Multiple basic-leucine zipper proteins regulate induction of the mouse heme oxygenase-1 gene by arsenite

Gong, Peng; Stewart, Daniel P.; Hu, Bin; Vinson, Charles; Alam, Jawed

doi:10.1016/s0003-9861(02)00404-6

Cited by 56 publications

(59 citation statements)

References 40 publications

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“…This increase in HO-1 expression was suppressed by about 60% at 16 and 24 h when cells were pretreated with BVR siRNA. The finding that siBVR did not completely block the induction of HO-1 by arsenite is consistent with the reported involvement of a number of transcription factors in the induction of HO-1 that are activated by arsenite (44) and indicate that BVR is not the sole transcription factor for the HO-1 response to arsenite. Furthermore, the finding that BVR siRNA in the absence of arsenite exposure did not significantly affect basal levels of HO-1 suggests that BVR influences arsenite-driven HO-1 induction.…”

Section: Arsenite-mediated Increase In Bvr Activity Is Not Accompaniesupporting

confidence: 88%

“…BVR is a member of the "leucine zipper" (bZip) family of mammalian and yeast transcription factors that include c-Fos, c-Jun, ATF-2/CREB, Bach 1, P45, NrF2 and -3, (bZip), sYAP, GCN 4 , and c-Myc (23)(24)(25)(26)(27)(28)(29)(30)(31)(32); the reductase in a homodimeric form binds to the 7-and 8-bp AP-1 and cAMP target genes, among them being ATF-2/CREB and c-jun (33). Arsenite is a reported regulator of bZip factors (44). BVR being a bZip transcription factor and activator of HO-1 could be among the list genes that are modulated by arsenite treatment.…”

mentioning

confidence: 99%

“…HO-1 and genes that are involved in apoptosis are among the targets for arsenite (9,(41)(42)(43)(44)(45). Arsenite activation and increased binding of a complex of proteins, which includes the Jun protein, to the CRE/AP-1 site of the HO-1 promoter are essential for stress response of the oxygenase to this stimulus as well as to other oxidants.…”

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confidence: 99%

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Small Interference RNA-mediated Gene Silencing of Human Biliverdin Reductase, but Not That of Heme Oxygenase-1, Attenuates Arsenite-mediated Induction of the Oxygenase and Increases Apoptosis in 293A Kidney Cells

Miralem

Torno

et al. 2005

Journal of Biological Chemistry

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BVR reduces biliverdin, the HO-1 and HO-2 product, to bilirubin. Human biliverdin (BVR) is a serine/threonine kinase activated by free radicals. It is a leucine zipper (bZip) DNA-binding protein and a regulatory factor for 8/7-bp AP-1-regulated genes, including HO-1 and ATF-2/CREB. Presently, small interference (si) RNA constructs were used to investigate the role of human BVR in sodium arsenite (

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Section: Arsenite-mediated Increase In Bvr Activity Is Not Accompaniesupporting

confidence: 88%

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confidence: 99%

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Small Interference RNA-mediated Gene Silencing of Human Biliverdin Reductase, but Not That of Heme Oxygenase-1, Attenuates Arsenite-mediated Induction of the Oxygenase and Increases Apoptosis in 293A Kidney Cells

Miralem

Torno

et al. 2005

Journal of Biological Chemistry

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“…ATF2 also binds to other promoter sequences on its target genes, including the interferon (IFN)-c promoter (i.e. 59-AAAACTTGTGAAAAT-ACGTAATCCT-39), the stress-response elements (StREs; 59-T/CGCTGAGTCA-39) and UV response elements (URE; 59-TGACAACA-39) (Gong et al, 2002;Lopez-Bergami et al, 2010;Ronai et al, 1998;van Dam and Castellazzi, 2001). Binding of ATF2-AP-1 dimers to DNA alters the local structure of DNA and facilitates the recruitment and directional orientation of other regulatory transcriptional complexes, which either enhance (i.e.…”

Section: Nuclear Functions Of Atf2mentioning

confidence: 99%

ATF2 – at the crossroad of nuclear and cytosolic functions

Lau

Ronai

2012

Journal of Cell Science

100

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SummaryAn increasing number of transcription factors have been shown to elicit oncogenic and tumor suppressor activities, depending on the tissue and cell context. Activating transcription factor 2 (ATF2; also known as cAMP-dependent transcription factor ATF-2) has oncogenic activities in melanoma and tumor suppressor activities in non-malignant skin tumors and breast cancer. Recent work has shown that the opposing functions of ATF2 are associated with its subcellular localization. In the nucleus, ATF2 contributes to global transcription and the DNA damage response, in addition to specific transcriptional activities that are related to cell development, proliferation and death. ATF2 can also translocate to the cytosol, primarily following exposure to severe genotoxic stress, where it impairs mitochondrial membrane potential and promotes mitochondrial-based cell death. Notably, phosphorylation of ATF2 by the epsilon isoform of protein kinase C (PKCe) is the master switch that controls its subcellular localization and function. Here, we summarize our current understanding of the regulation and function of ATF2 in both subcellular compartments. This mechanism of control of a non-genetically modified transcription factor represents a novel paradigm for 'oncogene addiction'.

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“…One of the adaptive responses to arsenic-induced oxidative stress is induction of haem oxygenase-1 (HMOX1), a rate-limiting enzyme of bilirubin (BR) biosynthesis (Gong et al, 2002;Maines, 1988). Bilirubin is a potent scavenger of ROS and its production, particularly in situation where cellular antioxidant capacity is reduced, is suggested to be a part of the cellular defence against oxidative stress (Gozzelino et al, 2010;Stocker et al, 1987).…”

Section: Introductionmentioning

confidence: 99%

Urinary excretion of bilirubin oxidative metabolites in arsenite-treated mice

Arthur

Lang

et al. 2012

J. Toxicol. Sci.

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Recently, two novel dipyrroles with m/z values 333 and 315 have been identified in vitro (Abu-Bakar et al., 2011;De Matteis et al., 2006) but their presence in biological samples has yet to be determined. In the present study, we measured urinary excretion of dipyrrolic BOMs, as stress markers in mice treated with sodium arsenite. MATERIALS AND METHODS Chemicals and AntibodiesSodium arsenite (iAsIII)) was purchased from Unilab ABSTRACT -Human exposure to inorganic arsenic (iAsIII), a potent oxidative stressor, causes liver injuries, which can lead to cancer. It is known that induction of haem oxygenase-1 (HMOX1) reduces arsenite-induced cytotoxicity in the liver. In a two-step reaction HMOX1 generates BR from haem and BR, in turn is oxidised to its oxidative metabolites by radical oxygen species (ROS). Bilirubin oxidative metabolites (BOMs), such as tripyrroles and propentdyopent have been identified and measured in rat and human urine. Additionally, two novel dipyrroles (with m/z values 333 and 315) have recently been identified in vitro (Abu-Bakar et al. (2011). Toxicol. Appl. Pharmacol., 257, 14-22) but their presence in biological samples has yet to be demonstrated. The aim of the present study was to identify the novel dipyrroles in urine of control and iAsIII treated mice. Acute iAsIII exposure generated transient oxidative stress in the liver, which associated with temporal induction of hepatic HMOX1, the rate-limiting enzyme of BR biosynthesis. The increase in the total BR levels was modest compared to the strong induction of HMOX1. Additionally, urinary dipyrroles (m/z values 333 and 315) escalated after iAsIII exposure. The results suggest that dipyrrolic BOMs can be used as marker for oxidative stress.

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Multiple basic-leucine zipper proteins regulate induction of the mouse heme oxygenase-1 gene by arsenite

Cited by 56 publications

References 40 publications

Small Interference RNA-mediated Gene Silencing of Human Biliverdin Reductase, but Not That of Heme Oxygenase-1, Attenuates Arsenite-mediated Induction of the Oxygenase and Increases Apoptosis in 293A Kidney Cells

Small Interference RNA-mediated Gene Silencing of Human Biliverdin Reductase, but Not That of Heme Oxygenase-1, Attenuates Arsenite-mediated Induction of the Oxygenase and Increases Apoptosis in 293A Kidney Cells

ATF2 – at the crossroad of nuclear and cytosolic functions

Urinary excretion of bilirubin oxidative metabolites in arsenite-treated mice

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