Evidence map›Paper›PMID 20697888›Full record

ArticleThe Journal of membrane biology2010

Protein kinase C activation has distinct effects on the localization, phosphorylation and detergent solubility of the claudin protein family in tight and leaky epithelial cells.

Anita Sjö, Karl-Eric Magnusson, Kajsa Holmgren Peterson

Open access · hybridAbstract read
In one paragraph

Article in The Journal of membrane biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

23 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
  2. Article
  3. Distinct Origin of Claudin7 in Early Tumor Endosomes Affects Exosome Assembly.International journal of biological sciences · 2019
    Article
  4. Review
  5. Review
  6. Bicellular Tight Junctions and Wound Healing.International journal of molecular sciences · 2018
    Review
  7. Article
  8. Article
  9. Review
  10. Non-invasive saliva human biomonitoring: development of an in vitro platform.Journal of exposure science & environmental epidemiology · 2017
    Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Changes in the phosphorylation of claudins during the course of experimental colitis.International journal of clinical and experimental pathology · 2015
    Article
  17. Article
  18. Article
  19. 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

3 authors at 1 institution in 1 country.

Anita SjöDivision of Medical Microbiology, Department of Clinical and Experimental Medicine, Linköping University, Linköping, Sweden. anita.sjo@liu.se.
Karl-Eric Magnusson
Kajsa Holmgren Peterson
Linköping University · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We have previously shown that protein kinase C (PKC) activation has distinct effects on the structure and barrier properties of cultured epithelial cells (HT29 and MDCK I). Since the claudin family of tight junction (TJ)-associated proteins is considered to be crucial for the function of mature TJ, we assessed their expression patterns and cellular destination, detergent solubility and phosphorylation upon PKC stimulation for 2 or 18 h with phorbol myristate acetate (PMA). In HT29 cells, claudins 1, 3, 4 and 5 and possibly claudin 2 were redistributed to apical cell-cell contacts after PKC activation and the amounts of claudins 1, 3 and 5, but not of claudin 2, were increased in cell lysates. By contrast, in MDCK I cells, PMA treatment resulted in redistribution of claudins 1, 3, 4 and 5 from the TJ and in reorganization of the proteins into more insoluble complexes. Claudins 1 and 4 were phosphorylated in both MDCK I and HT29 cells, but PKC-induced changes in claudin phosphorylation state were detected only in MDCK I cells. A major difference between HT29 and MDCK I cells, which have low and high basal transepithelial electrical resistance, respectively, was the absence of claudin 2 in the latter. Our findings show that PKC activation targets in characteristic ways the expression patterns, destination, detergent solubility and phosphorylation state of claudins in epithelial cells with different capacities to form an epithelial barrier.

Indexed as

AnimalsCell LineClaudin-1ClaudinsDogsEpithelial CellsFluorescent Antibody TechniqueHT29 CellsHumansImmunoblottingImmunoprecipitationMembrane ProteinsPhosphorylationProtein Kinase CTetradecanoylphorbol AcetateClaudin-1ClaudinsCLDN1 protein, humanMembrane ProteinsProtein Kinase CTetradecanoylphorbol Acetate

Identifiers

PMID20697888
PMCPMC2927686
OpenAlexW2015696617

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.