Evidence map›Paper›PMID 17373574›Full record

ArticlePharmaceutical research2007

Melittin as an epithelial permeability enhancer I: investigation of its mechanism of action in Caco-2 monolayers.

Sam Maher, Linda Feighery, David J Brayden, Siobhán McClean

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Article in Pharmaceutical research, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
2.8field-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

13 citing papers in PubMed, 38 citations in OpenAlex.

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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

4 authors at 2 institutions in 1 country.

Sam MaherInstitute of Technology Tallaght Dublin, Belgard Road, Tallaght, Dublin, Ireland.
Linda Feighery
David J Brayden
Siobhán McClean
Tallaght University Hospital · IEUniversity College Dublin · IE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

purposeMelittin is an amphipathic antimicrobial peptide which has been shown to enhance the permeability of mannitol and reduce transepithelial electrical resistance (TER) across Caco-2 monolayers. The aim of this work was to further examine the potential of melittin as a paracellular permeability enhancer and to investigate the mechanism of interaction with tight junction proteins in Caco-2. MATERIALS AND

methodsThe permeability of a range of fluorescent markers of differing molecular weights across monolayers was examined and immunofluorescence and western blotting analysis of tight junction proteins were also carried out. The mechanism of TER reduction was also examined using cell signalling inhibitors.

resultsApical but not basolateral addition of melittin increased the permeability of a range FITC-dextrans (4-70 kDa) across monolayers. Melittin effects were reversible and no cytotoxicity was evident in polarized Caco-2 epithelia at the concentrations used. Altered expression of ZO-1, E-cadherin and F-actin was also detected. The phospholipase A2 inhibitors, aristolochic acid and indomethacin and the cyclooxygenase inhibitor, piroxicam, partially attenuated melittin-induced TER reduction, suggesting that part of the mechanism by which melittin opens tight junctions involves prostaglandin signalling.

conclusionsApically-added melittin opens tight junctions, causing dramatic TER reductions with significant increases in flux of dextrans. These effects appear mediated in part via PLA2 and involve alterations in specific tight junction proteins.

Indexed as

ActinsAristolochic AcidsCaco-2 CellsCadherinsCell SurvivalCyclooxygenase InhibitorsDextransDose-Response Relationship, DrugElectric ImpedanceEnzyme InhibitorsFluorescein-5-isothiocyanateHumansIndomethacinIntestinal AbsorptionIntestinal MucosaMelittenActinsaristolochic acid IAristolochic AcidsCadherinsCyclooxygenase InhibitorsDextransEnzyme InhibitorsFluorescein-5-isothiocyanatefluorescein isothiocyanate dextranIndomethacinMelittenMembrane ProteinsPhospholipases APhospholipases A2PhosphoproteinsPiroxicamProstaglandin-Endoperoxide SynthasesProstaglandinsTJP1 protein, humanZonula Occludens-1 Protein

Identifiers

PMID17373574
OpenAlexW2162927541

What OpenQuestion holds

Textmetadata
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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.