Source:http://linkedlifedata.com/resource/pubmed/id/10355851
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5
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pubmed:dateCreated |
1999-7-15
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pubmed:abstractText |
The effect of ornithine alpha-ketoglutarate (OKG) on cytochrome P-450 enzyme activities was studied in a well-defined model of injury (burn followed by fasting then subsequent hypocaloric diet) administered to young rats for 3 d. Hepatic microsomes were prepared by ultracentrifugation and levels of cytochromes P-450 were determined spectrophotometrically. The activities of ethoxy-resorufin-O-deethylase (EROD), benzyloxy-resorufin-O-dealkylase (BROD), and erythromycin demethylase were measured as markers of P-450 1A, 2A, and 3A isotypes respectively. The level of total hepatic microsomal proteins (8 mg/mL) remained constant. The level of cytochrome P-450 (1.14+/-0.08 nmol/mg microsomal proteins) was decreased by a hypocaloric diet (23%, P = 0.003) and burn further enhanced this phenomenon (15%, P = 0.03). Both healthy and burned rats receiving OKG showed the same level of cytochrome P-450 as the rats fed ad libitum. OKG supplementation counteracted the enhancement (40%) of EROD activity induced by hypocaloric diet but did not influence BROD and erythromycin demethylase activities. OKG sustained cytochrome P-450 levels in rats fed a hypocaloric diet, even after burning. These findings indicate that OKG may favor drug metabolism in this injured population.
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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/Aryl Hydrocarbon Hydroxylases,
http://linkedlifedata.com/resource/pubmed/chemical/Cytochrome P-450 CYP1A1,
http://linkedlifedata.com/resource/pubmed/chemical/Cytochrome P-450 CYP2B1,
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/Ornithine,
http://linkedlifedata.com/resource/pubmed/chemical/Oxidoreductases, N-Demethylating,
http://linkedlifedata.com/resource/pubmed/chemical/ornithine alpha-ketoglutarate
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0899-9007
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
15
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
379-83
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:10355851-Animals,
pubmed-meshheading:10355851-Aryl Hydrocarbon Hydroxylases,
pubmed-meshheading:10355851-Burns,
pubmed-meshheading:10355851-Cytochrome P-450 CYP1A1,
pubmed-meshheading:10355851-Cytochrome P-450 CYP2B1,
pubmed-meshheading:10355851-Cytochrome P-450 CYP3A,
pubmed-meshheading:10355851-Cytochrome P-450 Enzyme System,
pubmed-meshheading:10355851-Energy Intake,
pubmed-meshheading:10355851-Male,
pubmed-meshheading:10355851-Microsomes, Liver,
pubmed-meshheading:10355851-Ornithine,
pubmed-meshheading:10355851-Oxidoreductases, N-Demethylating,
pubmed-meshheading:10355851-Rats,
pubmed-meshheading:10355851-Rats, Sprague-Dawley
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pubmed:year |
1999
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pubmed:articleTitle |
Ornithine alpha-ketoglutarate counteracts the decrease of liver cytochrome P-450 content in burned rats.
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pubmed:affiliation |
Département de Pharmacologie, Hôpital Cochin, Paris, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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