Evidence map›Paper›PMID 22361748›Full record

ArticleCell death & disease2012

Occludin is required for apoptosis when claudin-claudin interactions are disrupted.

N Beeman, P G Webb, H K Baumgartner

Open access · goldAbstract read
In one paragraph

Article in Cell death & disease, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
3.4field-weighted citation impact, top 9% 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

50 citing papers in PubMed, 80 citations in OpenAlex.

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  10. Protective role of cGAS in NASH is related to the maintenance of intestinal homeostasis.Liver international : official journal of the International Association for the Study of the Liver · 2023
    Article
  11. Effects ofFood and waterborne parasitology · 2023
    Article
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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.

N BeemanDepartment of Physiology and Biophysics, University of Colorado Denver, School of Medicine, Aurora, CO 80045, USA.
P G Webb
H K Baumgartner
University of Colorado Denver · US

Funding

CTSA INFRASTRUCTURE FOR PEDIATRIC RESEARCHUL1RR025780 · NCRR · UNIVERSITY OF COLORADO DENVER · PI SOKOL, RONALD J. · 2008 to 2011
$61.3M
NCRR NIH HHS UL1 RR025780
6 · The paper itself

Abstract

Disruption of tight junctions is often seen during pathogen infection, inflammation, and tumor progression. Mislocalization of the tight junction proteins occludin and claudin in mammary epithelial monolayers leads to apoptosis through the extrinsic pathway. To further investigate the mechanism of this response, a normal mammary epithelial cell line (EpH4) as well as primary mammary epithelial cells were treated with a claudin-disrupting mimic peptide, DFYNP (aspartic acid-phenylalanine-tyrosine-asparagine-proline). Using fluorescent indicators, we found that caspase-3 activation, resulting from treatment with DFYNP, was restricted to EpH4 and primary mammary epithelial cells with mislocalized claudin-4. Mislocalized claudin-4 and occludin were colocalized in non-junctional puncta, and both molecules were found in the death-inducing signaling complex (DISC) where they colocalized with Fas, fas-associated protein with death domain (FADD), active caspase-8 and caspase-3 at distinct apical domains. Importantly, caspase-3 activation was totally repressed in primary mammary epithelial cells from occludin null mice. Thus, the apoptotic response appears to be initiated by the movement of occludin to the DISC suggesting that this molecule has signaling properties that initiate cell death when its tight junction location is disrupted.

Indexed as

AnimalsApoptosisCaspase 3Caspase 8Claudin-4ClaudinsDeath Domain Receptor Signaling Adaptor ProteinsEpithelial CellsFas-Associated Death Domain Proteinfas ReceptorFemaleGene ExpressionHumansMammary Glands, AnimalMembrane ProteinsMiceCaspase 3Caspase 8Claudin-4ClaudinsCLDN4 protein, humanCldn4 protein, mouseDeath Domain Receptor Signaling Adaptor ProteinsFadd protein, mouseFas-Associated Death Domain ProteinFas protein, mousefas ReceptorMembrane ProteinsOccludinOCLN protein, humanOcln protein, mouseOligopeptides

Identifiers

PMID22361748
PMCPMC3288343
OpenAlexW2054394416

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.