Oocyte destruction by polycyclic aromatic hydrocarbons is not linked to the inducibility of ovarian aryl hydrocarbon (benzo(a)pyrene) hydroxylase activity in (DBA/2N X C57BL/6N) F1 X DBA/2N backcross mice. 1982

D R Mattison, and M S Nightingale

The role of the Ah locus and ovarian aryl hydrocarbon (benzo(a)pyrene) hydroxylase activity (AHH, EC 1.14.14.1) in ovotoxicity produced by the polycyclic aromatic hydrocarbons benzo(a)pyrene (BP), 3-methylcholanthrene (3-MC), and 7,12-dimethylbenz(a)anthracene (DMBA) was explored in Ah-responsive and Ah-nonresponsive (DBA/2N X C57BL/6N) F1 X DBA/2N backcross (F1 X D2) mice. The F1 X D2 backcross mice were phenotyped by zoxazolamine muscle paralysis time and separated into responsive and nonresponsive groups. Basal ovarian AHH activity was similar in both responsive and nonresponsive phenotypes (0.2 fluorescence units/mg/30 minutes). After treatment with one of the three polycyclic hydrocarbons (100 mg/kg, IP), ovarian AHH activity was induced only in the responsive F1 X D2 phenotype (0.4 fluorescence units/mg/30 minutes), demonstrating that inducibility of ovarian AHH activity is associated with the Ahb allele. Although responsive and nonresponsive backcross mice difference in inducibility of ovarian AHH activity, no difference was observed in the rate of, or sensitivity to, primordial oocyte destruction by the three tested polycyclic hydrocarbons. At 15 days after treatment with a single injection of BP (100 mg/kg, IP), approximately 30% of the primordial oocytes were destroyed in both responsive and nonresponsive F1 X D2 mice. The time course for oocyte destruction over the 15-day observation period was similar in both phenotypes. DMBA (100 mg/kg, IP) destroyed all of the primordial oocytes between 9 and 12 days after treatment with similar time courses in both responsive and nonresponsive phenotypes. Treatment with 3-MC (100 mg/kg, IP) destroyed approximately 40% and 70% of the primordial oocytes in responsive and nonresponsive F1 X D2 mice, respectively. Although ovarian metabolism of polycyclic hydrocarbons is necessary for ovotoxicity, oocyte destruction is not linked to the Ah locus. Sensitivity to, or the time course of, ovotoxicity by polycyclic aromatic hydrocarbons most likely reflects the biological sum of the processes of metabolic activation, detoxication, and repair and cannot be simply represented by a single enzymatic assay such as ovarian AHH activity.

UI MeSH Term Description Entries
D008748 Methylcholanthrene A carcinogen that is often used in experimental cancer studies. 20-Methylcholanthrene,3-Methylcholanthrene,20 Methylcholanthrene,3 Methylcholanthrene
D009865 Oocytes Female germ cells derived from OOGONIA and termed OOCYTES when they enter MEIOSIS. The primary oocytes begin meiosis but are arrested at the diplotene state until OVULATION at PUBERTY to give rise to haploid secondary oocytes or ova (OVUM). Ovocytes,Oocyte,Ovocyte
D010053 Ovary The reproductive organ (GONADS) in female animals. In vertebrates, the ovary contains two functional parts: the OVARIAN FOLLICLE for the production of female germ cells (OOGENESIS); and the endocrine cells (GRANULOSA CELLS; THECA CELLS; and LUTEAL CELLS) for the production of ESTROGENS and PROGESTERONE. Ovaries
D010063 Ovum A mature haploid female germ cell extruded from the OVARY at OVULATION. Egg,Egg, Unfertilized,Ova,Eggs, Unfertilized,Unfertilized Egg,Unfertilized Eggs
D011083 Polycyclic Compounds Compounds which contain two or more rings in their structure. Compounds, Polycyclic
D004790 Enzyme Induction An increase in the rate of synthesis of an enzyme due to the presence of an inducer which acts to derepress the gene responsible for enzyme synthesis. Induction, Enzyme
D005260 Female Females
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D001189 Aryl Hydrocarbon Hydroxylases A large group of cytochrome P-450 (heme-thiolate) monooxygenases that complex with NAD(P)H-FLAVIN OXIDOREDUCTASE in numerous mixed-function oxidations of aromatic compounds. They catalyze hydroxylation of a broad spectrum of substrates and are important in the metabolism of steroids, drugs, and toxins such as PHENOBARBITAL, carcinogens, and insecticides. Microsomal Monooxygenases,Xenobiotic Monooxygenases,Hydroxylases, Aryl Hydrocarbon,Monooxygenases, Microsomal,Monooxygenases, Xenobiotic
D001579 Benzopyrene Hydroxylase A drug-metabolizing, cytochrome P-448 (P-450) enzyme which catalyzes the hydroxylation of benzopyrene to 3-hydroxybenzopyrene in the presence of reduced flavoprotein and molecular oxygen. Also acts on certain anthracene derivatives. An aspect of EC 1.14.14.1. Benzopyrene-3-Monooxygenase,Benzo(a)pyrene Hydroxylase,Benzo(a)pyrene Monooxygenase,Benzopyrene 3 Monooxygenase,Hydroxylase, Benzopyrene

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