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

Ohno, Marumi; Darwish, Wageh S.; Ikenaka, Yoshinori; Miki, Wataru; Ishizuka, Mayumi

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

Ohno, Marumi; Darwish, Wageh S.; Ikenaka, Yoshinori et al.

Food and Chemical Toxicology, 2011, 49(6), 1285-1291

Permalink : https://hdl.handle.net/2115/46205

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アクセス権	open access
URI	https://hdl.handle.net/2115/46205
タイトル	Astaxanthin can alter CYP1A-dependent activities via two different mechanisms : Induction of protein expression and inhibition of NADPH P450 reductase dependent electron transfer
著者	Ohno, Marumi ; Darwish, Wageh S. ; Ikenaka, Yoshinori ; Miki, Wataru ; Ishizuka, Mayumi
著者名 Ohno, Marumi
著者名 Darwish, Wageh S.
e-Rad_Researcher 40543509 著者名 Ikenaka, Yoshinori
著者名 Miki, Wataru
e-Rad_Researcher 50332474 著者名 Ishizuka, Mayumi
言語	英語
キーワード	Astaxanthin
	Cytochrome P450 1A
	Conjugating enzyme
	Metabolic activation
	Benzo[a]pyrene
	NADPH P450 reductase
発行日	2011-06
出版者	Elsevier
収録物名	Food and Chemical Toxicology
巻(号)	49(6)
ページ	1285-1291
抄録	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.
資源タイプ	学術雑誌論文
出版タイプ	Accepted Manuscript
PISSN	0278-6915
関連情報	PMID 21414371
関連情報 (isVersionOf)	出版社版DOI https://doi.org/10.1016/j.fct.2011.03.009