Evidence map›Paper›PMID 24140708›Full record

ArticleFree radical biology & medicine2014

Poly(ADP-ribose) polymerase-1 modulates Nrf2-dependent transcription.

Tongde Wu, Xiao-Jun Wang, Wang Tian, Melba C Jaramillo, Alexandria Lau, Donna D Zhang

Open access · greenAbstract read
In one paragraph

Article in Free radical biology & medicine, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
1.4field-weighted citation impact, top 19% 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

32 citing papers in PubMed, 48 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

6 authors at 1 institution in 1 country.

Tongde WuDepartment of Pharmacology & Toxicology, College of Pharmacy, University of Arizona, Tucson, AZ 85721, USA.
Xiao-Jun WangDepartment of Pharmacology & Toxicology, College of Pharmacy, University of Arizona, Tucson, AZ 85721, USA.
Wang TianDepartment of Pharmacology & Toxicology, College of Pharmacy, University of Arizona, Tucson, AZ 85721, USA.
Melba C JaramilloDepartment of Pharmacology & Toxicology, College of Pharmacy, University of Arizona, Tucson, AZ 85721, USA.
Alexandria LauDepartment of Pharmacology & Toxicology, College of Pharmacy, University of Arizona, Tucson, AZ 85721, USA.
Donna D ZhangDepartment of Pharmacology & Toxicology, College of Pharmacy, University of Arizona, Tucson, AZ 85721, USA; Arizona Cancer Center, University of Arizona, Tucson, AZ 85724, USA. Electronic address: dzhang@pharmacy.arizona.edu.
University of Arizona · US

Funding

SOUTHWEST ENVIRONMENTAL HEALTH SCIENCES CENTERP30ES006694 · NIEHS · UNIVERSITY OF ARIZONA · PI DEAN BILLHEIMER · 1994 to 2026
$36.7M
Training in Environmental Toxicology of Human DiseaseT32ES007091 · NIEHS · UNIVERSITY OF ARIZONA · PI Nathan J Cherrington · 1985 to 2026
$10.7M
The protective role of Nrf2 in arsenic-induced toxicity and carcinogenicityR01ES015010 · NIEHS · UNIVERSITY OF ARIZONA · PI ZHANG, DONNA D · 2006 to 2015
$3.4M
Investigation of an anti-cancer phytochemical targeting Nrf2R01CA154377 · NCI · UNIVERSITY OF ARIZONA · PI ZHANG, DONNA D · 2011 to 2015
$1.5M
NCI NIH HHS R01 CA154377NCI NIH HHS R01CA154377NIEHS NIH HHS ES015010NIEHS NIH HHS P30 ES006694NIEHS NIH HHS P30ES006694NIEHS NIH HHS R01 ES015010NIEHS NIH HHS T32 ES007091
6 · The paper itself

Abstract

The basic leucine zipper transcription factor Nrf2 has emerged as a master regulator of intracellular redox homeostasis by controlling the expression of a battery of redox-balancing antioxidants and phase II detoxification enzymes. Under oxidative stress conditions, Nrf2 is induced at the protein level through redox-sensitive modifications on critical cysteine residues in Keap1, a component of an E3 ubiquitin ligase complex that targets Nrf2 for proteasomal degradation. Poly(ADP-ribose) polymerase-1 (PARP-1) is historically known to function in DNA damage detection and repair; however, recently PARP-1 has been shown to play an important role in other biochemical activities, such as DNA methylation and imprinting, insulator activity, chromosome organization, and transcriptional regulation. The exact role of PARP-1 in transcription modulation and the underlying mechanisms remain poorly defined. In this study, we report that PARP-1 forms complexes with the antioxidant response element (ARE) within the promoter region of Nrf2 target genes and upregulates the transcriptional activity of Nrf2. Interestingly, PARP-1 neither physically interacts with Nrf2 nor promotes the expression of Nrf2. In addition, PARP-1 does not target Nrf2 for poly(ADP-ribosyl)ation. Instead, PARP-1 interacts directly with small Maf proteins and the ARE of Nrf2 target genes, which augments ARE-specific DNA-binding of Nrf2 and enhances the transcription of Nrf2 target genes. Collectively, these results suggest that PARP-1 serves as a transcriptional coactivator, upregulating the transcriptional activity of Nrf2 by enhancing the interaction among Nrf2, MafG, and the ARE.

Indexed as

Transcription, GeneticAnimalsAntioxidant Response ElementsCell Line, TumorFibroblastsGene Expression RegulationHumansMafG Transcription FactorMiceNF-E2-Related Factor 2Oxidation-ReductionPoly (ADP-Ribose) Polymerase-1Poly(ADP-ribose) PolymerasesPromoter Regions, GeneticProtein BindingRepressor ProteinsMAFG protein, humanMafG Transcription FactorNFE2L2 protein, humanNF-E2-Related Factor 2PARP1 protein, humanPoly (ADP-Ribose) Polymerase-1Poly(ADP-ribose) PolymerasesRepressor ProteinsAREFree radicalsMafNrf2PARP-1Transcriptional coactivator

Identifiers

PMID24140708
PMCPMC3945083
OpenAlexW2025229552

What OpenQuestion holds

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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.