Protection against the bacterial mutagenicity of heterocyclic amines by purpurin, a natural anthraquinone pigment
| Autor: | Toshiko Hayatsu, Kazuo Nakayama, Hikoya Hayatsu, Sakae Arimoto-Kobayashi, Ken-ichi Fujita, Mikio Tada, Tetsuya Kamataki, Timothy H. Marczylo |
|---|---|
| Rok vydání: | 1999 |
| Předmět: |
Male
Salmonella typhimurium endocrine system Health Toxicology and Mutagenesis Anthraquinones Mutagen Epigallocatechin gallate medicine.disease_cause Anthraquinone Ames test chemistry.chemical_compound Cytochrome P-450 CYP1A2 Lectins Genetics medicine Animals Biotransformation chemistry.chemical_classification Chlorophyllin fungi food and beverages Antimutagenic Agents Rats Enzyme Biochemistry chemistry Heterocyclic amine Antimutagen Carbolines |
| Zdroj: | Mutation Research/Genetic Toxicology and Environmental Mutagenesis. 444:451-461 |
| ISSN: | 1383-5718 |
| DOI: | 10.1016/s1383-5718(99)00109-6 |
| Popis: | Purpurin (1,2,4-trihydroxy-9,10-anthraquinone) is a naturally occurring anthraquinone pigment found in species of madder root. We have found that the presence of purpurin in bacterial mutagenicity assays is responsible for a marked inhibition of mutagenicity induced by food-derived heterocyclic amines. Purpurin was found to be a better inhibitor of Trp-P-2-dependent mutagenicity than either epigallocatechin gallate or chlorophyllin both of which are well-established anti-mutagenic components of diet. Inhibition of Trp-P-2(NHOH) mutagenicity by purpurin was dependent upon pH. It was a better inhibitor in neutral than acidic conditions. Purpurin was protective against the direct mutagen Trp-P-2(NHOH) in both the presence and the absence of hepatic S9 but required pre-incubation. Finally, purpurin was responsible for the inhibition of human CYP1A2 and human NADPH-cytochrome P450 reductase and a decrease in the bioactivation of Trp-P-2 by these enzymes when they were expressed in Salmonella typhimurium TA1538ARO. However, inhibition of Trp-P-2(NHOH)-dependent mutations suggests purpurin also has a direct effect on this mutagen in addition to inhibiting its formation by CYP1A2. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full Text from ScienceDirect