Evidence map›Paper›PMID 24706762›Full record

ArticleThe Journal of biological chemistry2014

Selective up-regulation of human selenoproteins in response to oxidative stress.

Zahia Touat-Hamici, Yona Legrain, Anne-Laure Bulteau, Laurent Chavatte

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed, 1 pooled it
7.2field-weighted citation impact, top 2% 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

51 citing papers in PubMed, 1 synthesis or guideline pooled it, 102 citations in OpenAlex.

  1. Pooled it
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  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Biological and Catalytic Properties of Selenoproteins.International journal of molecular sciences · 2023
    Review
  13. Article
  14. Article
  15. Review
  16. Review
  17. Article
  18. Article
  19. Article
  20. Nrf2 in Cancer, Detoxifying Enzymes and Cell Death Programs.Antioxidants (Basel, Switzerland) · 2021
    Review
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

4 authors at 4 institutions in 1 country.

Zahia Touat-HamiciFrom the Centre de Génétique Moléculaire, CNRS, UPR3404, 91198 Gif-sur-Yvette, France.
Yona LegrainFrom the Centre de Génétique Moléculaire, CNRS, UPR3404, 91198 Gif-sur-Yvette, France.
Anne-Laure Bulteauthe Centre de Recherche Institut Cochin, INSERM U567, CNRS UMR 8104, 75005 Paris, France, and the Laboratoire de Chimie Analytique Bio-Inorganique et Environnement, CNRS/UPPA, UMR5254, 64000 Pau, France.
Laurent ChavatteFrom the Centre de Génétique Moléculaire, CNRS, UPR3404, 91198 Gif-sur-Yvette, France, the Laboratoire de Chimie Analytique Bio-Inorganique et Environnement, CNRS/UPPA, UMR5254, 64000 Pau, France laurent.chavatte@univ-pau.fr.
Centre de Génétique Moléculaire · FRCentre National de la Recherche Scientifique · FRInstitut Cochin · FRLaboratoire de Chimie · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Selenocysteine is inserted into selenoproteins via the translational recoding of a UGA codon, normally used as a stop signal. This process depends on the nature of the selenocysteine insertion sequence element located in the 3' UTR of selenoprotein mRNAs, selenium bioavailability, and, possibly, exogenous stimuli. To further understand the function and regulation of selenoproteins in antioxidant defense and redox homeostasis, we investigated how oxidative stress influences selenoprotein expression as a function of different selenium concentrations. We found that selenium supplementation of the culture media, which resulted in a hierarchical up-regulation of selenoproteins, protected HEK293 cells from reactive oxygen species formation. Furthermore, in response to oxidative stress, we identified a selective up-regulation of several selenoproteins involved in antioxidant defense (Gpx1, Gpx4, TR1, SelS, SelK, and Sps2). Interestingly, the response was more efficient when selenium was limiting. Although a modest change in mRNA levels was noted, we identified a novel translational control mechanism stimulated by oxidative stress that is characterized by up-regulation of UGA-selenocysteine recoding efficiency and relocalization of SBP2, selenocysteine-specific elongation factor, and L30 recoding factors from the cytoplasm to the nucleus.

Indexed as

Oxidative StressCell NucleusCytoplasmGene ExpressionGlutathione PeroxidaseGlutathione Peroxidase GPX1HEK293 CellsHumansHydrogen PeroxideImmunoblottingMembrane ProteinsMicroscopy, FluorescenceOxidantsPhospholipid Hydroperoxide Glutathione PeroxidaseReactive Oxygen SpeciesReverse Transcriptase Polymerase Chain ReactionGlutathione PeroxidaseGlutathione Peroxidase GPX1GPX1 protein, humanHydrogen PeroxideMembrane ProteinsOxidantsPhospholipid Hydroperoxide Glutathione PeroxidaseReactive Oxygen SpeciesSeleniumSelenocysteineSelenoproteinsSELENOS protein, humanGlutathione PeroxidaseOxidative StressSECISSeleniumSelenoproteomeThioredoxin ReductaseTranslation RegulationUGA Recoding

Identifiers

PMID24706762
PMCPMC4031530
OpenAlexW2011181458

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.