Evidence map›Paper›PMID 28038463›Full record

ArticleOncotarget2017

SETMAR isoforms in glioblastoma: A matter of protein stability.

Audrey Dussaussois-Montagne, Jérôme Jaillet, Laetitia Babin, Pierre Verrelle, Lucie Karayan-Tapon, Sylvaine Renault, Cécilia Rousselot-Denis, Ilyess Zemmoura, Corinne Augé-Gouillou

Open access · diamondAbstract read
In one paragraph

Article in Oncotarget, 2017. 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
0.3field-weighted citation impact, top 30% 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, 19 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

9 authors at 5 institutions in 1 country.

Audrey Dussaussois-MontagneEA 6306 IGC, University François Rabelais, 37200 Tours, France.
Jérôme JailletEA 6306 IGC, University François Rabelais, 37200 Tours, France.
Laetitia BabinEA 6306 IGC, University François Rabelais, 37200 Tours, France.
Pierre VerrelleEA 7283 CREaT, Université d'Auvergne, BP 10448, 63000 Clermont-Ferrand, France.
Lucie Karayan-TaponINSERM U1084, Laboratoire de Neurosciences Expérimentales et Cliniques, F-86021 Poitiers, France.
Sylvaine RenaultEA 6306 IGC, University François Rabelais, 37200 Tours, France.
Cécilia Rousselot-DenisCHRU of Tours, Unité d'Anatomie et Cytologie Pathologiques, 37000 Tours, France.
Ilyess ZemmouraINSERM U930 Imagerie & Cerveau, University François Rabelais, 37000 Tours, France.
Corinne Augé-GouillouEA 6306 IGC, University François Rabelais, 37200 Tours, France.
Université de Tours · FRCentre Hospitalier Universitaire de Tours · FRInserm · FRLaboratoire de Neurosciences Expérimentales et CliniquesUniversité Clermont Auvergne · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Glioblastomas (GBMs) are the most frequent and the most aggressive brain tumors, known for their chemo- and radio-resistance, making them often incurable. We also know that SETMAR is a protein involved in chromatin dynamics and genome plasticity, of which overexpression confers chemo- and radio-resistance to some tumors. The relationships between SETMAR and GBM have never been explored. To fill this gap, we define the SETMAR status of 44 resected tumors and of GBM derived cells, at both the mRNA and the protein levels. We identify a new, small SETMAR protein (so called SETMAR-1200), enriched in GBMs and GBM stem cells as compared to the regular enzyme (SETMAR-2100). We show that SETMAR-1200 is able to increase DNA repair by non-homologous end-joining, albeit with a lower efficiency than the regular SETMAR protein. Interestingly, the regular/small ratio of SETMAR in GBM cells changes depending on cell type, providing evidence that SETMAR expression is regulated by alternative splicing. We also demonstrate that SETMAR expression can be regulated by the use of an alternative ATG. In conclusion, various SETMAR proteins can be synthesized in human GBM that may each have specific biophysical and/or biochemical properties and characteristics. Among them, the small SETMAR may play a role in GBMs biogenesis. On this basis, we would like to consider SETMAR-1200 as a new potential therapeutic target to investigate, in addition to the regular SETMAR protein already considered by others.

Indexed as

Alternative SplicingAnimalsBrain NeoplasmsCell Line, TumorCHO CellsCricetulusEnzyme StabilityGene Expression Regulation, EnzymologicGene Expression Regulation, NeoplasticGlioblastomaHistone-Lysine N-MethyltransferaseHumansNeoplastic Stem CellsProtein IsoformsRNA, MessengerTime FactorsHistone-Lysine N-MethyltransferaseProtein IsoformsRNA, MessengerSETMAR protein, humanalternative ATGglioblastomaNHEJ repairprotein half-liveSETMAR

Identifiers

PMID28038463
PMCPMC5354774
OpenAlexW2567110406

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.