Evidence map›Paper›PMID 22932898›Full record

ArticleThe Journal of biological chemistry2012

A proteasome inhibitor-stimulated Nrf1 protein-dependent compensatory increase in proteasome subunit gene expression reduces polycomb group protein level.

Sivaprakasam Balasubramanian, Santosh Kanade, Bingshe Han, Richard L Eckert

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

21 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Epigenetic regulation of Keap1-Nrf2 signaling.Free radical biology & medicine · 2015
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
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  18. Review
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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

4 authors at 1 institution in 1 country.

Sivaprakasam BalasubramanianDepartment of Biochemistry and Molecular Biology, University of Maryland School of Medicine, Baltimore, Maryland 21201, USA.
Santosh Kanade
Bingshe Han
Richard L Eckert
University of Maryland, Baltimore · US

Funding

UNIVERSITY OF MARYLAND GREENEBAUM CANCER CENTERSUPPORT GRANTP30CA134274 · NCI · UNIVERSITY OF MARYLAND BALTIMORE · PI FEYRUZ VIRGILIA RASSOOL · 2008 to 2026
$51.0M
Polycomb proteins and skin cancer preventionR01CA131074 · NCI · UNIVERSITY OF MARYLAND BALTIMORE · PI ECKERT, RICHARD L. · 2008 to 2017
$4.6M
Polycomb genes and keratinocyte functionR01AR053851 · NIAMS · UNIVERSITY OF MARYLAND BALTIMORE · PI ECKERT, RICHARD L. · 2008 to 2012
$2.2M
NCI NIH HHS P30 CA134274NCI NIH HHS R01 CA131074NIAMS NIH HHS R01 AR053851
6 · The paper itself

Abstract

The polycomb group (PcG) proteins, Bmi-1 and Ezh2, are important epigenetic regulators that enhance skin cancer cell survival. We recently showed that Bmi-1 and Ezh2 protein level is reduced by treatment with the dietary chemopreventive agents, sulforaphane and green tea polyphenol, and that this reduction involves ubiquitination of Bmi-1 and Ezh2, suggesting a key role of the proteasome. In the present study, we observe a surprising outcome that Bmi-1 and Ezh2 levels are reduced by treatment with the proteasome inhibitor, MG132. We show that this is associated with a compensatory increase in the level of mRNA encoding proteasome protein subunits in response to MG132 treatment and an increase in proteasome activity. The increase in proteasome subunit level is associated with increased Nrf1 and Nrf2 level. Moreover, knockdown of Nrf1 attenuates the MG132-dependent increase in proteasome subunit expression and restores Bmi-1 and Ezh2 expression. The MG132-dependent loss of Bmi-1 and Ezh2 is associated with reduced cell proliferation, accumulation of cells in G(2), and increased apoptosis. These effects are attenuated by forced expression of Bmi-1, suggesting that PcG proteins, consistent with a prosurvival action, may antagonize the action of MG132. These studies describe a compensatory Nrf1-dependent, and to a lesser extent Nrf2-dependent, increase in proteasome subunit level in proteasome inhibitor-treated cells and confirm that PcG protein levels are regulated by proteasome activity.

Indexed as

ApoptosisCell Line, TumorCysteine Proteinase InhibitorsEnhancer of Zeste Homolog 2 ProteinG2 PhaseGene Expression Regulation, EnzymologicHumansLeupeptinsNuclear Respiratory Factor 1Polycomb Repressive Complex 2Proteasome Endopeptidase ComplexProteasome InhibitorsUbiquitinationbenzyloxycarbonylleucyl-leucyl-leucine aldehydeCysteine Proteinase InhibitorsEnhancer of Zeste Homolog 2 ProteinEZH2 protein, humanLeupeptinsNRF1 protein, humanNuclear Respiratory Factor 1Polycomb Repressive Complex 2Proteasome Endopeptidase ComplexProteasome Inhibitors

Identifiers

PMID22932898
PMCPMC3476285
OpenAlexW2070867195

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.