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Cited by 121Genomics, phytochemicals, and oxidative stressIron Metabolism and DisordersHeme Oxygenase-1 and Carbon Monoxide

The DOI matches its Crossref record; 74 of the 74 references it cites were found in a registry or an index.

JunD activates transcription of the human ferritin H gene through an antioxidant response element during oxidative stress

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Tsuji, Yoshiaki·2005·Oncogene
DOI 10.1038/sj.onc.1208901PMC PMC2365508
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Abstract

Ferritin is the major intracellular iron storage protein that sequesters excess free iron to minimize generation of iron-catalysed reactive oxygen species. We previously demonstrated that expression of ferritin heavy chain (ferritin H) was induced by pro-oxidants, which is a part of cellular antioxidant response to protect cells from oxidative damage. In this study, we have identified that the antioxidant/electrophile response element (ARE) located 4.5 kb upstream to the human ferritin H transcription initiation site is responsible for the oxidant response. The human ferritin H ARE comprises two copies of bidirectional AP1 motifs. Mutations in each AP1 motif significantly impaired protein binding and the function of the ARE, indicating that both of the AP1 motifs are required for pro-oxidant-mediated activation of the ferritin H gene. We identified that JunD, an AP1 family basic-leucine zipper (bZip) transcription factor, is one of the ferritin H ARE binding proteins and activates ferritin H transcription in HepG2 hepatocarcinoma cells. Gel retardation assay demonstrated that H2O2 (hydrogen peroxide) or t-BHQ (tert-butylhydroquinone) treatment increased total protein binding as well as JunD binding to the ferritin H ARE. Chromatin immunoprecipitation assay showed that H2O2 treatment induced JunD binding to the ferritin H ARE. Both H2O2 and t-BHQ induced phosphorylation of JunD at Ser-100, an activated form of JunD. Furthermore, overexpression of JunD induced endogenous ferritin H protein synthesis. Since JunD has recently been demonstrated to protect cells from several stress stimuli including oxidative stress, these results suggest that, in addition to NFE2-related factor 2 (Nrf2) as a major ARE regulatory protein, JunD is another ARE regulatory protein for transcriptional activation of the human ferritin H gene and probably other antioxidant genes containing the conserved ARE sequences by which JunD may confer cytoprotection during oxidative stress.

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Metadata

Authors
Tsuji, Y.
Affiliations
North Carolina State University (US)
Corresponding author
Tsuji, Yoshiaki
ORCID
Tsuji, Yoshiaki
Venue
Oncogene
Publisher
Springer Science and Business Media LLC
Published
2005-07-11
Volume
24
Issue
51
Pages
7567-7578
ISSN
  • 0950-9232 (ISSN-L)
  • 1476-5594
DOI
10.1038/sj.onc.1208901
PMC
PMC2365508
OpenAlex
W2023470803
Cited by
121
References
74
Citations by year
2026: 1 · 2025: 2 · 2023: 3 · 2022: 6 · 2021: 2 · 2020: 3 · 2019: 2 · 2018: 4 · 2017: 3 · 2016: 10 · 2015: 6 · 2014: 9 · 2013: 9 · 2012: 12
FWCI
3.01
Type
journal article
Language
en
Open access
Licence
Locations
  • Oncogene (publishedVersion)
  • PubMed (publishedVersion)
  • Europe PMC (PubMed Central) (acceptedVersion)
  • PubMed Central (acceptedVersion)
Funders
  • Wake Forest University
  • North Carolina State University
  • National Institute for Health and Care Research
  • National Institutes of Health
  • Wake Forest School of Medicine
  • National Institute of Diabetes and Digestive and Kidney Diseases (DK60007, R01DK060007)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics, phytochemicals, and oxidative stress
  • Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heme Oxygenase-1 and Carbon Monoxide
Keywords
JunD, antioxidant response element, oxidative stress, AP-1 transcription factor, bZIP transcription factors, transcriptional activation, hydrogen peroxide, tert-butylhydroquinone, Nrf2, iron storage, hepatocellular carcinoma cells, cytoprotection
MeSH terms
Antioxidants, Leukemia, Erythroblastic, Acute, Ferritins, Carcinoma, Hepatocellular, Humans, Iron, Liver Neoplasms, Transcription, Genetic, Tumor Cells, Cultured, Proto-Oncogene Proteins c-jun, Oxidative Stress, Transcription Factor AP-1, Protein Isoforms, Response Elements

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