Evidence map›Paper›PMID 21768092›Full record

ArticleThe Journal of biological chemistry2011

Roles of the 15-kDa selenoprotein (Sep15) in redox homeostasis and cataract development revealed by the analysis of Sep 15 knockout mice.

Marina V Kasaikina, Dmitri E Fomenko, Vyacheslav M Labunskyy, Salil A Lachke, Wenya Qiu, Juliet A Moncaster, Jie Zhang, Mark W Wojnarowicz, Sathish Kumar Natarajan, Mikalai Malinouski and 8 more

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed
–field-weighted citation impact
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

58 citing papers in PubMed.

  1. Review
  2. Review
  3. Insights into the interaction between UGGT, the gatekeeper of folding in the ER, and its partner, the selenoprotein SEP15.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  4. Review
  5. Article
  6. Biological and Catalytic Properties of Selenoproteins.International journal of molecular sciences · 2023
    Review
  7. Article
  8. Review
  9. Selenoproteins and the senescence-associated epitranscriptome.Experimental biology and medicine (Maywood, N.J.) · 2022
    Review
  10. Article
  11. Review
  12. Review
  13. Article
  14. Review
  15. Review
  16. Article
  17. Review
  18. Article
  19. Selenoprotein F knockout leads to glucose and lipid metabolism disorders in mice.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2020
    Article
  20. 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

18 authors.

Marina V KasaikinaDivision of Genetics, Department of Medicine, Brigham and Women's Hospital and Harvard Medical School, Boston, Massachusetts 02115, USA.
Dmitri E Fomenko
Vyacheslav M Labunskyy
Salil A Lachke
Wenya Qiu
Juliet A Moncaster
Jie Zhang
Mark W Wojnarowicz
Sathish Kumar Natarajan
Mikalai Malinouski
Ulrich Schweizer
Petra A Tsuji
Bradley A Carlson
Richard L Maas
Marjorie F Lou
Lee E Goldstein
Dolph L Hatfield
Vadim N Gladyshev

Funding

Selenoproteins as Targets for Cancer PreventionR01CA080946 · NCI · UNIVERSITY OF NEBRASKA LINCOLN · PI GLADYSHEV, VADIM N. · 2001 to 2018
$4.5M
Role of Selenium in Development and HealthZIABC005317 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI HATFIELD, DOLPH · 2009 to 2014
$2.7M
Role of Selenium-containing Proteins in Cancer and DevelopmentZIABC010889 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI HATFIELD, DOLPH · 2009 to 2012
$2.2M
Intramural NIH HHSNCI NIH HHS CA080946NCI NIH HHS R01 CA080946
6 · The paper itself

Abstract

The 15-kDa selenoprotein (Sep15) is a thioredoxin-like, endoplasmic reticulum-resident protein involved in the quality control of glycoprotein folding through its interaction with UDP-glucose:glycoprotein glucosyltransferase. Expression of Sep15 is regulated by dietary selenium and the unfolded protein response, but its specific function is not known. In this study, we developed and characterized Sep15 KO mice by targeted removal of exon 2 of the Sep15 gene coding for the cysteine-rich UDP-glucose:glycoprotein glucosyltransferase-binding domain. These KO mice synthesized a mutant mRNA, but the shortened protein product could be detected neither in tissues nor in Sep15 KO embryonic fibroblasts. Sep15 KO mice were viable and fertile, showed normal brain morphology, and did not activate endoplasmic reticulum stress pathways. However, parameters of oxidative stress were elevated in the livers of these mice. We found that Sep15 mRNA was enriched during lens development. Further phenotypic characterization of Sep15 KO mice revealed a prominent nuclear cataract that developed at an early age. These cataracts did not appear to be associated with severe oxidative stress or glucose dysregulation. We suggest that the cataracts resulted from an improper folding status of lens proteins caused by Sep15 deficiency.

Indexed as

HomeostasisAmino Acid SequenceAnimalsBrainCataractGene Expression Regulation, DevelopmentalHEK293 CellsHumansLens, CrystallineMaleMiceMice, KnockoutMolecular Sequence DataMolecular WeightMutant ProteinsNIH 3T3 CellsMutant ProteinsRNA, MessengerSelenof protein, mouseSelenoprotein PSelenoproteins

Identifiers

PMID21768092
PMCPMC3190948

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.