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

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Title: Astaxanthin can alter CYP1A-dependent activities via two different mechanisms : Induction of protein expression and inhibition of NADPH P450 reductase dependent electron transfer
Authors: Ohno, Marumi Browse this author
Darwish, Wageh S. Browse this author
Ikenaka, Yoshinori Browse this author →KAKEN DB
Miki, Wataru Browse this author
Ishizuka, Mayumi Browse this author →KAKEN DB
Keywords: Astaxanthin
Cytochrome P450 1A
Conjugating enzyme
Metabolic activation
Benzo[a]pyrene
NADPH P450 reductase
Issue Date: Jun-2011
Publisher: Elsevier
Journal Title: Food and Chemical Toxicology
Volume: 49
Issue: 6
Start Page: 1285
End Page: 1291
Publisher DOI: 10.1016/j.fct.2011.03.009
PMID: 21414371
Abstract: Astaxanthin (Ax), a xanthophyll carotenoid, is reported to induce cytochrome P450 (CYP) 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.
Type: article (author version)
URI: http://hdl.handle.net/2115/46205
Appears in Collections:獣医学院・獣医学研究院 (Graduate School of Veterinary Medicine / Faculty of Veterinary Medicine) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 石塚 真由美

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