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

R. C. Bast; J. P. Whitlock; H. Miller; H. J. Rapp; H. V. Gelboin

doi:10.1038/250664a0

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

R. C. Bast, J. P. Whitlock, H. Miller, H. J. Rapp, H. V. Gelboin

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Abstract

MICROSOMAL mixed-function oxygenases metabolise a variety of exogenous compounds, including drugs, pesticides and carcinogens, as well as endogenous substances such as steroids^1,2. 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 forms^1-4. Hydroxylase activity and cytochrome P-450 have been found in various tissues of animals^1,2 and man^5-12. 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.

Original language	English (US)
Pages (from-to)	664-665
Number of pages	2
Journal	Nature
Volume	250
Issue number	5468
DOIs	https://doi.org/10.1038/250664a0
State	Published - 1974
Externally published	Yes

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title = "Aryl hydrocarbon (benzo(a)pyrene) hydroxylase in human peripheral blood monocytes",

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.",

author = "Bast, {R. C.} and Whitlock, {J. P.} and H. Miller and Rapp, {H. J.} and Gelboin, {H. V.}",

year = "1974",

doi = "10.1038/250664a0",

language = "English (US)",

volume = "250",

pages = "664--665",

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T1 - Aryl hydrocarbon (benzo(a)pyrene) hydroxylase in human peripheral blood monocytes

AU - Bast, R. C.

AU - Whitlock, J. P.

AU - Miller, H.

AU - Rapp, H. J.

AU - Gelboin, H. V.

PY - 1974

Y1 - 1974

N2 - 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.

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

Abstract

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