Evidence map›Paper›PMID 1316269›Full record

ArticleThe EMBO journal1992

Mutation of a cysteine in the first transmembrane segment of Na,K-ATPase alpha subunit confers ouabain resistance.

C M Canessa, J D Horisberger, D Louvard, B C Rossier

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
5.9field-weighted citation impact, top 3% 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

31 citing papers in PubMed, 108 citations in OpenAlex.

  1. Sensational site: the sodium pump ouabain-binding site and its ligands.American journal of physiology. Cell physiology · 2024
    Review
  2. Displacement of the NaProceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Ouabain modulates ciliogenesis in epithelial cells.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  8. Ouabain binding site in a functioning Na+/K+ ATPase.The Journal of biological chemistry · 2011
    Article
  9. Article
  10. Article
  11. Review. Peering into an ATPase ion pump with single-channel recordings.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2009
    Review
  12. Article
  13. Review
  14. Ouabain affinity determining residues lie close to the Na/K pump ion pathway.Proceedings of the National Academy of Sciences of the United States of America · 2006
    Article
  15. A third Na+-binding site in the sodium pump.Proceedings of the National Academy of Sciences of the United States of America · 2005
    Article
  16. Article
  17. Article
  18. Review
  19. Structural insights into the binding of cardiac glycosides to the digitalis receptor revealed by solid-state NMR.Proceedings of the National Academy of Sciences of the United States of America · 2000
    Article
  20. Does the colonic H,K-ATPase also act as an Na,K-ATPase?Proceedings of the National Academy of Sciences of the United States of America · 1998
    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 1 institution in 1 country.

C M CanessaInstitut de Pharmacologie et de Toxicologie de l'Université, Lausanne, Switzerland.
J D Horisberger
D Louvard
B C Rossier
University of Lausanne · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The cardiac glycoside ouabain inhibits Na,K-ATPase by binding to the alpha subunit. In a highly ouabain resistant clone from the MDCK cell line, we have found two alleles of the alpha subunit in which the cysteine, present in the wild-type first transmembrane segment, is replaced by a tyrosine (Y) or a phenylalanine (F). We have studied the kinetics of ouabain inhibition by measuring the current generated by the Na,K-pump in Xenopus oocytes injected with wild-type and mutated alpha 1 and wild-type beta 1 subunit cRNAs. When these mutations, alpha 1C113Y and alpha 1C113F [according to the published sequence [Verrey et al. (1989) Am. J. Physiol., 256, F1034] were introduced in the alpha 1 subunit of the Na,K-ATPase from Xenopus laevis, the inhibition constant (Ki) of ouabain increased greater than 1000-fold compared with wild-type. A more conservative mutation, serine alpha 1C113S did not change the Ki. We observed that the decreased affinity for ouabain was mainly due to a faster dissociation, but probably also to a slower association. Thus we propose that an amino acid residue of the first transmembrane segment located deep in the plasma membrane participates in the structure and the function of the ouabain binding site.

Indexed as

MutationAmino Acid SequenceAnimalsBase SequenceCell LineCloning, MolecularCysteineDNADrug ResistanceKineticsMolecular Sequence DataOuabainPhenylalaninePolymerase Chain ReactionSequence AlignmentSodium-Potassium-Exchanging ATPaseCysteineDNAOuabainPhenylalanineSodium-Potassium-Exchanging ATPaseTyrosine

Identifiers

PMID1316269
PMCPMC556624
OpenAlexW2283470641

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.