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senecio/glutathione
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Senecio latifolius induces in vitro hepatocytotoxicity in a human cell line.
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The objectives of this study were twofold: (i) to determine the mechanism(s) of Senecio-induced toxicity in human hepatoblastoma cells (HepG2) in vitro and whether such toxicity could be prevented using N-acetyl-cysteine (NAC), and (ii) to evaluate whether caspases are involved in Senecio-induced
Dietary selenium status and pyrrolizidine alkaloid metabolism in vitro by rat liver microsomes.
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The effect of dietary selenium status on the metabolism of pyrrolizidine alkaloids (monocrotaline, and mixed pyrrolizidine alkaloid from Senecio jacobaea) by rat liver microsomes in vitro was studied. In two experiments, there was no difference in the rate of metabolism of alkaloid by microsomes
Effect of phenobarbital on toxicity of pyrrolizidine (Senecio) alkaloids in sheep.
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The effect of prolonged phenobarbital (PB) administration on the toxicity of Senecio jacobaea (SJ) was studied in sheep. Hepatic microsomal mixed function oxidase (MFO) activity was monitored. Pentobarbital sleeping times were decreased after 17 d of treatment, indicating initial induction of MFO.
Effect of consumption of milk from goats fed Senecio jacobaea on hepatic drug metabolizing enzyme activities in rats.
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Milk from lactating goats fed tansy ragwort (Senecio jacobaea) was evaluated for its ability to influence hepatic drug metabolism. The milk after being freeze-dried was fed to male rats for 1 week ad lib. A significant reduction in the activities of hepatic aminopyrine N-demethylase and aryl
Consumption of poisonous plants (Senecio jacobaea, Symphytum officinale, Pteridium aquilinum, Hypericum perforatum) by rats: chronic toxicity, mineral metabolism, and hepatic drug-metabolizing enzymes.
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Effect of dietary tancy ragwort (Senecio jacobaea), comfrey (Symphytum officinale), bracken (Pteridium aquilinum) and alfalfa (Medicago sativa) on hepatic drug-metabolizing enzymes in rats were measured. Tansy ragwort and bracken increased (P less than 0.05) the activity of glutathione transferase
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