High expression of cytochrome P450 2a-5 (coumarin 7-hydroxylase) in mouse hepatomas
β Scribed by Valery Kobliakov; Ludmila Kulikova; Dimitri Samoilov; Matti A. Lang
- Book ID
- 102502403
- Publisher
- John Wiley and Sons
- Year
- 1993
- Tongue
- English
- Weight
- 421 KB
- Volume
- 7
- Category
- Article
- ISSN
- 0899-1987
No coin nor oath required. For personal study only.
β¦ Synopsis
Abstract
A high level of Cyp2aβ5 was found in spontaneous and transplanted mouse hepatomas compared with normal liver. Increased expression of Cyp2aβ5 was associated with an increase in coumarin 7βhydroxylation, a marker activity of Cyp2aβ5, and the corresponding mRNA, suggesting that regulation of Cyp2aβ5 in hepatomas is pretranslational. In contrast, the total P450 content and arylhydrocarbon hydroxylase and amidopyrene demethylase activities decreased. Pyrazole, a strong inducer of Cyp2aβ5 in normal mouse livers, also increases this isozyme in hepatomas. A parallel increase in the corresponding mRNA suggests that pyrazole, like the formation of hepatomas, affects the regulation of Cyp2aβ5 pretranslationally.
π SIMILAR VOLUMES
Cytochrome P450 (CYP) 2A5 is involved in the metabolism of carcinogens like aflatoxin B1 and N-nitrosodiethylamine (NDEA), and CYP2A5 levels are increased in some pathological states of the liver (e.g., infectious hepatitis and porphyria). We analyzed the expression of CYP2A5 during experimental liv
We analyzed the function of a DNA domain located upstream of the cytochrome P4501A1 gene in wild-type (Hepa lclc7) mouse hepatoma cells and in high-activityvariant (HAV) cells that overtranscribe the gene in response to the inducer 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD). Transfection experiments