Evidence map›Paper›PMID 9600998›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1998

Does the colonic H,K-ATPase also act as an Na,K-ATPase?

M Cougnon, P Bouyer, G Planelles, F Jaisser

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.9field-weighted citation impact, top 8% 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

20 citing papers in PubMed, 79 citations in OpenAlex.

  1. Review
  2. Increased colonic KScientific reports · 2021
    Article
  3. Article
  4. Iron is a substrate of theThe Journal of biological chemistry · 2017
    Article
  5. Article
  6. Article
  7. P2C-Type ATPases and Their Regulation.Molecular neurobiology · 2016
    Review
  8. Article
  9. Review
  10. A link between fertility and K+ homeostasis: role of the renal H,K-ATPase type 2.Pflugers Archiv : European journal of physiology · 2013
    Article
  11. Article
  12. Article
  13. Discovery and validation of colonic tumor-associated proteins via metabolic labeling and stable isotopic dilution.Proceedings of the National Academy of Sciences of the United States of America · 2009
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. The functional role of beta subunits in oligomeric P-type ATPases.Journal of bioenergetics and biomembranes · 2001
    Review
  20. 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

4 authors at 2 institutions in 1 country.

M CougnonInstitut National de la Santé et de la Recherche Médicale, U. 467, Faculté de Médecine Necker, Université Paris V, F-75015 Paris, France.
P Bouyer
G Planelles
F Jaisser
Inserm · FRUniversité Paris Cité · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We previously have demonstrated that the colonic P-ATPase alpha subunit cDNA encodes an H,K-ATPase when expressed in Xenopus laevis oocytes. Besides its high level of amino acid homology (75%) with the Na,K-ATPase, the colonic H,K-ATPase also shares a common pharmacological profile with Na,K-ATPase, because both are ouabain-sensitive and Sch 28080-insensitive. These features raise the possibility that an unrecognized property of the colonic H, K-ATPase would be Na+ translocation. To test this hypothesis, ion-selective microelectrodes were used to measure the intracellular Na+ activity of X. laevis oocytes expressing various combinations of P-ATPase subunits. The results show that expression in oocytes of the colonic H,K-ATPase affects intracellular Na+ homeostasis in a way similar to the expression of the Bufo marinus Na,K-ATPase; intracellular Na+ activity is lower in oocytes expressing the colonic H,K-ATPase or the B. marinus Na,K-ATPase than in oocytes expressing the gastric H,K-ATPase or a beta subunit alone. In oocytes expressing the colonic H,K-ATPase, the decrease in intracellular Na+ activity persists when diffusive Na+ influx is enhanced by functional expression of the amiloride-sensitive epithelial Na+ channel, suggesting that the decrease is related to increased active Na+ efflux. The Na+ decrease depends on the presence of K+ in the external medium and is inhibited by 2 mM ouabain, a concentration that inhibits the colonic H,K-ATPase. These data are consistent with the hypothesis that the colonic H,K-ATPase may transport Na+, acting as an (Na,H),K-ATPase. Despite its molecular and functional characterization, the physiological role of the colonic (Na,H),K-ATPase in colonic and renal ion homeostasis remains to be elucidated.

Indexed as

AnimalsBiological TransportColonDNA, ComplementaryH(+)-K(+)-Exchanging ATPaseRatsSodium-Potassium-Exchanging ATPaseXenopusDNA, ComplementaryH(+)-K(+)-Exchanging ATPaseSodium-Potassium-Exchanging ATPase

Identifiers

PMID9600998
PMCPMC27839
OpenAlexW2135950988

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.