ArticleMilitary Medical Research2015
The roles of carboxylesterase and CYP isozymes on the in vitro metabolism of T-2 toxin.
Article in Military Medical Research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 22 citations in OpenAlex.
- Article
- Identification of Biotransformation Products of T-2 Toxin in HepG2 Cells Using LC-Q-TOF MS.Foods (Basel, Switzerland) · 2024Article
- Possible Mechanisms of the Interplay between Drugs and Mycotoxins-Is There a Possible Impact?Toxins · 2022Review
- Fluorine impairs carboxylesterase 1-mediated hydrolysis of T-2 toxin and increases its chondrocyte toxicity.Frontiers in nutrition · 2022Article
- Mycotoxins: Biotransformation and Bioavailability Assessment Using Caco-2 Cell Monolayer.Toxins · 2020Review
- Porcine cytochrome P450 3A: current status on expression and regulation.Archives of toxicology · 2020Review
- Enzymes for Detoxification of Various Mycotoxins: Origins and Mechanisms of Catalytic Action.Molecules (Basel, Switzerland) · 2019Review
- Impact of Subacute Exposure to T-2 Toxin and Zearalenone on the Pharmacokinetics of Midazolam as CYP3A Probe Drug in a Porcine Animal Model: A Pilot Study.Frontiers in pharmacology · 2019Article
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Authors and funding
6 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundT-2 toxin poses a great threat to human health because it has the highest toxicity of the currently known trichothecene mycotoxins. To understand the in vivo toxicity and transformation mechanism of T-2 toxin, we investigated the role of one kind of principal phase I drug-metabolizing enzymes (cytochrome P450 [CYP450] enzymes) on the metabolism of T-2 toxin, which are crucial to the metabolism of endogenous substances and xenobiotics. We also investigated carboxylesterase, which also plays an important role in the metabolism of toxic substances.
methodsA chemical inhibition method and a recombinant method were employed to investigate the metabolism of the T-2 toxin by the CYP450 enzymes, and a chemical inhibition method was used to study carboxylesterase metabolism. Samples incubated with human liver microsomes were analyzed by high performance liquid chromatography-triple quadrupole mass spectrometry (HPLC- QqQ MS) after a simple pretreatment.
resultsIn the presence of a carboxylesterase inhibitor, only 20 % T-2 toxin was metabolized. When CYP enzyme inhibitors and a carboxylesterase inhibitor were both present, only 3 % of the T-2 toxin was metabolized. The contributions of the CYP450 enzyme family to T-2 toxin metabolism followed the descending order CYP3A4, CYP2E1, CYP1A2, CYP2B6 or CYP2D6 or CYP2C19.
conclusionCarboxylesterase and CYP450 enzymes are of great importance in T-2 toxin metabolism, in which carboxylesterase is predominant and CYP450 has a subordinate role. CYP3A4 is the principal member of the CYP450 enzyme family responsible for T-2 toxin metabolism. The primary metabolite produced by carboxylesterase is HT-2, and the main metabolite produced by CYP 3A4 is 3'-OH T-2. The different metabolites show different toxicities. Our results will provide useful data concerning the toxic mechanism, the safety evaluation, and the health risk assessment of T-2 toxin.
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