Evidence map›Paper›PMID 2153683›Full record

ArticleThe Journal of cell biology1990

Identification of a membrane-cytoskeletal complex containing the cell adhesion molecule uvomorulin (E-cadherin), ankyrin, and fodrin in Madin-Darby canine kidney epithelial cells.

W J Nelson, E M Shore, A Z Wang, R W Hammerton

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1990. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 84 papers.

0numbers the graph read from it
0cells of the map it votes in
84citing papers in PubMed
13.9field-weighted citation impact, top 1% 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

84 citing papers in PubMed, 289 citations in OpenAlex.

  1. Ameloblastin and its multifunctionality in amelogenesis: A review.Matrix biology : journal of the International Society for Matrix Biology · 2024
    Review
  2. Article
  3. IL-13 Impairs Tight Junctions in Airway Epithelia.International journal of molecular sciences · 2019
    Article
  4. The Role of Nonerythroid SpectrinJournal of oncology · 2019
    Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. The Na-K-ATPase α₁β₁ heterodimer as a cell adhesion molecule in epithelia.American journal of physiology. Cell physiology · 2012
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Shear stress-induced changes of membrane transporter localization and expression in mouse proximal tubule cells.Proceedings of the National Academy of Sciences of the United States of America · 2010
    Article
  19. Article
  20. Article

24 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 1 institution in 1 country.

W J NelsonInstitute for Cancer Research, Fox Chase Cancer Center, Philadelphia, Pennsylvania 19111.
E M Shore
A Z Wang
R W Hammerton
Fox Chase Cancer Center · US

Funding

WORD PROCESSING CENTER--COREP30CA006927 · NCI · RESEARCH INST OF FOX CHASE CAN CTR · PI Margaret von Mehren · 1985 to 2026
$138.8M
Topogenesis of NA/K-ATPASE in Polarized Epithelial CellsR37GM035527 · NIGMS · STANFORD UNIVERSITY · PI NELSON, W. JAMES · 2003 to 2012
$7.4M
Topogenesis of Na/K-ATPase in Polarized MDCK Epithelial CellsR01GM035527 · NIGMS · STANFORD UNIVERSITY · PI NELSON, W. JAMES · 1986 to 2015
$3.3M
NCI NIH HHS CA 06927NCRR NIH HHS RR 05539NIGMS NIH HHS GM 35527
6 · The paper itself

Abstract

Cell-cell contact is an important determinant in the formation of functionally distinct plasma membrane domains during the development of epithelial cell polarity. In cultures of Madin-Darby canine kidney (MDCK) epithelial cells, cell-cell contact induces the assembly and accumulation of the Na+,K+-ATPase and elements of the membrane-cytoskeleton (ankyrin and fodrin) at the regions of cell-cell contact. Epithelial cell-cell contact appears to be regulated by the cell adhesion molecule uvomorulin (E-cadherin) which also becomes localized at the lateral plasma membrane of polarized cells. We have sought to determine whether the colocalization of these proteins reflects direct molecular interactions which may play roles in coordinating cell-cell contact and the assembly of the basal-lateral domain of the plasma membrane. Recently, we identified a complex of proteins containing the Na+,K+-ATPase, ankyrin, and fodrin in extracts of whole MDCK cells (Nelson, W.J., and R. W. Hammerton. 1989. J. Cell Biol. 108:893-902). We have now examined cell extracts for protein complexes containing the cell adhesion molecule uvomorulin. Proteins were solubilized from whole MDCK cells and fractionated in sucrose gradients. The sedimentation profile of solubilized uvomorulin is well separated from the majority of cell surface proteins, suggesting that uvomorulin occurs in a protein complex. A distinct portion of uvomorulin (30%) cosediments with ankyrin and fodrin (approximately 10.5S). Further fractionation of cosedimenting proteins in nondenaturing polyacrylamide gels reveals a discrete band of proteins that binds antibodies specific for uvomorulin, Na+,K+-ATPase, ankyrin, and fodrin. Significantly, ankyrin and fodrin, but not Na+K+-ATPase, coimmunoprecipitate in a complex with uvomorulin using uvomorulin antibodies. This result indicates that separate complexes exist containing ankyrin and fodrin with either uvomorulin or Na+,K+-ATPase. These results are discussed in the context of the possible roles of uvomorulin-induced cell-cell contact in the assembly of the membrane-cytoskeleton and associated membrane proteins (e.g., Na+,K+-ATPase) at the contact zone and in the development of cell polarity.

Indexed as

AnimalsAnkyrinsBlood ProteinsCadherinsCarrier ProteinsCell Adhesion MoleculesCell CommunicationCell MembraneCells, CulturedCentrifugation, Density GradientCytoskeletonDogsElectrophoresis, Polyacrylamide GelEpithelial CellsEpitheliumKidneyAnkyrinsBlood ProteinsCadherinsCarrier ProteinsCell Adhesion MoleculesMembrane ProteinsMicrofilament ProteinsSodium-Potassium-Exchanging ATPaseSpectrin

Identifiers

PMID2153683
PMCPMC2116020
OpenAlexW2150814613

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.