Evidence map›Paper›PMID 22049022›Full record

ArticleMolecular biology of the cell2012

Rapid degradation of cyclooxygenase-1 and hematopoietic prostaglandin D synthase through ubiquitin-proteasome system in response to intracellular calcium level.

Misato Yazaki, Kaori Kashiwagi, Kosuke Aritake, Yoshihiro Urade, Ko Fujimori

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2012. 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
1.2field-weighted citation impact, top 22% 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, 26 citations in OpenAlex.

  1. Article
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  7. Review
  8. Article
  9. The COP9 signalosome and vascular function: intriguing possibilities?American journal of cardiovascular disease · 2015
    Review
  10. Review
  11. De novo expression of connexin hemichannels in denervated fast skeletal muscles leads to atrophy.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  12. Article
  13. Article
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

5 authors at 2 institutions in 1 country.

Misato YazakiLaboratory of Biodefense and Regulation, Osaka University of Pharmaceutical Sciences, Takatsuki, Osaka, Japan.
Kaori Kashiwagi
Kosuke Aritake
Yoshihiro Urade
Ko Fujimori
Osaka University · JPOsaka University of Pharmaceutical Sciences · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cyclooxygenase (COX)-1 and hematopoietic prostaglandin (PG) D synthase (H-PGDS) proteins, which are both involved in the arachidonate cascade, were stable in human megakaryocytic MEG-01 cells. In contrast, once the intracellular calcium level was increased by treatment with a calcium ionophore, both protein levels rapidly decreased with a half-life of less than 30 and 120 min for COX-1 and H-PGDS, respectively. In the presence of a proteasome inhibitor, COX-1 and H-PGDS proteins accumulated within 10 and 30 min, respectively, and concurrently appeared as the high-molecular-mass ubiquitinated proteins within 30 and 60 min, respectively, after an increase in the intracellular calcium level. The ubiquitination of these proteins was also observed when ADP, instead of a calcium ionophore, was used as an inducer to elevate the intracellular calcium level. When the entry of calcium ion into the cells was inhibited by ethylene glycol tetraacetic acid (EGTA), the ubiquitination of COX-1 and H-PGDS was clearly suppressed; and the addition of CaCl(2) to the medium cleared the EGTA-mediated suppression of the ubiquitination. These results indicate that COX-1 and H-PGDS were rapidly ubiquitinated and degraded through the ubiquitin-proteasome system in response to the elevation of the intracellular calcium level.

Indexed as

Adenosine DiphosphateArachidonic AcidCalcimycinCalcium IonophoresCalcium SignalingCell LineCyclooxygenase 1Half-LifeHumansIntramolecular OxidoreductasesLeupeptinsLipocalinsProteasome Endopeptidase ComplexProteasome InhibitorsProtein StabilityProteolysisAdenosine DiphosphateArachidonic Acidbenzyloxycarbonylleucyl-leucyl-leucine aldehydeCalcimycinCalcium IonophoresCyclooxygenase 1Intramolecular OxidoreductasesLeupeptinsLipocalinsprostaglandin R2 D-isomeraseProteasome Endopeptidase ComplexProteasome InhibitorsPTGS1 protein, humanUbiquitinated Proteins

Identifiers

PMID22049022
PMCPMC3248891
OpenAlexW2135479237

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.