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    Quantitative analysis of cytochrome P450 isoforms in human liver microsomes by the combination of proteomics and chemical probe-based assay

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    Publication date
    2014
    Author
    Liu, X.
    Hu, L.
    Ge, G.
    Yang, B.
    Ning, J.
    Sun, S.
    Yang, L.
    Pors, Klaus
    Gu, J.
    Keyword
    Amino acid sequence; Cytochrome P-45- enzyme system; Humans; Isotope labelling; Microsomes; Molecular sequence data; Protein isoforms; Proteomics; Tandem mass spectroscopy; Biomedicine; Cytochrome P450; Mrm; Protein quantification
    Peer-Reviewed
    Yes
    
    Metadata
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    Abstract
    Cytochrome P450 (CYP) is one of the most important drug-metabolizing enzyme families, which participates in the biotransformation of many endogenous and exogenous compounds. Quantitative analysis of CYP expression levels is important when studying the efficacy of new drug molecules and assessing drug-drug interactions in drug development. At present, chemical probe-based assay is the most widely used approach for the evaluation of CYP activity although there are cross-reactions between the isoforms with high sequence homologies. Therefore, quantification of each isozyme is highly desired in regard to meeting the ever-increasing requirements for carrying out pharmacokinetics and personalized medicine in the academic, pharmaceutical, and clinical setting. Herein, an absolute quantification method was employed for the analysis of the seven isoforms CYP1A2, 2B6, 3A4, 3A5, 2C9, 2C19, and 2E1 using a proteome-derived approach in combination with stable isotope dilution assay. The average absolute amount measured from twelve human liver microsomes samples were 39.3, 4.3, 54.0, 4.6, 10.3, 3.0, and 9.3 (pmol/mg protein) for 1A2, 2B6, 3A4, 3A5, 2C9, 2C19, and 2E1, respectively. Importantly, the expression level of CYP3A4 showed high correlation (r = 0.943, p < 0.0001) with the functional activity, which was measured using bufalin-a highly selective chemical probe we have developed. The combination of MRM identification and analysis of the functional activity, as in the case of CYP3A4, provides a protocol which can be extended to other functional enzyme studies with wide application in pharmaceutical research.
    URI
    http://hdl.handle.net/10454/10502
    Version
    No full-text available in the repository
    Citation
    Liu X, Hu L, Ge G et al (2014) Quantitative analysis of cytochrome P450 isoforms in human liver microsomes by the combination of proteomics and chemical probe-based assay. Proteomics. 14(16): 1943-1951.
    Link to publisher’s version
    https://doi.org/10.1002/pmic.201400025
    Type
    Article
    Collections
    Life Sciences Publications

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