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• W2039031803 endingPage "344" @default.
• W2039031803 startingPage "337" @default.
• W2039031803 abstract "Vitamins E and K share structurally related side chains and are degraded to similar final products. For vitamin E the mechanism has been elucidated as initial omega-hydroxylation and subsequent beta-oxidation. For vitamin K the same mechanism can be suggested analogously. omega-Hydroxylation of vitamin E is catalyzed by cytochrome p450 enzymes, which often are induced by their substrates themselves via the activation of the nuclear receptor PXR. Vitamin E is able to induce CYP3A-forms and to activate a PXR-driven reporter gene. It is shown here that K-type vitamins are also able to activate PXR. A ranking showed that compounds with an unsaturated side chain were most effective, as are tocotrienols and menaquinone-4 (vitamin K(2)), which activated the reporter gene 8-10-fold. Vitamers with a saturated side chain, like tocopherols and phylloquinone were less active (2-5-fold activation). From the fact that CYPs commonly responsible for the elimination of xenobiotics are involved in the metabolism of fat-soluble vitamins and the ability of the vitamins to activate PXR it can be concluded that supranutritional amounts of these vitamins might be considered as foreign." @default.
• W2039031803 created "2016-06-24" @default.
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• W2039031803 date "2003-12-01" @default.
• W2039031803 modified "2023-10-16" @default.
• W2039031803 title "Homologous metabolic and gene activating routes for vitamins E and K" @default.
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• W2039031803 doi "https://doi.org/10.1016/s0098-2997(03)00029-3" @default.
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