Evidence map›Paper›PMID 22277755›Full record

ReviewAmerican journal of physiology. Cell physiology2012

The Na-K-ATPase α₁β₁ heterodimer as a cell adhesion molecule in epithelia.

Olga Vagin, Laura A Dada, Elmira Tokhtaeva, George Sachs

Open access · greenAbstract readReview
In one paragraph

Review in American journal of physiology. Cell physiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.

0numbers the graph read from it
0cells of the map it votes in
67citing papers in PubMed
3.1field-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

67 citing papers in PubMed, 100 citations in OpenAlex.

  1. Article
  2. Hypercapnia Effects on Lung Function.Comprehensive Physiology · 2026
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  4. Pathogenicity ofWorld journal of clinical oncology · 2025
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  5. Connecting the Dots: AMOG/βInternational journal of molecular sciences · 2025
    Review
  6. Review
  7. Article
  8. Review
  9. Article
  10. Review
  11. Biomolecules · 2024
    Article
  12. Article
  13. NaInternational journal of molecular sciences · 2024
    Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article

7 more citing papers are in PubMed but not listed here.

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 3 institutions in 1 country.

Olga VaginDepartment of Physiology, School of Medicine, University of California Los Angeles and Veterans Administration Greater Los Angeles Health Care System, Los Angeles, California, USA. olgav@ucla.edu
Laura A Dada
Elmira Tokhtaeva
George Sachs
University of California, Los Angeles · USNorthwestern University · USVA Greater Los Angeles Healthcare System · US

Funding

Role and Regulation of Sodium, Potasium ATPase in LungR37HL048129 · NHLBI · NORTHWESTERN UNIVERSITY AT CHICAGO · PI SZNAJDER, JACOB I · 2008 to 2017
$4.0M
Role of Na, K-ATPase beta isoforms in pump sorting and epithelial integrityR01DK077149 · NIDDK · BRENTWOOD BIOMEDICAL RESEARCH INSTITUTE · PI VAGIN, OLGA · 2007 to 2010
$811k
NHLBI NIH HHS R37 HL048129NHLBI NIH HHS R37-HL-48129NIDDK NIH HHS DK-077149NIDDK NIH HHS R01 DK077149
6 · The paper itself

Abstract

The ion gradients generated by the Na-K-ATPase play a critical role in epithelia by driving transepithelial transport of various solutes. The efficiency of this Na-K-ATPase-driven vectorial transport depends on the integrity of epithelial junctions that maintain polar distribution of membrane transporters, including the basolateral sodium pump, and restrict paracellular diffusion of solutes. The review summarizes the data showing that, in addition to pumping ions, the Na-K-ATPase located at the sites of cell-cell junction acts as a cell adhesion molecule by interacting with the Na-K-ATPase of the adjacent cell in the intercellular space accompanied by anchoring to the cytoskeleton in the cytoplasm. The review also discusses the experimental evidence on the importance of a specific amino acid region in the extracellular domain of the Na-K-ATPase β(1) subunit for the Na-K-ATPase trans-dimerization and intercellular adhesion. Furthermore, a possible role of N-glycans linked to the Na-K-ATPase β(1) subunit in regulation of epithelial junctions by modulating β(1)-β(1) interactions is discussed.

Indexed as

Protein MultimerizationAnimalsCell Adhesion MoleculesEpithelial CellsHumansIntercellular JunctionsProtein Structure, QuaternarySodium-Potassium-Exchanging ATPaseCell Adhesion MoleculesSodium-Potassium-Exchanging ATPase

Identifiers

PMID22277755
PMCPMC3361946
OpenAlexW2090605131

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.