Activities of human recombinant cytochrome P450 isoforms and human hepatic microsomes for the hydroxylation ofAlternaria toxins
Mycotoxin Research, ISSN: 0178-7888, Vol: 24, Issue: 3, Page: 117-123
2008
- 29Citations
- 12Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
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Metrics Details
- Citations29
- Citation Indexes28
- 28
- CrossRef18
- Policy Citations1
- 1
- Captures12
- Readers12
- 12
Article Description
The Alternaria toxins alternariol (AOH), alternariol-9-methyl ether (AME), altenuene (ALT) and isoaltenuene (iALT) undergo extensive oxidative metabolism, but the cytochrome P450 (CYP) isoforms responsible for the reported hydroxylation reactions are yet unknown. In the present study, the activities of twelve human CYP isoforms for the hydroxylation of AOH, AME, ALT and iALT at different positions have been determined. The most active monooxygenase for AOH and AME was CYP1A1, and lower activities were observed for CYP1A2, 2C19 and 3A4. Hydroxylation at C-2 of AOH and AME was the preferred reaction of most isoforms. For ALT and iALT, CYP2C19 had the highest activity, followed by 2C9 and 2D6. The dominating metabolite of all active isoforms was the 8-hydroxylated ALT and iALT. The activities of the CYP isoforms are consistent with the pattern of metabolites of theAlternaria toxins obtained with pooled human hepatic microsomes. Based on the activities of the CYP isoforms, a significant extrahepatic hydroxylation must be expectede.g. in the lung and esophagus for AOH and AME, and in the intestine and ovaries for ALT and iALT. As all major hydroxylation products are catechols, the extrahepatic metabolism ofAlternaria toxins may be of toxicological relevance. © 2008 Society of Mycotoxin Research and Springer.
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=65149096626&origin=inward; http://dx.doi.org/10.1007/bf03032337; http://www.ncbi.nlm.nih.gov/pubmed/23604745; http://link.springer.com/10.1007/BF03032337; http://www.springerlink.com/index/pdf/10.1007/BF03032337; http://www.springerlink.com/index/10.1007/BF03032337; https://dx.doi.org/10.1007/bf03032337; https://link.springer.com/article/10.1007/BF03032337
Springer Science and Business Media LLC
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