulation. Qualitatively similar results were obtained in mouse parietal cells. Confocal microscopy revealed stimulation-induced translocation of H+,K+-ATPase from tubulovesicles towards the luminal pole of parietal cells, whereas distribution of KCNQ1 K+ channels did not change to the same extent. In COS cells the 293B-related substance IKs124 blocked hKCNE2/hKCNQ1 with an IC50 of 8 nM. Inhibition of hKCNE1- and hKCNE3-containing channels was weaker with IC50 values of 370 and 440 nM, respectively. In conclusion, KCNQ1 coassembles with KCNE2 to form acid-activated luminal K+ channels of parietal cells. KCNQ1/KCNE2 is activated during acid secretion via several pathways but probably not by targeting of the channel to the membrane. IKs124 could serve as a leading compound in the development of subunit-specific KCNE2/KCNQ1 blockers to treat peptic ulcers.

Indexed as

Adenosine TriphosphateAmino Acid SequenceAnimalsChlorocebus aethiopsCOS CellsGastric MucosaHumansKCNQ1 Potassium ChannelKCNQ Potassium ChannelsMiceMolecular Sequence DataParietal Cells, GastricPotassium Channels, Voltage-GatedRatsAdenosine TriphosphateKCNE2 protein, humanKcne2 protein, mouseKCNQ1 Potassium ChannelKCNQ1 protein, humanKcnq1 protein, mouseKcnq1 protein, ratKCNQ Potassium ChannelsPotassium Channels, Voltage-Gated

Identifiers

PMID15579540
PMCPMC1665368
OpenAlexW2158337460

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.