Evidence map›Paper›PMID 21680747›Full record

ArticleThe Journal of biological chemistry2011

Histone deacetylase 9 is a negative regulator of adipogenic differentiation.

Tapan K Chatterjee, Gila Idelman, Victor Blanco, Andra L Blomkalns, Mark G Piegore, Daniel S Weintraub, Santosh Kumar, Srinivas Rajsheker, David Manka, Steven M Rudich and 7 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 84 papers.

0numbers the graph read from it
0cells of the map it votes in
84citing papers in PubMed
4.1field-weighted citation impact, top 5% 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

84 citing papers in PubMed, 146 citations in OpenAlex.

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24 more citing papers are in PubMed but not listed here.

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

17 authors at 2 institutions in 1 country.

Tapan K ChatterjeeDepartment of Internal Medicine, Division of Cardiovascular Diseases, University of Cincinnati, Cincinnati, Ohio 45267, USA. tapan.chatterjee@uc.edu
Gila Idelman
Victor Blanco
Andra L Blomkalns
Mark G Piegore
Daniel S Weintraub
Santosh Kumar
Srinivas Rajsheker
David Manka
Steven M Rudich
Yaoliang Tang
David Y Hui
Rhonda Bassel-Duby
Eric N Olson
Jerry B Lingrel
Shuk-Mei Ho
Neal L Weintraub
University of Cincinnati · USThe University of Texas Southwestern Medical Center · US

Funding

Vascular Protection During HypertensionP01HL062984 · NHLBI · UNIVERSITY OF IOWA · PI SIGMUND, CURT DANIEL · 2000 to 2015
$22.2M
Angiotensin II, oxidative stress, and aneurysm formationR01HL076684 · NHLBI · UNIVERSITY OF IOWA · PI WEINTRAUB, NEAL L · 2005 to 2013
$3.0M
Susceptible Window of High Fat Diet/Bisphenol A Programming of Breast Cancer RiskU01ES019480 · NIEHS · UNIVERSITY OF CINCINNATI · PI HO, SHUK-MEI · 2010 to 2014
$2.2M
NHLBI NIH HHS HL076684NHLBI NIH HHS HL62984NHLBI NIH HHS P01 HL062984NHLBI NIH HHS R01 HL076684NIEHS NIH HHS ES019480NIEHS NIH HHS U01 ES019480
6 · The paper itself

Abstract

Differentiation of preadipocytes into mature adipocytes capable of efficiently storing lipids is an important regulatory mechanism in obesity. Here, we examined the involvement of histone deacetylases (HDACs) and histone acetyltransferases (HATs) in the regulation of adipogenesis. We find that among the various members of the HDAC and HAT families, only HDAC9 exhibited dramatic down-regulation preceding adipogenic differentiation. Preadipocytes from HDAC9 gene knock-out mice exhibited accelerated adipogenic differentiation, whereas HDAC9 overexpression in 3T3-L1 preadipocytes suppressed adipogenic differentiation, demonstrating its direct role as a negative regulator of adipogenesis. HDAC9 expression was higher in visceral as compared with subcutaneous preadipocytes, negatively correlating with their potential to undergo adipogenic differentiation in vitro. HDAC9 localized in the nucleus, and its negative regulation of adipogenesis segregates with the N-terminal nuclear targeting domain, whereas the C-terminal deacetylase domain is dispensable for this function. HDAC9 co-precipitates with USF1 and is recruited with USF1 at the E-box region of the C/EBPα gene promoter in preadipocytes. Upon induction of adipogenic differentiation, HDAC9 is down-regulated, leading to its dissociation from the USF1 complex, whereas p300 HAT is up-regulated to allow its association with USF1 and accumulation at the E-box site of the C/EBPα promoter in differentiated adipocytes. This reciprocal regulation of HDAC9 and p300 HAT in the USF1 complex is associated with increased C/EBPα expression, a master regulator of adipogenic differentiation. These findings provide new insights into mechanisms of adipogenic differentiation and document a critical regulatory role for HDAC9 in adipogenic differentiation through a deacetylase-independent mechanism.

Indexed as

3T3-L1 CellsAdipose TissueAnimalsCell DifferentiationDown-RegulationHistone DeacetylasesImmunoprecipitationMaleMiceMice, Inbred C57BLMice, KnockoutPolymerase Chain ReactionRepressor ProteinsRNA, MessengerHdac9 protein, mouseHistone DeacetylasesRepressor ProteinsRNA, Messenger

Identifiers

PMID21680747
PMCPMC3149373
OpenAlexW1965417249

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.