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PubMed1991

Effects of sodium metabisulphite, hydrogen peroxide and heat on aflatoxin B1 in lafun and gari--two cassava products.

Sodium metabisulphite and hydrogen peroxide alone or in combination with heat (50-70 degrees C) were found to be effective in degrading aflatoxin B1 (AFB1) in lafun and gari. Hydrogen peroxide (H2O2) at a concentration of 3% in the aqueous phase gave a 12.5% degradation of aflatoxin B1 in lafun and at 50 degrees C, degradation levels of 25% and 50% were obtained with 6.0 and 9.0% H2O2, respectively. When sodium metabisulphite was applied during the production of gari (a fermented cassava product heated to 50-70 degrees C during production) AFB1 degradation levels were found to be 65.8%, 60.9%, 41.5% and 36.6%, respectively, for sodium metabisulphite levels of 1.0%, 0.8%, 0.5% and 0.3%.

Aflatoxin B1↗
PubMed1987

Killing and mutation of human lymphoblast cells by aflatoxin B1: evidence for an inducible repair response.

Diploid human lymphoblast cells exhibit apparent saturation of mutation induced by exposure to aflatoxin B1, despite a linear increase in the amount and proportion of the aflatoxin-DNA adducts formed. The saturation is neither a cell cycle phenomenon nor a result of a genetically heterozygous population. Examination of the biphasic nature of aflatoxin-DNA adduct loss in vivo shows initial, rapid removal of all adduct species, followed by a slow loss of the aflatoxin-N7-guanine adduct alone. We hypothesize that these data reveal two modes of adduct loss in these cells. The first is an inducible, error-free system that is short-lived, turning off as adduct levels fall below the induction threshold of some 1000 total adducts/cell. The second loss is slower and results from spontaneous depurination of remaining aflatoxin-N7-guanines. Our data are in agreement with the possibility that apurinic sites thus generated are responsible for the mutation observed. A major paradox arises from the fact that aflatoxin-related premutagenic depurinations are estimated to be only 10% of the number of spontaneous depurinations estimated by others to occur in human cells in a 1-h period.

Aflatoxin B1↗
PubMed1990

Comparative uptake, vascular transport, and cellular internalization of aflatoxin-B1 and benzo(a)pyrene.

Studies of the uptake of benzo(a)pyrene (BaP) and aflatoxin-B1 (AFB1) after gastric instillation showed that BaP was absorbed via the intestinal lymphatic drainage and transported to the vascular circulation sequestered within lipoproteins in thoracic duct lymph, while AFB1 was absorbed with water soluble compounds into the gastrointestinal venous drainage and was not transported in association with lipoproteins. BaP was taken up into plasma lipoproteins over a broad concentration range, while AFB1 was not sequestered within lipoproteins over the same concentration range. Low density lipoproteins (LDL) facilitated BaP uptake into fibroblasts and impeded BaP uptake into hepatocytes. High density lipoproteins (HDL) facilitated BaP uptake into hepatocytes and impeded BaP uptake into fibroblasts. The uptake of AFB1 into either fibroblasts or hepatocytes was not affected by lipoproteins.

Aflatoxin B1↗
PubMed1984

Detection of aflatoxin B1 in serum samples of male Japanese subjects by radioimmunoassay and high-performance liquid chromatography.

Aflatoxin B1 (AFB1) was detected in serum samples of healthy Japanese males by radioimmunoassay and high-performance liquid chromatography. Blood samples were obtained from 20 subjects after fasting and from 80 subjects after lunch. The subjects ranged in age from 20 to 63 years of age. Measurement of AFB1 in the samples was performed by radioimmunoassay and was confirmed by high-performance liquid chromatography using a mu Porasil column and a C18-mu Bondapak column after the conversion of AFB1 to its water adduct AFB2a. AFB1 was detected in 5 of 20 fasting blood samples [20 to 56 pg/ml of serum; 33.6 +/- 14.6 (S.D.)] and in 29 of 80 serum samples taken after lunch (20 to 1169 pg/ml of serum; 218.1 +/- 268.3). Mass spectral analysis of the material obtained after high-performance liquid chromatography separation from serum samples confirmed the presence of AFB1.

Adult↗
PubMed1984

The influence of partial hepatectomy on the biphasic response of gamma glutamyl transpeptidase to aflatoxin B1.

We previously observed a biphasic response in rat hepatic gamma glutamyl transpeptidase (GGT) activity to aflatoxin B1 (AFB1) feeding [9]. We have extended this observation to examine the effect of partial hepatectomy (PH) on the activity and distribution of GGT at different stages of the feeding regime. In control-fed animals GGT levels were elevated 3-7 days after PH with increased activity in periportal hepatocytes. In animals fed a sub-carcinogenic dose of AFB1 (up to 4 weeks) the effect of PH on GGT activity was similar to that in control animals, but increased activity was mainly due to biliary hyperplasia. There was no obvious difference between animals returned to control diet after PH and those returned to toxic diet. In animals fed 4-15 weeks the percentage increase in GGT activity 1 week after PH correlated with length of time on AFB1 diet before operation, with an increase in number and size of altered foci. These results further support the idea that there is a preliminary toxic response in GGT activity followed by a secondary response more closely related to the carcinogenic process.

Aflatoxin B1↗
PubMedDate not supplied

Enzyme-linked immunosorbent assay of aflatoxin B1 in naturally contaminated corn and cottonseed.

Naturally contaminated corn and cottonseed samples were screened for aflatoxin B1 (AFB1) by a direct competitive enzyme-linked immunosorbent assay (ELISA). Samples were blended 5 min in an extraction solvent of methanol-water-dimethylformamide (70 + 29 + 1) and filtered. Filtrates were assayed by direct competition between AFB1 in the corn and cottonseed samples and AFB1-peroxidase conjugate for binding to specific antibody adsorbed to a solid phase microtiter plate. Standard curves prepared using the extract of AFB1-free corn and cottonseed samples, and extraction solvent only, showed negligible interference by the sample extract in the performance of ELISA. The AFB1 content in corn and dehulled cottonseed samples as determined by ELISA ranged from 7 to 422 micrograms/kg and 7 to 3,258 micrograms/kg, respectively. When ELISA estimates of AFB1 in corn were compared with values obtained by thin layer chromatography (CB method), the correlation coefficient (n = 10) was 0.95. Average interassay and subsample coefficients of variation for ELISA in corn were 21.4 and 22.0%, respectively. When ELISA estimates of AFB1 in cottonseed were compared with values obtained by liquid chromatography (Pons method), the correlation coefficient (n = 15) was 0.96. Using this ELISA, 36 duplicate sample extracts can be screened for AFB1 in less than 2 h.

Aflatoxin B1↗
PubMed1988

Binding of aflatoxin B1 to melanin.

Whole-body autoradiography of pigmented C57BL mice injected with 3H-labelled aflatoxin B1 (AFB1) showed a high degree of labelling of melanin-containing tissues, such as the melanin of eyes and hair follicles. The corresponding tissues in albino NMRI mice contained only low amounts of the label. Liquid chromatography of extracts of pigmented mouse eyes showed the presence of only non-metabolized AFB1. Analysis of the binding of AFB1 to melanin from bovine eyes using the method of Scatchard revealed two classes of binding sites. Incubations in the presence of metallic cations did not affect the binding, indicating that ionic forces play no role in the affinity. Comparisons of the binding of AFB1 to the bovine-eye pigment in media containing n-propanol, ethanol or methanol indicated that hydrophobic interactions play a role in the affinity. Apposition of the aromatic rings in AFB1 and the indole nuclei of the melanin may also result in van der Waals' forces, and the combination of these two types of forces may underly the binding of AFB1 to melanin. The melanin binding implies that AFB1 is retained in pigmented tissues at higher concentrations than in any other tissue of the body. The biological implication of this accumulation is now known, but the possibility that there may be an increased risk for the induction of melanomas is discussed.

Aflatoxin B1↗
PubMed1984

Aflatoxin B1: effect on the synthesis and degradation of mitochondrial proteins in hepatocyte monolayers.

The effect of aflatoxin B1 (AFB1), a hepatocarcinogen, on mitochondrial and general protein synthesis and degradation has been studied. AFB1 (0.003, 0.03, 0.25 micrograms ml-1) inhibited total protein synthesis over a 5 h period by 30, 64 and 82%, respectively, measured by incorporation of [3H]leucine. After 24 h in the presence of AFB1 inhibition was 23, 77 and 100%, respectively. AFB1 inhibited total hepatocyte protein degradation in a concentration independent manner by approximately 50% i.e., from 1.4% h-1 to 0.7% h-1. The immediate effect of AFB1 on mitoribosomal and total mitochondrial protein synthesis and mitochondrial degradation has been assessed by two methods. Mitoribosomal synthesis of proteins was inhibited over a 5 h period by AFB1 in a concentration independent manner by approximately 43%. Total mitochondrial protein synthesis showed a 23 and 45% inhibition by AFB1 (0.003 and 0.03 micrograms AFB1 ml-1) over a 4 h period and 25 and 72% inhibition, respectively, after 24 h in culture. The rate of mitochondrial protein degradation was not altered. AFB1 inhibits dibutyryl cyclic AMP-induced tyrosine amino transferase (TAT) activity in hepatocytes by 57% at 0.003 micrograms ml-1 and 100% at 0.03 micrograms ml-1 over a 24 h period. Dibutyryl cyclic AMP increases the rate of degradation of proteins in hepatocyte monolayers from 1.4% h-1 to 2.7% h-1 and was inhibited at both concentrations of AFB1 used. AFB1 causes a rapid inhibition of total hepatocyte protein synthesis, synthesis of proteins in hepatocyte mitochondria and the synthesis of imported mitochondrial proteins. General hepatocyte and dibutyryl cyclic AMP-induced protein degradation are significantly inhibited by AFB1 whereas the degradation of mitochondrial proteins is unaffected.

Aflatoxin B1↗
PubMed1980

Cleavage of lambda repressor and induction of recA protein synthesis elicited by aflatoxin B1 metabolites in Escherichia coli.

In Escherichia coli lambda lysogens incubated with activated aflatoxin B1, the rate of synthesis of RecA protein is markedly increased while lambda repressor is cleaved, but not that of the non-inducible mutant lambdacIind-. Following a 10 min lag period, lambda repressor is almost totally cleaved within 40 min of incubation. Cleavage of lambda repressor is inhibited by chloramphenicol. Synthesis of RecA protein and cleavage of lambda repressor are two characteristic processes induced in E. coil by DNA damaging agents such as u.v. light or mitomycin C. Our results favour the idea that in aflatoxin B1-treated lysogens, DNA lesions activate RecA protein to cleave LexA protein, the repressor of the recA gene, and lambda repressor. DNA damage, which may represent a relatively small fraction of the total cellular lesions, promotes the derepression of specific genes that control epigenetic as well as genetic processes in bacteria.

Aflatoxin B1↗
PubMed1992

Molecular cloning and heterologous expression of a cDNA encoding a mouse glutathione S-transferase Yc subunit possessing high catalytic activity for aflatoxin B1-8,9-epoxide.

Resistance to the carcinogenic effects of aflatoxin B1 (AFB1) in the mouse is due to the constitutive expression of an Alpha-class glutathione S-transferase (GST), YcYc, with high detoxification activity towards AFB1-8,9-epoxide. A cDNA clone (pmusGST Yc) for a murine GST Yc polypeptide has been isolated. Sequencing has shown the cDNA insert of pmusGST Yc to be 922 bp in length, with an open reading frame of 663 bp that encodes a polypeptide of M(r) 25358. The primary structure of the murine GST Yc subunit predicted by pmusGST Yc is in complete agreement with the partial amino acid sequence of the aflatoxin-metabolizing mouse liver GST described previously [McLellan, Kerr, Cronshaw & Hayes (1991) Biochem. J. 276, 461-469]. A plasmid, termed pKK-musGST Yc, which permits the expression of the murine Yc subunit in Escherichia coli, has been constructed. The murine GST expressed in E. coli was purified and found to be catalytically active towards several GST substrates, including AFB1-8,9-epoxide. This enzyme was also found to possess electrophoretic and immunochemical properties closely similar to those of the GST Yc subunit from mouse liver. However, the GST synthesized in E. coli and the constitutive mouse liver Alpha-class GST exhibited small differences in their chromatographic behaviour during reverse-phase h.p.l.c. Automated Edman degradation revealed alanine to be the N-terminal amino acid in the GST Yc subunit expressed in E. coli, whereas the enzyme in mouse liver possesses a blocked N-terminus. Although sequencing showed that the purified Yc subunit from E. coli lacked the initiator methionine, the amino acid sequence obtained over the first eleven N-terminal residues agreed with that predicted from the cDNA clone, pmusGST Yc. Comparison of the deduced amino acid sequence of the mouse Yc polypeptide with the primary structures of the rat Alpha-class GST enzymes revealed that it is more closely related to the ethoxyquin-induced rat liver Yc2 subunit than to the constitutively expressed rat liver Yc1 subunit. The significance of the fact that both mouse Yc and rat Yc2 exhibit high catalytic activity towards AFB1-8,9-epoxide, whereas rat Yc1 possesses little activity towards this compound, is discussed in terms of structure/function.

Aflatoxin B1↗
PubMed1982

Mechanisms of dietary modification of aflatoxin B1 carcinogenesis.

Trout were fed a range of dietary components which altered their carcinogenic response to aflatoxin B1 (AFB1). Dietary protein at levels substantially exceeding nutritional requirements were synergistic with AFB1. Cyclopropene fatty acids (CPFA) were carcinogenic when fed alone at 20 or 55 ppm, and synergistic when fed with AFB1. In contrast, several flavonoid and indole compounds, especially beta-naphthoflavone (beta-NF) and indole-3-carbinol, inhibited the carcinogenic response when fed prior to and along with AFB1. The mechanisms by which some of these dietary factors modulate AFB1 carcinogenesis were investigated. Dietary beta-naphthoflavone was shown to substantially induce the levels of mixed function oxidase (MFO) activities assayed in vitro. These changes were accompanied by alterations in AFB1 metabolism and binding in freshly isolated hepatocytes. AFB1 incubated in hepatocytes freshly isolated from fish fed beta-NF diet was metabolized more rapidly, showed enhanced rates of detoxication reactions, and decreased accumulation of AFB1-DNA adducts compared to control hepatocytes. These results suggest that beta-NF inhibits AFB1 carcinogenesis at least in part by altering MFO activities such that detoxication is enhanced and initial DNA damage by AFB1 is reduced. In contrast, high dietary protein is a synergist for AFB1 carcinogenesis, and this appears to occur primarily by enhancing the transformation probability for AFB1-initiated genome damage. Fish treated with AFB1 as embryos and then reared on high protein diets had substantially higher incidences of hepatocellular carcinoma (86%) than similarly treated fish fed normal protein diet (44%) or high protein controls without AFB1 exposure (0-2%). The synergistic behavior of dietary CPFAs also appears to partially involve enhanced transformation following DNA damage by AFB1. Fish exposed as embryos to AFB1 and then fed CPFA-containing diets are known to show promotion effects similar to the high protein results (Hendricks, J.D., Proc. 11th Int. Symp. of the Princess Takamatsu Cancer Research Fund, in press.) However, factors other than promotion are involved in the synergism between CPFA and AFB1. Preliminary studies indicate that dietary CPFAs repress MFO activities and depress DNA damage by AFB1 in vitro. If this occurs in vivo, then the net synergistic effect of dietary CPFAs would involve depression of initial AFB1-induced DNA damage, but highly efficient promotion of transformation from the remaining lesions.

Aflatoxin B1↗
PubMedDate not supplied

A survey of the occurrence of aflatoxin B1 in peanut butters by enzyme-linked immunosorbent assay.

A survey was carried out in 1986 for the occurrence of aflatoxin B1 in peanut butters (129 samples) obtained from specialist Health Food outlets. The results showed that 6.2% of the samples exceeded 10 micrograms/kg of aflatoxin, 8% contained between 2.5 and 10 micrograms/kg, and in the remainder (86%) aflatoxin could not be detected at a limit of 2.5 micrograms/kg. These results show a lower contamination by aflatoxin than found in these products in previous surveys (1982-1984). An aflatoxin B1-specific enzyme-linked immunosorbent assay (ELISA) was employed for the first time in these analyses; and to make an assessment of its performance positive aflatoxin results, together with a random selection of those below the ELISA limit of detection, were additionally analysed by conventional extraction and clean-up followed by HPLC. The ELISA technique offered a significant improvement in speed of analysis over conventional approaches, enabling a six-fold increase in sample throughput compared to that required for conventional analysis, together with other advantages.

Aflatoxin B1↗
PubMed1982

Geno- and cytotoxicity of nitrosamines, aflatoxin B1, and benzo[a]-pyrene in continuous cultures of rat hepatoma cells.

Two closely related hepatoma cell lines were examined for their response to carcinogens requiring metabolic activation: H5, a dedifferentiated line expressing cytochrome P-448-dependent monooxygenase(s); and HF1-4, a differentiated line which also expresses cytochrome P-450-dependent monooxygenase(s). The hepatocarcinogens dimethyl- and diethylnitrosamine and aflatoxin B1, preferred substrates for cytochrome P-450-dependent monooxygenase(s), and the non-hepatocarcinogen benzo[a]pyrene, which is preferentially metabolized by cytochrome P-448-dependent monooxygenase forms, were used as test agents. Their effects were compared to those of the directly alkylating agents N-methyl-N'-nitro-N-nitrosoguanidine (MNNG) and N-ethyl-N-nitrosourea (ENU). The cytotoxicity was evaluated by plating efficiency, the genotoxicity by the appearance of alkaline labile DNA sites. The nitrosamines had a cytotoxic and genotoxic effect on the differentiated HF1-4 cells, but had no effect on H5 cells. Aflatoxin B1 affected both cell lines, but was approximately 10-times more potent in the HF1-4 than in the H5 cells. In contrast to the nitrosamines and the mycotoxin, benzo[a]-pyrene exerted a stronger effect on the dedifferentiated cell line. Pretreatment of cultures with dexamethasone increased both the cytotoxicity and genotoxicity of the hepatotoxic agents. MNNG and ENU induced a similar degree of DNA-damage after short-term (2 h) exposure in the two cell lines. When cells were allowed to recover for 16 h HF1-4 cells, but not H5 cells, regained their full growth potential suggesting a marked capacity for the repair of MNNG- and ENU-induced lesions in the HF1-4 cells. The results indicate that continuous lines of mammalian cells may retain a considerable degree of organ-specific response to chemical carcinogens. Hepatoma cells of the type described above may be useful for screening the wide spectrum of chemicals which are potentially genotoxic in liver and in extrahepatic tissues and for analyzing their metabolic activation and mechanism of action.

Aflatoxin B1↗
PubMed2002

Comparative study on the characterization of antisera of anti-aflatoxin B1 from rabbit and laying hen.

Polyclonal antisera specific for aflatoxin B1 (AFB1) were developed in rabbits and laying hens immunized with AFB1 conjugated to bovine serum albumin (AFB1-BSA). During the immunization schedule, AFB1-specific antisera from rabbits started to obviously be secreted after 60 days of the first AFB1-BSA injection, reached to a peak at day 120, and started to go down at day 135; while in regard to laying hens, antibodies began to largely be produced at day 90, arrived to a peak at day 135, and began to go down at day 165. The rabbits consistently produced anti-AFB1 antisera in 2-fold higher amounts than the laying hens during the antisera production process. But rabbits' and laying hens' antisera to AFB1 were found not to be apparently different in cross-reaction with aflatoxin analogs. Both rabbits' and laying hens' antisera could be used as immunological reagents for detecting AFB1 in agricultural commodities.

Aflatoxin B1↗
PubMedDate not supplied

Chromosome damage by dothistromin in human peripheral blood lymphocyte cultures: a comparison with aflatoxin B1.

The clastogenic potential of the pine tree fungal toxin dothistromin was studied by metaphase chromosome analysis of stimulated human peripheral blood lymphocytes exposed in vitro. The frequency of gaps, breaks, deletions and exchanges was scored in a series of cultures from 3 different donors. 50 cells were analysed for each dose level on coded slides. Testing was performed with and without added metabolic activation (as S9 mix) and aflatoxin B1 was used as a positive control in all experiments. Dothistromin caused a dose-dependent increase in the frequency of gaps and deletions which was not dependent on added metabolic activation. Even at high doses of dothistromin only a very small number of complex exchange-type aberrations were seen. This is in contrast to aflatoxin B1 where such aberrations were seen at low dose levels and especially in cultures to which S9 mix was added. High doses of dothistromin caused culture toxicity manifesting as haemolysis of the donor red blood cells and reduction of mitotic index. Culture toxicity occurred without a marked increase in aberration frequency. This toxicity may be masking any major potential for clastogenicity by dothistromin.

Aflatoxin B1↗
PubMed1995

Preparation and characterization of monoclonal antibodies against aflatoxin B1.

Five hybridoma cell lines producing monoclonal antibodies (MAb) against Aflatoxin B1 (AFB1) were established after fusion of mouse myeloma cells (SP-2/O-Ag-14) with spleen cells isolated from male BALB/c mice immunized with AFB1-BSA conjugate. Among these, one MAb, designated AFB1-2H8, was of the subtype IgG3 and the acidic fluid of which gave high dilution titers (1:5 x 10(5). The sensitivity of a competitive inhibition enzyme immunoassay (CIEIA) using AFB1-2H8 for AFB1 demonstrated that the linear range was 0.5-50 ng/ml and the minimum detectable concentration of AFB1 was 0.01 ng/ml. The specificity of the MAb was determined and showed no significant crossreaction with any of the metabolites tested. So th-- MAb and the CIEIA described may be useful in the detection of AFB1 in food and feed.

Aflatoxin B1↗
PubMed2002

Expression of human microsomal epoxide hydrolase in Saccharomyces cerevisiae reveals a functional role in aflatoxin B1 detoxification.

The metabolism and genotoxicity of the carcinogenic mycotoxin, aflatoxin B1 (AFB), was studied in the lower eukaryotic yeast Saccharomyces cerevisiae. Recombinant strains of yeast were engineered to express human cDNAs for CYP1A1, CYP1A2, and microsomal epoxide hydrolase (mEH). Coexpression of mEH with CYP1A1 or CYP1A2 resulted in significant decreases in measurements of AFB genotoxicity. In cells expressing CYP1A2 and mEH, the level of AFB-DNA adducts was decreased by 50% relative to cells expressing CYP1A2 alone. Mitotic recombination, as assayed by gene conversion at the trp5 locus, was diminished by 50% or greater in cells coexpressing mEH and CYP1A2 compared to CYP1A2 alone. The mutagenicity of AFB in the Ames assay was also decreased by approximately 50% when AFB was incubated with microsomes containing CYP1A1 or CYP1A2 and mEH versus CYP1A1 or CYP1A2 alone. The biotransformation of AFB by CYPs is known to involve the generation of a reactive epoxide intermediate, AFB-8,9-epoxide, but previous direct biochemical and kinetic studies have failed to demonstrate any functional role for mEH in AFB detoxification. By reconstructing a metabolic pathway in intact yeast, we have shown, for the first time, that mEH may play a role in mitigating the carcinogenic effects of AFB.

Aflatoxin B1↗
PubMed1997

Aflatoxin B1 activation in human lung.

Inhalation exposure to the carcinogen aflatoxin B1 (AFB1) in certain occupations is considerable. Because circumstantial epidemiological evidence suggests that AFB1 inhalation may cause primary lung cancer, we investigated AFB1 activation by human lung microsomes. Microsomes were incubated with [3H]AFB1 (124 microM), and activation to the AFB1-8,9-epoxide was measured as the AFB1-glutathione (AFB1-GSH) conjugate by HPLC. The formation of AFB1-GSH was in the range of 0.05-0.073 fmol/mg protein/min. The role of cytochrome P450 (CYP) 3A in this activation was investigated by oxidation of nifedipine (a prototype substrate for CYP 3A), by immunoinhibition, and by immunoblot analysis. Nifedipine oxidation varied from 0.2 to 19.2 pmol/mg protein/min in microsomes from different subjects, but did not correlate with AFB1 activation. Anti-human polyclonal CYP 3A4 IgG inhibited AFB1 activation. CYP 3A isoforms were immunoestimated to be in the range of 0.01-1.90 pmol/mg protein. Neither CYP 1A2 nor associated activity was detected in the lung microsomes. These data indicate that human lung microsomes activate AFB1 to form the exo-AFB1-8,9-epoxide and that CYP(s) of the 3A subfamily may be responsible for this activity. The relatively low amount of AFB1 activation in human lung compared to that in human liver can be explained by the scarcity of CYP-containing cells in the lung. In situ AFB1 activation and resultant carcinogenic risk are distinctly possible in occupational settings where inhalation of AFB1-contaminated dusts occurs.

Aflatoxin B1↗