Evidence map›Paper›PMID 15216416›Full record

ArticleThe Journal of membrane biology2004

Ouabain binding to Na+,K+-ATPase relaxes cell attachment and sends a specific signal (NACos) to the nucleus.

R G Contreras, C Flores-Maldonado, A Lázaro, L Shoshani, D Flores-Benitez, I Larré, M Cereijido

Abstract readComparative Study
PubMed Publisher
In one paragraph

Article in The Journal of membrane biology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

29 citing papers in PubMed, 78 citations in OpenAlex.

  1. Review
  2. Biomolecules · 2024
    Article
  3. NaInternational journal of molecular sciences · 2024
    Review
  4. Article
  5. Article
  6. Toxins · 2019
    Article
  7. Review
  8. Review
  9. Na⁺Molecules (Basel, Switzerland) · 2017
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. The Na-K-ATPase α₁β₁ heterodimer as a cell adhesion molecule in epithelia.American journal of physiology. Cell physiology · 2012
    Review
  17. Digitoxin and its analogs as novel cancer therapeutics.Experimental hematology & oncology · 2012
    Article
  18. Article
  19. Ouabain modulates ciliogenesis in epithelial cells.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  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

7 authors at 1 institution in 1 country.

R G ContrerasDepartment of Physiology, Biophysics and Neurosciences, Av., Center for Research & Advanced Studies, Instituto Politécnico Nacional 2508, 07300, México, D.F., Mexico. rcontrer@fisio.cinvestav.mx
C Flores-Maldonado
A Lázaro
L Shoshani
D Flores-Benitez
I Larré
M Cereijido
Instituto Politécnico Nacional · MX

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Abstract. In previous work we described a "P-->A mechanism" that transduces occupancy of the pump ( P) by ouabain into changes in phosphorylation, stimulation of mitogen-activated protein kinase (MAPK), and endocytosis of cell-cell- and cell-substrate-attaching molecules ( A), thereby causing a release of the cell from the monolayer. In the present work we try to understand the mechanism of this effect; whether, in order to trigger the P-->A mechanism, ouabain should block the pumping activity of Na(+),K(+)-ATPase as pump, or whether it would suffice that the drug occupies this enzyme as a receptor. We assay a series of drugs known to act on the pump, such as ouabain, digoxin, digitoxin, palytoxin, oligomycin, strophanthidin, neothyoside-A, proscillaridin-A, etc. We gauge their ability to block the pump by measuring the K(+) content in the cells, and their ability to detach the cells from the monolayer by determining the amount of protein remaining in the culturing well. None of the drugs tested was able to cause detachment without stopping the pump. Ouabain also enhances phosphorylation, yet pump inhibition and signal transduction do not seem to be intimately associated in a causal chain, but to occur simultaneously. To investigate the response of the site of cell attachment, we analyze the position of beta-catenin by fluorescence confocal microscopy, and find that this adherent junction-associated molecule is sent to the nucleus, where it is known to act as a transcriptional cofactor.

Indexed as

Animalsbeta CateninCell AdhesionCell LineCell NucleusCytoskeletal ProteinsDogsEnzyme ActivationKidneyOuabainProtein BindingSignal TransductionSodium-Potassium-Exchanging ATPaseTrans-ActivatorsTranscription Factorsbeta CateninCytoskeletal ProteinsOuabainSodium-Potassium-Exchanging ATPaseTrans-ActivatorsTranscription Factors

Identifiers

PMID15216416
OpenAlexW2134189925

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.