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Aryl hydrocarbon (benzo(a)pyrene) hydroxylase in human peripheral blood monocytes

Nature volume 250, pages 664–665 (1974)Cite this article

Abstract

MICROSOMAL mixed-function oxygenases metabolise a variety of exogenous compounds, including drugs, pesticides and carcinogens, as well as endogenous substances such as steroids1,2. One oxygenase, aryl hydrocarbon hydroxylase (AHH), is important in both the detoxification of some carcinogenic polycyclic hydrocarbons and the activation of others to more carcinogenic forms1–4. Hydroxylase activity and cytochrome P-450 have been found in various tissues of animals1,2 and man5–12. AHH activity increases in many tissues after treatment with polycyclic hydrocarbons. In certain inbred mouse strains this increase appears to be regulated by a single autosomal dominant gene13, and a correlation between enzyme levels and susceptibility to methylcholanthrene-induced tumorigenesis has been reported14. Data obtained by Shaw and his colleagues point to genetic regulation of AHH in human populations15.

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Authors and Affiliations

  1. Biology Branch and Chemistry Branch, National Cancer Institute, Bethesda, Maryland, 20014

    R. C. BAST JUN., J. P. WHITLOCK JUN., H. MILLER, H. J. RAPP & H. V. GELBOIN

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  1. R. C. BAST JUN.
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  2. J. P. WHITLOCK JUN.
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  3. H. MILLER
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  4. H. J. RAPP
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  5. H. V. GELBOIN
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BAST, R., WHITLOCK, J., MILLER, H. et al. Aryl hydrocarbon (benzo(a)pyrene) hydroxylase in human peripheral blood monocytes. Nature 250, 664–665 (1974). https://doi.org/10.1038/250664a0

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