Source:http://linkedlifedata.com/resource/pubmed/id/10826654
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2000-6-13
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pubmed:abstractText |
The induction of a variety of drug-metabolizing enzymes by six anthraquinones (AQs) has been investigated in the liver and small intestine of rat. In the liver, the intragastric administration for 3 days of 100 mg/kg 9,10-anthraquinone (9,10-AQ). 1-hydroxy-AQ, 1,4-dihydroxy-AQ, but not 1,2-dihydroxy-AQ and 2-carboxy-AQ, resulted in a significant induction of the UDP-GT, DT-diaphorase, P450 1A-linked monooxygenase activities and in particular the methoxyresorufin-O-demethylase (MEROD), an activity dependent on P450 1A2. Immunoblot analysis indicated that 1-hydroxy-AQ and 1,4-dihydroxy-AQ induced P450 1A2 but not 1A1 and 9,10-AQ induced both P4501A2 and P4502B. Northern blotanalysis, using a cDNA probe for CYP 1A1 and CYP 1A2, confirmed that the AQs induce CYP 1A2 but not 1A1 mRNA. In the mucosa of small intestine, none of the above-mentioned enzymatic activities were enhanced following AQ administration. The induction mechanism of the hepatic enzymes by AQs is not known and it deserves a further study as it might be independent from the activation of the Ah-receptor as reported for other tricyclic compounds. The results from inhibition experiments showed that the hydroxylated AQs were strong inhibitors of P450 1A2-dependent monooxygenases. This suggests that long-term ingestion of certain AQs, may affect the toxicity of other components present in the diet through the hepatic induction or inhibition of P450 1A2.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Anthraquinones,
http://linkedlifedata.com/resource/pubmed/chemical/Cytochrome P-450 CYP1A1,
http://linkedlifedata.com/resource/pubmed/chemical/Cytochrome P-450 CYP1A2,
http://linkedlifedata.com/resource/pubmed/chemical/Glucuronosyltransferase,
http://linkedlifedata.com/resource/pubmed/chemical/Glutathione Transferase,
http://linkedlifedata.com/resource/pubmed/chemical/NAD(P)H Dehydrogenase (Quinone),
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/UDP-glucuronosyltransferase, UGT1A3
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0009-2797
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
14
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pubmed:volume |
126
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
63-77
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:10826654-Animals,
pubmed-meshheading:10826654-Anthraquinones,
pubmed-meshheading:10826654-Cytochrome P-450 CYP1A1,
pubmed-meshheading:10826654-Cytochrome P-450 CYP1A2,
pubmed-meshheading:10826654-Glucuronosyltransferase,
pubmed-meshheading:10826654-Glutathione Transferase,
pubmed-meshheading:10826654-Immunoblotting,
pubmed-meshheading:10826654-Intestine, Small,
pubmed-meshheading:10826654-Liver,
pubmed-meshheading:10826654-Male,
pubmed-meshheading:10826654-NAD(P)H Dehydrogenase (Quinone),
pubmed-meshheading:10826654-RNA, Messenger,
pubmed-meshheading:10826654-Rats,
pubmed-meshheading:10826654-Rats, Sprague-Dawley
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pubmed:year |
2000
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pubmed:articleTitle |
Heterogenous effects of anthraquinones on drug-metabolizing enzymes in the liver and small intestine of rat.
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pubmed:affiliation |
Laboratory of Genetic and Biochemical Toxicology, Istituto di Mutagenesi e Differenziamento del CNR, Pisa, Italy.
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pubmed:publicationType |
Journal Article
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