Tumor Promoter Arsenite Stimulates Histone H3 Phosphoacetylation of Proto-oncogenes c-fos and c-jun Chromatin in Human Diploid Fibroblasts

Li, Ji; Gorospe, Myriam; Barnes, Janice; Liu, Yusen

doi:10.1074/jbc.m300269200

Cited by 95 publications

(64 citation statements)

References 49 publications

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“…Moreover, several reports found coincidence of MAPK-dependent phosphorylation of histone H3 at Ser 10 and acetylation of histone H3 at Lys 14 at the gene promoters of fos and others and the expression of these genes (35,36). Some evidence has been provided that H3 phosphorylation at Ser 10 may have a role in the regulation of transcription by acting as a signal for subsequent acetylation of lysines and, in particular, histone H3 Lys 14 (37)(38)(39).…”

Section: Discussionmentioning

confidence: 99%

“…Therefore, Listeria-activated MAPKs might phosphorylate H3 directly at the il8 gene promoter. However, several other kinases including ribosomal S6 kinase-2 (51) and mitogen-and stress-activated protein kinase-1 (35), which are nuclear effectors of p38 MAPK and ERK1/2, have been implicated in H3 phosphorylation at Ser 10 , although results are somewhat controversial (52).…”

Section: Discussionmentioning

confidence: 99%

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Intracellular Bacteria Differentially Regulated Endothelial Cytokine Release by MAPK-Dependent Histone Modification

Schmeck¹,

Beermann²,

Laak³

et al. 2005

The Journal of Immunology

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Epigenetic histone modifications contribute to the regulation of eukaryotic gene transcription. The role of epigenetic regulation in immunity to intracellular pathogens is poorly understood. We tested the hypothesis that epigenetic histone modifications influence cytokine expression by intracellular bacteria. Intracellular Listeria monocytogenes, but not noninvasive Listeria innocua, induced release of distinct CC and CXC chemokines, as well as Th1 and Th2 cytokines and growth factors by endothelial cells. Cytokine expression was in part dependent on p38 MAPK and MEK1. We analyzed global histone modification and modifications in detail at the gene promoter of IL-8, which depended on both kinase pathways, and of IFN-γ, which was not blocked by kinase inhibition. Intracellular Listeria induced time-dependent acetylation (lysine 8) of histone H4 and phosphorylation/acetylation (serine 10/lysine 14) of histone H3 globally and at the il8 promoter in HUVEC, as well as recruitment of the histone acetylase CREB-binding protein. Inhibitors of p38 MAPK and MEK1 reduced lysine 8 acetylation of histone H4 and serine 10/lysine 14 phosphorylation/acetylation of histone H3 in Listeria-infected endothelial cells and disappearance of histone deacetylase 1 at the il8 promoter in HUVEC. In contrast, IFN-γ gene transcription was activated by Listeria monocytogenes independent of p38 MAPK and MEK1, and histone phosphorylation/acetylation remained unchanged in infected cells at the IFN-γ promoter. Specific inhibition of histone deacetylases by trichostatin A increased Listeria-induced expression of IL-8, but not of IFN-γ, underlining the specific physiological impact of histone acetylation. In conclusion, MAPK-dependent epigenetic modifications differentially contributed to L. monocytogenes-induced cytokine expression by human endothelial cells.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Intracellular Bacteria Differentially Regulated Endothelial Cytokine Release by MAPK-Dependent Histone Modification

Schmeck¹,

Beermann²,

Laak³

et al. 2005

The Journal of Immunology

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“…These oxidative effects of As 2 O 3 result in the disruption of key signal transduction pathways, leading to the induction of apoptosis (Li et al, 2002). Indeed, As 2 O 3 activates the MAPK signaling pathways (Cavigelli et al, 1996;Meriin et al, 1999;Verma et al, 2002) and therefore induces the phosphorylation of a subset of transcription factors (AP-1, Elk, ATF2, CREB and others) (Bebien et al, 2003), PML (Hayakawa and Privalsky, 2004) and histones (Li et al, 2002(Li et al, , 2003aHe et al, 2003). This leads to the increased transcription of critical apoptosisand proliferation-associated genes including among others, the proto-oncogenes c-fos, c-jun and Egr-1 (Lim et al, 1998;Bernstam and Nriagu, 2000;Liu et al, 2003) and caspases (Li et al, 2002).…”

Section: Introductionmentioning

confidence: 99%

Retinoic acid and arsenic trioxide cooperate for apoptosis through phosphorylated RXR alpha

et al. 2005

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Arsenite trioxide (As 2 O 3 ) induces apoptosis in several cell lines by disturbing key signal transduction pathways through its oxidative properties. Here, we report that As 2 O 3 also induces the phosphorylation of the retinoid receptor RXRa, subsequent to oxidative damages and the activation of the stress-activated protein kinases cascade (JNKs). We also report that RA amplifies both As 2 O 3 -induced phosphorylation of RXRa and apoptosis. Taking advantage of 'rescue' F9 cell lines expressing RXRa mutated at its phosphorylation sites, in an RXRa null background, we provide evidence that RXRa is a key element involved in that potentiating effect. Finally, we demonstrate that As 2 O 3 also abrogates the transactivation of RA-target genes.

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“…Aberrant expressed genes can be classified into many categories such as stress response genes, hormone-related genes, cytokines, apoptotic genes, cell cycle regulatory genes, proteolytic genes, and proto-oncogenes (Kitchin, 2001;Yih et al, 2002;Zheng et al, 2003;Chen et al, 2004). In particular, genes important in controlling cell proliferation and transformation are aberrantly expressed during the arsenic-induce carcinogenesis (Shimizu et al, 1998;Chen et al, 2001;Hamadeh et al, 2002;Li et al, 2003;Liu et al, 2004;Benbrahim-Tallaa et al, 2005).…”

Section: Introductionmentioning

confidence: 99%

Activation of Nrf2 by arsenite and monomethylarsonous acid is independent of Keap1-C151: enhanced Keap1–Cul3 interaction

Wang

Sun

Chen

et al. 2008

Toxicology and Applied Pharmacology

127

101

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Drinking water contaminated with arsenic, a human carcinogen, is a worldwide health issue. An understanding of cellular signaling events in response to arsenic exposure and rational designing of strategies to reduce arsenic damages by modulating signaling events are important to fight against arsenic-induced diseases. Previously, we reported that activation of the Nrf2-mediated cellular defense pathway confers protection against toxic effects induced by sodium arsenite [As(III)] or monomethylarsonous acid [MMA(III)]. Paradoxically, arsenic has been reported to induce the Nrf2-dependent signaling pathway. Here, we report the unique mechanism of Nrf2 induction by arsenic. Similar to tert-butylhydroquinone (tBHQ) or sulforaphane (SF), arsenic induced the Nrf2-dependent response through enhancing Nrf2 protein levels by inhibiting Nrf2 ubiquitination and degradation. However, the detailed action of arsenic in Nrf2 induction is different from that of tBHQ or SF. Arsenic markedly enhanced the interaction between Keap1 and Cul3, subunits of the E3 ubiquitin ligase for Nrf2, which led to impaired dynamic assembly/disassembly of the E3 ubiquitin ligase and thus decreased its ligase activity. Furthermore, induction of Nrf2 by arsenic is independent of the previously identified C151 residue in Keap1 that is required for Nrf2 activation by tBHQ or SF. Distinct mechanisms of Nrf2 activation by seemingly harmful and beneficial reagents provide a molecular basis to design Nrf2-activating agents for therapeutic intervention.

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Tumor Promoter Arsenite Stimulates Histone H3 Phosphoacetylation of Proto-oncogenes c-fos and c-jun Chromatin in Human Diploid Fibroblasts

Cited by 95 publications

References 49 publications

Intracellular Bacteria Differentially Regulated Endothelial Cytokine Release by MAPK-Dependent Histone Modification

Intracellular Bacteria Differentially Regulated Endothelial Cytokine Release by MAPK-Dependent Histone Modification

Retinoic acid and arsenic trioxide cooperate for apoptosis through phosphorylated RXR alpha

Activation of Nrf2 by arsenite and monomethylarsonous acid is independent of Keap1-C151: enhanced Keap1–Cul3 interaction

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