Microsomal Metabolism of Dimethylnitrosamine and the Cytochrome P-450 Dependency of Its Activation to a Mutagen

Peter Czygan; Helmut Greim; Anthony J. Garro; Ferenc Hutterer; Fenton Schaffner; Hans Popper; Otto Rosenthal

Microsomal Metabolism of Dimethylnitrosamine and the Cytochrome P-450 Dependency of Its Activation to a Mutagen

Peter Czygan, Helmut Greim, Anthony J. Garro, Ferenc Hutterer, Fenton Schaffner, Hans Popper, Otto Rosenthal

Research output: Contribution to journal › Article › peer-review

223 Scopus citations

Abstract

Oxidative demethylation of the secondary carcinogen dimethylnitrosamine (DMN) by isolated mouse liver micro-somes and the activation of DMN to a bacterial mutagen followed similar kinetics. The rates of demethylation and DMN activation increased following induction of the cytochrome P-450 mixed-function oxidase system by polychlorinated biphenyls. Both the oxidative demethylation and the activation of DMN to a mutagen were inhibited by carbon monoxide, and the inhibition was maximally reversed by monochromatic light at 450 nm. These observations indicate that both microsomal metabolism and activation of DMN to a mutagen are cytochrome P-450 dependent.

Original language	English
Pages (from-to)	2983-2986
Number of pages	4
Journal	Cancer Research
Volume	33
Issue number	11
State	Published - Nov 1973
Externally published	Yes

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title = "Microsomal Metabolism of Dimethylnitrosamine and the Cytochrome P-450 Dependency of Its Activation to a Mutagen",

abstract = "Oxidative demethylation of the secondary carcinogen dimethylnitrosamine (DMN) by isolated mouse liver micro-somes and the activation of DMN to a bacterial mutagen followed similar kinetics. The rates of demethylation and DMN activation increased following induction of the cytochrome P-450 mixed-function oxidase system by polychlorinated biphenyls. Both the oxidative demethylation and the activation of DMN to a mutagen were inhibited by carbon monoxide, and the inhibition was maximally reversed by monochromatic light at 450 nm. These observations indicate that both microsomal metabolism and activation of DMN to a mutagen are cytochrome P-450 dependent.",

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year = "1973",

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T1 - Microsomal Metabolism of Dimethylnitrosamine and the Cytochrome P-450 Dependency of Its Activation to a Mutagen

AU - Czygan, Peter

AU - Greim, Helmut

AU - Garro, Anthony J.

AU - Hutterer, Ferenc

AU - Schaffner, Fenton

AU - Popper, Hans

AU - Rosenthal, Otto

PY - 1973/11

Y1 - 1973/11

N2 - Oxidative demethylation of the secondary carcinogen dimethylnitrosamine (DMN) by isolated mouse liver micro-somes and the activation of DMN to a bacterial mutagen followed similar kinetics. The rates of demethylation and DMN activation increased following induction of the cytochrome P-450 mixed-function oxidase system by polychlorinated biphenyls. Both the oxidative demethylation and the activation of DMN to a mutagen were inhibited by carbon monoxide, and the inhibition was maximally reversed by monochromatic light at 450 nm. These observations indicate that both microsomal metabolism and activation of DMN to a mutagen are cytochrome P-450 dependent.

AB - Oxidative demethylation of the secondary carcinogen dimethylnitrosamine (DMN) by isolated mouse liver micro-somes and the activation of DMN to a bacterial mutagen followed similar kinetics. The rates of demethylation and DMN activation increased following induction of the cytochrome P-450 mixed-function oxidase system by polychlorinated biphenyls. Both the oxidative demethylation and the activation of DMN to a mutagen were inhibited by carbon monoxide, and the inhibition was maximally reversed by monochromatic light at 450 nm. These observations indicate that both microsomal metabolism and activation of DMN to a mutagen are cytochrome P-450 dependent.

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SN - 0008-5472

VL - 33

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JO - Cancer Research

JF - Cancer Research

IS - 11

ER -

Microsomal Metabolism of Dimethylnitrosamine and the Cytochrome P-450 Dependency of Its Activation to a Mutagen

Abstract

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