Mammalian peroxidases activate anticancer drug ellipticine to intermediates forming deoxyguanosine adducts in DNA identical to those found in vivo and generated from 12-hydroxyellipticine and 13-hydroxyellipticine

Abstract

This is the first report on the molecular mechanism of ellipticine oxidation by peroxidases (human myeloperoxidase, human and ovine cyclooxygenases, bovine lactoperoxidase, horseradish peroxidase) to species forming ellipticine-DNA adducts.

Keywords

• ellipticine
• anticancer drug
• peroxidase
• cytochrome P450
• DNA adduct
• xenobiotic-metabolizing enzymes
• covalent binding
• breast-cancer
• catalyzed activation
• elliptinium acetate
• mediated oxidation
• antitumor agent
• cell-line
• Sudan-I