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    Phosphorylation of xenobiotic-metabolizing cytochromes P450.

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    Authors
    Oesch-Bartlomowicz, B.
    Oesch, F.
    Issue Date
    2008-11
    
    Metadata
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    Abstract
    The regulation of cytochromes P450 (CYPs) by induction mediated by xenobiotics is well known. Our team has discovered an additional important regulation of xenobiotic-metabolizing CYPs by phosphorylation. Individual CYPs are phosphorylated by different protein kinases, leading to CYP isoenzyme-selective changes in the metabolism of individual substrates and consequent profound changes in the control of mutagenic and cytotoxic metabolites. Some CYPs are phosphorylated by protein kinase C and some by the cyclic adenosine monophosphate (cAMP) dependent protein kinase A. We found that cAMP not only leads to drastic changes in the activity of individual CYPs, but also drastic changes in the nuclear localization of the CYP-related transcription factor Ah receptor (AHR). The consequences are very different from those of AHR nuclear translocation mediated by its classic ligands (such as dioxin and many polycyclic aromatic hydrocarbons) and may represent the long-sought physiological function of the AHR. The disturbance of this physiological function of AHR by extremely persistent high-affinity xenobiotic ligands such as dioxin may represent the most important contributing factor for their potent toxicity.
    Citation
    Anal. Bioanal. Chem. 2008, 392 (6):1085-1092
    Journal
    Analytical and bioanalytical chemistry
    URI
    http://hdl.handle.net/10146/82633
    DOI
    10.1007/s00216-008-2315-2
    PubMed ID
    18704375
    Additional Links
    http://www.springerlink.com/content/1317418n45376145/
    Type
    Article
    Language
    en
    ISSN
    1618-2650
    Sponsors
    The authors thank the EU Network of Excellence ECNIS (Environmental Cancer, Nutrition and Individual Susceptibility) operating within the EU Sixth Framework Programme, Priority 5: “Food Quality and Safety” (contract no. 513943) for support.
    ae974a485f413a2113503eed53cd6c53
    10.1007/s00216-008-2315-2
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