Xanthine oxidase-catalyzed DNA binding of dihydrodiol derivatives of nitro-polycyclic aromatic hydrocarbons |
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| Authors: | K K Colvert P P Fu |
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| Affiliation: | 1. Department of Pharmacology and Toxicology, University of Louisville, Louisville, KY 40292, USA;2. Department of Environmental Health Science, Guangdong Provincial Key Laboratory of Tropical Disease Research, School of Public Health, Southern Medical University, Guangzhou 510515, China;3. Biostatisitcs and Bioinformatics Shared Facility, JGB Cancer Center and Department of Bioinformatics and Biostatistics, University of Louisville, Louisville, KY 40292, USA;1. Institute of Experimental Physiology (IFISE-CONICET), Suipacha 570, 2000 Rosario, Argentina;2. University of Connecticut, School of Pharmacy, Department of Pharmaceutical Sciences, Storrs, CT, USA;3. Institute of Pharmacological Investigations (ININFA-CONICET), University of Buenos Aires, Buenos Aires, Argentina;4. Department of Clinical Pharmacology and Pharmacoepidemiology, University of Heidelberg, Heidelberg, Germany;1. Phytochemical Laboratory, Department of Chemical Engineering, Faculty of Engineering, Universiti Malaysia Sabah, Kota Kinabalu, Malaysia;2. Laboratory of Applied Biochemistry and Microbiology, Department of Biochemistry, Faculty of Sciences, University of Annaba, Annaba, Algeria |
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| Abstract: | Xanthine oxidase, a mammalian nitroreductase, catalyzed the covalent binding of a series of nitro-polycyclic aromatic hydrocarbons (nitro-PAHs) trans-dihydrodiols to DNA. Some of the trans-dihydrodiols bound to DNA to a greater extent than their parent nitro-PAHs; however, when the dihydrodiol moiety was peri to the nitro substituent low levels of binding were observed. These data illustrate that ring-oxidation and hydrolysis of nitro-PAHs to their trans-dihydrodiols followed by nitroreduction is a potential metabolic pathway leading to DNA adducts in mammals. |
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