Evidence map›Paper›PMID 12881705›Full record

ArticleOncogene2003

Selective abrogation of the proinvasive activity of the trefoil peptides pS2 and spasmolytic polypeptide by disruption of the EGF receptor signaling pathways in kidney and colonic cancer cells.

Sylvie Rodrigues, Samir Attoub, Quang-Dé Nguyen, Erik Bruyneel, Christelle M Rodrigue, Bruce R Westley, Felicity E B May, Lars Thim, Marc Mareel, Shahin Emami and 1 more

Abstract read
PubMed Publisher
In one paragraph

Article in Oncogene, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
6.1field-weighted citation impact, top 4% 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

16 citing papers in PubMed, 67 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

11 authors at 4 institutions in 5 countries.

Sylvie RodriguesINSERM U482, Signal Transduction and Cellular Functions in Diabetes and Digestive Cancers, Hôpital Saint-Antoine, 75571 Paris, France.
Samir Attoub
Quang-Dé Nguyen
Erik Bruyneel
Christelle M Rodrigue
Bruce R Westley
Felicity E B May
Lars Thim
Marc Mareel
Shahin Emami
Christian Gespach
Inserm · FRGhent University Hospital · BEUniversity of Newcastle Australia · AUNovo Nordisk (Denmark) · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Trefoil peptides (TFFs) are now considered as scatter factors, proinvasive and angiogenic agents acting through cyclooxygenase-2 (COX-2)- and thromboxane A2 receptor (TXA2-R)-dependent signaling pathways. As expression and activation levels of the epidermal growth factor receptor (EGFR) predict the metastatic potential of human colorectal cancers, the purpose of this study was to establish whether the EGF receptor tyrosine kinase (EGFR-TK) contributes to cellular invasion induced by TFFs in kidney and colonic cancer cells. Both the dominant negative form of the EGFR (HER-CD533) and the EGFR-TK inhibitor ZD1839 (Iressa) abrogated cellular invasion induced by pS2, spasmolytic polypeptide (SP) and the src oncogene, but not by ITF and the TXA2-R. Similarly, EGFR-TK inhibition by ZD1839 reversed the invasive phenotype promoted by the constitutively activated form of the EGFR (EGFRvIII) and the EGFR agonists transforming growth factor alpha (TGFalpha), amphiregulin and EGF. We also provide evidence that TFFs, EGFRvIII, and TGFalpha trigger common proinvasive pathways using the PI3'-kinase and Rho/Rho- kinase cascades. These findings identify the EGFR-TK as a key signaling element for pS2- and SP-mediated cellular invasion. It is concluded that although pS2, SP and ITF belong to the same family of inflammation- and cancer-associated regulatory peptides, they do not control identical signaling networks.

Indexed as

MucinsMuscle ProteinsNeuropeptidesProteinsAmphiregulinAnimalsCells, CulturedColonic NeoplasmsDogsEGF Family of ProteinsEnzyme InhibitorsEpidermal Growth FactorErbB ReceptorsGefitinibGenes, srcGlycoproteinsAmphiregulinAREG protein, humanAreg protein, ratEGF Family of ProteinsEnzyme InhibitorsEpidermal Growth FactorErbB ReceptorsGefitinibGlycoproteinsGrowth SubstancesIntercellular Signaling Peptides and ProteinsMucinsMuscle ProteinsNeuropeptidesPeptidesPhosphatidylinositol 3-KinasesProteinsQuinazolinesReceptors, ThromboxaneTFF1 protein, humanTff2 protein, ratTFF3 protein, ratTransforming Growth Factor alphaTrefoil Factor-1Trefoil Factor-2Trefoil Factor-3Tumor Suppressor Proteins

Identifiers

PMID12881705
OpenAlexW2083044332

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.