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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
8
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pubmed:dateCreated |
1997-10-20
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pubmed:abstractText |
There exists a diversity of pathways in mammalian cells serving to activate primary aromatic amines. 1 N-Oxidative mixed-function turnover usually involves participation of the cytochrome P450 superfamily, while catalysis by the flavin-containing monooxygenases is restricted to a few amines capable of forming imine tautomers. Surprisingly, haemoglobin metabolizes cytotoxic and carcinogenic arylamines via a monooxygenase-like mechanism, but peroxygenase activity is also operative. 2 In extrahepatic tissues that exhibit only a low level of monooxygenases, peroxidative transformations, as are brought about by prostaglandin H synthase, myeloperoxidase or lactoperoxidase, predominate in amine activation. Non-mammalian peroxidases frequently used as model systems include horseradish peroxidase and chloroperoxidase. 3 Non-enzymatic, light-induced conversion of aromatic amines to free radical or N-oxy products proceeds either via direct photolysis of the nitrogenous compounds or through attack by lipid-derived reactive intermediates generated during irradiation. 4 The interplay of the various tissue-specific processes of arylamine activation serves to explain differences in susceptibility toward the biological actions of primary aromatic amines.
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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/Amines,
http://linkedlifedata.com/resource/pubmed/chemical/Cytochrome P-450 Enzyme System,
http://linkedlifedata.com/resource/pubmed/chemical/Hydrocarbons,
http://linkedlifedata.com/resource/pubmed/chemical/Oxygen,
http://linkedlifedata.com/resource/pubmed/chemical/Peroxidase
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0960-3271
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
16
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
441-8
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pubmed:dateRevised |
2005-11-16
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pubmed:meshHeading |
pubmed-meshheading:9292284-Amines,
pubmed-meshheading:9292284-Animals,
pubmed-meshheading:9292284-Biotransformation,
pubmed-meshheading:9292284-Cytochrome P-450 Enzyme System,
pubmed-meshheading:9292284-Humans,
pubmed-meshheading:9292284-Hydrocarbons,
pubmed-meshheading:9292284-Oxygen,
pubmed-meshheading:9292284-Peroxidase,
pubmed-meshheading:9292284-Species Specificity
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pubmed:year |
1997
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pubmed:articleTitle |
Primary aromatic amines: their N-oxidative bioactivation.
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pubmed:affiliation |
Walther-Straub-Institut für Pharmokologie und Toxikologie, Universität München, Germany.
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pubmed:publicationType |
Journal Article,
Review
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