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PubMed1975

Retention of tritium during the binding of tritiated benz(a)pyrene to DNA.

Chemical conversion of generally tritiated benzo(a)pyrene to 6 and 1,6-substituted derivatives resulted in 30% and 48% loss of tritium respectively. Metabolism of [3H], [14C]-benzo(a)pyrene by rat liver microsomes yielded 3-hydroxybenzo(a)pyrene with 30% loss of tritium, a mixture of quinones with 50% loss of tritium and three dihydrodiol metabolites which had retained all the tritium of the parent hydrocarbon. DNA isolated from mouse embryo cells which had been exposed to [3H], [14C]-benzo(a)pyrene, and DNA with this hydrocarbon bound following in vitro rat liver microsomal incubation were degraded enzymically and the hydrocarbon-deoxyribonucleoside products isolated. The tritium contents of the products obtained from both DNA samples were very close to those of the original double labelled benzo(a)pyrene. These results are inconsistent with a phenol or quinone intermediate being responsible for the reaction with DNA, but fully consistent with a diol epoxide intermediate as proposed by Sims et al. (1974).

Animals↗
PubMed1976

Rat liver microsome-mediated binding of benzo(a)pyrene metabolites to DNA.

Individual metabolites of benzo (a) pyrene were isolated from rat liver microsomal incubation of the parent hydrocarbon, and subsequently bound to DNA in separate incubations with microsomes. Of the metabolites examined, by far the greatest binding resulted with 7,8-dihydro-7,8-dihydroxy-benzo(a)pyrene (BP-7,8-diol); the binding od the benzo (a) pyrene phenols (BP-OH) was about 50% that of the 7,8-diol. Analysis of the hydrocarbon-deoxyribonucleoside derivatives obtained by enzymic degradation of these DNA samples revealed that the binding of BP-7,8-diol was accounted for mainly by a single product identical to one of the product identical to one of the products obtained from DNA with bound benzo(a)pyrene. Furthermore, the microsome-induced binding of BP-OH to DNA yielded mainly a single product identical in chromatographic behaviour to the major product derived from benzo(a)pyrene when bound to DNA during incubation with microsomes.

Animals↗
PubMed1990

Activation of benzo(a)pyrene-7,8-dihydrodiol in rat uterus: an in vitro study.

Peroxidatic metabolism of benzo(a)pyrene-7,8-dihydrodiol by calcium containing extracts of rat uteri was investigated. Covalently bound and soluble metabolites of benzo(a)pyrene-7,8-dihydrodiol were quantitated by radiometry and high performance liquid chromatography, respectively. 1. Uterine extracts incubated with benzo(a)pyrene-7,8-dihydrodiol activated this proximate mutagen to protein binding metabolite(s). 2. Hydrogen peroxide increased the protein binding and yielded a substantial amount of benzo(a)pyrene-trans-anti-tetrahydrotetrol, suggesting the peroxyl-type free-radical epoxidation process. 3. The results indicate that rat uterine peroxidase is able to catalyze free-radical activation of benzo(a)pyrene-7,8-dihydrodiol by epoxidation to its 9,10-dihydrodiolepoxide, a known ultimate mutagen and carcinogen.

Animals↗
PubMed2000

Use of Pyrene Spectroscopic Probes in the Study of Colloidal Systems.

The interfacial behavior of polyethylene oxide (PEO) end-labeled with the often-used fluorescent probe pyrene was monitored to asess the effect of use of such hydrophobic probes on system behavior. Mixtures of labeled and unlabeled PEO were adsorbed on silica and the resulting suspension properties noted. The suspension behavior was found to be markedly different, depending on the ratio of labeled-to-unlabeled PEO employed. While it was "safe" to use pyrene probes in amounts of 3% or less for spectroscopic investigation of PEO effects, it was found that ratios equal to, or greater than, 1 : 3 produced anomalous behavior of the silica suspensions. This was manifested in the form of decreased suspension stability, as evidenced by significantly higher settling rates. Similar experiments using free pyrene revealed that these effects could be attributed to the chemical attachment of the pyrene probe to the polyethylene oxide chain. Fluorescence spectroscopy was used to simultaneously monitor the behavior of the adsorbed polyethylene oxide molecules. These results were used to explain the observed suspension behavior as a function of the labeled-to-unlabeled polymer mixing ratio. Bridging effects facilitated by hydrophobic interaction between pyrene end groups is proposed as the reason for the observed phenomena. Copyright 2000 Academic Press.

Journal Article↗
PubMed1980

Kinetics of the inhibition of styrene oxide and benzo(a)pyrene-4,5-oxide hydration in rat liver microsomes by cadmium.

The kinetics of the inhibition by cadmium of styrene oxide and benzo(a)pyrene-4,5-oxide hydration were studied in a microsomal preparation from rat liver. Cadmium inhibited the hydration of styrene oxide in an apparently noncompetitive manner, whereas the inhibition of benzo(a)pyrene-4,5-oxide hydration showed a competitive mechanism. Styrene oxide inhibited the hydration of benzo(a)pyrene-4,5-oxide competitively and cyclohexene oxide inhibited the hydration of both styrene oxide and benzo(a)pyrene-4,5-oxide competitively. The present data suggest that cadmium is bound near the active centre of the enzyme. Occupation of this site by cadmium inhibits the enzymic hydration of the polycyclic benzo(a)pyrene-4,5-oxide molecule competitively, and that of the smaller monocyclic alkene oxide of styrene noncompetitively. The estimated Ki values were below 10 mu mol for hydration of both substrates indicating that cadmium is a very potent inhibitor of epoxide hydration.

Animals↗
PubMed1980

The non-covalent binding of benzo[a]pyrene and its hydroxylated metabolites to intracellular proteins and lipid bilayers.

The non-covalent interactions of benzo[a]pyrene (BP) and several of its hydroxylated metabolites with ligandin, aminoazodye-binding protein A (Z-protein, fatty acid binding protein) and lecithin bilayers have been studied by equilibrium dialysis, an adsorption technique and fluorescence spectroscopy. Binding affinities expressed as v/c (where v = moles of BP or BP metabolite bound per mole of protein or lipid and c = unbound concentration), were measured at concentrations sufficiently low that there was no self-association of the unbound compounds as judged by their fluorescence characteristics. 3-Hydroxybenzo[a]pyrene (BP-3-phenol), 4,5-dihydro-4,5-dihydroxybenzo[a]pyrene (BP-4,5-dihydrodiol) and 7,8-dihydro-7,8-dihydroxybenzo[a]pyrene (BP-7,8-dihydrodiol) bind more strongly (v/c = 10(5)-5 x 10(5) l x mol-1) to all three binders than does BP itself (v/c = 10(4)-7 x 10(4) l x mol-1). 9,10-Dihydro-9,10-dihydroxybenzo[a]pyrene (BP-9,10-dihydrodiol) binds to ligandin with an affinity similar to those of the other BP metabolites studied here, but binds much less strongly to both protein A and lecithin (v/c = 10(4) and 3 x 10(4) x mol-1, respectively). The low affinity of BP-9,10-dihydrodiol for lecithin would account for earlier findings that on incubation of BP with isolated rat hepatocytes, this metabolite egressed from the cells to the extracellular medium much more readily than either BP-4,5-dihydrodiol or BP-7,8-dihydrodiol. Calculations based on these results suggest that within hepatocytes BP and its metabolites, including BP-9,10-dihydrodiol, will be found almost exclusively associated (> 98%) with lipid membranes.

Adsorption↗
PubMed1983

Hydrolysis of 1-triacontanoyl-2-(pyren-1-yl)hexanoyl-sn-glycero-3-phosphocholine by human pancreatic phospholipase A2.

A novel fluorescent phospholipid analogue, 1-triacontanoyl-2-(pyren-1-yl)hexanoyl-sn-glycero-3-phosphocholine (C30PHPC) was employed as a substrate for human pancreatic phospholipase A2. C30PHPC has a main endothermic phase transition with Tm at 46 degrees C as determined by differential scanning calorimetry (DSC). For an aqueous dispersion of C30PHPC the ratio of the intensities of pyrene excimer and monomer fluorescence emission, (IE/IM) has a maximum between 32 and 36 degrees C. The excimer emission intensity (at 480 nm) exceeds the monomer emission intensity (at 400 nm) 6.5-fold thus indicating a close packing of the phospholipid pyrene moieties in the lipid phase. C30PHPC has a limiting mean molecular area of 37 A2 at surface pressure 35 dyn cm-1 as judged by the compression isotherm at an air-water interphase. The hydrolysis of C30PHPC by human pancreatic phospholipase A2 was followed by monitoring the increase in the pyrene monomer fluorescence emission intensity occurring as a consequence of transfer of the reaction product, pyren-1-yl hexanoic acid into the aqueous phase. The enzyme reaction exhibited an apparent Km of 2.0 microM substrate. Calcium at a concentration of 0.2 mM activated the enzyme 4-fold. Maximal hydrolytic rates were obtained at 45 degrees C and at pH between 5.5 and 6.5. The enzyme reaction could be inhibited by 5 mM EDTA, confirming the absolute requirement for Ca2+ of this enzyme. The present fluorimetric assay easily detects hydrolysis of C30PHPC in the pmol min-1 range. Accordingly, less than nanogram levels of human pancreatic phospholipase A2 can be detected.

Fluorescent Dyes↗
PubMed1979

DNA--benzo[a]pyrene adducts formed in a Salmonella typhimurium mutagenesis assay system.

The DNA adducts formed in Salmonella typhimurium when bacteria are incubated with radioactive benzo[a]pyrene and liver microsomal enzymes from several sources has been investigated. When enzyme preparations from Aroclor I254 or 3-methylcholanthrene induced C57BL/6N (B6) mice were used to mediate activation, the predominant product was an adduct between the 10 position of 7 beta, 8 alpha-dihydroxy-9 alpha, 10 alpha epoxy-7,8,9,10-tetrahydrobenzo[a]pyrene and the N-2 position of deoxyguanosine. Similar results were obtained with human liver and with Aroclor-induced rat-liver enzyme preparations. This adduct is also the major DNA product previously found when human tissues or certain rodent cells were incubated with benzo[a]pyrene. On the other hand, when activation of benzo[a]pyrene was mediated by a phenobarbital-induced B6 mouse-liver enzyme preparation, the extent of binding was quite low and the profile of DNA adducts in S. typhimurium DNA was quite different. Thus, under appropriate conditions, the activation and DNA binding of benzo[a]pyrene inthe microsome mediated S. typhimurium mutagenesis assay generally resembles that seen in intact mammalian cells. Caution must be exercised, however, in the choice of microsome-activation systems.

Animals↗
PubMed1982

Test-condition-dependent influence of harman and nonharman on benzo[a]pyrene mutagenesis in Salmonella.

The enhancing or decreasing effect of harman or norharman on benzo[a]pyrene mutagenesis depends mainly on the metabolizing system (S9) used. When mammalian activation was performed by using liver homogenates from mice induced by 3-methylcholanthrene, phenobarbital or Aroclor 1254, then the mutagenicity of benzo[a]pyrene in Salmonella typhimurium TA98 decreased upon addition of harman or norharman. In the presence of rat-liver homogenate induced by Aroclor 1154, however, harman enhanced the number of benzo[a]pyrene revertants, whereas norharman did not show any significant alteration of the benzo[a]pyrene mutagenicity. Further tests carried out with phenobarbital-induced mouse-liver homogenate showed that, within certain limits, neither variations of the amount of S9 extract nor the amount of the cofactors nor the relative proportions of the test substances had any influence on the antagonistic effect of harman or norharman on the benzo[a]pyrene mutagenesis.

Alkaloids↗
PubMedDate not supplied

Nitroreduction of 6-nitrobenzo[a]pyrene: a potential activation pathway in humans.

6-Nitrobenzo[a]pyrene, an environmental pollutant, was metabolized by human intestinal microflora to 6-nitrosobenzo[a]pyrene and 6-aminobenzo[a]pyrene. The two-electron reduction product 6-nitrosobenzo[a]pyrene exhibited strong direct-acting mutagenicity in the Salmonella typhimurium assay. These results imply that 6-nitrobenzo[a]pyrene can be hazardous to human health via a nitroreduction activation pathway and opens the possibility that other nitro-polycyclic aromatic hydrocarbons that are not direct-acting mutagens may be activated in vivo by a similar mechanism.

Benzopyrenes↗
PubMed1979

Metabolism of benzo[a]pyrene in isolated human scalp hair follicles.

Human scalp hair follicles contain an enzyme system that metabolizes the carcinogen benzo[a]pyrene. The major ethyl acetate soluble metabolites are 7,8-dihydro-7,8-dihydroxybenzo[a]pyrene,9,10-dihydro-9,10-dihydroxybenzo[a]pyrene and 3-hydroxybenzo[a]pyrene. Addition of 1,1,1-trichloropropene-2,3-oxide (TCPO), an inhibitor of epoxide hydratase, prevents the formation of the dihydrodiols. The overall metabolism can be inhibited by the addition of alpha-naphthoflavone. The metabolism of benzo[a]pyrene in a cell culture of human scalp hair follicles has also been investigated. The results show that the activity of arylhydrocarbon hydroxylase (AHH) and epoxide hydratase (EH) is maintained in culture.

Adult↗
PubMedDate not supplied

Bioactivation of benzo(a)pyrene-7,8-dihydrodiol catalyzed by lipoxygenase purified from human term placenta and conceptal tissues.

Bioactivation of 14C-benzo(a)pyrene-7,8-dihydrodiol catalyzed by lipoxygenase purified from human term placenta of nonsmoking women and intrauterine conceptal tissues (at 4 weeks of gestation) was investigated. Incubation of 14C-benzo(a)pyrene-7,8-dihydrodiol with 3 mM linoleic acid in the presence of lipoxygenase purified from either human term placenta or intrauterine conceptal tissues resulted in co-oxidation generating several soluble and protein-bound metabolites of benzo(a)pyrene-7,8-dihydrodiol. The co-oxidation was inhibited significantly by the specific lipoxygenase inhibitor, nordihydroguaiaretic acid. Substitution for the active enzyme in the reaction mixture with heat denatured enzyme resulted in almost complete abolition of benzo(a)pyrene-7,8-dihydrodiol co-oxidation. These results suggest that lipoxygenase in the placentas and intrauterine conceptal tissues is capable of metabolizing benzo(a)pyrene-7,8-dihydrodiol to several reactive metabolites and may represent one of the major xenobiotic metabolizing pathways of bioactivating chemicals in the intrauterine compartment.

Biotransformation↗
PubMed2006

Bioaccumulation of cyclopenta[cd]pyrene and benzo[ghi]fluoranthene by mussels transplanted in a coastal lagoon.

The bioaccumulation of two isomeric non-alternant non-priority polycyclic aromatic hydrocarbons (PAHs), namely cyclopenta[cd]pyrene and benzo[ghi]fluoranthene, was investigated in caged mussels (Mytilus galloprovincialis) exposed for 30 days in three sites of a coastal lagoon (Pialassa Baiona, Ravenna, Italy) contaminated by pyrogenic PAHs. The concentration of cyclopenta[cd]pyrene and benzo[ghi]fluoranthene increased from undetectable levels in reference mussels withdrawn from the Adriatic sea to 10-30 ng g(-1) dry weight in transplanted mussels. Other contaminants bioaccumulated by caged mussels included pyrene, fluoranthene and mercury. Whilst the isomer concentration ratio pyrene/fluoranthene in biota was comparable to that observed in sediments, the cyclopenta[cd]pyrene/benzo[ghi]fluoranthene ratio was much lower in mussels than in sediments. The lower sediment biota accumulation factor of cyclopenta[cd]pyrene with respect to that of benzo[ghi]fluoranthene was tentatively attributed to the greater biological activity of the former compound, which contains a reactive olefinic bond in the cyclopenta fused ring moiety. Given the higher mutagenic activity of cyclopenta[cd]pyrene with respect to other priority PAHs, its bioaccumulation from contaminated sediments may rise considerably the overall toxicity of PAH residues in exposed biota.

Animals↗
PubMed2005

Pyrene absorption can be a convenient method for probing critical micellar concentration (cmc) and indexing micellar polarity.

The critical micellar concentration (cmc) of both ionic and non-ionic surfactants can be conveniently determined from the measurements of UV absorption of pyrene in surfactant solution. The results on a number of surfactants have agreed with that realized from pyrene fluorescence measurements as well as that obtained following conductometric, tensiometric and calorimetric methods. The absorbance vs [surfactant] profiles for all the major UV spectral peaks of pyrene have been found to be sigmoidal in nature which were analyzed according to Sigmoidal-Boltzmann equation (SBE) to evaluate the cmcs of the studied surfactants. The difference between the initial and the final asymptotes (a(i) and a(f), respectively) of the sigmoidal profile, Delta a = (a(f)-a(i)) and the slope of the sigmoid, S(sig) have been observed to depend on the type of the surfactant. The Delta a has shown a linear correlation with the ratio of the fluorescence intensities of the first and the third vibronic peaks, I1/I3 of pyrene which is considered as a measure of the environmental polarity (herein micellar interior) of the probe (pyrene). Thus, Delta a values have the prospect for use as another index for the estimation of polarity of micellar interior.

Journal Article↗
PubMed2006

Solubilization of pyrene in aqueous micellar solutions of gemini surfactants C12-s-C12.2Br.

Solubilization of pyrene in aqueous micellar solutions of quaternary ammonium gemini surfactants C(12)-s-C(12).2Br has been examined by UV spectra and steady fluorescence spectra at 30 degrees C. The results showed that pyrene molecules were incorporated in the palisade layers of the micelles and interacted with the quarterary ammonium head groups through cation-pi interaction, resulting in red shift of the UV absorption spectrum. C(12)-s-C(12)2Br (s=3,4,6) micelles have stronger ability for solubilization of pyrene than conventional surfactant C(12)TABr micelles. With increasing spacer length of C(12)-s-C(12).2Br, the micelles become more adaptable to solubilizing pyrene, which even forms the dimers as in the case of s=3,4,6, while pyrene solubilizes in the micelles (s=2) mainly in single-molecule form due to the more compact structure of the micelle in comparison with that at s>2.

Journal Article↗
PubMed1983

Induction of benzo(a)pyrene hydroxylase in Aspergillus ochraceus TS: evidences of multiple forms of cytochrome P-450.

The filamentous fungus Aspergillus ochraceus TS produces an inducible microsomal cytochrome P-450 linked monooxygenase which is capable of hydroxylating benzo(a)pyrene in presence of O2 and NADPH. The addition of Benzo(a)pyrene, 3-Methyl cholanthrene, beta-Naphthoflavone and other aryl hydrocarbons during the induction period causes dramatic improvement in the kinetics of benzo(a) pyrene hydroxylation as was evidenced by large decrease in Km and increase in Vmax values. On the other hand, treatment with Phenobarbital, Polychlorinated biphenyl and Progesterone has no significant effect on the kinetics of benzo(a)pyrene hydroxylation although a significant induction of NADPH-Cyt C reductase activity was observed in all the three cases. Again, both Phenobarbital and 3-Methyl cholanthrene induced microsomes exhibit the characteristic reduced metyrapone difference spectra. These findings together with the results obtained with flavone on the metabolism of benzo(a)pyrene by various microsomal preparations suggest a parallel induction of multiple forms of cytochrome P-450 as observed in mammalian liver under identical condition.

Aryl Hydrocarbon Hydroxylases↗
PubMed1994

Exploration of physical principles underlying lipid regular distribution: effects of pressure, temperature, and radius of curvature on E/M dips in pyrene-labeled PC/DMPC binary mixtures.

In a previous study, we observed a series of dips in the plot of E/M (the ratio of excimer to monomer fluorescence intensity) versus the mole fraction of 1-palmitoyl-2-(10-pyrenyl)decanoyl-sn-glycerol-3-phosphatidylcholine (Pyr-PC) in Pyr-PC/DMPC binary mixtures at 30 degrees C. In the present study, we have characterized the physical nature of E/M dips in Pyr-PC/DMPC binary mixtures by varying pressure, temperature, and vesicle diameter. The E/M dips at 66.7 and at 71.4 mol% PyrPC in DMPC multilamellar vesicles remain discernible at 30-43 degrees C. At higher temperatures (e.g., 53 degrees C), the depth of the dip abruptly becomes smaller. This result agrees with the idea that E/M dips appear as a result of regular distribution of pyrene-labeled acyl chains into hexagonal super-lattices at critical mole fractions. Regular distribution is a self-ordering phenomenon. Usually, in self-ordered systems, the number of structural defects increases with increasing temperature, and thermal fluctuations eventually result in an order-to-disorder transition. The effect of vesicle diameter on the E/M dip at 66.7 mol% Pyr-PC in DMPC has been studied at 37.5 degrees C by using unilamellar vesicles of varying sizes. The E/M dip is observable in large unilamellar vesicles; however, the depth of the E/M dip decreases when the vesicle diameter is reduced. When the vesicle diameter is reduced to about 64 nm, the dip becomes shallow and split. This result suggests that the curvature-induced increase in the separation of lipids in the outer monolayer decreases the tendency of regular distribution for pyrene-labeled acyl chains. Regular distribution is believed to arise from the long-range repulsive interaction between Pyr-PC molecules due to the elastic deformation of the lipid matrix around the bulky pyrene moiety. When the radius of curvature becomes small, outer monolayer lipids are more separated. Therefore, pyrene-containing acyl chains fit better into the membrane matrix, which alleviates the deformation of the lattice and diminishes the long-range repulsive interactions between pyrene-containing acyl chains. Furthermore, we have shown a striking difference in the pressure dependence of E/M at critical Pyr-PC mole fractions and at noncritical mole fractions. In the pressure range between 0.001 and 0.7 kbar at 30 degrees C, E/M decreases steadily with increasing pressure at noncritical mole fractions; in contrast, E/M changes little with pressure at critical mole fractions (e.g., 33.3 and 50.0 mol% Pyr-PC). The pressure data suggest that membrane free volume in the liquid crystalline state of the bilayer is less abundant at critical Pyr-PC mole fractions than at noncritical mole fractions.

Dimyristoylphosphatidylcholine↗
PubMed2000

Fate of sediment-associated pyrene and benzo

Bioaccumulation, depuration and biotransformation of radiolabelled pyrene and benzo[a]pyrene were studied in the freshwater oligochaete Lumbriculus variegatus in spiked Lake Mekrijärvi (Eastern Finland) sediment in two sets of experiments (I and II). In experiment I bioaccumulation, depuration and biotransformation of PAHs were studied. In experiment II biotransformation was investigated further using three different solvent extractions and the ability of L. variegatus to biotransform was based on the change of proportion of the parent PAH in tissue. Bioaccumulation of both chemicals was fast and an apparent steady level was reached within a week. Biotransformation results obtained by solvent extractions were in agreement with each other, although hexane appeared to be less efficient solvent for B[a]P than chloroform:methanol or ethyl acetate:acetone/cyclohexane. The relative proportion of parent PAHs in tissues decreased continously during the 504 and the 336 h exposures in experiments I and II, respectively. After 336 h exposure in experiment II, approximately 60% of pyrene and 90% of B[a]P associated radioactivity was still in the parent compound. Depuration of the parent compounds in clean sediment was fast. Most of the parent chemicals were depurated within 72 h but the possible biotransformation products remained mainly in tissues. Feeding behavior of the animals (sediment ingesting vs. noningesting) did not affect pyrene biotransformation but the proportion of parent B[a]P in tissues was larger in feeding animals. This was probably due to faster uptake rate of B[a]P to feeders than nonfeeders and slow biotransformation rate of the chemical. Our results suggest that biotransformation of pyrene and B[a]P in L. variegatus is likely and it should be taken into account when studying bioaccumulation of PAHs in assessing hazard of sediment contamination.

Journal Article↗