NO activates NRF2 expression

Are all these mediated by NRF2 reactive cysteines…or are they mediated by KEAP1 reactive cysteines?nitric oxide nrf2

… or nitric oxide amplifies heme oxygenase-1 induction: involvement of the transcription factor Nrf2.group of 2 »
P Naughton, M Hoque, CJ Green, R Foresti, R … – Cell Mol Biol (Noisy-le-grand), 2002 – ncbi.nlm.nih.gov
Interaction of heme with nitroxyl or nitric oxide amplifies heme
oxygenase-1 induction: involvement of the transcription factor Nrf2.
Cited by 14Related ArticlesCachedWeb SearchImport into EndNoteFind It @ MUBL Direct

Nitric oxide stimulates Nrf2 nuclear translocation in vascular endothelium.Find It @ MUgroup of 3 »
BJ Buckley, ZM Marshall, AR Whorton – Biochem Biophys Res Commun, 2003 – ncbi.nlm.nih.gov
Click here to read Nitric oxide stimulates Nrf2 nuclear translocation in
vascular endothelium. Buckley BJ, Marshall ZM, Whorton AR.
Cited by 12Related ArticlesCachedWeb SearchImport into EndNote

… through the pathway of phosphatidylinositol 3-kinase: The role of nitric oxide synthase in rat …Find It @ MUgroup of 2 »
KW Kang, SH Choi, SG Kim – Nitric Oxide, 2002 – ingentaconnect.com
peroxynitrite plays an essential role in nuclear translocation of Nrf2 and ARE
activation through the pathway of PI3-kinase and that nitric oxide synthase is
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Curcumin activates the haem oxygenase-1 gene via regulation of Nrf2 and the antioxidant-responsive …group of 6 »
E Balogun, M Hoque, P Gong, E Killeen, CJ Green, R … – Biochem J, 2003 – biochemj.org
D., Touchard, C., Boinapally, S., Choi, AM and Cook, JL (1999) Nrf2, a Cap CJ and
Motterlini, R. (1997) Thiol compounds interact with nitric oxide in regulating
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Nitric Oxide-induced Transcriptional Up-regulation of Protective Genes by Nrf 2 via the Antioxidant …Find It @ MUgroup of 6 »
S Dhakshinamoorthy, AG Porter – J Biol Chem, 2004 – jbc.org
1 Nitric oxide-induced transcriptional up-regulation of protective genes by Nrf2
via the antioxidant response element counteracts apoptosis of neuroblastoma
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Interaction of heme with nitroxyl or nitric oxide amplifies heme oxygenase-1 induction: involvement of the transcription factor Nrf2.

Heme oxygenase-1 (HO-1) is a cytoprotective enzyme, the expression of which is highly sensitive to induction by pro-oxidant stimuli including the substrate heme and reactive oxygen species. Conceptually, the perception that HO-1 plays a key role in response to oxidative damage is paralleled by evidence showing high expression of HO-1 in a variety of cell systems challenged with nitric oxide (NO) or NO-derivatives, thus revealing a potential biological function for HO-1 against nitrosative stress. In this study, we report that exposure of cardiac cells to hemin (5-20 microM) in combination with compounds that liberate nitroxyl (HNO/NO-) or release NO significantly potentiates HO-1 mRNA and protein expression leading to a remarkable increase in heme oxygenase activity under both normoxic and hypoxic conditions. The amplification of the heme oxygenase pathway appears to involve a direct interaction between heme and the NO groups, as the ability of both NO(-)- and NO-releasing agents to induce HO-1 is totally lost by their pre-incubation for 1 hr in complete medium prior to cell treatment but is highly preserved by addition of hemin during the preincubation step. In addition, we show that the redox-sensitive transcription factor Nrf2 is highly expressed in the nuclear fraction of cells exposed to the NO- generator and that this effect is totally abolished by the presence of N-acetyl-L-cysteine. Interestingly, the expression of Nrf2 is gradually intensified by treating cells with a combination of the NO- releaser and increasing concentrations of hemin. Thus, a strict parallelism exists between the extent of HO-1 induction and expression of Nrf2 elicited by the heme-NO interaction. We propose that modification of the iron protoporphyrin centers by NO groups to modulate HO-1 expression might be regarded as a molecular switch to maximize heme oxygenase enzymatic activity and consequently mitigate the redox imbalance imposed by oxidative and nitrosative stress.

Nitric oxide stimulates Nrf2 nuclear translocation in vascular endothelium.Find It @ MUgroup of 3 »
BJ Buckley, ZM Marshall, AR Whorton – Biochem Biophys Res Commun, 2003 – ncbi.nlm.nih.gov
Click here to read Nitric oxide stimulates Nrf2 nuclear translocation in
vascular endothelium. Buckley BJ, Marshall ZM, Whorton AR.
Cited by 12Related ArticlesCachedWeb SearchImport into EndNote

Vascular endothelial cells respond to nitric oxide by activating MAPK pathways and upregulating stress-activated proteins such as gamma-glutamylcysteine synthetase (gamma-GCS) and heme oxygenase-1 (HO-1). Since consensus sequences for the antioxidant response element (ARE) are found in the promoters of the gamma-GCS and HO-1 genes, we examined nuclear translocation of Nrf2, a CNC-bZIP protein which binds to and activates the ARE. We found a dramatic increase in Nrf2 nuclear translocation 1-8h following the nitric oxide donor spermine NONOate. Translocation was inhibited by pretreatment of cells with N-acetylcysteine suggesting involvement of an oxidative mechanism in this response. Translocation was also blocked by PD 98059 and SB 203580, inhibitors of ERK and p38 pathways, respectively. In addition to effects on Nrf2 subcellular localization, spermine NONOate increased Nrf2 protein levels by a mechanism which was inhibited by PD 98059. Pretreatment with N-acetylcysteine, PD 98059, and SB 203580 decreased HO-1 upregulation in spermine NONOate-treated cells. These results suggest that ERK and p38 pathways may regulate nitric oxide-mediated adaptive responses in vascular endothelium via translocation of Nrf2 and activation of the ARE.

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