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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1992-6-16
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pubmed:abstractText |
Rats fed an ethanol-containing diet for 4 weeks showed a 3- to 5-fold increase over isocalorically pair-fed controls with respect to cytosolic NAD(P)H-quinone oxidoreductase (NQOR) (E.C.1.6.99.2) with both menadione and dichlorophenol-indophenol as substrates. Rates of NAD(P)H-dependent p-nitrosophenol (pNSP) reduction catalyzed by rat liver cytosolic fractions were increased 1.5- to 2-fold upon pretreatment of the animal with ethanol. NQOR contributed almost exclusively to the NADPH-dependent C-nitrosoreductase activity in cytosol as judged by the strong inhibition of the reaction by dicoumarol. In contrast, NADH-dependent C-nitrosoreductase activity was inhibited 70-80% by pyrazole and thus may be attributed mainly to alcohol dehydrogenase(s). Highly purified rat liver cytosolic NQOR catalyzed the NADH- and NADPH-dependent reduction of pNSP to p-aminophenol. We therefore suggest that ethanol ingestion enhances the reduction of the C-nitrosoaromatics formed upon cytosolic metabolism of arylamines or nitroarenes by two mechanisms. Increased NADPH-dependent reduction is mediated by the induction of cytosolic NQOR while an NADH-dependent pathway responds to the increased availability of reduced cofactor upon ethanol ingestion and involves mainly the alcohol dehydrogenase-mediated reduction of such compounds.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/4-aminophenol,
http://linkedlifedata.com/resource/pubmed/chemical/4-nitrosophenol,
http://linkedlifedata.com/resource/pubmed/chemical/Alcohol Dehydrogenase,
http://linkedlifedata.com/resource/pubmed/chemical/Alcohol Oxidoreductases,
http://linkedlifedata.com/resource/pubmed/chemical/Aminophenols,
http://linkedlifedata.com/resource/pubmed/chemical/Ethanol,
http://linkedlifedata.com/resource/pubmed/chemical/Mutagens,
http://linkedlifedata.com/resource/pubmed/chemical/NAD(P)H Dehydrogenase (Quinone),
http://linkedlifedata.com/resource/pubmed/chemical/Nitroso Compounds,
http://linkedlifedata.com/resource/pubmed/chemical/alcohol oxidase
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0003-9861
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
295
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
223-9
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:1586150-Alcohol Dehydrogenase,
pubmed-meshheading:1586150-Alcohol Oxidoreductases,
pubmed-meshheading:1586150-Aminophenols,
pubmed-meshheading:1586150-Animals,
pubmed-meshheading:1586150-Cytosol,
pubmed-meshheading:1586150-Ethanol,
pubmed-meshheading:1586150-Hydrogen-Ion Concentration,
pubmed-meshheading:1586150-Liver,
pubmed-meshheading:1586150-Male,
pubmed-meshheading:1586150-Mutagens,
pubmed-meshheading:1586150-NAD(P)H Dehydrogenase (Quinone),
pubmed-meshheading:1586150-Nitroso Compounds,
pubmed-meshheading:1586150-Oxidation-Reduction,
pubmed-meshheading:1586150-Rats,
pubmed-meshheading:1586150-Rats, Inbred Strains
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pubmed:year |
1992
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pubmed:articleTitle |
Role of cytosolic NAD(P)H-quinone oxidoreductase and alcohol dehydrogenase in the reduction of p-nitrosophenol following chronic ethanol ingestion.
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pubmed:affiliation |
Department of Biochemistry, Louisiana State University, Baton Rouge 70803.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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