Next Article in Journal
Next Article in Special Issue
Previous Article in Journal
Int. J. Mol. Sci. 2013, 14(6), 10809-10818; doi:10.3390/ijms140610809
Article

Chicken Cytochrome P450 1A5 Is the Key Enzyme for Metabolizing T-2 Toxin to 3'OH-T-2

,
 and *
Received: 10 April 2013; in revised form: 12 May 2013 / Accepted: 17 May 2013 / Published: 23 May 2013
(This article belongs to the Special Issue Xenobiotic Metabolism)
View Full-Text   |   Download PDF [1130 KB, uploaded 19 June 2014]
Abstract: The transmission of T-2 toxin and its metabolites into the edible tissues of poultry has potential effects on human health. We report that T-2 toxin significantly induces CYP1A4 and CYP1A5 expression in chicken embryonic hepatocyte cells. The enzyme activity assays of CYP1A4 and CYP1A5 heterologously expressed in HeLa cells indicate that only CYP1A5 metabolizes T-2 to 3'OH-T-2 by the 3'-hydroxylation of isovaleryl groups. In vitro enzyme assays of recombinant CYP1A5 expressed in DH5α further confirm that CYP1A5 can convert T-2 into TC-1 (3'OH-T-2). Therefore, CYP1A5 is critical for the metabolism of trichothecene mycotoxin in chickens.
Keywords: T-2 toxin; chicken CYP1A5; metabolism T-2 toxin; chicken CYP1A5; metabolism
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Export to BibTeX |
EndNote


MDPI and ACS Style

Shang, S.; Jiang, J.; Deng, Y. Chicken Cytochrome P450 1A5 Is the Key Enzyme for Metabolizing T-2 Toxin to 3'OH-T-2. Int. J. Mol. Sci. 2013, 14, 10809-10818.

AMA Style

Shang S, Jiang J, Deng Y. Chicken Cytochrome P450 1A5 Is the Key Enzyme for Metabolizing T-2 Toxin to 3'OH-T-2. International Journal of Molecular Sciences. 2013; 14(6):10809-10818.

Chicago/Turabian Style

Shang, Shufeng; Jiang, Jun; Deng, Yiqun. 2013. "Chicken Cytochrome P450 1A5 Is the Key Enzyme for Metabolizing T-2 Toxin to 3'OH-T-2." Int. J. Mol. Sci. 14, no. 6: 10809-10818.


Int. J. Mol. Sci. EISSN 1422-0067 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert