Evidence map›Paper›PMID 22361822›Full record

ArticleMolecular endocrinology (Baltimore, Md.)2012

Protein arginine methyltransferase 5 (Prmt5) promotes gene expression of peroxisome proliferator-activated receptor γ2 (PPARγ2) and its target genes during adipogenesis.

Scott E LeBlanc, Silvana Konda, Qiong Wu, Yu-Jie Hu, Christine M Oslowski, Saïd Sif, Anthony N Imbalzano

Open access · bronzeAbstract read
In one paragraph

Article in Molecular endocrinology (Baltimore, Md.), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

46 citing papers in PubMed, 66 citations in OpenAlex.

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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

7 authors at 2 institutions in 1 country.

Scott E LeBlancDepartment of Cell Biology, University of Massachusetts Medical School, 55 Lake Avenue North, Worcester, Massachusetts 01655, USA.
Silvana Konda
Qiong Wu
Yu-Jie Hu
Christine M Oslowski
Saïd Sif
Anthony N Imbalzano
University of Massachusetts Chan Medical School · USThe Ohio State University · US

Funding

PILOT AND FEASIBILITY PROGRAMP30DK032520 · NIDDK · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI CZECH, MICHAEL P · 1986 to 2010
$14.6M
TRANSCRIPTION FACTOR FUNCTION IN CHROMATINR01GM056244 · NIGMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI IMBALZANO, ANTHONY N · 1997 to 2019
$6.7M
Epigenetic Control of AdipogenesisR01DK084278 · NIDDK · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI IMBALZANO, ANTHONY N, SIF, SAID · 2009 to 2010
$746k
Spatial changes in gene organization during adipogenesisR21DK079239 · NIDDK · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI IMBALZANO, ANTHONY N · 2007 to 2008
$442k
Control of Adipogenesis by Arginine MethyltransferasesF32DK082263 · NIDDK · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI LEBLANC, SCOTT E · 2009 to 2012
$159k
NIDDK NIH HHS 5P30DK32520NIDDK NIH HHS F32 DK082263NIDDK NIH HHS F32DK082263NIDDK NIH HHS P30 DK032520NIDDK NIH HHS R01 DK084278NIDDK NIH HHS R01DK084278NIDDK NIH HHS R21 DK079239NIDDK NIH HHS R21DK079239NIGMS NIH HHS R01 GM056244
6 · The paper itself

Abstract

Regulation of adipose tissue formation by adipogenic-regulatory proteins has long been a topic of interest given the ever-increasing health concerns of obesity and type 2 diabetes in the general population. Differentiation of precursor cells into adipocytes involves a complex network of cofactors that facilitate the functions of transcriptional regulators from the CCATT/enhancer binding protein, and the peroxisome proliferator-activated receptor (PPAR) families. Many of these cofactors are enzymes that modulate the structure of chromatin by altering histone-DNA contacts in an ATP-dependent manner or by posttranslationally modifying the histone proteins. Here we report that inhibition of protein arginine methyltransferase 5 (Prmt5) expression in multiple cell culture models for adipogenesis prevented the activation of adipogenic genes. In contrast, overexpression of Prmt5 enhanced adipogenic gene expression and differentiation. Chromatin immunoprecipitation experiments indicated that Prmt5 binds to and dimethylates histones at adipogenic promoters. Furthermore, the presence of Prmt5 promoted the binding of ATP-dependent chromatin-remodeling enzymes and was required for the binding of PPARγ2 at PPARγ2-regulated promoters. The data indicate that Prmt5 acts as a coactivator for the activation of adipogenic gene expression and promotes adipogenic differentiation.

Indexed as

Gene Expression3T3-L1 CellsAdipocytesAdipogenesisAnimalsAntigens, DifferentiationCCAAT-Enhancer-Binding ProteinsChromatin Assembly and DisassemblyFibroblastsGene Expression RegulationHistonesIntra-Abdominal FatMethylationMicePPAR gammaPromoter Regions, GeneticAntigens, DifferentiationCCAAT-Enhancer-Binding ProteinsCEBPA protein, mouseHistonesPPAR gammaPrmt5 protein, mouseProtein-Arginine N-MethyltransferasesProtein Methyltransferases

Identifiers

PMID22361822
PMCPMC3327358
OpenAlexW2010630026

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.