Metabolic activation of emodin in the reconstituted cytochrome P-450 system of the hepatic microsomes of rats |
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| Authors: | H Tanaka N Morooka K Haraikawa Y Ueno |
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| Affiliation: | 1. Department of Biological Mechanisms and Functions, Graduate School of Bioagricultural Sciences, Nagoya University, Furo-cho, Chikusa-ku, Nagoya, Aichi 464-8601, Japan;2. Graduate School of Agriculture, Meiji University, 1-1-1 Higashi-Mita, Tama-ku, Kawasaki, Kanagawa 214-8571, Japan;3. Chemical Genetics Laboratory, RIKEN, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan;4. Chemical Genomics Research Group, RIKEN Center for Sustainable Resource Science, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan;5. Division of Functional Genomics, Advanced Science Research Centre, Kanazawa University, 13-1 Takaramachi, Kanazawa, Ishikawa 920-0934, Japan;1. Instituto de Investigaciones en Materiales, Universidad Nacional Autónoma de México, Circuito Exterior s/n Ciudad Uiversitaria, Coyoacán, México, DF 04510, Mexico;2. Instituto Politecnico Nacional, ESIQIE-SEPI-DIQI, Laboratorio de Investigación en Materiales Porosos, Catálisis Ambiental y Química Fina (LiMpCa-QuF), UPALM Edif. 7 P.B. Zacatenco, GAM, México, DF 07738, Mexico |
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| Abstract: | Studies were undertaken to elucidate further the mechanism by which emodin, an anthraquinoid mycotoxin and constituent of rhubarb, was converted into a direct-acting mutagen to Salmonella typhimurium TA1537 by the hepatic microsomes and the reconstituted cytochrome P-450 system. Emodin was activated into a mutagenic principle(s) in the reconstituted cytochrome P-450 system, and its mutagenicity was significantly higher with the fraction II (P-448 type) than the fraction I (P-450 type) derived from the hepatic microsomes of PCB-induced rats. Thin-layer chromatographic analysis revealed that the purified cytochrome II-a (maximal CO-differential spectrum at 448.0 nm and high-spin form) activity converted emodin into 2-hydroxy-emodin, a direct-acting mutagen. |
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