Evidence map›Paper›PMID 20351094›Full record

ArticleThe Journal of biological chemistry2010

Sp1 regulates chromatin looping between an intronic enhancer and distal promoter of the human heme oxygenase-1 gene in renal cells.

Jessy Deshane, Junghyun Kim, Subhashini Bolisetty, Thomas D Hock, Nathalie Hill-Kapturczak, Anupam Agarwal

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

44 citing papers in PubMed, 69 citations in OpenAlex.

  1. Article
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  5. Review
  6. E2F7 drives autotaxin/Enpp2 transcription via chromosome looping: Repression by p53 in murine but not in human carcinomas.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2023
    Article
  7. Article
  8. Human Heme Oxygenase-1 Promoter Activity Is Mediated by Z-DNA Formation.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  9. Article
  10. Article
  11. Induction of Heme Oxygenase-1 by 15d-Prostaglandin JAntioxidants (Basel, Switzerland) · 2022
    Article
  12. Genome-wide screens identify specific drivers of mutantProceedings of the National Academy of Sciences of the United States of America · 2022
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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

6 authors at 1 institution in 1 country.

Jessy DeshaneDepartment of Medicine, Nephrology Research and Training Center, University of Alabama at Birmingham, Birmingham, Alabama 35294, USA.
Junghyun Kim
Subhashini Bolisetty
Thomas D Hock
Nathalie Hill-Kapturczak
Anupam Agarwal
Pediatric Nephrology of Alabama · US

Funding

UAB-UCSD O'Brien Core Center for Acute Kidney Injury ResearchP30DK079337 · NIDDK · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI AGARWAL, ANUPAM · 2008 to 2022
$18.3M
Human Heme Oxygenase-1 Gene Regulation in Renal InjuryR01DK059600 · NIDDK · UNIVERSITY OF FLORIDA · PI AGARWAL, ANUPAM, GEORGE, JAMES F · 2002 to 2019
$4.5M
Cytokine Modulation of Heme Oxygenase-1 in Chronic Kidney Transplant RejectionR01DK075532 · NIDDK · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI AGARWAL, ANUPAM · 2006 to 2010
$1.4M
Heme Oxygenase-1 Gene Expression by TGF-Beta1R01DK071875 · NIDDK · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI AGARWAL, ANUPAM · 2006 to 2008
$638k
NIDDK NIH HHS DK059600NIDDK NIH HHS DK071875NIDDK NIH HHS DK075332NIDDK NIH HHS DK079337NIDDK NIH HHS P30 DK079337NIDDK NIH HHS R01 DK059600NIDDK NIH HHS R01 DK071875NIDDK NIH HHS R01 DK075532
6 · The paper itself

Abstract

HO-1 (heme oxygenase-1) is an inducible microsomal enzyme that catalyzes the degradation of pro-oxidant heme. The goal of this study was to characterize a minimal enhancer region within the human HO-1 gene and delineate its role in modulating HO-1 expression by participation with its promoter elements in renal epithelial cells. Deletion analysis and site-directed mutagenesis identified a 220-bp minimal enhancer in intron 1 of the HO-1 gene, which regulates hemin-mediated HO-1 gene expression. Small interfering RNA, decoy oligonucleotides, site-directed mutagenesis, and chromatin immunoprecipitation assays confirmed the functional interaction of Sp1 with a consensus binding sequence within the 220-bp region. Mutations of regulatory elements within the -4.5 kb promoter region (a cyclic AMP response and a downstream NF-E2/AP-1 element, both located at -4.0 kb, and/or an E-box sequence located at -44 bp) resulted in the loss of enhancer activity. A chromosome conformation capture assay performed in human renal epithelial (HK-2) cells demonstrated hemin-inducible chromatin looping between the intronic enhancer and the -4.0 kb promoter region in a time-dependent manner. Restriction digestion with ApaLI (which cleaves the 220-bp enhancer) led to a loss of stimulus-dependent chromatin looping. Sp1 small interfering RNA and mithramycin A, a Sp1 binding site inhibitor, resulted in loss of the loop formation between the intronic enhancer and the distal HO-1 promoter by the chromosome conformation capture assay. These results provide novel insight into the complex molecular interactions that underlie human HO-1 regulation in renal epithelial cells.

Indexed as

Gene Expression Regulation, EnzymologicApoptosisCell LineChromatinChromatin ImmunoprecipitationEnhancer Elements, GeneticHeme Oxygenase-1HeminHumansKidneyMutagenesisPlasmidsPromoter Regions, GeneticRNA, Small InterferingSp1 Transcription FactorTransfectionChromatinHeme Oxygenase-1HeminRNA, Small InterferingSp1 Transcription Factor

Identifiers

PMID20351094
PMCPMC2878004
OpenAlexW2050345313

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.