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( Tae Cheon Jeong ),( Nam Hee Kim ),( Sang Kyu Lee ),( Mi Jeong Kang ),( Hye Gwang Jeong ),( Won Ku Kang ) 한국응용약물학회 2014 Biomolecules & Therapeutics(구 응용약물학회지) Vol.22 No.2
Effects of diallyl sulfide (DAS) on thioacetamide-induced hepatotoxicity and immunotoxicity were investigated. When maleSprague-Dawley rats were treated orally with 100, 200 and 400 mg/kg of DAS in corn oil for three consecutive days, the activityof cytochrome P450 (CYP) 2E1-selective p-nitrophenol hydroxylase was dose-dependently suppressed. In addition, the activitiesof CYP 2B-selective benzyloxyresorufin O-debenzylase and pentoxyresorufin O-depentylase were significantly induced bythe treatment with DAS. Western immunoblotting analyses also indicated the suppression of CYP 2E1 protein and/or the inductionof CYP 2B protein by DAS. To investigate a possible role of metabolic activation by CYP enzymes in thioacetamide-inducedhepatotoxicity, rats were pre-treated with 400 mg/kg of DAS for 3 days, followed by a single intraperitoneal treatment with 100 and200 mg/kg of thioacetamide in saline for 24 hr. The activities of serum alanine aminotransferase and aspartate aminotransferasesignificantly elevated by thioacetamide were protected in DAS-pretreated animals. Likewise, the suppressed antibody responseto sheep erythrocytes by thioacetamide was protected by DAS pretreatment in female BALB/c mice. Taken together, our presentresults indicated that thioacetamide might be activated to its toxic metabolite(s) by CYP 2E1, not by CYP 2B, in rats and mice.
Inhibition of Cytochrome P -450 by safrole in Rat Liver Microsomes
Tae Cheon Jeong,Jeong Woo Park,Suck Young Choe,Jih Hyun Kim,Byung Sam Kim,Kyu Hwan Yang 생화학분자생물학회 1993 BMB Reports Vol.26 No.2
Inhibition kinetics of cytochrome P-450 (P-450)-dependent monooxgenases by an environmental carcinogen safrole (1-allyl-3,4-methylenedioxybenzene) was studied in rat liver microsomes. The activities of P-450ⅠA1-specific ethoxyresorufin O-deethylase (EROD), P-450ⅡB-specific pentoxyresorufin O-dealkylase (PROD), and P-450ⅡE1-specific p-nitrophenol hydroxylase (PNPH) were inhibited dose-dependently when safrole was added into the reaction mixtures from 50 to 400 μM. Meanwhile, the P-450ⅢA1-specific erythromycin N-demethylase (ERDM) was not inhibited at all by safrole up to 400 μM. The inhibition pattern studies for each reaction in Dixon and Cornish-Bowden plots showed three distinct kinetics; mixed inhibition for EROD, uncompetitive for PROD, and noncompetitive for PNPH. The K_i` values of safrole for EROD and PNPH were 95.4 and 215.1μM respectively. The K_i` values of safrole for PROD was 9.48 μM. These results suggest that safrole inhibits microsomal P-450 isozyme-specific monooxygenases with distinct mechanisms and safrole could be used as an useful inhibitor to study P-450-mediated monooxygenase reactions.
Effects of Polycyclic Aromatic Hydrocarbons on Liver and Lung Cytochrome P450s in Mice
JiYoungKim,SangKyuLee,ChunHwaKim,TaeWonJeon,문창규,Hye-SookLee,SunDongYoo,EungSeokLee,TaeCheonJeong 대한약학회 2003 Archives of Pharmacal Research Vol.26 No.5
Certain polycyclic aromatic hydrocarbons (PAHs) have been reported to induce cytochrome P450 (CYP) 1A1 and 1A2. In the present study, the effects of six well-known PAHs, such as benzo[a]pyrene, benz[a]anthracene, dibenz[a,h]anthracene, chrysene, benzo[k]fluorancene and benzo[b]fluorancene, on the activities of hepatic and pulmonary CYP enzymes were investigated in male ICR mice. When mice were treated intraperitoneally with 3, 10 and 30 mg/ kg of individual PAHs for 3 consecutive days, the activities of ethoxyresorufin- and methoxyresorufin- O-dealkylases were significantly and differentially induced in both liver and lung. Moreover, other CYP isozyme-associated monooxygenase activities were also induced significantly in liver and lung with characteristic induction profiles. Our present results suggest that individual PAHs might have inductive effects on CYP isozymes, and that the characteristic inductive effects of individual PAHs on certain CYP isozymes would be developed as a marker for determining exposure to certain PAHs.
Induction of Cytochrome P450 1A and 2B by a- and b-Ionone in Sprague Dawley Rats
HyeGwangJeong,Young-JinChun,Chul-HoYun,Chang-KiuMoon,Hye-SookLee,SangSeopHan,Eung-SeokLee,TaeCheonJeong 대한약학회 2002 Archives of Pharmacal Research Vol.25 No.3
b-Ionone has been reported to induce the cytochrome P450 (P450) 2B1 in rats. In this study, the effects of b-ionone and an isomer, a-ionone, on liver P450 1A and 2B expression in Sprague Dawley rats were investigated. Subcutaneous administration of a- and b-ionone 72 and 48 hr prior to sacrificing the animals induced the liver microsomal P450 1A and 2B proteins. P450 2B1 induction was associated with the accumulation of its corresponding mRNA. Induction by b-ionone was much higher than that by a-ionone in both the mRNA and protein levels. When the route of administration was compared, P450 2B was induced more strongly after oral administration compared to that after subcutaneous injection. A single oral dose of 100, 300 and 600 mg/kg of a- and b-ionone for 24 h induced P450 2B1-selective pentoxyresorufin Odepentylase activity comparably in a dose-dependent manner. In addition, a- and b-ionone induced the P450 1A and 2B proteins. These results suggest that a- and b-ionone might be potent P450 2B1 inducers in rats, and that both ionones may be useful for examining the role of metabolic activation in chemical-induced toxicity where metabolic activation is required.