کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
8993135 | 1113466 | 2005 | 10 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Essential Role of Singlet Oxygen Species in Cytochrome P450-dependent Substrate Oxygenation by Rat Liver Microsomes
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کلمات کلیدی
p-Nitrophenol hydroxylationDeferoxamineDMPOTMPD4-Oxo-TEMPOESR1O2CYP2E1P450NADPHDFOCAT2,2,6,6-Tetramethyl-4-piperidone - 2،2،6،6-تترامتیل-4-پیپریدونDMSO - DMSOROS - ROS·OH - · OHHydrogen peroxide - آب اکسیژنهSinglet oxygen (1O2) - اکسیژن تک (1O2)Singlet oxygen - اکسیژن مجزاDimethylsulfoxide - دیمتیل سولفواکسیدSuperoxide anion radical - رادیکال آنیون سوپراکسیدHydroxyl radical - رادیکال هیدروکسیلElectron spin resonance - رزونانس اسپین الکترونSOD - سدSuperoxide dismutase - سوکسوکس دیسموتازCytochrome P450 - سیتوکروم پی۴۵۰NADH - نادانRate constant - نرخ ثابتNicotinamide adenine dinucleotide reduced form - نیکوتین آمید آدنین دینوکلئوتید فرم کاهش یافته استnicotinamide adenine dinucleotide phosphate reduced form - نیکوتین آمید آدنین دینکلوتید فسفات کاهش می یابدH2O2 - هیدروژن پراکسیدCatalase - کاتالازReactive oxygen species - گونههای فعال اکسیژن
موضوعات مرتبط
علوم پزشکی و سلامت
داروسازی، سم شناسی و علوم دارویی
اکتشاف دارویی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Essential Role of Singlet Oxygen Species in Cytochrome P450-dependent Substrate Oxygenation by Rat Liver Microsomes Essential Role of Singlet Oxygen Species in Cytochrome P450-dependent Substrate Oxygenation by Rat Liver Microsomes](/preview/png/8993135.png)
چکیده انگلیسی
Previously, we reported that singlet oxygen (1O2) was involved in rat liver microsomal P450-dependent substrate oxygenations in such reactions as p-hydroxylation of aniline, O-deethylation of 7-ethoxycoumarin, Ï- and (Ï-1)-hydroxylations of lauric acid, O-demethylation of p-nitroanisole, and N-demethylation of aminopyrine. In order to confirm the generality of 1O2 involvement, we have further investigated which kinds of reactive oxygen species (ROS) are formed during P450-dependent substrate oxygenation in microsomes. We examined CYP2E1-dependent hydroxylation of p-nitrophenol in rat liver microsomes in the presence of some ROS scavengers, because CYP2E1 has been reported to predominantly generate ROS in the hepatic microsomes and to relate with the oxidative stress in the body. The addition of 1O2 quenchers, β-carotene, suppressed the hydroxylation of p-nitrophenol. Furthermore, a nonspecific P450 inhibitor, SKF525A, and a ferric chelator, deferoxamine, both suppressed the hydroxylation. No other ROS scavengers such as superoxide dismutase (SOD), catalase, or mannitol altered the reaction. 1O2 was detectable during the reaction in the microsomes as measured by an electron spin resonance (ESR) spin-trapping method when 2,2,6,6-tetramethyl-4-piperidone (TMPD) was used as a spin-trapping reagent. The 1O2 was quenched by additions of β-carotene, p-nitrophenol, and SKF525A. The reactivity of p-nitrophenol and 1O2 correlated linearly with its hydrox- ylation rate in the microsomes. On the basis of these results, we conclude that 1O2 contributes to the p-nitrophenol hydroxylation in rat liver microsomes, by adding a new example of 1O2 involvement in the CYP2E1-dependent substrate oxygenations.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Drug Metabolism and Pharmacokinetics - Volume 20, Issue 1, 2005, Pages 14-23
Journal: Drug Metabolism and Pharmacokinetics - Volume 20, Issue 1, 2005, Pages 14-23
نویسندگان
Seiko Hayashi, Hiroyuki Yasui, Hiromu Sakurai,