@article{VivianiDaenikenSchlatteretal.1980,
  author    = {Viviani, A. and D{\"a}niken, A. von and Schlatter, C. and Lutz, Werner K.},
  title     = {Effect of selected induction of microsomal and nuclear aryl hydrocarbon monooxygenase and epoxide hydrolase as well as cytoplasmic glutathione S-epoxide transferase on the covalent binding of the carcinogen benzo(a)pyrene to rat liver DNA in vivo},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-61114},
  year      = {1980},
  abstract  = {Groups of four adult male rats [ZUR:SIV -Z] were pretreated with corn oil (control; 2 ml/kg/day i. p. for 3 days), trans-stilbene-oxide (SO; 200 mg/kg/day i. p. for 2 days), 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD; 10 \(\mu\)g/kg i. p. once, 4 days before killing), phenobarbital (PB; 1 gjliter in the drinking water for 8 days), and dieldrin (20 mg/kg/day i. p. for 3 or 9 days). They received an injection of [G-\(^3\)H]benzo(a)pyrene (BaP, 31 \(\mu\)g/kg, 7.4. 10\(^9\) dpm/kg; i. v.) 16 h before killing. In the liver of each rat, five enzymatic activities and the covalent binding of BaP to DNA have been determined. The rnicrosomal aryl hydrocarbon monooxygenase activity (AHM) ranged frorn 75\% of control (SO) to 356\% (TCDD), the nuclear AHM from 63\% (SO) to 333\% (TCDD). Microsomal epoxide hydrolase activity (EH) was induced up to 238\% (PB), nuclear EH ranged from 86\% (TCDD) to 218\% (PB). A different extent of induction was observed in the two compartments. Highest induction of glutathione S-epoxide transferase activity (GST) was found with PB (202\%). The DNA binding of BaP was modulated within 79\% (dieldrin, 9 days) and 238\% of control (TCDD). An enzyme digest of control DNA was analysed by Sephadex LH-20 chromatography. Multiple linear regression analysis with all data expressedas o/o of control yielded the following equation: DNA Binding = 1.49 · Microsomal AHM- 1.07 · Nuclear AHM+ 0.33 · Microsomal EH- 0.52 · N uclear EH+ 0.11 · Cytoplasmic GST + 58.2. From this analysis it is concluded that (1) AHM located in the endoplasmic reticulum is most important in the formation of DNA-binding metabolites, (2) EH in the same compar.tment is not determinative in thls respect nor has it a protective effect, (3) both membrane-bound enzyme activities located in the nucleus may inactivate potential ultimate carcinogens, and ( 4) cytoplasmic GST probably cannot reduce DNA binding due to its subcellular localization.},
  subject      = {Toxikologie},
  language  = {en}
}
@article{VivianiLutz1978,
  author    = {Viviani, A. and Lutz, Werner K.},
  title     = {Modulation of the binding of the carcinogen benzo(a)pyrene to rat liver DNA in vivo by selective induction of microsomal and nuclear aryl hydrocarbon hydroxylase activity},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-61150},
  year      = {1978},
  abstract  = {The lnfluence of mlcrosomal and nuclear aryl hydrocarbon hydroxylase (AHH) actlvlty on the covalent blndlng of [G·3H]benzo(a )pyrene to rat llver DNA was evaluated in viWJ. lnductlon of mlcrosomal AHH was obtalned alter phenobarbltal treatment (160\% of control), whlch also lncreased DNA blndlng to 190\%, but left the nuclear actlvlty unchanged. Nuclear AHH was lnduced wlth dleldrln (150\%), and the blndlng was decreased to 75\%, whereaa the mlcrosomal AHH was at control Ievei. The lncreaslng effect of mlcrosomal AHH lnductlon as weil as the decreaslng effect of nuclear AHH lnductlon on the blndlng was shown clearly when the data of the Individual rata were uaed to solve the equatlon Binding = e•(mlcroeomal AHH) + b•(nuclear AHH) + c Multiple linear regresslon analysls wlth the data from 10 anlmala reaulted ln positive valuea for a and c, a negative value for b, and a good multiple correlatlon coefflclent of r = 0.974. Pretreatment wlth 3-methylcholanthrene ln· duced mlcrosomal AHH to 380\% of control and nuclear AHH to 590\% and lncreased the blndlng' to 175,.-o. The blndlng was hlgher than predlcted by the formula found, probably because the lncreaslng lnfluence of lnduced mlcrosomal AHH overahadowed the decreaslng effect of the nuclear AHH. The study ahows clearly that the blndlng of a forelgn compound to DNA in viWJ Ia dependent not only on mlcrosomal enzyme actlvltles but also on nuclear actlvltles even lf the latter are conslderably lower than thoae of mlcrosomes.},
  subject      = {Toxikologie},
  language  = {en}
}
@article{VivianiLutzSchlatter1978,
  author    = {Viviani, A. and Lutz, Werner K. and Schlatter, C.},
  title     = {Time course of the induction of aryl hydrocarbon hydroxylase in rat liver nuclei and microsomes by phenobarbital, 3-methylcholanthrene, 2,3,7,8-tetrachloro-dibenzo-p-dioxin, dieldrin and other inducers},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-61182},
  year      = {1978},
  abstract  = {Aryl hydrocarbon hydroxylase (AHH) has been measured in male rat Jiver nucJei and microsomes after treatment of adult animals with various inducers for up to 14 days. After daily i.p. injections of 3-methylcholanthrene (MC, 20 mg/kg) the nuclear activity increased to a maximum of 600 per cent of the control activity after 4 days whereas the microsomal activity was 400 per cent of control at the same date. After 12 days, both activities equilibrated at 400 per cent. A similar time course was found after a single i.p. injection of 2,3,7,8-tetrachloro-dibenzo-p-dioxin (TCDD, 0.01 mg/kg) with an induction to .500 and 300 per cent for nuclei and microsomes, respectiveJy. after 2 days, and to 400 per cent for both after 12 days. PhenobarbitaJ (PB) was given continuously in the drinking water (I g/1) and induced the microsomal activity to 200 per cent after 8 days and 170 per cent after 14 days. The nuclear activity was only slightly induced to a constant Ievei of 130 per cent between day 8 and 14. Dieldrin did not significantly increase the microsomal activity after daiJy i.p. injections (20 mg/kg), but the nuclear activity raised to 200 per cent after 3 days and levelled down tocontrol valuesafter 12 days. Other inducers tested were benz[a)anthracene (BA), hexachlorobenzene (HCB} and 1,1.1-trichloro-2,2-bis(p-chlorophenyl)ethane (DDT). The induction pattern with BA was similar tothat of MC, a modeJ compound for the group of cytochrome P448 inducers. The induction by HCB and DDT resembled that by PB. a typical cytochrome P450 inducer.},
  subject      = {Toxikologie},
  language  = {en}
}
@inproceedings{VivianiLutz1979,
  author    = {Viviani, A. and Lutz, Werner K.},
  title     = {Modulation of the in vivo covalent binding of the carcinogen benzo(a)pyrene to rat liver DNA by selective induction of microsomal and nuclear aryl hydrocarbon hydroxylase activity},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-80132},
  year      = {1979},
  abstract  = {The influence of microsomal (mAHH) and nuclear (nAHH) aryl hydrocarbon hydroxylase activity on the covalent binding of t:titiated benzo(a)pyrene to rat liver DNA was evaluated in vivo. Induction ofmAHH was obtained after phenobarbitone treatment (180\% of control), which increased DNA binding to 210\%, but left the nAHH unchanged. mAHH and nAHH were slightly indilced with dieldrin (130\% and 120\%), but the binding remairred unchanged. The increasing effect of mAHlt as weil as the possibly decreasing effect of nAHH induction on the binding became obvious when the data of 11 individual rats were used to solve the equation Binding = aX(mAHH) + bX(nAHH) + c. Multiple linear regression analysis resulted in positive values for a and c, a negative value for b, and a multiple correlation coefficient R = 0.82. An influence of other enzymes involved in the metabolism of benzo(a)pyrene cannot be excluded. The Study shows clearly that the binding of a foreign compound to DNA in vivo is not only dependent on microsomal enzyme activities but also on nuclear activities even if the latter are considerably lower than those of mic'rosomes.},
  subject      = {DNA},
  language  = {en}
}