Evidence map›Paper›PMID 22613720›Full record

ArticleThe Journal of biological chemistry2012

Melittin modulates keratinocyte function through P2 receptor-dependent ADAM activation.

Anselm Sommer, Anja Fries, Isabell Cornelsen, Nancy Speck, Friedrich Koch-Nolte, Gerald Gimpl, Jörg Andrä, Sucharit Bhakdi, Karina Reiss

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.7field-weighted citation impact, top 11% 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

26 citing papers in PubMed, 45 citations in OpenAlex.

  1. Melittin attenuates imiquimod-induced psoriatic dermatitis in mice: a role for autophagy activation via PI3K/Akt/mTOR pathway suppression.Saudi pharmaceutical journal : SPJ : the official publication of the Saudi Pharmaceutical Society · 2026
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  10. Role of ADAM10 and ADAM17 in Regulating CD137 Function.International journal of molecular sciences · 2021
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  18. Roles of extracellular nucleotides and P2 receptors in ectodomain shedding.Cellular and molecular life sciences : CMLS · 2016
    Review
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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

9 authors at 5 institutions in 1 country.

Anselm SommerDepartment of Dermatology, Christian-Albrecht University Kiel, 24098 Kiel, Germany.
Anja Fries
Isabell Cornelsen
Nancy Speck
Friedrich Koch-Nolte
Gerald Gimpl
Jörg Andrä
Sucharit Bhakdi
Karina Reiss
Institute of Medical Microbiology and Hygiene · DEKiel University · DEJohannes Gutenberg University Mainz · DEResearch Center Borstel - Leibniz Lung Center · DEUniversität Hamburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Melittin, the major component of the bee venom, is an amphipathic, cationic peptide with a wide spectrum of biological properties that is being considered as an anti-inflammatory and anti-cancer agent. It modulates multiple cellular functions but the underlying mechanisms are not clearly understood. Here, we report that melittin activates disintegrin-like metalloproteases (ADAMs) and that downstream events likely contribute to the biological effects evoked by the peptide. Melittin stimulated the proteolysis of ADAM10 and ADAM17 substrates in human neutrophil granulocytes, endothelial cells and murine fibroblasts. In human HaCaT keratinocytes, melittin induced shedding of the adhesion molecule E-cadherin and release of TGF-α, which was accompanied by transactivation of the EGF receptor and ERK1/2 phosphorylation. This was followed by functional consequences such as increased keratinocyte proliferation and enhanced cell migration. Evidence is provided that ATP release and activation of purinergic P2 receptors are involved in melittin-induced ADAM activation. E-cadherin shedding and EGFR phosphorylation were dose-dependently reduced in the presence of ATPases or P2 receptor antagonists. The involvement of P2 receptors was underscored in experiments with HEK cells, which lack the P2X7 receptor and showed strikingly increased response to melittin stimulation after transfection with this receptor. Our study provides new insight into the mechanism of melittin function which should be of interest particularly in the context of its potential use as an anti-inflammatory or anti-cancer agent.

Indexed as

ADAM10 ProteinADAM17 ProteinADAM ProteinsAdenosine TriphosphateAmyloid Precursor Protein SecretasesAnimalsBlotting, WesternCadherinsCell LineCells, CulturedCell SurvivalDose-Response Relationship, DrugEmbryo, MammalianErbB ReceptorsExtracellular Signal-Regulated MAP KinasesFibroblastsADAM10 ProteinADAM10 protein, humanADAM17 ProteinADAM17 protein, humanAdam17 protein, mouseADAM ProteinsAdenosine TriphosphateAmyloid Precursor Protein SecretasesCadherinsErbB ReceptorsExtracellular Signal-Regulated MAP KinasesMelittenMembrane ProteinsReceptors, Purinergic P2X7

Identifiers

PMID22613720
PMCPMC3390642
OpenAlexW2049445130

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.