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Oxidative Stress and Signal Transduction pp 441–469Cite as

Gene Expression of DT-Diaphorase in Cancer Cells

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Abstract

NQOs are flavoproteins that catalyze the obligatory two-electron reductive metabolism and detoxification of quinones and its derivatives.1,2 Several reports indicate the presence of two or more isozymic forms of NQOs in the rat, mouse, and human liver.1,2 In humans, genetic evidence indicates that the different forms of NQOs are encoded by four gene loci.3 Two of these loci (designated as NQO1 and NQO2) have been cloned and sequenced.4-7 NQO1 activity has also been cloned from the rat and mouse liver.8-11 Among various NQOs, NQO1 is the beststudied enzyme. NQO1 is a cytosolic protein, occurs as a dimer in vivo, is made up of two homomonomeric subunits with individual molecular weights of 32 kDa, requires NADH or NADPH as a cofactor for the enzymatic activity, and is strongly inhibited by low concentrations of dicoumarol.12-15 Both the human and rat cDNA encode for a protein of 274 residues.4 The NQO1 protein is shown to metabolize 2,6-dichlorophenolindophenol, menadione, vitamin K, benzo(α)-pyrene-3,6-quinone, 2,6-dimethylbenzoquinone, methylene blue, p-benzoquinone, 1,4-naphthoquinone, 2-methyl-l,4-benzoquinone, and several other quinones with high affinity.12,13,16 The second isoenzymic form of the NQO (designated as NQO2) was recently identified by cDNA cloning from human liver.5 The human NQO2 cDNA and protein are 54 and 49% similar to human liver cytosolic NQO1 cDNA and protein, respectively.5 The initiation codon (ATG) of the NQO2 cDNA aligns perfectly with the initiation codons of human and rat NQO1 cDNAs.5,17 However, the NQO2-encoded protein is 43 amino acids shorter at the carboxy terminal end as compared to that of NQO1 and failed to catalyze high-affinity reduction of 2,6-dichlorophenolindophenol and menadione. Interestingly, both proteins were equally active in catalyzing the nitroreduction of antitumor drug CB10-200.7

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Authors
  1. Venugopal Radjendirane
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  2. Pius Joseph
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  3. Anil K. Jaiswal
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Editors and Affiliations

  1. University of Southern California, USA

    Henry Jay Forman  & Enrique Cadenas  & 

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© 1997 Springer Science+Business Media Dordrecht

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Radjendirane, V., Joseph, P., Jaiswal, A.K. (1997). Gene Expression of DT-Diaphorase in Cancer Cells. In: Forman, H.J., Cadenas, E. (eds) Oxidative Stress and Signal Transduction. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-5981-8_18

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  • DOI: https://doi.org/10.1007/978-1-4615-5981-8_18

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4613-7741-2

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