Metabolism of arylhydrazines by cytochrome P-450 mixed function oxidases and prostaglandin(H)synthase from mouse lungs

Terence Lawson

doi:10.1016/0304-3835(87)90010-3

Metabolism of arylhydrazines by cytochrome P-450 mixed function oxidases and prostaglandin(H)synthase from mouse lungs

Terence Lawson

Eppley Institute for Cancer Research

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

10 Scopus citations

Abstract

The arylhydrazines 4-methylphenylhydrazine hydrochloride, N′-acetyl-4-methylphenylhydrazine and N′-acetyl-4-hydroxymethylphenylhydrazine (HMPH) were metabolized by ram seminal vesicle prostaglandin(H)synthase (P(H)S) and by cytochrome P-450- and P(H)S-dependent enzymes from mouse lung. Based on the K_m-values, the cytochrome P-450 enzymes were the most efficient, suggesting that they would be responsible for the metabolic activation of these compounds in vivo. Cytochrome P-450-dependent metabolism was inhibited by metyrapone and SKF-525A, ruling out the involvement of flavin mono-oxygenase. Agaritine, an arylhydrazide, was poorly metabolized by both systems.

Original language	English (US)
Pages (from-to)	193-200
Number of pages	8
Journal	Cancer Letters
Volume	34
Issue number	2
DOIs	https://doi.org/10.1016/0304-3835(87)90010-3
State	Published - Feb 1987

ASJC Scopus subject areas

Oncology
Cancer Research

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10.1016/0304-3835(87)90010-3

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title = "Metabolism of arylhydrazines by cytochrome P-450 mixed function oxidases and prostaglandin(H)synthase from mouse lungs",

abstract = "The arylhydrazines 4-methylphenylhydrazine hydrochloride, N′-acetyl-4-methylphenylhydrazine and N′-acetyl-4-hydroxymethylphenylhydrazine (HMPH) were metabolized by ram seminal vesicle prostaglandin(H)synthase (P(H)S) and by cytochrome P-450- and P(H)S-dependent enzymes from mouse lung. Based on the Km-values, the cytochrome P-450 enzymes were the most efficient, suggesting that they would be responsible for the metabolic activation of these compounds in vivo. Cytochrome P-450-dependent metabolism was inhibited by metyrapone and SKF-525A, ruling out the involvement of flavin mono-oxygenase. Agaritine, an arylhydrazide, was poorly metabolized by both systems.",

author = "Terence Lawson",

note = "Funding Information: and a Laboratory Cancer Research Core grant",

year = "1987",

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doi = "10.1016/0304-3835(87)90010-3",

language = "English (US)",

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journal = "Cancer Letters",

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T1 - Metabolism of arylhydrazines by cytochrome P-450 mixed function oxidases and prostaglandin(H)synthase from mouse lungs

AU - Lawson, Terence

N1 - Funding Information: and a Laboratory Cancer Research Core grant

PY - 1987/2

Y1 - 1987/2

N2 - The arylhydrazines 4-methylphenylhydrazine hydrochloride, N′-acetyl-4-methylphenylhydrazine and N′-acetyl-4-hydroxymethylphenylhydrazine (HMPH) were metabolized by ram seminal vesicle prostaglandin(H)synthase (P(H)S) and by cytochrome P-450- and P(H)S-dependent enzymes from mouse lung. Based on the Km-values, the cytochrome P-450 enzymes were the most efficient, suggesting that they would be responsible for the metabolic activation of these compounds in vivo. Cytochrome P-450-dependent metabolism was inhibited by metyrapone and SKF-525A, ruling out the involvement of flavin mono-oxygenase. Agaritine, an arylhydrazide, was poorly metabolized by both systems.

AB - The arylhydrazines 4-methylphenylhydrazine hydrochloride, N′-acetyl-4-methylphenylhydrazine and N′-acetyl-4-hydroxymethylphenylhydrazine (HMPH) were metabolized by ram seminal vesicle prostaglandin(H)synthase (P(H)S) and by cytochrome P-450- and P(H)S-dependent enzymes from mouse lung. Based on the Km-values, the cytochrome P-450 enzymes were the most efficient, suggesting that they would be responsible for the metabolic activation of these compounds in vivo. Cytochrome P-450-dependent metabolism was inhibited by metyrapone and SKF-525A, ruling out the involvement of flavin mono-oxygenase. Agaritine, an arylhydrazide, was poorly metabolized by both systems.

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Metabolism of arylhydrazines by cytochrome P-450 mixed function oxidases and prostaglandin(H)synthase from mouse lungs

Abstract

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