Evidence map›Paper›PMID 22947142›Full record

ArticleBMC genomics2012

Microarray analysis revealing common and distinct functions of promyelocytic leukemia protein (PML) and tumor necrosis factor alpha (TNFα) signaling in endothelial cells.

Xiwen Cheng, Hung-Ying Kao

Open access · goldAbstract read
In one paragraph

Article in BMC genomics, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

17 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
  2. Interleukin-1β Stimulates Matrix Metalloproteinase 10 Secretion: A Possible Mechanism in Trophoblast-Dependent Spiral Artery Remodeling.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025
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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

2 authors at 1 institution in 1 country.

Xiwen ChengDepartment of Biochemistry, School of Medicine, Case Western Reserve University (CWRU) and the Comprehensive Cancer Center of CWRU and University Hospital of Cleveland (UHC), Cleveland, OH 44106, USA.
Hung-Ying Kao
Case Western Reserve University · US

Funding

Alpha actinin 4: its functions and regulationR01DK078965 · NIDDK · CASE WESTERN RESERVE UNIVERSITY · PI KAO, HUNG-YING · 2009 to 2013
$1.7M
Histone deacetylase 7 and its interacting proteins in endothelial cellsR01HL093269 · NHLBI · CASE WESTERN RESERVE UNIVERSITY · PI KAO, HUNG-YING · 2010 to 2013
$1.5M
NHLBI NIH HHS R01 HL093269NIDDK NIH HHS DK078965NIDDK NIH HHS R01 DK078965
6 · The paper itself

Abstract

backgroundPromyelocytic leukemia protein (PML) is a tumor suppressor that is highly expressed in endothelial cells nonetheless its role in endothelial cell biology remains elusive. Tumor necrosis factor alpha (TNFα) is an important cytokine associated with many inflammation-related diseases. We have previously demonstrated that TNFα induces PML protein accumulation. We hypothesized that PML may play a role in TNFα signaling pathway. To identify potential PML target genes and investigate the putative crosstalk between PML's function and TNFα signaling in endothelial cells, we carried out a microarray analysis in human primary umbilical endothelial cells (HUVECs).

resultsWe found that PML and TNFα regulate common and distinct genes involved in a similar spectrum of biological processes, pathways and human diseases. More importantly, we found that PML is required for fine-tuning of TNFα-mediated immune and inflammatory responses. Furthermore, our data suggest that PML and TNFα synergistically regulate cell adhesion by engaging multiple molecular mechanisms. Our biological functional assays exemplified that adhesion of U937 human leukocytes to HUVECs is co-regulated by PML and TNFα signaling.

conclusionsTogether, our study identified PML as an essential regulator of TNFα signaling by revealing the crosstalk between PML knockdown-mediated effects and TNFα-elicited signaling, thereby providing novel insights into TNFα signaling in endothelial cells.

Indexed as

Cell AdhesionGene Expression RegulationHumansHuman Umbilical Vein Endothelial CellsMicroarray AnalysisNuclear ProteinsPromyelocytic Leukemia ProteinSignal TransductionTranscription FactorsTumor Necrosis Factor-alphaTumor Suppressor ProteinsU937 CellsNuclear ProteinsPML protein, humanPromyelocytic Leukemia ProteinTranscription FactorsTumor Necrosis Factor-alphaTumor Suppressor Proteins

Identifiers

PMID22947142
PMCPMC3542097
OpenAlexW2084085000

What OpenQuestion holds

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LicenceCC BY
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.