Evidence map›Paper›PMID 28262838›Full record

ArticleScientific reports2017

Galectin-3 is a non-classic RNA binding protein that stabilizes the mucin MUC4 mRNA in the cytoplasm of cancer cells.

Lucie Coppin, Audrey Vincent, Frédéric Frénois, Belinda Duchêne, Fatima Lahdaoui, Laurence Stechly, Florence Renaud, Céline Villenet, Isabelle Van Seuningen, Emmanuelle Leteurtre and 7 more

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. 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
1.8field-weighted citation impact, top 16% 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, 42 citations in OpenAlex.

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  12. hnRNPL expression dynamics in the embryo and placenta.Gene expression patterns : GEP · 2023
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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

17 authors at 6 institutions in 1 country.

Lucie CoppinUniv. Lille, UMR-S 1172 - JPARC - Jean-Pierre Aubert Research Center, F-59000 Lille, France.
Audrey VincentUniv. Lille, UMR-S 1172 - JPARC - Jean-Pierre Aubert Research Center, F-59000 Lille, France.
Frédéric FrénoisUniv. Lille, RADEME (Research team on rare developmental and metabolic diseases), F-59000 Lille, France.
Belinda DuchêneUniv. Lille, UMR-S 1172 - JPARC - Jean-Pierre Aubert Research Center, F-59000 Lille, France.
Fatima LahdaouiUniv. Lille, UMR-S 1172 - JPARC - Jean-Pierre Aubert Research Center, F-59000 Lille, France.
Laurence StechlyCHU Lille, Service de Biochimie « Hormonologie, Métabolisme-Nutrition, Oncologie », F-59000 Lille, France.
Florence RenaudUniv. Lille, UMR-S 1172 - JPARC - Jean-Pierre Aubert Research Center, F-59000 Lille, France.
Céline VillenetUniv. Lille, CHU Lille, Plate-forme de génomique fonctionnelle, Centre de Biologie et Pathologie, F-59037 Lille cedex, France.
Isabelle Van SeuningenUniv. Lille, UMR-S 1172 - JPARC - Jean-Pierre Aubert Research Center, F-59000 Lille, France.
Emmanuelle LeteurtreUniv. Lille, UMR-S 1172 - JPARC - Jean-Pierre Aubert Research Center, F-59000 Lille, France.
Johann DionEquipe Ingénierie Moléculaire et Glycobiologie, UMR CNRS 6286, Unité Fonctionnalité et Ingénierie des Protéines, Faculté des Sciences et Techniques, F-44322 Nantes cedex 3, France.
Cyrille GrandjeanEquipe Ingénierie Moléculaire et Glycobiologie, UMR CNRS 6286, Unité Fonctionnalité et Ingénierie des Protéines, Faculté des Sciences et Techniques, F-44322 Nantes cedex 3, France.
Françoise PoirierEquipe « Morphogenèse, homéostasie et pathologies » Institut Jacques Monod - UMR 7592 CNRS - Université Paris Diderot, F-75205 Paris Cedex 13, France.
Martin FigeacUniv. Lille, CHU Lille, Plate-forme de génomique fonctionnelle, Centre de Biologie et Pathologie, F-59037 Lille cedex, France.
Delphine DelacourEquipe CAM « Cell adhesion and mechanics" Institut Jacques Monod - UMR 7592 CNRS - Université Paris Diderot, F-75205 Paris Cedex 13, France.
Nicole PorchetUniv. Lille, UMR-S 1172 - JPARC - Jean-Pierre Aubert Research Center, F-59000 Lille, France.
Pascal PignyUniv. Lille, UMR-S 1172 - JPARC - Jean-Pierre Aubert Research Center, F-59000 Lille, France.
Inserm · FRCentre National de la Recherche Scientifique · FRUniversité de Lille · FRCentre de Recherche Jean Pierre Aubert · FRInstitut de Biologie de Lille · FRCentre Hospitalier Universitaire de Lille · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Pancreatic cancer cells express high levels of MUC1, MUC4 and MUC16 mRNAs that encode membrane-bound mucins. These mRNAs share unusual features such as a long half-life. However, it remains unknown how mucin mRNA stability is regulated. Galectin-3 (Gal-3) is an endogenous lectin playing important biological functions in epithelial cells. Gal-3 is encoded by LGALS3 which is up-regulated in pancreatic cancer. Despite the absence of a RNA-recognition motif, Gal-3 interacts indirectly with pre-mRNAs in the nucleus and promotes constitutive splicing. However a broader role of Gal-3 in mRNA fate is unexplored. We report herein that Gal-3 increases MUC4 mRNA stability through an intermediate, hnRNP-L which binds to a conserved CA repeat element in the 3'UTR in a Gal-3 dependent manner and also controls Muc4 mRNA levels in epithelial tissues of Gal3

Indexed as

AnimalsBlood ProteinsCytoplasmEpithelial CellsGalectin 3GalectinsGene Expression RegulationHumansMice, Inbred C57BLMice, KnockoutMucin-4Pancreatic NeoplasmsRNA, MessengerRNA StabilityBlood ProteinsGalectin 3GalectinsLGALS3 protein, humanMUC4 protein, humanMucin-4RNA, Messenger

Identifiers

PMID28262838
PMCPMC5338267
OpenAlexW2594684759

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.