Effect of β-naphthoflavone on AhR-regulated genes (CYP1A1, 1A2, 1B1, 2S1, Nrf2, and GST) and antioxidant enzymes in various brain regions of pig

Nannelli, Annalisa; Rossignolo, Francesco; Tolando, Roberto; Rossato, Paolo; Longo, Vincenzo; Gervasi, Pier Giovanni

doi:10.1016/j.tox.2009.09.010

Cited by 46 publications

(30 citation statements)

References 67 publications

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“…Since the dealkylating activity of CYP1A1 is well-known for ethoxylated substrates [114,115,156], NAS formation from melatonin seems likely for this isoenzyme, too. In addition to other CYPs not related to melatonin metabolism, CYP1A2 [60,88,126], CYP1A1 [60,88], CYP1B1 [79,88], and CYP2C19 [58,59,159] are also expressed in the brain. The presence of these CYP isoenzymes indicates that, at least, a certain fraction of melatonin should be either 6-hydroxylated or O-demethylated in the CNS (Fig.…”

Section: Cytochrome P 450 Metabolismmentioning

confidence: 99%

Melatonin Metabolism in the Central Nervous System

Hardeland¹

2010

111

110

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Abstract:The metabolism of melatonin in the central nervous system is of interest for several reasons. Melatonin enters the brain either via the pineal recess or by uptake from the blood. It has been assumed to be also formed in some brain areas. Neuroprotection by melatonin has been demonstrated in numerous model systems, and various attempts have been undertaken to counteract neurodegeneration by melatonin treatment. Several concurrent pathways lead to different products. Cytochrome P 450 subforms have been demonstrated in the brain. They either demethylate melatonin to Nacetylserotonin, or produce 6-hydroxymelatonin, which is mostly sulfated already in the CNS. Melatonin is deacetylated, at least in pineal gland and retina, to 5-methoxytryptamine. N 1 -acetyl-N 2 -formyl-5-methoxykynuramine is formed by pyrrole-ring cleavage, by myeloperoxidase, indoleamine 2,3-dioxygenase and various non-enzymatic oxidants. Its product, N 1 -acetyl-5-methoxykynuramine, is of interest as a scavenger of reactive oxygen and nitrogen species, mitochondrial modulator, downregulator of cyclooxygenase-2, inhibitor of cyclooxygenase, neuronal and inducible NO synthases. Contrary to other nitrosated aromates, the nitrosated kynuramine metabolite, 3-acetamidomethyl-6-methoxycinnolinone, does not re-donate NO. Various other products are formed from melatonin and its metabolites by interaction with reactive oxygen and nitrogen species. The relative contribution of the various pathways to melatonin catabolism seems to be influenced by microglia activation, oxidative stress and brain levels of melatonin, which may be strongly changed in experiments on neuroprotection. Many of the melatonin metabolites, which may appear in elevated concentrations after melatonin administration, possess biological or pharmacological properties, including N-acetylserotonin, 5-methoxytryptamine and some of its derivatives, and especially the 5-methoxylated kynuramines.

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Section: Cytochrome P 450 Metabolismmentioning

confidence: 99%

Melatonin Metabolism in the Central Nervous System

Hardeland¹

2010

111

110

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“…Glutamate-cysteine ligase catalytic subunit is the target gene of Nrf2, the regulator of Nrf2 glutathione, and is an important antioxidant agent in humans (Cortese et al, 2008). Glutathione S-transferase (GST) catalyzed by glutathione can eliminate harmful and toxic compounds of the body, whereas GST can activate Nrf2 induction for detoxification (Nannelli et al, 2009). Heme oxygenase-1 (HMOX1, HO-1) responds mainly to toxicity caused by an oxidation stimulus, and can induce Nrf2 to activate the secondary detoxifying enzyme reaction (Itoh et al, 2004).…”

Section: Resultsmentioning

confidence: 99%

In vitro free radicals scavenging activity and antioxidant capacity of solid-state fermented wheat bran and its potential modulation of antioxidative molecular targets in chicken PBMC

Wang

Chang

et al. 2016

R. Bras. Zootec.

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-The purpose of this study was to demonstrate the in vitro free radical scavenging activity and antioxidant capacity in solid-state fermented wheat bran and its potential modulation of antioxidative molecular targets in chicken peripheral blood mononuclear cells (PBMC). After solid-state fermentation of wheat bran by white rot fungi for 12 d, the scavenging action of the fermented wheat bran extracts was 1, 1-diphenyl-2-picrylhydrazyl (DPPH), and the free radicals increased significantly, approximately 1.5-fold. Trolox equivalent antioxidant capacity of 1 mg/mL fermented wheat bran extracts was increased from 100 to 150 mM trolox antioxidant capacity after 12 d of fermentation. Moreover, the extracts exhibited 50% of the chelating capacity observed for ferrous iron (Fe2+) after fermenting for 12 d. In vitro, and under the stimulus of fermented wheat bran, the antioxidant gene expression (GST, HO-1, Nrf2, and GCLC genes) of PBMC was more than double that of the PBS, ascorbic acid, and unfermented wheat bran. The expression of fermented wheat bran was the lowest for the NOX1 and ROMO1 genes. Solid-state wheat bran fermented by white rot fungi can increase the scavenging action of DPPH, the trolox equivalent antioxidant capacity, and the chelating capacity of ferrous iron; in addition, in vitro, it can regulate the expression of antioxidant molecular targets in chicken PBMC.

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“…Evidence from Yang et al (6) indicates that natural flavones from grape seed extract elevate the activities of CAT, SOD and GPx, and mitigate the H 2 O 2 insult to muscle cells, further suggesting that flavones serve an antioxidant role. It has been demonstrated previously that β-Naphthoflavone serves as a modulator of antioxidant enzyme activity (19). However, a previous study has indicated that antioxidant enzyme activity is unaffected following treatment with certain flavones (33).…”

Section: Discussionmentioning

confidence: 96%

“…Therefore, the specific components of botanical extracts that are neuroprotective and their underlying mechanisms are typically poorly understood, resulting in restricted application of many botanical extracts in clinical settings. It has been demonstrated that Naphthoflavone upregulates the expression or activity of antioxidant-associated enzymes, including glutathione peroxidase (GPx), quinone oxidoreductase-1, glutathione transferase and heme oxygenase-1 (19)(20)(21)(22), and represses ROS-producing enzymes such as nicotinamide adenine dinucleotide phosphate (NADPH) oxidase (23). This suggests a potential effect exerted by Naphthoflavone in antioxidation.…”

Section: Introductionmentioning

confidence: 99%

α- and β-Naphthoflavone synergistically attenuate H2O2-induced neuron SH-SY5Y cell damage

Zhu

et al. 2017

Experimental and Therapeutic Medicine

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Abstract. Previous studies have demonstrated an association between neurological diseases and oxidative stress (OS).Naphthoflavone is a synthetic derivative of naturally occurring flavonoids that serves an important role in the treatment and prevention of OS-related diseases. The current study was designed to apply α-and β-Naphthoflavone individually and in combination to counteract the detrimental effects of OS on neurons in vitro. Neuronal SH-SY5Y cells were subjected to 20 µM H 2 O 2 , followed by exposure to 20 µM α-Naphthoflavone and/or 10 µM β-Naphthoflavone. Results indicated that α-and β-Naphthoflavone effectively antagonized the apoptosis-promoting effect of H 2 O 2 on neuronal SH-SY5Y cells, and that β-Naphthoflavone significantly (P<0.05) reversed H 2 O 2 -inhibited cell viability. Notably, co-treatment of α-and β-Naphthoflavone reversed the H 2 O 2 -induced apoptosis rate elevation and cell viability reduction. Further analysis demonstrated that H 2 O 2 inhibited the activities of antioxidant enzymes including catalase, superoxide dismutase and glutathione peroxidase, but this was reversed by the co-treatment with α-and β-Naphthoflavone and selectively enhanced by the treatment with α-or β-Naphthoflavone. H 2 O 2 -stimulated p38 mitogen-activated protein kinase activation was repressed following treatment with α-and/or β-Naphthoflavone, along with a decreased expression of the apoptosis-related factors and inhibited caspase-3 activation. In conclusion, co-treatment with α-and β-Naphthoflavone minimized H 2 O 2 -led neuron damage compared with treatment with α-or β-Naphthoflavone, suggesting a synergetic effect between α-and β-Naphthoflavone. This indicates that utilizing α-and β-Naphthoflavone together in the clinical setting may provide a novel therapeutic for neurological disease.

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Effect of β-naphthoflavone on AhR-regulated genes (CYP1A1, 1A2, 1B1, 2S1, Nrf2, and GST) and antioxidant enzymes in various brain regions of pig

Cited by 46 publications

References 67 publications

Melatonin Metabolism in the Central Nervous System

Melatonin Metabolism in the Central Nervous System

In vitro free radicals scavenging activity and antioxidant capacity of solid-state fermented wheat bran and its potential modulation of antioxidative molecular targets in chicken PBMC

α- and β-Naphthoflavone synergistically attenuate H2O2-induced neuron SH-SY5Y cell damage

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