Evidence map›Paper›PMID 24413684›Full record

ArticleCarcinogenesis2014

Tumor suppressor PDCD4 inhibits NF-κB-dependent transcription in human glioblastoma cells by direct interaction with p65.

Soon-Kyung Hwang, Alyson R Baker, Matthew R Young, Nancy H Colburn

Open access · greenAbstract read
In one paragraph

Article in Carcinogenesis, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed, 1 pooled it
1.9field-weighted citation impact, top 15% 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

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

  1. Pooled it
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  14. Review
  15. Control Mechanisms of the Tumor Suppressor PDCD4: Expression and Functions.International journal of molecular sciences · 2019
    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 3 institutions in 1 country.

Soon-Kyung HwangLaboratory of Cancer Prevention, Center for Cancer Research, National Cancer Institute, Frederick National Laboratory, 1050 Boyles Street, Bldg 576, Rm 101, Frederick, MD 21702, USA police042@naver.com.
Alyson R BakerLaboratory of Cancer Prevention, Center for Cancer Research, National Cancer Institute, Frederick National Laboratory, 1050 Boyles Street, Bldg 576, Rm 101, Frederick, MD 21702, USA.
Matthew R YoungLaboratory of Cancer Prevention, Center for Cancer Research, National Cancer Institute, Frederick National Laboratory, 1050 Boyles Street, Bldg 576, Rm 101, Frederick, MD 21702, USA.
Nancy H ColburnLaboratory of Cancer Prevention, Center for Cancer Research, National Cancer Institute, Frederick National Laboratory, 1050 Boyles Street, Bldg 576, Rm 101, Frederick, MD 21702, USA.
National Cancer Institute · USCenter for Cancer Research · USFrederick National Laboratory for Cancer Research · US

Funding

The Role of Pdcd4 in Translation, Tumorigenesis and Tumor ProgressionZIABC010026 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI COLBURN, NANCY H. · 2009 to 2013
$2.7M
Intramural NIH HHSNCI NIH HHS ZIA BC 010026
6 · The paper itself

Abstract

PDCD4 is a tumor suppressor induced by apoptotic stimuli that regulates both translation and transcription. Previously, we showed that overexpression of PDCD4 leads to decreased anchorage-independent growth in glioblastoma (GBM)-derived cell lines and decreased tumor growth in a GBM xenograft model. In inflammatory cells, PDCD4 stimulates tumor necrosis factor-induced activation of the transcription factor NF-κB, an oncogenic driver in many cancer sites. However, the effect of PDCD4 on NF-κB transcriptional activity in most cancers including GBM is still unknown. We studied the effect of PDCD4 on NF-κB-dependent transcriptional activity in GBM by stably overexpressing PDCD4 in U251 and LN229 cells. Stable PDCD4 expression inhibits NF-κB transcriptional activation measured by a luciferase reporter. The molecular mechanism by which PDCD4 inhibits NF-κB transcriptional activation does not involve inhibited expression of NF-κB p65 or p50 proteins. PDCD4 does not inhibit pathways upstream of NF-κB including the activation of IKKα and IKKβ kinases or degradation of IκBα, events needed for nuclear transport of p65 and p50. PDCD4 overexpression does inhibit localization of p65 but not p50 in the nucleus. PDCD4 protein interacts preferentially with p65 protein as shown by co-immunoprecipitation and confocal imaging. PDCD4 overexpression inhibits the mRNA expression of two NF-κB target genes in a p65-dependent manner. These results suggest that PDCD4 can significantly inhibit NF-κB activity in GBM cells by a mechanism that involves direct or indirect protein-protein interaction independent of the expected mRNA-selective translational inhibition. These findings offer novel opportunities for NF-κB-targeted interventions to prevent or treat cancer.

Indexed as

Gene Expression Regulation, NeoplasticApoptosisApoptosis Regulatory ProteinsBlotting, WesternCell MovementCell ProliferationChromatin ImmunoprecipitationGlioblastomaHumansImmunoprecipitationNF-kappa B p50 SubunitReal-Time Polymerase Chain ReactionReverse Transcriptase Polymerase Chain ReactionRNA-Binding ProteinsRNA, MessengerTranscription Factor RelAApoptosis Regulatory ProteinsNF-kappa B p50 SubunitPDCD4 protein, humanRNA-Binding ProteinsRNA, MessengerTranscription Factor RelA

Identifiers

PMID24413684
PMCPMC4076808
OpenAlexW2328415948

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.