Involvement of lauric acid hydroxylase in the activation of β-substituted nitrosamines

T. A. Lawson

Research output: Contribution to journalArticle

7 Scopus citations

Abstract

The mutagenicity of N-nitrosobis (2-hydroxypropyl) amine (BHP), N-nitrosobis(2-oxopropyl)amine (BOP) and N-nitroso-(2-hydroxy-propyl) (2-oxopropyl) amine (HPOP) was measured in V79 cells. Hepatocytes, used to metabolize (activate) the nitrosamines, were isolated from untreated Syrian hamsters (control) and hamsters treated with clofibrate (CLO) or dehydroepian-drosterone (DHEA) in vivo. BHP and HPOP mutagenicity increased 3- and 2-fold when hepatocytes from CLO- and DHEA-treated hamsters were used. BOP mutagenicity did not increase. 10-Undecynoic acid, a lauric acid hydroxylase inhibitor, inhibited the increase in BHP and HPOP mutagenicity by 80-90% but did not affect that of BOP. Antimycin A1, a fatty acyl coenzyme A β-oxidase inhibitor did not affect the mutagenicity of these nitrosamines. Lauric acid hydroxylase, probably omega-1 hydroxylase (cytochrome P-450 IVA2), appears to be involved in the activation of BHP and HPOP.

Original languageEnglish (US)
Pages (from-to)177-182
Number of pages6
JournalCancer Letters
Volume59
Issue number2
DOIs
Publication statusPublished - Aug 1991

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Keywords

  • cytochrome P-450
  • mutagenicity
  • nitrosamines
  • pancreas

ASJC Scopus subject areas

  • Oncology
  • Cancer Research

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