| Publication |
Sentence |
Publish Date |
Extraction Date |
Species |
| Akiko Matsumoto, Toshihiro Kawamoto, Mikako Horita, Tatsuya Takahashi, Toyohi Isse, Tsunehiro Oyama, Masayoshi Ichib. Single-dose ethanol administration downregulates expression of cytochrome p450 2E1 mRNA in aldehyde dehydrogenase 2 knockout mice. Alcohol (Fayetteville, N.Y.). vol 41. issue 8. 2008-02-14. PMID:17980998. |
on the other hand, it is well established that one of the cytochrome p450 enzymes, cyp2e1, is an activator of carcinogens (e.g., nitorosamines) and a generator of oxidative stress, and it is shown that cyp2e1 was induced by ethanol via gene transcriptional regulation. |
2008-02-14 |
2023-08-12 |
mouse |
| Akiko Matsumoto, Toshihiro Kawamoto, Mikako Horita, Tatsuya Takahashi, Toyohi Isse, Tsunehiro Oyama, Masayoshi Ichib. Single-dose ethanol administration downregulates expression of cytochrome p450 2E1 mRNA in aldehyde dehydrogenase 2 knockout mice. Alcohol (Fayetteville, N.Y.). vol 41. issue 8. 2008-02-14. PMID:17980998. |
in the present study, to examine the consequences of aldh2 polymorphism on transcriptional regulation of cyp2e1 in liver tissue, aldh2+/+ and aldh2-/- mice were orally administered 5 g/kg body weight of ethanol and the levels of cyp2e1 mrna in liver tissue then analyzed. |
2008-02-14 |
2023-08-12 |
mouse |
| Akiko Matsumoto, Toshihiro Kawamoto, Mikako Horita, Tatsuya Takahashi, Toyohi Isse, Tsunehiro Oyama, Masayoshi Ichib. Single-dose ethanol administration downregulates expression of cytochrome p450 2E1 mRNA in aldehyde dehydrogenase 2 knockout mice. Alcohol (Fayetteville, N.Y.). vol 41. issue 8. 2008-02-14. PMID:17980998. |
the level of cyp2e1 mrna 12h after the ethanol administration tended to be higher than the 0-h group in aldh2+/+ mice, however, it was significantly lower than the 0-h group in aldh2-/- mice. |
2008-02-14 |
2023-08-12 |
mouse |
| Kiyoshi Nagata, Hiroyuki Suzuki, Shuhei Sakaguch. Common pathogenic mechanism in development progression of liver injury caused by non-alcoholic or alcoholic steatohepatitis. The Journal of toxicological sciences. vol 32. issue 5. 2008-01-31. PMID:18198478. |
one central pathway appears to be the induction of the cyp2e1 form of cytochrome p450 enzymes by ethanol. |
2008-01-31 |
2023-08-12 |
Not clear |
| Yong-Dae Kim, Sang-Yong Eom, Masanori Ogawa, Tsunehiro Oyama, Toyohi Isse, Jong-Won Kang, Yan Wei Zhang, Toshihiro Kawamoto, Heon Ki. Ethanol-induced oxidative DNA damage and CYP2E1 expression in liver tissue of Aldh2 knockout mice. Journal of occupational health. vol 49. issue 5. 2008-01-22. PMID:17951967. |
this study shows that acute ethanol consumption increases oxidative dna damage and that expression of cyp2e1 protein may play a pivotal role in the induction of oxidative dna damage. |
2008-01-22 |
2023-08-12 |
mouse |
| Marta Kot, Władysława A Danie. Effect of cytochrome P450 (CYP) inducers on caffeine metabolism in the rat. Pharmacological reports : PR. vol 59. issue 3. 2008-01-17. PMID:17652830. |
ethanol (mainly a cyp2e1 inducer) modestly increased the rates of the n-demethylation reactions. |
2008-01-17 |
2023-08-12 |
rat |
| Graham R Jang, Robert Z Harri. Drug interactions involving ethanol and alcoholic beverages. Expert opinion on drug metabolism & toxicology. vol 3. issue 5. 2008-01-17. PMID:17916057. |
most of these interactions do not seem to involve cyp2e1, the enzyme initially characterized and cloned based on its ability to metabolize and be induced by ethanol. |
2008-01-17 |
2023-08-12 |
Not clear |
| Nikolas J Hodges, Richard M Green, James K Chipman, Mark Graha. Induction of DNA strand breaks and oxidative stress in HeLa cells by ethanol is dependent on CYP2E1 expression. Mutagenesis. vol 22. issue 3. 2008-01-08. PMID:17284772. |
induction of dna strand breaks and oxidative stress in hela cells by ethanol is dependent on cyp2e1 expression. |
2008-01-08 |
2023-08-12 |
Not clear |
| Nikolas J Hodges, Richard M Green, James K Chipman, Mark Graha. Induction of DNA strand breaks and oxidative stress in HeLa cells by ethanol is dependent on CYP2E1 expression. Mutagenesis. vol 22. issue 3. 2008-01-08. PMID:17284772. |
induction of cytochrome p4502e1 (cyp2e1) is considered to be an important mechanism by which ethanol can cause toxicity related to oxidative stress both in vivo and in vitro. |
2008-01-08 |
2023-08-12 |
Not clear |
| Nikolas J Hodges, Richard M Green, James K Chipman, Mark Graha. Induction of DNA strand breaks and oxidative stress in HeLa cells by ethanol is dependent on CYP2E1 expression. Mutagenesis. vol 22. issue 3. 2008-01-08. PMID:17284772. |
in the current study, we used hela cells with doxycycline-regulated cyp2e1 expression to test the hypothesis that induction of cyp2e1 could lead to secondary dna oxidation that could potentially contribute to the carcinogenicity of ethanol in vivo. |
2008-01-08 |
2023-08-12 |
Not clear |
| Nikolas J Hodges, Richard M Green, James K Chipman, Mark Graha. Induction of DNA strand breaks and oxidative stress in HeLa cells by ethanol is dependent on CYP2E1 expression. Mutagenesis. vol 22. issue 3. 2008-01-08. PMID:17284772. |
overexpression of cyp2e1 protein was not associated with oxidative stress per se as assessed by markers of lipid peroxidation (cis-parinaric acid oxidation), glutathione depletion and elevation of intracellular reactive oxygen species (dichlorofluoroscin oxidation) in the presence or absence of ethanol substrate (10 mm, 24 h). |
2008-01-08 |
2023-08-12 |
Not clear |
| Nikolas J Hodges, Richard M Green, James K Chipman, Mark Graha. Induction of DNA strand breaks and oxidative stress in HeLa cells by ethanol is dependent on CYP2E1 expression. Mutagenesis. vol 22. issue 3. 2008-01-08. PMID:17284772. |
in contrast, however, after pre-incubation of cells with l-buthionine-(s,r)-sulphoximine (bso, 10 microm) which caused a 75% reduction in intracellular reduced glutathione (gsh) levels, cyp2e1 expression resulted in oxidative stress as assessed by all of these markers and dna strand breaks but only in the presence of ethanol (10 mm). |
2008-01-08 |
2023-08-12 |
Not clear |
| Tsunehiro Oyama, Yong-Dae Kim, Toyohi Isse, Pham Thi Thu Phuong, Masanori Ogawa, Tetsunosuke Yamaguchi, Tsuyoshi Kinaga, Yasunori Yashima, Heon Kim, Toshihiro Kawamot. A pilot study on subacute ethanol treatment of ALDH2 KO mice. The Journal of toxicological sciences. vol 32. issue 4. 2007-12-26. PMID:17965556. |
we evaluated the effects of subacute ethanol treatment on the survival rate, expression of aldh1, aldh2, cytochrome p450 (cyp) 1a1, cyp2e1 and cyp4b1 in wild (aldh2+/+) mice (c57bl/6) and aldh2 knock out (aldh2-/-) mice. |
2007-12-26 |
2023-08-12 |
mouse |
| Tsunehiro Oyama, Yong-Dae Kim, Toyohi Isse, Pham Thi Thu Phuong, Masanori Ogawa, Tetsunosuke Yamaguchi, Tsuyoshi Kinaga, Yasunori Yashima, Heon Kim, Toshihiro Kawamot. A pilot study on subacute ethanol treatment of ALDH2 KO mice. The Journal of toxicological sciences. vol 32. issue 4. 2007-12-26. PMID:17965556. |
cyp2e1 is more inducible to ethanol toxicity in aldh2-/- mice compared with aldh2+/+ mice when ethanol is administered according to the results of quantitative pcr. |
2007-12-26 |
2023-08-12 |
mouse |
| Terrence M Donohue, Arthur I Cederbaum, Samuel W French, Shirish Barve, Bin Gao, Natalia A Osn. Role of the proteasome in ethanol-induced liver pathology. Alcoholism, clinical and experimental research. vol 31. issue 9. 2007-10-16. PMID:17760783. |
the review will summarize recent findings on: (1) the interactions between the proteasome and the ethanol metabolizing enzyme, cyp2e1; (2) the dynamics of proteasome inhibition by ethanol in animal models and cultured cells; (3) ethanol-elicited suppression of proteasome activity and its effect on signal transduction; (4) the role of proteasome inhibition in cytokine production by liver cells; and (5) ethanol elicited suppression of peptide hydrolysis and the potential effects on antigen presentation. |
2007-10-16 |
2023-08-12 |
Not clear |
| Masahiro Konishi, Hiromasa Ishi. Role of microsomal enzymes in development of alcoholic liver diseases. Journal of gastroenterology and hepatology. vol 22 Suppl 1. 2007-10-02. PMID:17567472. |
ethanol-inducible cyp2e1 is of interest because of its ability to metabolize and activate many toxicologically important substrates including ethanol, ccl(4), acetaminophen, and n-nitrosodimethylamine, to more toxic products. |
2007-10-02 |
2023-08-12 |
human |
| Masahiro Konishi, Hiromasa Ishi. Role of microsomal enzymes in development of alcoholic liver diseases. Journal of gastroenterology and hepatology. vol 22 Suppl 1. 2007-10-02. PMID:17567472. |
major interest in cyp2e1 reflects the ability of this enzyme to oxidize ethanol, to generate reactive products from ethanol oxidation (e.g. |
2007-10-02 |
2023-08-12 |
human |
| Yu Guo, Hui Wang, Chun Zhan. Establishment of rat precision-cut fibrotic liver slice technique and its application in verapamil metabolism. Clinical and experimental pharmacology & physiology. vol 34. issue 5-6. 2007-08-15. PMID:17439408. |
the results showed that the pcfls viability remained steady throughout the 6 h of culture when the thickness of slices was 300 microm and ph of the medium was 7.0; cyp inducers (phenobarbital and ethanol) enhanced cyp2e1, cyp3a1/2 and uridine diphosphate-glucuronate transferase (udpgt) activities, respectively, in a time-dependent manner. |
2007-08-15 |
2023-08-12 |
rat |
| Kristina K Wolf, Sheryl G Wood, Jenna L Allard, Jane A Hunt, Nadia Gorman, Brooke W Walton-Strong, Juliana G Szakacs, Su X Duan, Qin Hao, Michael H Court, Lisa L von Moltke, David J Greenblatt, Vsevolod Kostrubsky, Elizabeth H Jeffery, Steven A Wrighton, Frank J Gonzalez, Peter R Sinclair, Jacqueline F Sinclai. Role of CYP3A and CYP2E1 in alcohol-mediated increases in acetaminophen hepatotoxicity: comparison of wild-type and Cyp2e1(-/-) mice. Drug metabolism and disposition: the biological fate of chemicals. vol 35. issue 7. 2007-07-24. PMID:17392391. |
however, we previously found that alcohol [ethanol and isopentanol (eip)] causes increases in apap hepatotoxicity in cyp2e1(-/-) mice, indicating that cyp2e1 is not essential. |
2007-07-24 |
2023-08-12 |
mouse |
| Yong Wang, Hongming Wang, Yonghua Wang, Chuanlu Yang, Ling Yang, Keli Ha. Theoretical study of the mechanism of acetaldehyde hydroxylation by compound I of CYP2E1. The journal of physical chemistry. B. vol 110. issue 12. 2007-06-28. PMID:16553429. |
recent experimental studies revealed that cytochrome p450 2e1 (cyp2e1) could metabolize not only ethanol but also its primary product, acetaldehyde, accompanying the well-known acetaldehyde dehydrogenases (aldh) in the metabolism of acetaldehyde. |
2007-06-28 |
2023-08-12 |
Not clear |