Evidence map›Paper›PMID 24451378›Full record

ArticleThe Journal of biological chemistry2014

Histone deacetylase inhibitors modulate the transcriptional regulation of guanylyl cyclase/natriuretic peptide receptor-a gene: interactive roles of modified histones, histone acetyltransferase, p300, AND Sp1.

Prerna Kumar, Satyabha Tripathi, Kailash N Pandey

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

29 citing papers in PubMed, 45 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

3 authors at 1 institution in 1 country.

Prerna KumarDepartment of Physiology, Tulane University Health Sciences Center, School of Medicine, New Orleans, Louisiana 70112.
Satyabha TripathiDepartment of Physiology, Tulane University Health Sciences Center, School of Medicine, New Orleans, Louisiana 70112.
Kailash N PandeyDepartment of Physiology, Tulane University Health Sciences Center, School of Medicine, New Orleans, Louisiana 70112. Electronic address: kpandey@tulane.edu.
Tulane University · US

Funding

Translational Research in Hypertension and Renal BiologyP30GM103337 · NIGMS · TULANE UNIVERSITY OF LOUISIANA · PI NAVAR, LUIS GABRIEL · 2012 to 2016
$5.8M
ANP RECEPTOR--MOLECULAR APPROACH OF SIGNALING MECHANISMSR01HL057531 · NHLBI · TULANE UNIVERSITY OF LOUISIANA · PI PANDEY, KAILASH N · 1997 to 2013
$2.5M
ANP Receptor: Molecular approach of signaling mechanismsR56HL057531 · NHLBI · TULANE UNIVERSITY OF LOUISIANA · PI PANDEY, KAILASH N · 2009 to 2009
$373k
NHLBI NIH HHS HL 57531NHLBI NIH HHS R01 HL057531NHLBI NIH HHS R56 HL057531NIGMS NIH HHS P30 GM103337
6 · The paper itself

Abstract

Atrial natriuretic peptide (ANP) binds guanylyl cyclase-A/natriuretic peptide receptor-A (GC-A/NPRA) and produces the intracellular second messenger, cGMP, which regulates cardiovascular homeostasis. We sought to determine the function of histone deacetylases (HDACs) in regulating Npr1 (coding for GC-A/NPRA) gene transcription, using primary mouse mesangial cells treated with class-specific HDAC inhibitors (HDACi). Trichostatin A, a pan inhibitor, and mocetinostat (MGCD0103), a class I HDAC inhibitor, significantly enhanced Npr1 promoter activity (by 8- and 10-fold, respectively), mRNA levels (4- and 5.3-fold, respectively), and NPRA protein (2.7- and 3.5-fold, respectively). However, MC1568 (class II HDAC inhibitor) had no discernible effect. Overexpression of HDAC1 and HDAC2 significantly attenuated Npr1 promoter activity, whereas HDAC3 and HDAC8 had no effect. HDACi-treated cultured cells in vitro and intact animals in vivo showed significantly reduced binding of HDAC1 and -2 and increased accumulation of acetylated H3-K9/14 and H4-K12 at the Npr1 promoter. Deletional analyses of the Npr1 promoter along with ectopic overexpression and inhibition of Sp1 confirmed that HDACi-induced Npr1 gene transcription is accomplished by Sp1 activation. Furthermore, HDACi attenuated the interaction of Sp1 with HDAC1/2 and promoted Sp1 association with p300 and p300/cAMP-binding protein-associated factor; it also promoted the recruitment of p300 and p300/cAMP-binding protein-associated factor to the Npr1 promoter. Our results demonstrate that trichostatin A and MGCD0103 enhanced Npr1 gene expression through inhibition of HDAC1/2 and increased both acetylation of histones (H3-K9/14, H4-K12) and Sp1 by p300, and their recruitment to Npr1 promoter. Our findings define a novel epigenetic regulatory mechanism that governs Npr1 gene transcription.

Indexed as

Epigenesis, GeneticAnimalsBenzamidesCell LineGlomerular MesangiumHistone AcetyltransferasesHistone Deacetylase InhibitorsHistone DeacetylasesHistonesHydroxamic AcidsMicep300-CBP-Associated Factorp300-CBP Transcription FactorsPromoter Regions, GeneticPyrimidinesReceptors, Atrial Natriuretic Factoratrial natriuretic factor receptor ABenzamidesHistone AcetyltransferasesHistone Deacetylase InhibitorsHistone DeacetylasesHistonesHydroxamic Acidsmocetinostatp300-CBP-Associated Factorp300-CBP Transcription FactorsPyrimidinesReceptors, Atrial Natriuretic FactorSp1 Transcription Factortrichostatin AChromatin Histone ModificationGene TranscriptionHistone Deacetylase InhibitorsNatriuretic Peptidesp300Sp1

Identifiers

PMID24451378
PMCPMC3945360
OpenAlexW2071383476

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.