Mechanism of concentration-dependent induction of heme oxygenase-1 by resveratrol in human aortic smooth muscle cells

Juan, Shu Hui; Cheng, Tzu-Hurng; Lin, Han; Chu, Yen Ling; Lee, Wen Sen

doi:10.1016/j.bcp.2004.09.015

Cited by 146 publications

(90 citation statements)

References 29 publications

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“…53,58,59 The present study has only explored the link between biliverdin/hBVR and the p65 (RelA) subunit of the transcription factor, and using the criteria of DNA binding, promoter analysis and protein:protein interaction has identified this subunit as the target of biliverdin/ BVR regulation, wherein biliverdin is the inhibitory factor and BVR tempers the inhibitory action of its substrate. Since NF-jB is also a transcription factor for HO-1 gene regulation, 60 our finding that the product of HO activity inhibits NF-jB while hBVR stimulates it, suggesting the concept of a ''feed-back regulatory cycle.'' Taken together, evidence acquired in this study suggests that despite their having opposite effects on the activity of NF-jB, biliverdin and hBVR, depending on conditions, both could serve beneficial functions in the cell.…”

Section: Discussionmentioning

confidence: 62%

Biliverdin inhibits activation of NF‐κB: Reversal of inhibition by human biliverdin reductase

Gibbs

Maines

2007

Intl Journal of Cancer

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hBVR functions in the cell as a reductase and as a kinase. In the first capacity, it reduces biliverdin, the product of HO activity, to the effective intracellular antioxidant, bilirubin; as a dual-specificity kinase (S/T/Y) it activates the MAPK and IGF/IRK receptor signal transduction pathways. NF-jB and the MAPK pathway are activated by ROS, which results in the activation of stress-inducible genes, including ho-1. Presently, we report on the negative effect of biliverdin on NF-jB activation and the converse effect of hBVR. Biliverdin, in a concentration-and time-dependent manner, inhibited transcriptional activity of NF-jB in HEK293A cells. Nuclear extracts from biliverdin-treated cells show reduced DNA binding of NF-jB in an electromobility shift assay, whereas extracts from cells treated with TNF-a showed enhanced binding. Coimmunoprecipitation data show hBVR binds to the 65 kDa subunit of NF-jB, and that this is dependent on activation by TNF-a. Overexpression of hBVR enhanced both the basal and TNF-amediated activation of NF-jB and also that of the NF-jB-activated iNOS gene. Also, overexpression of hBVR arrested the cell cycle in the G 1 /G 0 phase and reduced the number of cells in S phase. Similar results were observed with MCF-7 cells. Because of the Janus nature of NF-jB activity in the cell and the inhibitory action of biliverdin, the present findings provide a foundation for therapeutic intervention in inflammatory diseases and cancer that may be attained by preventing reduction of biliverdin. On the other hand, by increasing BVR levels beneficial functions of NF-jB might be augmented. ' 2007 Wiley-Liss, Inc.

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Section: Discussionmentioning

confidence: 62%

Biliverdin inhibits activation of NF‐κB: Reversal of inhibition by human biliverdin reductase

Gibbs

Maines

2007

Intl Journal of Cancer

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“…It has recently been shown that another polyphenol, resveratrol, induces HO-1 in human aortic smooth muscle cells only at low concentrations. Induction was dependent on NF-B being activated by low doses but inhibited by higher doses of resveratrol (Juan et al, 2005). Thus, the narrow HO-1-inducing dose range exhibited by curcumin, EGCG, and helenalin may reflect inhibition of NF-B at higher concentrations, possibly coupled with activation at lower doses.…”

Section: Discussionmentioning

confidence: 92%

“…HO-1 can be regulated via various transcription factors, which include AP-1 (via ERK and/or JNK), NF-B (HillKapturczak et al, 2001;Juan et al, 2005) and Nrf2 (Alam et al, 1999Balogun et al, 2003). In human renal proximal tubule cells, HO-1 induction by curcumin is blocked by an inhibitor of IB␣ phosphorylation (Hill-Kapturczak et al, 2001).…”

mentioning

confidence: 99%

“…In human renal proximal tubule cells, HO-1 induction by curcumin is blocked by an inhibitor of IB␣ phosphorylation (Hill-Kapturczak et al, 2001). In human aortic smooth muscle cells, HO-1 is induced by another dietary polyphenol, resveratrol, an effect that is eliminated by inhibitors of NF-B activation or IB␣ phosphorylation (Juan et al, 2005). Deletion of NF-B binding sites on the HO-1 promoter also strongly reduces activity.…”

mentioning

confidence: 99%

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Involvement of Nrf2, p38, B-Raf, and Nuclear Factor-κB, but Not Phosphatidylinositol 3-Kinase, in Induction of Hemeoxygenase-1 by Dietary Polyphenols

Andreadi

Howells²,

Atherfold³

et al. 2005

Mol Pharmacol

196

130

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The highly inducible enzyme, hemeoxygenase-1 (HO-1), metabolizes heme, thereby protecting a variety of cells against oxidative stress and apoptosis. Up-regulation by cancer chemopreventive agents has been reported, but its regulation and function in transformed cells are unclear. We compared induction by two dietary polyphenols, curcumin and epigallocatechin-3-gallate (EGCG), with that by the endogenous substrate hemin in epithelial and endothelial cells and examined the relevance to apoptosis. Curcumin or hemin (20 M) induced HO-1 in breast cells from 5 to 24 h. Curcumin (5-40 M) or hemin (5-100 M) induced HO-1 and nuclear levels of nuclear factor (erythroid-derived 2)-related factor (Nrf2) in a dose-dependent manner. EGCG had no effect in breast cells, but at 30 M, it induced nuclear translocation of Nrf2 and HO-1 expression in B-lymphoblasts. In all cases, induction was inhibited by pretreatment with the phosphatidylinositol 3-kinase (PI3K) inhibitor 2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one (LY294002) or the p38 inhibitor 4-(4-fluorophenyl)-2-(4-methylsulfinylphenyl)-5-(4-pyridyl)1H-imidazole (SB203580). The nuclear factor-B (NF-B)-DNA binding inhibitor helenalin (20 M) also prevented induction. However, wortmannin had no effect, suggesting that PI3K was not involved. Curcumin and hemin also induced nuclear Nrf2 and HO-1 effectively in wild-type mouse embryo fibroblasts (wt MEFs) and in B-Raf Ϫ/Ϫ MEFs but not in Nrf2 Ϫ/Ϫ MEFs. However, EGCG (5-20 M) induced HO-1 only in wt MEFs. Results suggest that signaling through p38 mitogen-activated protein kinase, NF-B, and Nrf2 as well as other unidentified molecules is involved in HO-1 induction by hemin and both polyphenols, but cell-specific factors also play a role, particularly with respect to EGCG. Induction of HO-1 by curcumin, EGCG, or low concentrations (5-10 M) of helenalin did not protect MDA-MB468 breast cells or B-lymphoblasts from apoptosis.

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“…In various models of oxidant stress, it has been reported that resveratrol inhibits the expression and activity of NADPH oxidase, enhances activity of several antioxidant enzymes, including that of the SOD and scavenges reactive oxygen free radicals (ROS) (46). Juan et al reported that resveratrol augments the expression of heme oxygenase-1 (HO-1) in human aortic smooth muscle cells, reducing ROS (47). The effect of resveratrol on lipid peroxidation, NADPH oxidase and xanthine oxidase are also well studied in different models (48,49).…”

Section: R E S E a R C H A R T I C L E M O L M Ementioning

confidence: 99%

Resveratrol Improves Survival and Prolongs Life Following Hemorrhagic Shock

Ayub

Poulose

Raju

2015

Mol Med

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Resveratrol has been shown to potentiate mitochondrial function and extend longevity; however, there is no evidence to support whether resveratrol can improve survival or prolong life following hemorrhagic shock. We sought to determine whether (a) resveratrol can improve survival following hemorrhage and resuscitation and (b) prolong life in the absence of resuscitation. Using a hemorrhagic injury (HI) model in the rat, we describe for the first time that the naturally occurring small molecule, resveratrol, may be an effective adjunct to resuscitation fluid. In a series of three sets of experiments we show that resveratrol administration during resuscitation improves survival following HI (p < 0.05), resveratrol and its synthetic mimic SRT1720 can significantly prolong life in the absence of resuscitation fluid (<30 min versus up to 4 h; p < 0.05), and resveratrol as well as SRT1720 restores left ventricular function following HI. We also found significant changes in the expression level of mitochondria-related transcription factors Ppar-α and Tfam, as well as Pgc-1α in the left ventricular tissues of rats subjected to HI and treated with resveratrol. The results indicate that resveratrol is a strong candidate adjunct to resuscitation following severe hemorrhage.

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Mechanism of concentration-dependent induction of heme oxygenase-1 by resveratrol in human aortic smooth muscle cells

Cited by 146 publications

References 29 publications

Biliverdin inhibits activation of NF‐κB: Reversal of inhibition by human biliverdin reductase

Biliverdin inhibits activation of NF‐κB: Reversal of inhibition by human biliverdin reductase

Involvement of Nrf2, p38, B-Raf, and Nuclear Factor-κB, but Not Phosphatidylinositol 3-Kinase, in Induction of Hemeoxygenase-1 by Dietary Polyphenols

Resveratrol Improves Survival and Prolongs Life Following Hemorrhagic Shock

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