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PubMed1988

Fate of the methyl group during the conversion of sterigmatocystin into O-methylsterigmatocystin and aflatoxin B1 by cell-free preparations of Aspergillus parasiticus.

Cell-free extracts of fungal mycelia of two aflatoxin non-producing isolates of Aspergillus parasiticus (SRRC 163 and SRRC 2043) were utilized for the study of enzyme activities involved in the latter stages of aflatoxin biosynthesis. The post-microsomal fractions (105,000 x g supernatant) of both SRRC 163 and SRRC 2043 were able to convert sterigmatocystin (ST) into O-methylsterigmatocystin (OMST); whereas the microsomal (105,000 x g pellet) preparation of only SRRC 163 was able to convert OMST into aflatoxin B1 (AFB1). S-Adenosylmethionine (SAM) was the primary substrate for the ST to OMST (methyltransferase) enzymatic conversion; [3H]OMST of specific activity 0.93 Ci/mmol was obtained in a reaction containing the [3H]SAM substrate (specific activity 1 Ci/mmol). After the terminal enzymatic conversion of OMST into AFB1, none of the radiolabel of the methyl group from OMST was found in AFB1. It is postulated that the methylation of ST may be required for subsequent enzymatic oxidation of OMST to aflatoxin B1.

Aflatoxin B1↗

PubMed1990

Effect of aflatoxin B1 on resistance induced by Bordetella bronchiseptica vaccine in rabbits.

The effects of aflatoxin B1 on the development of the immune response to oil-adjuvanted Bordetella bronchiseptica vaccine and on acquired resistance to bacterial challenge were studied in rabbits. The doses of aflatoxin used were insufficient to produce clinical intoxication. Rabbits were randomly assigned to three groups, each having six animals: control (T), vaccinated (V), and vaccinated plus aflatoxin (VA) at 0.05 mg/kg daily per os. Groups V and VA were vaccinated twice, and the three groups were subsequently challenged with virulent B. bronchiseptica. The average weight gain at weekly intervals was significantly reduced in group VA, and no statistically significant differences were found in the titers of agglutinating antibodies between groups V and VA. There were significant differences between groups V and VA in the extent and severity of the pneumonic process, group VA being most affected. Results indicated that agglutinating antibody titers were not related to the level of protection in the latter group. Other mechanisms, such as alveolar macrophage activity and cell-mediated immunity, were implicated in the impairment of the acquired resistance in rabbits subclinically intoxicated with aflatoxin.

Aflatoxin B1↗

PubMed1981

Histochemical assessment of 3 beta-hydroxysteroid dehydrogenase activity in the testes of rats following acute administration of aflatoxin B1.

Aflatoxin B1 (150 microgram) was administered i.p. to adult male rats on 3 occasions at intervals of 48 h. The testicular distribution and localisation of 3 beta-hydroxysteroid dehydrogenase (3 beta-HSD) was evaluated histochemically in rats killed 24 h after the last dose of aflatoxin, with or without human chorionic gonadotropin (HCG) stimulation. Diminished augmentation of seminal vesicle and prostate weights to HCG stimulation was recorded in male rats pretreated with aflatoxin. There were no convincing effects of aflatoxin pretreatment on the histochemical localisation and distribution of 3 beta-HSD in the testes of the rats used in this investigation.

3-Hydroxysteroid Dehydrogenases↗

PubMed1988

In vitro effect of aflatoxin B1 on the transcriptional activity of DNA template, chromatin and soluble DNA-dependent RNA polymerases in buffalo liver.

The effect of aflatoxin B1 on the DNA template and DNA-dependent RNA polymerases in buffalo liver was studied. Aflatoxin B1 inhibited both Mg2+- and Mn2+-activated RNA polymerases in a dose-dependent manner. At 10 micrograms the inhibition of both enzymes was almost complete. The inhibitory effect on the solubilized enzymes was higher than the chromatin-bound, suggesting a direct effect at the enzyme level. On the other hand, incubating DNA or deoxyribonucleoprotein (DNP) with 2 micrograms aflatoxin reduces its transcriptional capacity with a greater effect on the Mg2+-activated RNA polymerase than the Mn2+-activated enzyme. These results suggest that aflatoxin B1 inhibits in vitro transcription in buffalo liver at both enzyme and template levels.

Aflatoxin B1↗

PubMed1989

Differential changes in rat brain tryptophan, serotonin and tyrosine levels following acute aflatoxin B1 treatment.

Female Sprague-Dawley rats were treated acutely (12-h) with aflatoxin B1 (100 micrograms/kg i.p.) or vehicle (10% acetone in 0.9% NaCl) and regional brain levels of tryptophan, serotonin and tyrosine were assayed. Brainstem but not cerebellar or cortical tyrosine levels were decreased in aflatoxin B1-treated rats. Brain tryptophan was increased in all 3 brain regions by acute aflatoxin B1 treatment, while serotonin levels were unaltered in the cerebellum and cortex and decreased in the brainstem. These experiments indicate that acute aflatoxin B1 treatment differentially alters brain amino acids and serotonin and that changes in brain tryptophan, the serotonin precursor, do not parallel changes in brain serotonin.

Aflatoxin B1↗

PubMed1991

Mouse strain differences in glutathione S-transferase activity and aflatoxin B1 biotransformation.

Previous studies have suggested that mice are resistant to the carcinogenic effects of aflatoxin B1 (AFB1) and that this resistance is largely the result of expression of an isoenzyme of glutathione S-transferase (GST) with high activity toward AFB1-8,9-epoxide. Significant interstrain differences in cytosolic GST activities toward a variety of substrates have been reported in mice. If such differences exist for the conjugation of AFB1-8,9-epoxide, then there may be significant mouse strain differences in susceptibility to AFB1-induced hepatocarcinogenicity. The hepatic microsomal and cytosolic biotransformation of AFB1 was studied in 8 different strains of mice fed a purified diet. GST-mediated conjugation of AFB1-8,9-epoxide with glutathione and GST activity toward 1-chloro-2,4-dinitrobenzene (CDNB), 1,2-dichloro-4-nitrobenzene (DCNB), ethacrynic acid (ECA) and cumene hydroperoxide (CHP) were determined with cytosolic fractions from 8-10 pooled livers. Specific activities of cytochrome-P-450-mediated oxidation of AFB1 to aflatoxin Q1 (AFQ1), aflatoxin M1 (AFM1), and aflatoxin P1 (AFP1), as well as the reactive intermediate AFB1-8,9-epoxide, were determined with hepatic microsomal fractions from each mouse strain. No striking differences in specific activity between mouse strains were observed for any of the P-450- or GST-mediated enzymatic pathways measured, although some statistically significant differences were found. GST specific activities toward AFB1-8,9-epoxide, CDNB, DCNB, ECA and CHP ranged from 1.5-2.1, 2,830-5,370, 81-144, 38-69 and 32-73 nmol/mg protein/min, respectively. The rate of formation of AFB1-8,9-epoxide ranged from 208 to 465 pmol/mg protein/min. The specific activities of AFQ1,AFM1, and AFP1 formation by microsomes ranged from 36-70, 161-326, and 252-426 pmol/mg protein/min, respectively. Mice fed a standard rodent chow diet showed evidence of microsomal and cytosolic enzyme induction when compared to mice fed a purified diet. The lack of substantial differences in enzyme specific activities between mouse strains suggests that interstrain variations in the hepatocarcinogenic effects of AFB1 in mice should not be large.

Aflatoxin B1↗

PubMed1994

Determination of aflatoxin Q1 in urine by automated immunoaffinity column clean-up and liquid chromatography.

A liquid chromatographic system with an automated clean-up procedure for aflatoxin Q1 in human urine is described. The samples were cleaned up by using immunoaffinity columns originally designed for aflatoxin M1. The chromatographic system was a C18 column with an acidic mobile phase of acetonitrile-water containing potassium bromide. Fluorescence detection (365/440 nm) of aflatoxin Q1 was enhanced by addition of bromine, using post-column derivatization, which was studied by factorial designs. Average recovery of aflatoxin Q1 in spiked 10-ml urine samples was 88% (R.S.D. = 6.4%) at a level of 50 pg/ml. The determination limit was 49.5 pg/ml urine.

Aflatoxin M1↗

PubMed1985

The mercapturic acid pathway metabolites of a glutathione conjugate of aflatoxin B1.

A glutathione conjugate of aflatoxin B1 (AFB1) which has previously been identified as 8,9-dihydro-8-(S-glutathionyl)-9-hydroxy aflatoxin B1 (AFB1-GSH) (E.J. Moss, D.J. Judah, M. Przybylski and G.E. Neal, Biochem. J., 210 (1983) 227-233) has been degraded in vitro to all of the intermediates of the mercapturic acid pathway (MAP) and the chromatographic and spectral characteristics of each of these compounds investigated. The cysteinylglycyl conjugate (AFB1-Cys.Gly) was prepared by incubating the AFB1-GSH conjugate with a rat hepatoma cell line rich in gamma-glutamyl-transpeptidase (GGT). Incubations of the AFB1-Cys.Gly conjugate with dipeptidase produced a metabolite, which was purified and characterized by 1H-NMR spectroscopy as 8,9-dihydro-8-(S-cysteinyl)-9-hydroxy aflatoxin B1 (AFB1-Cys). The N-acetyl derivative of the AFB1-Cys conjugate resulted from the incubation of the AFB1-GSH conjugate in vitro with isolated rat kidney cells. Mass spectral data were consistent with the compound being 8,9-dihydro-8-(S-cysteinyl-(N-acetyl))-9-hydroxy aflatoxin B1 (AFB1-Nac.Cys). A chromatographically identical compound was obtained by the chemical acetylation of AFB1-Cys.

Acetylcysteine↗

PubMed2003

Palladium catalyzed kinetic and dynamic kinetic asymmetric transformations of gamma-acyloxybutenolides. Enantioselective total synthesis of (+)-Aflatoxin B1 and B2a.

The reaction of gamma-tert-butoxycarbonyloxy-2-butenolide with phenol nucleophiles in the presence of a Pd(0) complex with chiral ligands may be performed under conditions that favor either a kinetic resolution or a kinetic asymmetric transformation (KAT) or dynamic kinetic asymmetric transformation (DYKAT). Performing the reaction at high concentration (0.5 M) in the presence of a carbonate base favors the former, i.e., KAT; whereas, running the reaction at 0.1M in the presence of tetra-n-butylammonium chloride favors the DYKAT process. Syntheses of aflatoxin B(1) and B(2a) employs the DYKAT to introduce the stereochemistry. Starting with Pechmann condensation of the monomethyl ether of phloroglucinol, the requisite phenol nucleophile is constructed in two steps. The DYKAT proceeds with > 95% ee. A reductive Heck cyclization followed by a lanthanide catalyzed intramolecular acylation completes the synthesis of the pentacyclic nucleus in 3 steps. Reduction of the lactone provides aflatoxin B(2a) and its dehydration product B(1). This synthetic strategy creates an asymmetric synthesis of the former in only 7 steps and the latter in 9 steps. Thus, the ultimate synthetic sequence involves 3 + 5 --> 39 --> 40 --> 42 --> 43 --> 46 --> 47 --> 48 (aflatoxin B(2a)) --> 49 (aflatoxin B(1)).

4-Butyrolactone↗

PubMedDate not supplied

Comparison of six methods of analysis for the determination of aflatoxin B1 in feeding stuffs containing citrus pulp.

Six published methods of analysis for the determination of aflatoxin B1 have been compared for their suitability to determine aflatoxin B1 in feeding stuffs containing citrus pulp. These methods are the official European Community (EC) procedure, four procedures proposed in the European Community to replace this method and a new procedure developed by the authors of this article. In all procedures chloroform is used for initial extraction. Various clean-up systems are then applied. For the ultimate separation and detection, use is made of high performance liquid chromatography (HPLC) in three procedures and two-dimensional thin layer chromatography (TLC) in two procedures. One method allows either HPLC or TLC. All experiments were carried out with samples of a batch of feeding stuff containing citrus pulp, artificially contaminated with aflatoxins B1, B2, G1 and G2 at levels of ca 13, 5, 10 and 4 micrograms/kg respectively. Three methods were found to be suitable: a procedure in which gel permeation clean-up and two-dimensional TLC are used; a procedure in which TLC clean-up and reverse phase HPLC with postcolumn derivatization are used: a procedure in which cartridge clean-up and either HPLC or TLC are used. The latter method is preferred because its efficient clean-up yields a very clean extract, allowing the application of various systems of HPLC or TLC. Published recovery data of these three methods for aflatoxin B1 vary from 85-90% at a level of ca 10 micrograms/kg feeding stuff.

Aflatoxin B1↗

PubMedDate not supplied

A survey using normal-phase high-performance liquid chromatography of aflatoxins in domestic and imported foods in the USSR.

A survey of the occurrence of aflatoxins B1, B2, G1 and G2 in Soviet domestic and imported cereals and nuts (totalling 4532 samples) collected in 1985-87, showed that 26.9% of imported peanuts, 2.2% of corn and 28.3% of cotton seeds were contaminated by aflatoxins at levels exceeding the maximum tolerated level established in the USSR (5 micrograms/kg for aflatoxin B1 in foodstuffs of all types excluding baby foods); maximum concentrations were 3650, 600 and 153 micrograms/kg, respectively. A highly sensitive normal-phase high-performance liquid chromatographic method was developed. The detection limit was 0.1 microgram/kg and the coefficients of variation were 11% and 8.5% at contamination levels 10 and 100 micrograms/kg of aflatoxin B1, respectively.

Aflatoxin B1↗

PubMedDate not supplied

Survey of aflatoxin contamination of dried figs grown in Turkey in 1986.

A total of 284 dried fig samples, collected from fields during drying, and from warehouse and processing units in the Aegean region of Turkey in 1986, were examined for aflatoxin contamination. Aflatoxin B1, B2, and G1 were detected in 4, 2, and 2% of the samples, respectively, which were of the lower grade of figs taken from the drying stage. The average alfatoxin levels in positive samples were estimated to be 112.3 (B1), 50.6 (B2), and 61.4 ng/g (G1). The samples collected from storage (64 samples) and processing units (14 samples) contained no aflatoxins. The results of this survey show that aflatoxin contamination of Turkish dried figs in 1986 was highly correlated with the poorer grade of fig.

Aflatoxin B1↗

PubMed1998

Occurrence of aflatoxins B1, B2, G1, and G2 in peanuts and their products marketed in the region of Campinas, Brazil in 1995 and 1996.

Samples of peanuts and their products marketed in the region of Campinas, Brazil in 1995 and 1996 were analysed in terms of aflatoxin B1, B2, G1, and G2 by thin-layer chromatography, aiming at the protection of consumer health. Of the 80 samples analysed, 35 of peanuts and 45 of peanut products, 41 (51%) presented contamination with aflatoxin, 11 of them being peanuts (27%) and 30 being products (67%), in a range of 43 to 1099 micrograms/kg for B1 + B2 + G1 + G2 with a 90th percentile of 415 (B1 + G1) and of 615 (B1 + B2 + G1 + G2). The results also demonstrated that aflatoxin B1 (AFB1) reached the highest incidence and the highest upper limits compared with all the other aflatoxins.

Aflatoxin B1↗

PubMed1989

Interaction of aflatoxin B1 metabolites with cellular macromolecules in neonatal rats receiving carcinogen through mother's milk.

A single dose of 2 microCi [3H] aflatoxin B1 (AFB1) containing 20 micrograms AFB1 was administered to the lactating rat. This resulted in the excretion of AFB1-metabolites in the milk, which were transferred and distributed in many tissues of the offspring consuming milk for 48 h. An equal distribution of radioactivity in liver and lung of suckling rats as well as in their sub-cellular fractions was observed. No AFB1 metabolite binding was apparent with tissue DNA. However, considerable binding of aflatoxin residues was observed with protein followed by RNA. Three metabolites have been detected in the milk sample derived from the stomach of the suckling rats on thin layer chromatogram with Rf values of 0.2, 0.4 and 0.8. Pretreatment of lactating rats with phenobarbitone (PB: 80 mg/kg/3 days) prior to the administration of [3H]AFB1 caused an overall decrease in the radioactivity in the neonatal tissues, particularly lung and intestine (P less than 0.05). The fluorescent bands with Rf values of 0.2 and 0.4 were not visualized in the milk sample from the PB group. Subsequently, the binding of AFB1 residues to cellular macromolecules of neonatal tissues was decreased. PB treatment further resulted in lowering the glucuronide/sulphate conjugates of AFB1 in the milk consumed by suckling rats; AFB1-glutathione (GSH) conjugates were slightly increased. These results point out the possibility that aflatoxin metabolites bind to the tissues of offspring fed by mothers consuming aflatoxin contaminated diets thus leading to chronic effects.

Aflatoxin B1↗

PubMed1990

Linear dose-response relationship for DNA adducts in rat liver from chronic exposure to aflatoxin B1.

Male F-344 rats were given [3H]aflatoxin B1 (AFB1) in the drinking water at three exposure levels (0.02, 0.6, 20 micrograms/l, resulting in average dose levels of 2.2, 73, 2110 ng/kg per day). After 4, 6 and 8 weeks, DNA was isolated from the livers and analyzed for aflatoxin-DNA adducts. The level of DNA adducts did not increase significantly after 4 weeks, indicating that a steady-state for adduct formation and removal had nearly been reached. At 8 weeks, the adduct levels were 0.91, 32 and 850 nucleotide-aflatoxin adducts per 10(9) nucleotides, i.e. clearly proportional to the dose. At the high dose level, a near 50% tumor incidence would be expected in a 2-year bioassay with F-344 rats while the low dose used is within the range of estimated human dietary exposures to aflatoxin in Western countries. The proportionality seen between exposure and steady-state DNA adduct level is discussed with respect to a linear extrapolation of the tumor risk to low dose.

Administration, Oral↗

PubMed1982

Production of monoclonal antibodies to guanine imidazole ring-opened aflatoxin B1DNA, the persistent DNA adduct in vivo.

Monoclonal antibodiess were produced following immunisation of mice with guanine imidazole ring-opened aflatoxin B1 DNA (iro AFB1 DNA), coupled electrostatically to methylated keyhole limpet haemocyanin. Three monoclonal hybridoma lines producing antibodies specific for iro AFB1 DNA were grown as ascites tumours and suitable dilutions of the ascitic fluid (1:8000-1:50,000) used in a competitive enzyme linked immunosorbent assay (ELISA) to measure reactivity of the antibodies to a variety of aflatoxin and nucleic acid-related compounds. These antibodies recognise AFB1 bound to DNA at levels 10(4)-10(5) times lower concentration than unmodified calf thymus DNA or 8,9-dihydro-8,9-dihydroxy-aflatoxin B1: and show 2-5 times the affinity to iro AFB1 DNA compared to AFB1 DNA. The concentration of AFB1 in iro AFB1 DNA producing 50% inhibition in a competitive ELISA was 1.8 x 10(-7) molar. Using the most sensitive hybridoma line, levels of 1 adduct in 300,000 nucleotides would be detectable, which is the level of binding found in the rat and the hamster in vivo. These monoclonal antibodie should therefore prove useful in detecting these lesions in animal and human tissue samples exposed to aflatoxins.

Aflatoxin B1↗

PubMedDate not supplied

Characterization of iodine derivatives of aflatoxin B1 and G1 by thermospray mass spectrometry.

Thermospray mass spectrometry (TSMS) was used to identify the derivatives formed when iodine is reacted with aflatoxins B1 and G1 at approximately 70 degrees C to enhance fluorescence. It was found that stable derivatives were formed by addition of an iodine atom and a methoxy group across the double bond located on the furan ring of the aflatoxin B1 and G1 molecules. TSMS and TSMS/MS daughter spectra of the reaction products of aflatoxin B1 and G1 with iodine provide evidence of the addition of each moiety to produce the iodo-methoxy derivative. The addition of an iodine atom to one carbon and a methoxy group to the other carbon of the furan ring provided molecular weights of 470 and 486 for the products of aflatoxin B1 and G1, respectively.

Aflatoxin B1↗

PubMed1989

Characterization of three forms of cytochrome P-450 inducible by 3-methylcholanthrene in Golden hamster livers with special reference to aflatoxin B1 activation.

Three forms of cytochrome P-450 of liver microsomes of 3-methylcholanthrene-treated Golden hamsters were purified and characterized as regards their catalytic activity toward aflatoxin B1-related hepatocarcinogenic mycotoxins. These include two major forms, designated as cytochrome P-450-AFB (P-450-I) and P-450-II, and one minor form, P-450-III. Cytochromes P-450-AFB, P-450-II, and P-450-III have their absorption maximum in the carbon monoxide-complex of the reduced form at 448.5, 447.0, and 448.0 nm, have apparent molecular weights of 56,000, 58,000, and 59,500, and are in the low spin, high spin, and low spin state, respectively. Of these, cytochrome P-450-AFB was shown to be highly active in the mutagenic activation of aflatoxin B1-related hepatocarcinogens such as sterigmatocystin and O-methylsterigmatocystin. Activation of aflatoxin B1 by hepatic microsomes of 3-methylcholanthrene-treated hamsters was inhibited almost completely by the antibody against P-450-AFB but not by the antibody against P-450-II, indicating that P-450-AFB is the major component responsible for the activation of aflatoxin B1 by hamster liver. Western blot analysis demonstrated that no protein cross-reacted with the antibody to P-450-AFB in the liver microsomes from guinea pig, rat, mouse, and house musk shrew (Suncus murinus) treated with 3-methylcholanthrene, while one or two proteins cross-reacted with the antibody to P-450-II in the liver microsomes of these animals.

Aflatoxin B1↗