Evidence map›Paper›PMID 8500907›Full record

ArticleInfection and immunity1993

A bacterial protease perturbs the paracellular barrier function of transporting epithelial monolayers in culture.

A O Azghani, L D Gray, A R Johnson

Open access · bronzeAbstract read
In one paragraph

Article in Infection and immunity, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.4field-weighted citation impact, top 10% 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

27 citing papers in PubMed, 71 citations in OpenAlex.

  1. Review
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  10. Frontiers in cellular and infection microbiology · 2017
    Review
  11. Review
  12. Iron and zinc exploitation during bacterial pathogenesis.Metallomics : integrated biometal science · 2015
    Review
  13. 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.

A O AzghaniDepartment of Biochemistry, University of Texas Health Center, Tyler 75710.
L D Gray
A R Johnson
The University of Texas Health Science Center at Tyler · US

Funding

PSEUDOMONAS ELASTASE AND LUNG INJURYR01HL044473 · NHLBI · UNIVERSITY OF TEXAS HLTH CTR AT TYLER · PI AZGHANI, ALI O · 1992 to 1994
–
NHLBI NIH HHS HL44473
6 · The paper itself

Abstract

Tight junctions between cells and adhesion to the substratum maintain the barrier function of epithelia throughout the body. Damage to the epithelial barrier by microbial products allows penetration of bacteria and promotion of infection. We studied the effects of Pseudomonas elastase (PE) on the barrier function of epithelia by using Madin-Darby canine kidney (MDCK) epithelial cells; these cells form tight junctions (zonula occludens [ZO]) in vitro. PE decreased electrical resistance across the monolayers in a concentration- and time-dependent manner. Immunostaining of selected proteins of the ZO and zonula adherens was used to explore the effects of PE on junctional proteins. PE-treated monolayers of MDCK cells had markedly decreased immunostaining of ZO-1, a protein of the ZO, but light microscopy of PE-treated cells revealed no obvious morphologic changes. A chromium release assay indicated that, even with marked changes in transmonolayer electrical resistance, the permeability defect was not due to membrane disruption. Fluorescence staining of F-actin indicated diminution of cellular microfilaments in PE-treated cells, but E cadherin (uvomorulin), a protein of the zonula adherens, was unaffected by the enzyme. Elastases from porcine pancreas and human leukocytes with similar enzymatic activity (6 U/ml) did not decrease transmonolayer electrical resistance or degrade ZO-1. These results suggest that PE disturbs the barrier function of epithelial monolayers, in part, by changing the cell architecture and altering at least one protein of the ZO.

Indexed as

Bacterial ProteinsAnimalsBiological TransportCadherinsCells, CulturedCytochalasin BDogsEpitheliumFluorescent Antibody TechniqueHumansIntercellular JunctionsMetalloendopeptidasesPermeabilitySwineBacterial ProteinsCadherinsCytochalasin BMetalloendopeptidasespseudolysin, Pseudomonas aeruginosa

Identifiers

PMID8500907
PMCPMC280900
OpenAlexW1865065378

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.