Evidence map›Paper›PMID 27240165›Full record

ArticleeLife2016

Secretion of protein disulphide isomerase AGR2 confers tumorigenic properties.

Delphine Fessart, Charlotte Domblides, Tony Avril, Leif A Eriksson, Hugues Begueret, Raphael Pineau, Camille Malrieux, Nathalie Dugot-Senant, Carlo Lucchesi, Eric Chevet and 1 more

Open access · goldAbstract read
In one paragraph

Article in eLife, 2016. 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
4.5field-weighted citation impact, top 5% 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, 131 citations in OpenAlex.

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  11. Nanoplasmonic Single-Tumoroid Microarray for Real-Time Secretion Analysis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024
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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 5 institutions in 2 countries.

Delphine FessartOncogenesis, Stress and Signaling Laboratory, ERL440 Inserm, Université de Rennes 1, Rennes, France.ORCID 0000-0001-7566-5670
Charlotte DomblidesUniversité de Bordeaux, Bordeaux, France.
Tony AvrilOncogenesis, Stress and Signaling Laboratory, ERL440 Inserm, Université de Rennes 1, Rennes, France.
Leif A ErikssonDepartment of Chemistry and Molecular Biology, University of Gothenburg, Göteborg, Sweden.
Hugues BegueretHôpital Haut-Lévêque, Bordeaux, France.
Raphael PineauAnimalerie mutualisée, Université de Bordeaux, Bordeaux, France.
Camille MalrieuxINSERM U1218, Actions for onCogenesis understanding and Target Identification in ONcology (ACTION), Bordeaux, France.
Nathalie Dugot-SenantUniversité de Bordeaux, Bordeaux, France.
Carlo LucchesiBergonié Cancer Institute, Bordeaux, France.
Eric ChevetOncogenesis, Stress and Signaling Laboratory, ERL440 Inserm, Université de Rennes 1, Rennes, France.ORCID 0000-0001-5855-4522
Frederic DelomINSERM U1218, Actions for onCogenesis understanding and Target Identification in ONcology (ACTION), Bordeaux, France.ORCID 0000-0002-4600-7633
Université de Bordeaux · FRInserm · FRHôpital Cardiologique du Haut-Lévêque · FRInstitut Bergonié · FRUniversity of Gothenburg · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The extracellular matrix (ECM) plays an instrumental role in determining the spatial orientation of epithelial polarity and the formation of lumens in glandular tissues during morphogenesis. Here, we show that the Endoplasmic Reticulum (ER)-resident protein anterior gradient-2 (AGR2), a soluble protein-disulfide isomerase involved in ER protein folding and quality control, is secreted and interacts with the ECM. Extracellular AGR2 (eAGR2) is a microenvironmental regulator of epithelial tissue architecture, which plays a role in the preneoplastic phenotype and contributes to epithelial tumorigenicity. Indeed, eAGR2, is secreted as a functionally active protein independently of its thioredoxin-like domain (CXXS) and of its ER-retention domain (KTEL), and is sufficient, by itself, to promote the acquisition of invasive and metastatic features. Therefore, we conclude that eAGR2 plays an extracellular role independent of its ER function and we elucidate this gain-of-function as a novel and unexpected critical ECM microenvironmental pro-oncogenic regulator of epithelial morphogenesis and tumorigenesis.

Indexed as

CarcinogenesisCells, CulturedEpithelial CellsExtracellular MatrixHumansMucoproteinsNeoplasmsOncogene ProteinsProteinsAGR2 protein, humanMucoproteinsOncogene ProteinsProteinsAGR2cancercancer biologycell biologyendoplasmic reticulumhumanmouseorganoidsprotein disulphide isomerase

Identifiers

PMID27240165
PMCPMC4940162
OpenAlexW2410706815

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.