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  • Title: Forms of cytochrome P450 in the liver microsome of oxidized frying oil-fed guinea pigs.
    Author: Liu JF, Chan FC.
    Journal: J Nutr Sci Vitaminol (Tokyo); 2000 Oct; 46(5):240-5. PubMed ID: 11234917.
    Abstract:
    The aim of this study is to investigate the influence of oxidized frying oil (OFO) on the induction of individual forms of cytochrome P450 (CYP450) in guinea pigs. The OFO samples were obtained by frying potato chips in soybean oil at 200+/-5 degrees C for 24 h. Sixteen male weaning guinea pigs were fed for 12 wk on a diet which included 15% of either OFO or fresh soybean oil supplemented with 300 ppm ascorbic acid. It was demonstrated that guinea pigs fed with the OFO diet (D300) exhibited inferior growth rates and lower feed efficiency than the control group (F300). The vitamin C contents of plasma, liver, and kidney in the D300 group were lower than those in the F300 group. Further, the thiobarbituric acid-reactive substance content in D300 liver and kidney was higher than that in the F300 equivalent. The liver UDP-glucuronyl-transferase activity in the D300 group was higher than that in the F300 group, and there was no difference in comparing the glutathione-S-transferase activity levels of the two groups. Notably, the total CYP450 content and the NADPH-cytochrome c reductase activity were significantly elevated in the D300 group. The ethoxyresorufin O-deethylase activity, which mainly represents CYP1A1 activity, for the detection of CYP450 isozyme characteristics was elevated more in the D300 than in the F300 group. There was no difference in the pentoxyresorufin O-dealkylase activity, which mainly reflects the CYP2B isozyme, between the two groups. However, the quantity of CYP1A1 isoform determined in the D300 group did not differ from that in the F300 group, as revealed by SDS-PAGE and Western blot testing. Our results demonstrate that the relative enzyme activity to CYP1A1-like activity of the guinea pig hepatic xenobiotic metabolizing enzyme system may be induced by OFO feeding, but more advanced research is needed to identify the predominant form of CYP450 isozyme induced as a result of this condition.
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