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PubMed1996

Species-specific differences in hepatic mutant frequency and mutational spectrum among lambda/lacI transgenic rats and mice following exposure to aflatoxin B1.

In vivo mutations were studied in lambda/lacI (Big Blue) transgenic C57BL/6 mice and F344 rats following exposure to either AFB1 (aflatoxin B1) or DMSO vehicle. Fourteen days after exposure, livers were removed for DNA extraction and subsequent mutational analysis of the lacI gene. Mice injected with a single i.p. dose of AFB1 at 2.5 mg/kg did not show a significant increase in liver mutant frequency relative to vehicle-treated controls. DNA sequence analysis of lacI mutations collected from the AFB1-treated mice showed a pattern of mutation similar to that of the previously observed spontaneous mouse liver mutational spectrum. In contrast, rats subjected to one-tenth the mouse AFB1 dosage responded with an approximate 20-fold induction in liver mutant frequency over background. Sequencing of lacI mutations also revealed spectral differences between vehicle- and AFB1-treated rats. A large increase in G:C-->T:A transversions was observed among lacI mutations isolated from the AFB1-treated rats. This work is among the first multi-species in vivo mutagenicity studies using transgenic rodents harboring the same shuttle vector. Such multi-species in vivo assays may prove to be valuable in the areas of mechanistic analysis and risk assessment.

Aflatoxin B1↗
PubMed2006

Effects of aflatoxin B1 and fumonisin B1 on body weight, antibody titres and histology of broiler chicks.

1. Our objective was to evaluate the toxic effects of aflatoxin B1 (AFB1) and fumonisin B1 (FB1), administered singly or in combination to broilers. 2. Feeds were prepared with concentrations equal to 0, 50 and 200 microg AFB1/kg, and/or 0, 50 and 200 mg FB1/kg, and offered to broiler chicks from 8 to 41 d of age. The experimental design was totally randomised, in a 3 x 3 factorial arrangement with 9 treatments and 12 birds per treatment. Animals were vaccinated against Newcastle disease on d 14 of life and killed at 41 d. 3. Compared with controls, all mycotoxin-treated groups at 41 d had lower body weight and weight gain, and higher relative heart weight. The relative weight of the liver increased only in birds fed diets containing 200 mg FB1, singly or in combination with AFB1. 4. At 35 d, all groups receiving mycotoxin-treated rations had reduced geometrical mean antibody titres, with birds from groups fed combinations of AFB1 and FB1/kg having even lower values, when compared to the other groups. 5. Histological changes were observed only in liver from birds fed mycotoxin-contaminated rations, and in kidneys of birds fed the diet containing 200 microg AFB1 and 200 mg FB1/kg. Main alterations included vacuolar degeneration and cell proliferation of bile ducts in the liver, and hydropic degeneration in renal tubules in the kidneys. 6. We concluded that AFB1 and FB1 in combination have primarily additive effects on body weight, liver structure and immunological response of broilers at the concentrations used.

Aflatoxin B1↗
PubMed1993

Acute hepatic response to aflatoxin B1 in rats fed a methyl-deficient, amino acid-defined diet.

In order to evaluate the relative contribution of aflatoxin B1 (AFB1)-induced toxicity towards a methyl-deficient diet influenced AFB1 carcinogenesis, a no-observed-effect-level (NOEL) for AFB1, with reference to liver damage, was determined in rats fed a nutritionally complete amino acid-defined basal (CMS) diet or a choline-methionine-deficient (CMD) diet. After 3 weeks of dietary treatment, male Fischer 344 rats received a single, oral dose of AFB1 in the range of 100-600 pg/kg body weight. At 24, 48 and 72 h after AFB1 treatment, six serum biochemical parameters were analysed in parallel with histological examination of liver sections. In rats fed the CMS diet and receiving 250-600 micrograms/kg AFB1, serum levels of glutamyl oxalo-transaminase (SGOT), glutamyl pyruvic transaminase (SGPT), alkaline phosphatase (ALP) and total bilirubin increased, glucose levels decreased and gamma glutamyl transpeptidase (GGT) levels remained unchanged over the 72-h period following mycotoxin treatment. However, at 100 micrograms/kg AFB1, these serum parameters remained at control levels. Pathological examination of liver sections indicated no significant lesions at 100 micrograms/kg AFB1 confirming this as the non-necrogenic dose or NOEL in CMS diet group rats. In contrast, in CMD diet fed rats, serum or pathology data showed no obvious time- or dose-response to mycotoxin treatment, extensive hepatic lipidosis in response to dietary treatment being the only predominant lesion in this diet group. The milder response of CMD rat livers to a single dose of AFB1 suggest a possible reduction in the susceptibility of these livers to AFB1 toxicity.

Aflatoxin B1↗
PubMedDate not supplied

Carnosic acid from rosemary extracts: a potential chemoprotective agent against aflatoxin B1. An in vitro study.

Since oxidative stress plays an important role in the toxicity mechanism of several mycotoxins such as aflatoxin B1 (AFB1), the use of natural or synthetic free radical scavengers could be a potential chemopreventive strategy. Carnosic acid (CA) is the major polyphenolic compound present in rosemary plants and it can also be found in sage leaves. Its free radical scavenging properties were tested with two chemical methods. It was found that it has good free radical scavenging capacity at pH 7.4. This study also found that a 24 h pre-treatment with 10, 20 and 30 microm CA led to a clear, dose-dependent protective effect on cell toxicity, reducing cell death induced by a 24 h exposure with 10 microm AFB1, respectively, by 16% (P < 0.05), 26% (P < 0.01) and 63% (P < 0.001). It was also found that a 24 h pre-treatment with 20 and 30 microm CA achieved a reduction of ROS levels, respectively, of 146% (P < 0.001) and 173% (P < 0.001) in HepG2 cells exposed to 10 microm AFB1 for 8 h. Moreover, in cells pre-incubated with 30 microm CA for 24 h the concentration of 8-OH-deoxyguanine decreased by 57% (P < 0.001) with respect to the cells exposed for 24 h to 10 microm AFB1 alone. The results obtained with the in vitro and chemical studies support the theory that AFB1 induced oxidative stress plays an important role in the cytotoxic mechanism of this mycotoxin. Furthermore these findings suggest a starting point for developing alimentary strategies in order to counteract the damage caused by AFB1 contamination in feed and food.

8-Hydroxy-2'-Deoxyguanosine↗
PubMed2003

Immunotoxicity of aflatoxin B1 in rats: effects on lymphocytes and the inflammatory response in a chronic intermittent dosing study.

We investigated the effects of aflatoxin B1 (AFB1) on isolated splenic lymphocytes and the histo-morphologic changes in the spleens and liver of Fisher-344 male rats. Weaned animals were fed chow diets that contained 0, 0.01, 0.04, 0.4, or 1.6 ppm AFB1, using an intermittent dosing regimen (4 weeks on and 4 weeks off AFB1), for 40 weeks. An additional group of animals was fed the 1.6 ppm AFB1 diet continuously. The intermittent dosing regimen was designed to evaluate effects of cumulative dose and exposure for risk assessment comparisons. The percentages of T and B cells were affected as shown by flow cytometric analysis after the dosing cycles. The observed changes appeared to reverse or compensate to some extent after the off cycles. Lymphocytes were stimulated in culture for analysis of the production of IL-2, IL-1, and IL-6. Significantly increased production of IL-1 and IL-6 was seen in the second dosing cycle (12 weeks) and the second "off" cycle (16 weeks) at the higher doses. Inflammatory infiltrates were seen in the liver after eight weeks of continuous and intermittent dosing and were increased in size and number at 12 weeks in both 1.6 ppm dose groups correlating with the peak production of Il-1 and IL-6. We concluded that AFB1 effects on the immune system can be either stimulatory or suppressive dependent on a critical exposure window of dose and time. Immune cells in spleen such as T-lymphocytes and macrophages, both important mediators of inflammatory responses to tissue damage, were affected differently in the continuous and intermittent exposures to AFB1.

Administration, Oral↗
PubMed1997

Reaction of aflatoxin B1 exo-8,9-epoxide with DNA: kinetic analysis of covalent binding and DNA-induced hydrolysis.

The exo isomer of aflatoxin B1 (AFB1) 8,9-epoxide appears to be the only product of AFB1 involved in reaction with DNA and reacts with the N7 atom of guanine via an SN2 reaction from an intercalated state. Although the epoxide hydrolyzes rapidly in H2O (0.6 s-1 at 25 degrees C), very high yields of DNA adduct result. Experimental binding data were fit to a model in which the epoxide forms a reversible complex with calf thymus DNA (Kd = 0.43 mg ml-1, or 1.4 mM monomer equivalents) and reacts with guanine with a rate of 35 s-1. Stopped-flow kinetic analysis revealed attenuation of fluorescence in the presence of DNA that was dependent on DNA concentration. Kinetic spectral analysis revealed that this process represents conjugation of epoxide with DNA, with an extrapolated rate maximum of 42 s-1 and half-maximal velocity at a DNA concentration of 1.8 mg ml-1 (5.8 mM monomer equivalents). The rate of hydrolysis of the epoxide was accelerated by calf thymus DNA in the range of pH 6-8, with a larger enhancement at the lower pH (increase of 0.23 s-1 at pH 6.2 with 0.17 mg DNA ml-1). The same rate enhancement effect was observed with poly[dA-dT].poly[dA-dT], in which the epoxide can intercalate but not form significant levels of N7 purine adducts, and with single-stranded DNA. The increased rate of hydrolysis by DNA resembles that reported earlier for epoxides of polycyclic hydrocarbons and is postulated to involve a previously suggested localized proton field on the periphery of DNA. The epoxide preferentially intercalates between base pairs, and the proton field is postulated to provide acid catalysis to the conjugation reaction.

Aflatoxin B1↗
PubMed1983

Interrelationships in mice of antipyrine half-life, hepatic monooxygenase activities and liver S9-mediated mutagenicity of aflatoxin B1, benzo[alpha]pyrene 7,8-dihydrodiol, 2-acetylaminofluorene and N-nitrosomorpholine.

To evaluate the predictive value of serum antipyrine half-life AP(T1/2) as an index of hepatic carcinogen metabolism, groups of C57BL/6 and DBA/2 mice were treated with various inducers and inhibitors of cytochrome P-450-dependent monooxygenases (pregnenolone-16 alpha-carbonitrile (PCN), phenobarbital (PB), 5,6-benzoflavone (5,6-BF), 3-methylcholanthrene (MC), disulfiram (DIS), 7,8-BF). Groups of mice were also given ethanol (3% in drinking water) for 12 days. Within each group, mean serum AP-(T1/2) was compared with (i) the in vitro activity of hepatic microsomal benzo[alpha]pyrene (BP) 3-hydroxylase, 2-acetylaminofluorene (AAF)-N-hydroxylase and aldrin monooxygenase, and (ii) the liver S9-mediated mutagenicity of aflatoxin B1 (AFB), trans-7,8-dihydro-7,8-dihydroxybenzo[alpha]pyrene (BP 7,8-diol), 2-acetylaminofluorene and N-nitrosomorpholine (NMOR) in Salmonella typhimurium strains. Serum AP(T1/2) was only correlated negatively with the activity of BP 3-hydroxylase (P less than 0.001) and aldrin monooxygenase (P less than 0.001). No statistically significant correlation was found between serum AP(T1/2) and liver S9-mediated mutagenicity for any of the four carcinogens. On the basis of these results, we conclude that serum AP(T1/2) may not be a reliable index of the capacity of liver to convert carcinogens into reactive intermediates.

2-Acetylaminofluorene↗
PubMed2002

Effects of bicyclol on aflatoxin B1 metabolism and hepatotoxicity in rats.

AIM: To study the effect of new antihepatitis drug, bicyclol, on the metabolism and hepatotoxicity of aflatoxin B1 (AFB1) in rats. METHODS: Rats were given bicyclol 300 mg/kg/d ig for 3 d and then injected ip with AFB1 1.5 mg/kg. Liver damages were examined 16 h after ip AFB1. The in vitro metabolism of AFB1 by bicyclol-pretreated liver microsomes was investigated by HPLC assay. RESULTS: Bicyclol (300 mg/kg/d for 3 d) pretreatment provided protection against AFB1 hepatotoxicity as evidenced by the decrease of AFB1-elevated serum aminotransferase and hepatic malondialdehyde in rats. Bicyclol pretreatment slightly increased the production of the less toxic metabolite aflatoxin Q1. Bicyclol increased liver cytochrome P450 content, CYP 2B1-mediated 7-pentoxyresorufin O-dealkylase (PROD) activity, cytosolic glutathione (GSH) level, and GSH S-transferase (GST) activities. Moreover, bicyclol increased CYP 3A-mediated erythromycin-demethylase and CYP 1A-mediated 7-ethoxyresorufin O-deethylase (EROD) activities. CONCLUSION: Bicyclol protected rats against AFB1 hepatotoxicity by increasing the detoxifying metabolism of AFB1 in the liver.

Aflatoxin B1↗
PubMed1988

[Effect of beta-carotene on sister chromatid exchanges induced by MNNG and aflatoxin B1 in V79 cells].

In order to elucidate the mechanism of tumor prevention of beta-carotene, its effect on sister chromatid exchanges (SCE) induced by MNNG in cultured V79 cells, under condition free of the enzyme system to convert beta-carotene into vitamin A, was studied. It was found that SCE level was significantly increased by high doses beta-carotene (10(-5)-10(-4) M) and the enhancement of SCE was restored to its original level by addition of alpha-tocopherol (final concentration 2 micrograms/ml). This may be due to the latter inhibiting the oxidation of beta-carotene and reducing the amount of oxidated carotene, which is toxic for cultured cells. Combination of beta-carotene and alpha-tocopherol at low doses inhibited SCE induced by MNNG (P less than 0.05) but no protective activity was observed when used separately. It was also found that beta-carotene (2 x 10(-7) M) and retinol (16 micrograms/ml) inhibited SCE induced by aflatoxin B1, which is activated by S-9 mixture. The present data clearly show that the antitumor activity of beta-carotene may be attributed to both itself and its degraded compound vitamin A, and may take part in the initiation of carcinogenesis. Combination of beta-carotene and other cancer preventive drugs is more effective and safer than it used individually.

Aflatoxin B1↗
PubMedDate not supplied

[Detoxification of aflatoxin B1 by different chemical methods and evaluation of the effectiveness of the treatments applied].

Different chemical treatments were applied to solutions of Aflatoxin B1 in order to compare their efficacy for the detoxification of AfB1: sodium sulfite, sodium hydrogen sulfate, sodium hydroxide, ammonia, sodium hypochlorite, hydrogen peroxide. The rate of the detoxification of AfB1 has been followed by three experimental approaches: 1. Quantitative estimation of the unmodified AfB1 by HPLC chromatography. 2. Quantitative estimation of the most toxic metabolite. AfB1-epoxide by chemical transformation into the trishydroxy AfB1 derivative followed by HPLC analysis. 3. Determination of the bacterial mutagenic activity, following the Ames' test. Among the different detoxification methods that were compared, the treatment with sodium sulfite proved to be the most efficient and seems thus to be recommended for foods contaminated by AfB1.

Aflatoxin B1↗
PubMed1999

Effects of aflatoxin B1 on the hepatic microsomal mixed function oxidase system during phenobarbital and benzo(a)pyrene treatment in chickens.

Administration of 1.5 mg aflatoxin B1 (AFB1)/kg in DMSO as a single i.p. dose to 80 mg phenobarbital/kg i.p. for 3 d pretreated chickens showed significant decrease in the levels of electron transport components and drug metabolizing enzymes compared to phenobarbital administration alone. Induction of mixed function oxidase enzymes due to phenobarbital was not affected by the AFB1 pretreatment. AFB1 administration to 20 mg benzo(a)pyrene/kg in safflower seed oil i.p. for 2 d pretreated chickens showed significant decrease in cytochrome b5 and drug metabolizing enzymes when compared with benzo(a)pyrene treatment alone. However, cytochrome P450 level was slightly higher due to administration of AFB1 to benzo(a)pyrene-injected chickens. The results indicate that the phenobarbital-induced cytochrome P450 is more susceptible to AFB1 than benzo(a)pyrene-induced cytochrome P450.

Aflatoxin B1↗
PubMedDate not supplied

Identification of a novel dihydroxy metabolite of aflatoxin B1 produced in vitro and in vivo in rats and mice.

HPLC analysis of bile obtained from rats given aflatoxin B1 (AFB) demonstrates the presence of numerous polar metabolites. The glutathione conjugate derived from AFB 8,9-epoxide and the glucuronide conjugate of aflatoxin P1 (AFP) have previously been identified as the two major polar metabolites. The most polar peak present in bile from AFB-treated rats is converted to a less polar peak upon incubation with beta-glucuronidase, which has a parent ion m/e of 314 amu. Treatment of this aglycon with diazomethane produced a product which cochromatographs with aflatoxin M1 (AFM). From these data it is concluded that the most polar peak in bile from AFB-treated rats is the glucuronide conjugate of 4,9a-dihydroxyaflatoxin B1. This dihydroxy AFB metabolite was produced in vitro in mouse microsomal incubations, and time-course studies of its production suggest that it is largely formed by 9a-hydroxylation of AFP, although some may be formed by 4-O-demethylation of AFM. Direct incubation of AFP and AFM with mouse microsomes confirmed that this metabolite can be formed from both AFP and AFM. An HPLC method is described which is capable of base line resolution of this novel dihydroxyaflatoxin metabolite and eight other hydroxylated metabolites of AFB, as well as the glutathione conjugate of AFB 8,9-epoxide.

Aflatoxin B1↗
PubMed1992

Effect of aflatoxin B1 on in vitro production of interleukin-1 by bovine mononuclear phagocytes.

In this study we examined the effects of preincubation with aflatoxin B1 (AFB1) on the ability of bovine monocytes to produce the immunological mediator interleukin-1 (IL-1). Monocytes preincubated for 6-24 h with 10 micrograms ml-1 AFB1 demonstrated a diminished capacity to release IL-1 activity in response to bacterial lipopolysaccharide (LPS). Preincubation for less time, or with lower concentrations of AFB1, did not affect IL-1 release. Pretreatment of monocytes with AFB1 also resulted in diminished release of IL-1 activity in response to in vitro infection with Listeria monocytogenes. Incubation with AFB1 reduced the amount of IL-1 beta mRNA in LPS-stimulated bovine monocytes; however, this was observed only at high concentrations of AFB1 that non-specifically reduced steady-state transcription of actin mRNA. We therefore concluded that AFB1 does not specifically suppress monocyte release of IL-1, other than through its general inhibition of mRNA transcription.

Aflatoxin B1↗
PubMedDate not supplied

Comparative effects of scopoletin and aflatoxin B1 on bovine hepatic mitochondrial respiration in vitro.

A comparative study of the in vitro effects of the coumarin compounds, scopoletin and aflatoxin B1 (AFB1), on bovine (Bos indicus) hepatic mitochondrial respiration was carried out polarographically, using isocitrate -NAD+ (3 - site), succinate (2 - site), and reduced cytochrome c (1 - site), as respiratory substrates. Both scopoletin and AFB1 elicited a substrate--dependent stimulation or inhibition of the mitochondrial states 4 and 3 respiration. The results suggest that AFB1 has a higher tendency to inhibit the mitochondrial respiration than scopoletin, while scopoletin showed higher uncoupling effects than AFB1. The effects of scopoletin and AFB1 on mitochondria were more pronounced on the electron transport than on phosphorylation reaction. The extent (3-35%) of AFB1 induced inhibition of bovine mitochondrial respiration observed in this study, was appreciably lower than the values indicated in other animal species (rats and guinea fowls) reported in previous studies using equivalent concentrations of the toxin. These results were discussed in terms of the susceptibility of the animal species to the toxic effects of scopoletin and AFB1.

Aflatoxin B1↗
PubMed1994

The primary and secondary metabolism of aflatoxin B1 by rat hepatocytes cultured on matrigel.

Rat hepatocytes on culturing rapidly lose the ability to metabolize many xenobiotics including the mycotoxin aflatoxin B1 (AFB1). Rat hepatocytes cultured for 5 days on plastic retain < 10% of the initial cytochrome P450 content compared with 34% in cells grown on matrigel alone and 74% in cells cultured on matrigel plus phenobarbital (PB). Although microsomal activation of AFB1 was preserved in matrigel cultured hepatocytes and increased by PB in all the culturing conditions examined, the AFB1 macromolecular binding capacity was reduced to < 10% of that present in the initial cultures. This lack of correlation between cytochrome P450 levels, microsomal activation, and AFB1 binding involved cytosolic glutathione-S-transferase activity (GST). This increased in matrigel cultured cells and was further enhanced by PB. Western blotting of the cytosols showed that the expression of the alpha class GST subunit Yc2 correlated with AFB1-GSH conjugate formation. By contrast, expression of the alpha class GST Ya-type subunit showed no similar close correlation. The expression of pi class GST Yf subunit, which is associated with dedifferentiation in hepatocytes, was suppressed by culturing on matrigel. The results obtained using hepatocytes cultured on matrigel indicate that despite limitations, this comprises a potentially useful model for the in vivo situation.

Aflatoxin B1↗
PubMedDate not supplied

Glutathione conjugation of aflatoxin B1 exo- and endo-epoxides by rat and human glutathione S-transferases.

Much evidence supports the view that the rate of conjugation of glutathione (GSH) with aflatoxin B1 (AFB1) exo-epoxide is an important factor in determining the species variation in risk to aflatoxins and that induction of GSH S-transferases can yield a significant protective effect. An assay has been developed in which the enzymatic formation of the conjugates of GSH and AFB1 exo-epoxide and the recently described AFB1 endo-epoxide is measured directly. 1H NMR spectra are reported for both the AFB1 exo- and endo-epoxide-GSH conjugates. Structural assignments were made by comparison with AFB1 exo- and endo-epoxide-ethanethiol conjugates, for which nuclear Overhauser effects were measured to establish relative configurations. The endo-epoxide was found to be a good substrate for GSH conjugate formation in rat liver cytosol while mouse liver cytosol conjugated the exo-epoxide almost exclusively. Human liver cytosol conjugated both epoxide isomers to much lower extents than did cytosols prepared from rats or mice. Purified rat GSH S-transferases catalyzed the formation of the AFB1 exo-epoxide-GSH conjugate in the order 1-1 approximately 4-4 approximately 3-3 greater than 2-2 greater than 4-6 (7-7 and 8-8 did not form the exo-epoxide-GSH conjugate at levels above the nonenzymatic rate). The only rat GSH S-transferases that conjugated the endo-epoxide were 4-4 and 4-6, with 4-4 being the more active.(ABSTRACT TRUNCATED AT 250 WORDS)

Aflatoxin B1↗
PubMed1995

In vivo biotransformation of aflatoxin B1 and its interaction with cellular macromolecules in neonatal rats.

In this study, the ability of neonatal rat liver to metabolise [3H]aflatoxin B1 (AFB1) was compared to that of the adult animal. In order to make this comparison, neonatal and young adult rats were killed 2, 6, 12 and 24 h after injection with a single i.p. dose of AFB1. The rate of AFB1 adduct formation to nuclear DNA and protein was measured in hepatic and pulmonary tissues. The results demonstrated that AFB1 was epoxidized more rapidly by the adult's liver and lungs 2 h after the toxin administration, compared with those of the neonatal's (adult 30 pmol and neonatal 12 pmol AFB1 bound/mg DNA). However, these differences were more pronounced in hepatic than in pulmonary tissues. The same differences between AFB1-DNA adducts were also observed at different time points. These changes are certainly related to the level of hepatic cytochrome P-450. The delayed cytochrome P-450-dependent AFB1 activation in neonatal's liver provides time enough for de-epoxidation of slowly generated epoxide. The rate of AFB1-epoxide formation at this age was consistent with the activity of phase II metabolism of AFB1 (glutathione conjugation). In addition, the hydrolysis of AFB1-DNA adducts at a relatively higher rate by neonatal's liver may also contribute to the quick removal of the adducts. In spite of the aforementioned evidence which shows the capability of neonatal liver to handle AFB1, the fate of large amounts of free (non-metabolised) AFB1 deposited in neonatal's liver is not well understood.

Aflatoxin B1↗
PubMed1995

Dietary chlorophyllin is a potent inhibitor of aflatoxin B1 hepatocarcinogenesis in rainbow trout.

Epidemiological and experimental evidence indicates a strong relationship between diet and cancer. The purpose of this study was to examine the potential of chlorophyllin (CHL), a food-grade derivative of the ubiquitous green plant pigment chlorophyll, to inhibit experimental carcinogenesis. We report that CHL is a potent, dose-responsive inhibitor of aflatoxin B1 DNA adduction and hepatocarcinogenesis in the rainbow trout model when fed with carcinogen. CHL neither promoted nor suppressed carcinogenesis with chronic postinitiation feeding. By molecular dosimetry analysis, reduced aflatoxin B1-DNA adduction accounted quantitatively for reduced tumor response up to 2000 ppm dietary CHL, but an additional protective mechanism was operative at 4000 ppm CHL. The finding of potent inhibition (up to 77%) at CHL levels well within the chlorophyll content of some green leafy vegetables may have important implications in intervention and dietary management of human cancer risks.

Aflatoxin B1↗