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rdf:type |
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lifeskim:mentions |
umls-concept:C0003601,
umls-concept:C0003805,
umls-concept:C0010762,
umls-concept:C0010763,
umls-concept:C0012155,
umls-concept:C0023884,
umls-concept:C0025320,
umls-concept:C0034693,
umls-concept:C0057223,
umls-concept:C0059735,
umls-concept:C0207509,
umls-concept:C0392747,
umls-concept:C0443172,
umls-concept:C0449438,
umls-concept:C0521009,
umls-concept:C0535996,
umls-concept:C0608437,
umls-concept:C0960580,
umls-concept:C1142644,
umls-concept:C1280500,
umls-concept:C1321893,
umls-concept:C1707598,
umls-concept:C1707600
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pubmed:issue |
3
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pubmed:dateCreated |
1999-1-11
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pubmed:abstractText |
The aim of the present work was to investigate the influence of the intestinal microflora on the changes in hepatic cytochrome P450 apoproteins induced by dietary glucosinolates. Ten rats harbouring a conventional digestive microflora were offered either a diet containing 390 g myrosinase-free rapeseed meal/kg (n 5) or a control diet devoid of glucosinolates (n 5). A similar trial was performed using germ-free rats. After 4 weeks of exposure to the dietary regimens, animals were slaughtered and their livers removed for preparation of microsomes and analysis of cytochrome P450 (EC 1.14.14.1). The glucosinolate-rich diet decreased the concentration of total cytochrome P450 in conventional rats only (-34%). The bacterial status did not modify the concentration of apoproteins CYP1A2 and CYP2B1/B2, but greatly decreased the concentration of the male constitutive isoform CYP2C11 (-53 and -45% respectively in conventional and germ-free rats). Germ-free rats fed on the glucosinolate-rich diet had a greater concentration of CYP3A (+139%) and a lower concentration of CYP2E1 (-32%) than their counterparts fed on the control diet. However, these differences were absent in conventional animals. On the whole, the influence of the intestinal microflora on the changes in hepatic cytochrome P450 due to the consumption of cruciferous vegetables is very complex and obviously involves different mechanisms according to the apoprotein.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Aryl Hydrocarbon Hydroxylases,
http://linkedlifedata.com/resource/pubmed/chemical/CYP2C11 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Cytochrome P-450 CYP1A2,
http://linkedlifedata.com/resource/pubmed/chemical/Cytochrome P-450 CYP2B1,
http://linkedlifedata.com/resource/pubmed/chemical/Cytochrome P-450 CYP2E1,
http://linkedlifedata.com/resource/pubmed/chemical/Cytochrome P-450 CYP3A,
http://linkedlifedata.com/resource/pubmed/chemical/Cytochrome P-450 Enzyme System,
http://linkedlifedata.com/resource/pubmed/chemical/Cytochromes,
http://linkedlifedata.com/resource/pubmed/chemical/Glucosinolates,
http://linkedlifedata.com/resource/pubmed/chemical/Oxidoreductases, N-Demethylating,
http://linkedlifedata.com/resource/pubmed/chemical/Steroid 16-alpha-Hydroxylase,
http://linkedlifedata.com/resource/pubmed/chemical/Steroid Hydroxylases,
http://linkedlifedata.com/resource/pubmed/chemical/cytochrome P-448
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0007-1145
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
80
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
231-4
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:9875062-Animals,
pubmed-meshheading:9875062-Aryl Hydrocarbon Hydroxylases,
pubmed-meshheading:9875062-Brassica,
pubmed-meshheading:9875062-Cytochrome P-450 CYP1A2,
pubmed-meshheading:9875062-Cytochrome P-450 CYP2B1,
pubmed-meshheading:9875062-Cytochrome P-450 CYP2E1,
pubmed-meshheading:9875062-Cytochrome P-450 CYP3A,
pubmed-meshheading:9875062-Cytochrome P-450 Enzyme System,
pubmed-meshheading:9875062-Cytochromes,
pubmed-meshheading:9875062-Germ-Free Life,
pubmed-meshheading:9875062-Glucosinolates,
pubmed-meshheading:9875062-Intestines,
pubmed-meshheading:9875062-Liver,
pubmed-meshheading:9875062-Male,
pubmed-meshheading:9875062-Microsomes, Liver,
pubmed-meshheading:9875062-Oxidoreductases, N-Demethylating,
pubmed-meshheading:9875062-Rats,
pubmed-meshheading:9875062-Rats, Inbred F344,
pubmed-meshheading:9875062-Steroid 16-alpha-Hydroxylase,
pubmed-meshheading:9875062-Steroid Hydroxylases
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pubmed:year |
1998
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pubmed:articleTitle |
Effects of the bacterial status of rats on the changes in some liver cytochrome P450 (EC 1.14.14.1) apoproteins consequent to a glucosinolate-rich diet.
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pubmed:affiliation |
INRA, Unité d'Ecologie et de Physiologie du Système Digestif, Centre de Recherches de Jouy-en-Josas, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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