Effects of β-ionone on the expression of cytochrome P450s and NADPH-cytochrome P450 reductase in Sprague Dawley rats

Jeong, Tae Cheon; Gu, Hee Kyoung; Chun, Young Jin; Yun, Chul‐Ho; Roh, Jung Koo

doi:10.1016/s0009-2797(98)00044-1

Cited by 13 publications

(3 citation statements)

References 17 publications

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“…In a previous study, NADPH P450 reductase activity or its protein expression were not modulated by Ax treatment [ Gradelet et al, 1996]. On the other hand, -ionone increased protein expression of NADPH P450 reductase, leading to induction of the enzymatic activity [Jeong et al, 1998]. Since metabolites of Ax in rat are reported to possess -ionone architecture, it might be expected that Ax and its metabolites show opposite effects on the expression or activity of NADPH P450 reductase.…”

Section: Discussionmentioning

confidence: 97%

Astaxanthin can alter CYP1A-dependent activities via two different mechanisms: Induction of protein expression and inhibition of NADPH P450 reductase dependent electron transfer

Ohno

Darwish

Ikenaka

et al. 2011

Food and Chemical Toxicology

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1A-dependent activity. CYP1A is one of the most important enzymes participating in phase I metabolism for chemicals, and it can activate various mutagens. To investigate the effect of Ax on the metabolic activation of a typical promutagen, benzo[a]pyrene by CYP1A, we orally administrated Ax (100 mg / kg body weight / day for 3 days) to male Wistar rats. In the treated rat liver, expression of CYP1A1 mRNA, protein, and its activity were significantly increased (5.5-fold, 8.5-fold, and 2.5-fold, respectively). In contrast, the activities of phase II enzymes (glutathione S-transferase and glucuronosyl-transferase)were not modulated by Ax. As a consequence, the mutagenicity of benzo[a]pyrene was more enhanced in Ax-treated rats, compared with controls in the Ames assay. On the other hand, NADPH P450 reductase activity was decreased in liver microsomes from the treated group. This result suggests the possibility that Ax inhibits the electron supply necessary for CYP catalytic activities and decreases CYP1A activity indirectly. In conclusion, Ax intake can alter CYP1A-dependent activities through two different mechanisms: 1) induction of CYP1A1 mRNA, protein expression, and activity; and 2) inhibition of the electron supply for the enzyme.

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Section: Discussionmentioning

confidence: 97%

Astaxanthin can alter CYP1A-dependent activities via two different mechanisms: Induction of protein expression and inhibition of NADPH P450 reductase dependent electron transfer

Ohno

Darwish

Ikenaka

et al. 2011

Food and Chemical Toxicology

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“…In addition, RES can conjugate with glutathione (Davoine et al ., ), and some of the effects of RES may be related to the depletion of reductants. In animal cells, oxidized carotenoid derivatives have been reported to have a multitude of effects, including cytotoxicity (Lakshminarayana et al ., ), induction of aptotosis (Janakiram et al ., ; Kalariya et al ., ; Liu et al ., ), enzyme inactivation and inhibition of mitochondrial respiration (Siems et al ., , ; Hurst et al ., ), induction of P450 cytochrome (Jeong et al ., ), damage to DNA (Yeh and Wu, ; Kalariya et al ., ) and retinoid signaling antagonism or promotion (Kuntz et al ., ; Eroglu et al ., ). In addition, carotenoid oxidation products, such as dihydroactinidiolide (Figure ), are active components of pheromones in several insects (Rocca et al ., ), and act as cat attractants in some plant species (Zhao et al ., ).…”

Section: Carotenoid Oxidation Products Are Bioactivementioning

confidence: 99%

Carotenoid oxidation products as stress signals in plants

2013

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SUMMARYCarotenoids are known to play important roles in plants as antioxidants, accessory light-harvesting pigments, and attractants for pollinators and seed dispersers. A new function for carotenoids has recently emerged, which relates to the response of plants to environmental stresses. Reactive oxygen species, especially singlet oxygen, produced in the chloroplasts under stress conditions, can oxidize carotenoids leading to a variety of oxidized products, including aldehydes, ketones, endoperoxides and lactones. Some of those carotenoid derivatives, such as volatile b-cyclocitral, derived from the oxidation of b-carotene, are reactive electrophile species that are bioactive and can induce changes in gene expression leading to acclimation to stress conditions. This review summarizes the current knowledge on the non-enzymatic oxidation of carotenoids, the bioactivity of the resulting cleavage compounds and their functions as stress signals in plants.

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“…The primary antibodies against individual isozymes were purchased from Easybio System (Seoul, Korea). The specificity of the antibodies used was determined elsewhere [11], [12]. For immunoblotting, the nitrocellulose filters were developed with a mixture of 5-bromo-4-chloro-3-indolyl phosphate, nitroblue tetrazolium and 0.1 M Tris buffer (1 : 1 : 10) according to the manufacturer's instructions.…”

Section: Western Immunoblottingmentioning

confidence: 99%

Induction of Cytochrome P450s by Rutaecarpine and Metabolism of Rutaecarpine by Cytochrome P450s

Lee

Kim²,

Lee³

et al. 2004

Planta med

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Rutaecarpine is an alkaloid originally isolated from the unripe fruit of Evodia rutaecarpa. Recently, rutaecarpine has been characterized to have an anti-inflammatory activity through cyclooxygenase-2 inhibition. In the present studies, the effects of rutaecarpine on liver cytochrome P450 s (P450s) and P450 s involved in the metabolism of rutaecarpine were studied in vivo and in vitro, respectively, because the data are crucial in the early development of rutaecarpine as a new drug candidate. Oral administration to male ICR mice of rutaecarpine for 3 consecutive days induced liver P450 1A-, 2B- and 2E1-selective monooxygenase activities. The induction of P450 1A and 2B by rutaecarpine was confirmed by Western immunoblotting. When rutaecarpine was incubated with rat liver microsomes in the presence of an NADPH-generating system, five metabolites were detected by UV and mass spectral analyses. The 3-methylcholanthrene- and phenobarbital-induced microsomes greatly increased the formation of metabolites. Our present results suggest that rutaecarpine might induce P450 1A and 2B in mice, and that P450 1A and 2B might predominantly metabolize rutaecarpine in rat liver microsomes.

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Effects of β-ionone on the expression of cytochrome P450s and NADPH-cytochrome P450 reductase in Sprague Dawley rats

Cited by 13 publications

References 17 publications

Astaxanthin can alter CYP1A-dependent activities via two different mechanisms: Induction of protein expression and inhibition of NADPH P450 reductase dependent electron transfer

Astaxanthin can alter CYP1A-dependent activities via two different mechanisms: Induction of protein expression and inhibition of NADPH P450 reductase dependent electron transfer

Carotenoid oxidation products as stress signals in plants

Induction of Cytochrome P450s by Rutaecarpine and Metabolism of Rutaecarpine by Cytochrome P450s

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