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PubMed1992

Influence of four Nigerian food additives on the mutagenicity of aflatoxin B1.

The mutagenicity of aqueous extracts of four Nigerian food additives namely Xylopia aethiopica (Xa), Monodora species (Ms); fermented Litrillus lanatus-ogiri (Og) and fermented Parikia africans (African locust bean)-Iru (Ir) alone and in combination with different concentrations of aflatoxin B1 (0.05 microgram-0.25 micrograms) in the presence and absence of fecalase was studied using the Ames' salmonella mutagenicity assay system. Preliminary screening tests show the tester strain TA98 to be the most sensitive of the four tester strains (TA97, TA98, TA100, TA102) screened. The most mutagenic of the doses of the extracts are 3mg each of Xa and Ms per plate and 5mg each of Og and Ir per plate. A combination of these doses with different concentrations of aflatoxin B1 resulted in an enhanced mutagenicity of aflatoxin B1. The increases could not be accounted for by additive mutagenicity of the extracts and aflatoxin B1. Fecalase further increased the effects resulting from these combinations with the exception of Xa which showed a decrease in mutagenic induction. The increase may be indicative of the presence of some mutagenic glycosides in the extracts.

Adult↗
PubMed1986

Aflatoxin B1 transport in rat blood plasma. Binding to albumin in vivo and in vitro and spectrofluorimetric studies into the nature of the interaction.

Binding of [3H]aflatoxin B1 to rat plasma was investigated in vivo and in vitro. Column chromatographic and polyacrylamide gel electrophoretic analyses clearly demonstrated that aflatoxin B1 bound primarily plasma albumin. Very little binding activity was shown by other plasma proteins. Spectrofluorimetric studies were undertaken to gain some insight into the nature of the aflatoxin-albumin interaction. Quenching of the lone tryptophan fluorescence intensity upon aflatoxin binding was due, at least in part, to a ligand-induced conformational change in the albumin molecule. Aflatoxin B1 binds an apolar site with an association constant of 30 mM-1 at pH 7.4 and 20 degrees C. Neither charcoal treatment of rat albumin nor the presence of 0.15 M NaCl had any significant effect on the interaction. The association constant was pH-dependent, increasing about 1.7-fold as the pH increased from 6.1 to 8.4. This pH dependence is ascribed to a pH-induced conformational change in the albumin molecule. Thermodynamic studies indicated that the aflatoxin-albumin interaction was exothermic (delta H = -29.3 kJ X mol-1), with a delta S value of -13.8 J X mol-1 X K-1.

Aflatoxin B1↗
PubMedDate not supplied

Sampling plans for the determination of aflatoxin B1 in large shipments of animal feedstuffs.

Incremental samples (50, 100, and 500 g) were systematically collected from large shipments of copra meal pellets, copra cake, and palm kernel cake to study the distribution of aflatoxin B1 and evaluate adherence of distribution to the model, CV(2)is (EQ) = A + B/Mis (where CVis = coefficient of variation of the true concentration of aflatoxin B1 within the incremental samples; Mis = mass of the incremental samples; and A and B are constants). Also evaluated was the distribution of aflatoxin B1 among 1 kg composite samples, produced both by random combination of existing incremental samples and by collection of 1 kg composite samples (composed of 10 x 100 g increments) from additional batches of copra meal pellets and cottonseed cake. The efficiency of selected sample preparation (grinding and subdivision) procedures was compared, culminating in the development and description of a variety of sampling plans. The coefficient of variation (CV) among incremental samples varied from 0 to 38%, and was independent of incremental sample size. No significant difference (F-test, 5% significance level) was found between the efficacy of 4 sample preparation methods when these methods were applied to the commodities described above. Various sampling plans were evaluated with estimated CVs from 4.0 to 12.5%, for the aflatoxin B1 content of the composite samples.

Aflatoxin B1↗
PubMedDate not supplied

Indole-3-carbinol induces a rat liver glutathione transferase subunit (Yc2) with high activity toward aflatoxin B1 exo-epoxide. Association with reduced levels of hepatic aflatoxin-DNA adducts in vivo.

Aflatoxin B1 (AFB1), a metabolite of the grain mold Aspergillus flavus, is a potent hepatocarcinogen and widespread contaminant of human food supplies. AFB1-induced tumors or preneoplastic lesions in experimental animals can be inhibited by cotreatment with several compounds, including indole-3-carbinol (I3C), a component of cruciferous vegetables, and the well-known Ah receptor agonist beta-naphthoflavone (BNF). This study examines the influence of these two agents on the AFB1-glutathione detoxication pathway and AFB1-DNA adduction in rat liver. After 7 days of feeding approximately equally inhibitory doses of I3C (0.2%) or BNF (0.04%) alone or in combination, male Fischer 344 rats were administered [3H]AFB1 (0.5 mg/kg, 480 microCi/kg) intraperitoneally and killed 2 hr later. All three experimental diets inhibited in vivo AFB1-DNA adduction (BNF, 46%; I3C, 68%; combined, 51%). Based on Western blots using antibodies specific for the glutathione S-transferase (GST), subunit Yc2 (subunit 10) appeared to be substantially elevated by the diets containing I3C (I3C diet, 4.0-fold increase in band density; combined diet, 2.8-fold). The BNF diet appeared to elevate Yc2 to a lesser extent (2.2-fold increase in band density).(ABSTRACT TRUNCATED AT 250 WORDS)

Aflatoxin B1↗
PubMedDate not supplied

Effect of dietary exposure to aflatoxin B1 on resistance of young chickens to organophosphate pesticide challenge.

White leghorn chickens were placed on a diet containing 0, 1000, or 3000 ppb aflatoxin B1 for 7 weeks. At the end of that time, the birds were challenged orally with the organophosphate pesticide malathion. A malathion dose of 215 mg/kg resulted in significant clinical signs of cholinergic poisoning in 4/10, 5/10, and 8/10 birds fed 0, 1000, and 3000 ppb aflatoxin B1, respectively, and the chickens required antidotal atropine 40 min later. Activity of brain cholinesterase was significantly lower than control levels in all birds given this dose of malathion, with activities being 28% +/- 6, 21% +/- 2, and 15% +/- 2 of control values (Mean +/- standard error, N = 5) if fed 0, 1000, and 3000 ppb aflatoxin B1, respectively. Plasma cholinesterase values paralleled those of brain, with significantly more inhibition in samples from birds given 1000 and 3000 ppb aflatoxins with malathion. Brain and plasma cholinesterase activities in birds fed aflatoxins and given a dose of malathion below the threshold for cholinergic signs (125 mg/kg) were also lower than activities in birds given malathion alone. Although aflatoxin alone had no direct effect on the activities of these enzymes, it appears that this mycotoxin may contribute to the esterase inhibition that is a manifestation of the acute toxic effects of malathion in chickens.

Aflatoxin B1↗
PubMedDate not supplied

Intracellular localization of aflatoxin B1 in rat and human livers.

Hepatocytes of rats fed with a diet containing Aflatoxin B1 show a strong primary fluorescence both in cytoplasm and nucleus. This fluorescence does not exist in control animals fed either with nonfluorescent carcinogens or fluorescent molecules devoid of carcinogenicity. In this work, the primary fluorescence is likely to be due to the presence of aflatoxin B1 (and/or its fluorescent metabolites) in the liver. The same fluorescent microscopy technique was applied to human liver fragments originating from countries known for the high risk of primary liver cancer (Zaire, Uganda). A fluorescence similar to that observed in rat livers was demonstrated. This fluorescence may be due to the occurrence of aflatoxins in the liver.

Adenoma, Bile Duct↗
PubMed1978

Fluorescence studies of the interactions of serum albumin and rat alpha1-fetoprotein with aflatoxin B1. Specificity and binding parameters.

The interaction of bovine serum albumin and rat alpha1-fetoprotein with aflatoxin B1 has been followed by the fluorescence quenching of the protein in presence of the ligand. The binding parameters (n, number of sites and Kd, dissociation constant) have been determined for the bovine serum albumin-alflatoxin B1 system: n = 3.5 and Kd = 3.1 +/- 0.5 . 10(-5) M and for the alpha-fetoprotein-aflatoxin system: n = 4 and Kd = 3.7 +/-0.5 . 10(-5) M. The competition of anilino-naphthalene-sulfonate and aflatoxin B1 for the same hydrophobic sites on bovine serum albumin has been demonstrated. The fluorescence quenching of various proteins (lysozymes, egg-albumin, gamma-globulin) by aflatoxin B1 have shown that there is not a strict specificity of aflatoxin towards proteins.

Aflatoxins↗
PubMed2001

Isolation, partial characterization and growth characteristics of a bacterium resistant to aflatoxin B1.

A bacterium was isolated from the soil of dumping ground for cattle yard waste by enrichment culture containing aflatoxin B1. This bacterium was closely related to Bacillus firmus that was found to be a non-pathogenic bacterium. The minimum inhibitory concentration of aflatoxin B1 to the bacterium was found to be 80 microg ml(-1) as measured by total viable count and soluble protein content methods. The bacterium was sensitive to all the tested antibiotics. Plasmid curing by chemical agents did not show the resistance character residing in the plasmid. Protein profiles of cell extracts of aflatoxin B1 resistant bacterium grown in the presence and absence of the toxin showed 46 and 44 protein bands respectively in SDS-PAGE. It was observed that 39 bands were common in both the extracts and the remaining bands were showing differences near the high molecular weight range.

Aflatoxin B1↗
PubMed1980

Carcinogen aflatoxin B1 is located preferentially in internucleosomal deoxyribonucleic acid following exposure in vivo in rainbow trout.

The purpose of this work was to investigate the distribution in chromatin of deoxyribonucleic acid (DNA) adducts of aflatoxin B1, following exposure in vivo. Rainbow trout were injected intraperitoneally with radiolabeled aflatoxin B1, a potent procarcinogen known to readily induced hepatocellular carcinomas in these fish. After maximum incorporation, liver nuclei were prepared and digested with micrococcal nuclease. Mono-, di-, and trinucleosomal fractions were purified from several stages of nuclease digestion, and the lengths and specific activities of their DNA were determined. The results indicate that aflatoxin B1 is approximately 5 times as likely on a per nucleotide basis to localize on internucleosomal (linker) DNA as on nucleosomal core DNA in this system.

Aflatoxin B1↗
PubMed1983

Aflatoxicol and aflatoxins B1 and M1 in eggs and tissues of laying hens consuming aflatoxin-contaminated feed.

This study was undertaken to relate quantitatively the aflatoxin residue found in eggs and tissues to the aflatoxin intake via feed. Eighteen hens were fed an aflatoxin B1 (B1)-contaminated feed (8 micrograms/g) for 7 days, after which half the group was sacrificed; the remainder were sacrificed after an additional 7 days on an aflatoxin-free diet. Eggs were collected over the entire 14-day period. Aflatoxicol (R0), B1, or both were found in eggs and tissues (kidneys, liver, muscle, blood, and ova). Aflatoxin M1 (M1) (.04 to .1 ng/g) was found only in the kidneys. Levels of R0 and B1 were approximately the same in eggs, ova, kidneys, and liver. In eggs, the levels of R0 and B1 (.02 to .2 ng/g) increased steadily for 4 or 5 days, after which time the levels plateaued and then decreased after B1 withdrawal at the same rate as they had increased. At 7 days after withdrawal, only trace amounts of R0 (.01 ng/g) remained in eggs. All tissues, except blood, from hens sacrificed immediately before aflatoxin withdrawal contained R0 (.04 to .4 ng/g) or R0 and B1 (.04 to .8 ng/g). The R0 (.03 to .11 ng/g) was the only aflatoxin detected in muscle, and B1 (.05 to .07 ng/g) was the only aflatoxin in blood. Seven days after aflatoxin withdrawal, B1 (.08 ng/g) was found in one of nine livers and R0 (.01 to .04 ng/g) in eight of nine muscles analyzed, but no aflatoxins were found in any other tissues.

Aflatoxin B1↗
PubMed1998

Aflatoxin B1 and sulphobromophthalein binding to the dimeric human glutathione S-transferase A1-1: a fluorescence spectroscopic analysis.

The binding interactions between dimeric human class alpha glutathione S-transferase A1-1 (GST A1-1) and aflatoxin B1 or sulphobromophthalein (BSP) were characterised. Aflatoxin B1 binds to GST A1-1 with a stoichiometry of 1.1 mol/mol of dimeric enzyme. The binding interaction, which can be described by a hyperbolic saturation isotherm (Kd = 8+/-2 microM), does not induce major structural changes in the enzyme, nor does it inhibit enzymatic activity. The average distance between the single tryptophan residue (Trp20) of GST A1-1 and protein-bound aflatoxin B1 was calculated to be 22.7 A by means of fluorescence resonance energy transfer. The aflatoxin-binding region, according to this calculated distance, was determined to be located in the dimer interface cleft near the crystallographic two-fold axis. Hill-plot analyses suggest that a positive co-operative interaction exists between BSP and the dimeric GST A1-1 (h = 1.6+/-0.1; K' = 14+/-0.6 microM). The binding of BSP induces a conformational change in the enzyme which is accompanied by a decrease in the molecular flexibility and in the solvent-accessible properties of the enzyme's Trp20 residue. Site-directed mutagenesis of Trp20 (Trp20-->Phe) confirms that this residue is situated in the binding environment and although it is not essential for BSP binding, it is involved in the interaction. Furthermore, the structural change associated with BSP binding alters the hyperbolic character of the glutathione saturation curve. This indicates that there may also be a cooperative interaction between glutathione and BSP or that BSP binding induces asymmetric functioning of the two enzyme subunits so that they become unequal in catalytic activity.

Aflatoxin B1↗
PubMed1977

[Antibacterial properties of aflatoxin B1: cytotoxic effects on Bacilus thuringiensis (Berliner)].

In a sensitive strain of Bacillus thuringiensis (Berliner), aflatoxin B1 inhibited growth with a dose above 5.0 microgram/ml. With subinhibitory levels (0.5 - 5.0 microgram/ml) physiological damage (decreased growth rate) and cellular alteration (filamentous cells) were noted. With these doses the mycotoxin disturbs various metabolisms : DNA synthesis (gradual blockage of the specific bacteriophage multiplication and dispersion of nuclear apparatus in giant cells); protein synthesis (decrease of protease secretion (2.0 microgram/ml), thuricin excretion (3.0 microgram/ml) and inhibition of endotoxin formation (4.0 microgram/ml); specific activities (bacterial motility, flagellar arrangment and sporulation were respectively affected with 1.0, 0.5 and 4.0 microgram/ml). The mycotoxin did not affect the metabolism of a resistant mutant isolated in the presence of a lethal dose of aflatoxin B1 (mutation rate : 1.10(8) with 20 microgram/ml). The numerous bacterial responses to aflatoxin B1 indicate that the probable site of its toxic binding may not be restricted to a particular locus on the DNA. On the contrary these observations suggest that there exist many combining affinities of the mycotoxin for intracellular sites or interference with a key-function such as the messenger-RNA synthesis.

Aflatoxins↗
PubMed1992

Comparative assessment of the effect of aflatoxin B1 on hepatic dysfunction in some mammalian and avian species.

1. Aflatoxin B1 (1.5 mg/kg body weight, i.p.) was administered to rats, mice, quail and chickens to examine the comparative effect on hepatic microsomal drug-metabolizing enzymes, cytosolic glutathione S-transferase and serum enzymes. 2. Administration of aflatoxin B1 to rats resulted in a significant decrease in microsomal cytochrome P-450, NADPH-cytochrome c reductase, activities of aminopyrine N-demethylase, aniline hydroxylase, cytosolic glutathione S-transferase and liver glutathione content. However, no significant changes in these parameters were seen in mice. 3. Quail showed a significant decrease in the content of cytochrome P-450 and the activities of aminopyrine N-demethylase, aniline hydroxylase and cytosolic glutathione S-transferase. A similar treatment did not affect these biotransformation enzymes in chickens. 4. The activities of serum enzymes, sorbitol dehydrogenase, alanine aminotransferase and aspartate aminotransferase were increased significantly in rats and quail. Mice exhibited a significant increase in the activities of sorbitol dehydrogenase and aspartate aminotransferase, while chickens showed a significant increase only in alanine aminotransferase.

Aflatoxin B1↗
PubMedDate not supplied

Caffeine as main interfering compound in radioimmunoassay of aflatoxin B1 in coffee samples.

The content of caffeine in coffee extracts prepared for radioimmunoassay of aflatoxin B1 was determined by gas chromatography. The extracts from coffee beans and decaffeinated coffee contained 1.76-4.60 and 0.71-0.85 g caffeine/kg, respectively. These concentrations of caffeine caused false results in radioimmunoassay of aflatoxin B1 in the range 1.0-2.8 micrograms/kg for coffee beans and 0.3-0.4 micrograms/kg for decaffeinated coffee.

Aflatoxin B1↗
PubMed1987

Identification of O-methylsterigmatocystin as an aflatoxin B1 and G1 precursor in Aspergillus parasiticus.

An isolate of Aspergillus parasiticus CP461 (SRRC 2043) produced no detectable aflatoxins, but accumulated O-methylsterigmatocystin (OMST). When sterigmatocystin (ST) was fed to this isolate in a low-sugar medium, there was an increase in the accumulation of OMST, without aflatoxin synthesis. When radiolabeled [14C]OMST was fed to resting mycelia of a non-aflatoxin-, non-ST-, and non-OMST-producing mutant of A. parasiticus AVN-1 (SRRC 163), 14C-labeled aflatoxins B1 and G1 were produced; 10 nmol of OMST produced 7.8 nmol of B1 and 1.0 nmol of G1, while 10 nmol of ST produced 6.4 nmol of B1 and 0.6 nmol of G1. A time course study of aflatoxin synthesis in ST feeding experiments with AVN-1 revealed that OMST is synthesized by the mold during the onset of aflatoxin synthesis. The total amount of aflatoxins recovered from OMST feeding experiments was higher than from experiments in which ST was fed to the resting mycelia. These results suggest that OMST is a true metabolite in the aflatoxin biosynthetic pathway between sterigmatocystin and aflatoxins B1 and G1 and is not a shunt metabolite, as thought previously.

Aflatoxin B1↗
PubMed1975

Effect of aflatoxin B1 on lipids of rat tissues.

The effect of aflatoxin B1 on lipids of liver, kidney, adipose and plasma of rats was studied. A single dose administration (6 mg/kg body weight) increased liver and kidney weights and their total lipids within 24 h. Increase in liver lipids was confined mainly to phospholipid and cholesterol, whereas triglycerides showed a significant decrease. Adipose tissue triglycerides were, however, increased. Plasma showed decreases in triglycerides, free fatty acids and cholesterol. Incorporation studies with palmitate-1-14C revealed increased incorporation in adipose tissue lipids and decreased incorporation in liver and plasma lipids, thereby indicating an increased synthesis of lipids in adipose. Their mobilization to plasma was, however, inhibited, hence the low levels of triglyceride in liver. But the adrenals showed hypo-activity upon aflatoxin B1 administration.

Adipose Tissue↗
PubMed1995

Cassia senna inhibits mutagenic activities of benzo[a]-pyrene, aflatoxin B1, shamma and methyl methanesulfonate.

Ethanol extract of Senokot tablets (Cassia senna concentrate used as vegetable laxative), was found to be non-mutagenic while it inhibited the mutagenicity of benzo[a]pyrene, shamma, aflatoxin B1 and methyl methanesulfonate in the Ames histidine reversion assay using the Salmonella typhimurium tester strain TA98. While the Senokot extract completely inhibited the mutagenicity of promutagens (i.e. metabolic activation dependent) like benzo[a]pyrene and shamma, it reduced the mutagenic activity of the direct acting mutagen methyl methanesulfonate by only 58%. The mutagen aflatoxin B1 showed a 25-fold increase in the number of histidine revertants per plate at low concentrations (1.0-4.0 micrograms/plate) in the presence of metabolic activation system while at high concentrations (10.0-30.0 micrograms/plate) it proved to be weakly mutagenic (with a 5-fold increase in the number of histidine revertants/plate) without metabolic activation. The Senokot extract completely inhibited the mutagenic effect of low concentrations of aflatoxin B1 in the presence of metabolic activation but not that resulting from higher concentrations without metabolic activation. The results obtained with benzo[a]pyrene, shamma and aflatoxin B1 indicated that the antimutagenic effects of Senokot extract could be largely due to an interaction with the metabolic process involved in the activation of procarcinogens. However, the results obtained with methyl methanesulfonate suggested that factors in Senokot may also interact with direct mutagens to produce some antimutagenic effects. An ethanol extract of crude senna leaves found to be weakly mutagenic also inhibited (though less than Senokot) the mutagenic effect of benzo[a]pyrene suggesting that the antimutagenic principle is present in the complex plant material itself.

Aflatoxin B1↗
PubMed1978

The effects of aflatoxin B1 on rat fetal lung lipids.

The administration of aflatoxin B1 to rats on days 17 and 19 of pregnancy caused increased synthesis of the total lipids and the fatty acids, and decreased synthesis of the phosphatidyl choline in 21-day-old fetal lung. Aflatoxin B1 caused toxicity in the fetal lung as evidenced by the excessive accumulation of the lamellar bodies and the osmiophilic spheroids in the type II cells and the alveolar lumen, respectively. The rearrangement of the lamellar form to the continuous sheet-like tubular myelin form was reduced in the alveolar lumen of the treated lung.

Aflatoxins↗