Participation of altered upstream stimulatory factor in the induction of rat heme oxygenase-1 by cadmium

Maeshima, Hirotaka; Sato, Michihiko; Ishikawa, Kazunobu; Katagata, Yohtaro; Yoshida, Tadashi

doi:10.1093/nar/24.15.2959

Cited by 31 publications

(19 citation statements)

References 54 publications

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“…The identity of the Ebox binding protein as USF-1 was established using ChIP analyses, and thus the data suggest that USF-1 may be a target of ROS-induced signaling. Indeed, precedents for the involvement of USF-1 in oxidative stressmediated changes in gene expression have been previously established (4,31). In theory, an interaction between USF-1 and CREB, either directly or indirectly via the interaction with CREB-recruited coactivators, could promote the ROS effect on PGC-1␣ promoter activity leading to the ultimate upregulation of PGC-1␣ mRNA.…”

Section: Discussionmentioning

confidence: 99%

Interactions between ROS and AMP kinase activity in the regulation of PGC-1α transcription in skeletal muscle cells

Irrcher

Ljubicic²,

Hood³

2009

American Journal of Physiology-Cell Physiology

322

271

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Here we examined the effect of H 2O2 on the regulation of PGC-1␣ expression, and its relationship to AMPK activation. We demonstrate that 24 h of exogenous H2O2 treatment increased PGC-1␣ promoter activity and mRNA expression. Both effects were blocked with the addition of N-acetylcysteine, a ROS scavenger. These effects were mediated, in part, via upstream stimulatory factor-1/Ebox DNA binding and involved 1) interactions with downstream sequences and 2) the activation of AMPK. Elevated ROS led to the activation of AMPK, likely via a decline in ATP levels. The activation of AMPK using 5-aminoimidazole-4-carboxamide-1-␤-d-ribofuranoside increased PGC-1␣ promoter activity and mRNA levels but reduced ROS production. Thus the net effect of AMPK activation on PGC-1␣ expression was a result of increased transcriptional activation, counterbalanced by reduced ROS production. The effects of H2O2 on PGC-1␣ expression differed depending on the level of ROS within the cell. Low levels of ROS result in reduced PGC-1␣ mRNA in the absence of an effect on PGC-1␣ promoter activation. In contrast, elevated levels of H2O2 induce PGC-1␣ transcription indirectly, via AMPK activation. These data identify unique interactions between ROS and AMPK activation on the expression of PGC-1␣ in muscle cells. C2C12 cells; mitochondrial biogenesis; muscle gene expression; adenosine 5Ј-monophosphate kinase; upstream stimulatory factor-1; reactive oxygen species; peroxisome proliferator-activated receptor-␥ coactivator-1 protein-␣

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Section: Discussionmentioning

confidence: 99%

Interactions between ROS and AMP kinase activity in the regulation of PGC-1α transcription in skeletal muscle cells

Irrcher

Ljubicic²,

Hood³

2009

American Journal of Physiology-Cell Physiology

322

271

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“…An extended AP-1-like motif (19), dubbed the stress response element (or StRE) and recently shown to interact preferentially with Cap'n'Collar transcription factor family members (4), has also been implicated in signaling to HO-1 transcription by both oxidative stressors and antioxidants (4). Binding of an upstream stimulatory factor to a site immediately upstream (Ϫ51 to Ϫ35 bp) of the HO-1 transcriptional start site has also been implicated in HO-1 gene regulation in response to cadmium (25,35).…”

Section: Discussionmentioning

confidence: 99%

Urea and hypertonicity increase expression of heme oxygenase-1 in murine renal medullary cells

Tian

Bonkovsky

Shibahara

et al. 2001

American Journal of Physiology-Renal Physiology

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First Published August 15, 2001; 10.1152/ajprenal. 00358.2001.—Epithelial cells derived from the mammalian kidney medulla are responsive to urea at the levels of signal transduction and gene regulation. Hybridization of RNA harvested from control- and urea-treated murine inner medullary collecting duct (mIMCD3) cells with a cDNA expression array encoding stress-responsive genes suggested that heme oxygenase (HO)-1 mRNA was upregulated by urea. RNase protection assay confirmed this upregulation; hypertonicity also increased HO-1 mRNA expression but neither hypertonic NaCl nor urea were effective in the nonrenal 3T3 cell line. The effect on HO-1 expression appeared to be transcriptionally mediated on the basis of mRNA half-life studies and reporter gene analyses using the promoters of both human and chicken HO-1. Although urea signaling resembles that of heavy metal signaling in other contexts, the effect of urea on HO-1 transcription was independent of the cadmium response element in this promoter. Urea-inducible HO-1 expression was sensitive to antioxidants but not to scavengers of nitric oxide. Urea also upregulated HO-1 protein expression and pharmacological inhibition of HO-1 action with zinc protoporphyrin-sensitized mIMCD3 cells to the adverse effects of hypertonicity but not to urea. Coupled with the prior observation of others that HO-1 expression increases along the renal corticomedullary gradient, these data suggest that HO-1 expression may comprise an element of the adaptive response to hypertonicity and/or urea in renal epithelial cells.

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“…Annealed oligonucleotides were diluted to 25 ng/l in STE buffer. The 5Ј-end labeling was performed with T4 polynucleotide kinase (Promega) using 25 ng of double-stranded oligonucleotide and 25 Ci of [␥- 32 P]ATP (3000 Ci/ mmol; Amersham Biosciences, Little Chalfont, Buckinghamshire, United Kingdom). The labeled probes were purified using a Sephadex G-25 spin column (Amersham Biosciences).…”

Section: Methodsmentioning

confidence: 99%

“…Among the large variety of putative regulatory sites found in the promoter 5Ј-flanking region of human, rat, mouse, and chicken HO-1 genes (29), most investigations have focused on those that exhibit inducible responses to oxidative signals (30). Several AP-1-binding sites have been shown to be involved in the transcriptional induction of HO-1 by MAPKs, cyclic nucleotides, protein phosphatase inhibitors, and the polyphenol curcumin (31)(32)(33).…”

mentioning

confidence: 99%

Regulation of Heme Oxygenase-1 Expression through the Phosphatidylinositol 3-Kinase/Akt Pathway and the Nrf2 Transcription Factor in Response to the Antioxidant Phytochemical Carnosol

Martı́n

Rojo

Salinas

et al. 2004

Journal of Biological Chemistry

652

427

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The phosphatidylinositol 3-kinase (PI3K)/Akt pathway elicits a survival signal against multiple apoptotic insults. In addition, phase II enzymes such as heme oxygenase-1 (HO-1) protect cells against diverse toxins and oxidative stress. In this work, we describe a link between these defense systems at the level of transcriptional regulation of the antioxidant enzyme HO-1. The herb-derived phenol carnosol induced HO-1 expression at both mRNA and protein levels. Luciferase reporter assays indicated that carnosol targeted the mouse ho1 promoter at two enhancer regions comprising the antioxidant response elements (AREs). Moreover, carnosol increased the nuclear levels of Nrf2, a transcription factor governing AREs. Electrophoretic mobility shift assays and luciferase reporter assays with a dominantnegative Nrf2 mutant indicated that carnosol increased the binding of Nrf2 to ARE and induced Nrf2-dependent activation of the ho1 promoter. While investigating the signaling pathways responsible for HO-1 induction, we observed that carnosol activated the ERK, p38, and JNK pathways as well as the survival pathway driven by PI3K. Inhibition of PI3K reduced the increase in Nrf2 protein levels and activation of the ho1 promoter. Expression of active PI3K-CAAX (where A is aliphatic amino acid) was sufficient to activate AREs. The use of dominant-negative mutants of protein kinase C and Akt1, two kinases downstream from PI3K, demonstrated a requirement for active Akt1, but not protein kinase C. Moreover, the long-term antioxidant effect of carnosol was partially blocked by PI3K or HO-1 inhibitors, further demonstrating that carnosol attenuates oxidative stress through a pathway that involves PI3K and HO-1.High levels of reactive oxygen species cause damage to cells and are involved in several human pathologies, including neurodegenerative disorders and cancer (1, 2). Therefore, the use of compounds with antioxidant properties may help prevent or alleviate diseases in which oxidative stress is a primary cause (3). Carnosol, a diterpene derived from the herb rosemary, is a representative member of a family of plant-derived phenols, which also include curcumin, carnosic acid, phenylethyl isothiocyanate, epigallocatechin gallate, and other green tea polyphenols. These bioactive phytochemicals exhibit Michael acceptor function and therefore behave as antioxidants (4). In addition, being themselves xenobiotic compounds, they activate a xenobiotic response in the target cells affecting the expression of phase II enzymes such as NAD(P)H:quinone oxidoreductase, aldoketoreductase, glutathione S-transferase, ␥-glutamylcysteine synthetase, glutathione synthetase, and heme oxygenase-1 (HO-1) 1 (5-7). Heme oxygenase isozymes (HO-1 and HO-2) catalyze the stepwise degradation of heme to release free iron and equimolar concentrations of carbon monoxide and the linear tetrapyrrole biliverdin, which is converted to bilirubin by the enzyme biliverdin reductase (8). The HO-1 isozyme is a phase II enzyme that is transcriptionally regulated by a large...

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Participation of altered upstream stimulatory factor in the induction of rat heme oxygenase-1 by cadmium

Cited by 31 publications

References 54 publications

Interactions between ROS and AMP kinase activity in the regulation of PGC-1α transcription in skeletal muscle cells

Interactions between ROS and AMP kinase activity in the regulation of PGC-1α transcription in skeletal muscle cells

Urea and hypertonicity increase expression of heme oxygenase-1 in murine renal medullary cells

Regulation of Heme Oxygenase-1 Expression through the Phosphatidylinositol 3-Kinase/Akt Pathway and the Nrf2 Transcription Factor in Response to the Antioxidant Phytochemical Carnosol

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