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    NAD(P)H: quinone oxidoreductase 1 expression in kidney podocytes.

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    Authors
    Zappa, Francesco
    Ward, Timothy H
    Pedrinis, Ennio
    Butler, John
    McGown, Alan T
    Affiliation
    CRC Department of Drug Development, Paterson Institute for Cancer Research and Christie Hospital NHS Trust, Manchester, United Kingdom. fzappa@ticino.com
    Issue Date
    2003-03
    
    Metadata
    Show full item record
    Abstract
    NAD(P)H:quinone oxidoreductase 1 (NQO1; DT-diaphorase; DTD) is a cytosolic two-electron reductase, and compounds of the quinone family such as mitomycin C are efficiently bioactivated by this enzyme. The observation that DT-diaphorase is highly expressed in many cancerous tissues compared to normal tissues has provided us with a potentially selective target that can be exploited in the design of novel anticancer agents. Because of the relative lack of information about the cell-specific expression of DT-diaphorase, the purpose of this study was to map the distribution of this enzyme in normal human tissues. Fifteen tissue samples from normal human kidney were analyzed for expression of DT-diaphorase by immunohistochemistry (two-step indirect method). We found a specific high expression of DT-diaphorase in glomerular visceral epithelial cells (podocytes). These results suggest that a high expression of DT-diaphorase in podocytes could play a major role in the pathogenesis of renal toxicity and mitomycin C-induced hemolytic uremic syndrome, in which injury to the glomerular filtration mechanism is the primary damage, leading to a cascade of deleterious events including microangiopathic hemolytic anemia and thrombocytopenia. This observation has potential therapeutic implications because the DT-diaphorase metabolic pathway is influenced by many agents, including drugs, diet, and environmental cell factors such as pH and oxygen tension.
    Citation
    NAD(P)H: quinone oxidoreductase 1 expression in kidney podocytes. 2003, 51 (3):297-302 J. Histochem. Cytochem.
    Journal
    The Journal of Histochemistry and Cytochemistry
    URI
    http://hdl.handle.net/10541/82353
    PubMed ID
    12588957
    Type
    Article
    Language
    en
    ISSN
    0022-1554
    Collections
    All Paterson Institute for Cancer Research

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