UDP-glucuronosyltransferases 1A6 and 1A10 catalyze reduced menadione glucuronidation

Biochemical and Biophysical Research Communications

Volumn 371, Issue 2, 2008, Pages 247-250

  Nishiyama, Takahito ^a   Ohnuma, Tomokazu ^a   Inoue, Yuu ^a   Kishi, Takehiko ^a   Ogura, Kenichiro ^a   Hiratsuka, Akira ^a  

^a TOKYO UNIVERSITY OF PHARMACY AND LIFE SCIENCES   (Japan)

Author keywords

Menadione; NAD(P)H:Quinone oxidoreductase 1; Oxidative stress; UDP glucuronosyltransferase; UGT1A10; UGT1A6

Indexed keywords

GLUCURONOSYLTRANSFERASE 1A10; GLUCURONOSYLTRANSFERASE 1A6; GLUCURONOSYLTRANSFERASE 1A7; GLUCURONOSYLTRANSFERASE 1A8; GLUCURONOSYLTRANSFERASE 1A9; MENADIOL; MENADIONE; RECOMBINANT ENZYME; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE (PHOSPHATE) DEHYDROGENASE (QUINONE); REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;

ARTICLE; CATALYSIS; ENZYME ACTIVITY; ENZYME ANALYSIS; GLUCURONIDATION; HUMAN; INSECT CELL; NONHUMAN; PRIORITY JOURNAL; VITAMIN METABOLISM;

ANIMALS; CATALYSIS; CELLS, CULTURED; GLUCURONIC ACID; GLUCURONOSYLTRANSFERASE; HUMANS; JEJUNUM; LIVER; METABOLIC DETOXICATION, DRUG; MICROSOMES; NAD(P)H DEHYDROGENASE (QUINONE); RECOMBINANT PROTEINS; VITAMIN K 3;

EID: 43049168769     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2008.04.040     Document Type: Article

References (22)

1. Bolton J.L., Trush M.A., Penning T.M., Dryhurst G., and Monks T.J. Role of quinones in toxicology. Chem. Res. Toxicol. 13 (2000) 135-160
2. Monks T.J., Hanzlik R.P., Cohen G.M., Ross D., and Graham D.G. Contemporary issues in toxicology: quinone chemistry and toxicity. Toxicol. Appl. Pharmacol. 112 (1992) 2-16
3. Lamson D.W., and Plaza S.M. The anticancer effects of vitamin K. Altern. Med. Rev. 8 (2003) 303-318
4. O'Brien P.J. Molecular mechanisms of quinone cytotoxicity. Chem. Biol. Interact. 80 (1991) 1-41
5. Marnett L.J. Oxy radicals, lipid peroxidation and DNA damage. Toxicology 181-182 (2002) 219-222
6. Buffinton G.D., Öllinger K., Brunmark A., and Cadenas E. DT-diaphorase-catalysed reduction of 1,4-naphthoquinone derivatives and glutathionyl-quinone conjugates. Biochem. J. 257 (1989) 561-571
7. Cadenas E., and Sies H. Oxidative stress: excited oxygen species and enzyme activity. Adv. Enzyme Regul. 23 (1985) 217-237
8. Powis G., Svingen B.A., and Appel P. Quinone-stimulated superoxide formation by subcellular fractions, isolated hepatocytes, and other cells. Mol. Pharmacol. 20 (1981) 387-394
9. Thor H., Smith M.T., Hartzell P., Bellomo G., Jewell S.A., and Orrenius S. The metabolism of menadione (2-methyl-1,4-naphthoquinone) by isolated hepatocytes. J. Biol. Chem. 257 (1982) 12419-12425
10. Jarabak R., and Jarabak J. Effect of ascorbate on the DT-diaphorase-mediated redox cycling of 2-methyl-1,4-naphthoquinone. Arch. Biochem. Biophys. 318 (1995) 418-423
11. Chesis P.L., Levin D.E., Smith M.T., Ernster L., and Ames B.N. Mutagenicity of quinones: pathways of metabolic activation and detoxification. Proc. Natl. Acad. Sci. USA 81 (1984) 1696-1700
12. Cadenas E. Antioxidant and prooxidant functions of DT-diaphorase in quinone metabolism. Biochem. Pharmacol. 49 (1995) 127-140
13. 14C]menadione. Biochemistry 6 (1967) 62-68
14. Thompson R.M., Gerber N., Seibert R.A., and Desiderio E.M. Identification of 2-methyl-1,4-naphthohydroguinone monoglucuronide as a metabolite of 2-methyl-1,4-naphthoquinone (menadione) in rat bile. Res. Commun. Chem. Pathol. Pharmacol. 4 (1972) 543-552
15. Richert D.A. Studies on the detoxification of 2-methyl-1,4-naphtoquinone in rabbits. J. Biol. Chem. 189 (1951) 763-768
16. Nishiyama T., Kobori T., Arai K., Ogura K., Ohnuma T., Ishii K., Hayashi K., and Hiratsuka A. Identification of human UDP-glucuronosyltransferase isoform(s) responsible for the C-glucuronidation of phenylbutazone. Arch. Biochem. Biophys. 454 (2006) 72-79
17. Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
18. Gustafson D.L., Beall H.D., Bolton E.M., Ross D., and Waldren C.A. Expression of human NAD(P)H: quinone oxidoreductase (DT-diaphorase) in Chinese hamster ovary cells: effect on the toxicity of antitumor quinones. Mol. Pharmacol. 50 (1996) 728-735
19. de Haan L.H.J., Boerboom A.M.J.F., Rietjens I.M.C.M., van Capelle D., de Ruijter A.J.M., Jaiswal A.K., and Aarts J.M.M.J.G. A physiological threshold for protection against menadione toxicity by human NAD(P)H:quinone oxidoreductase (NQO1) in Chinese hamster ovary (CHO) cells. Biochem. Pharmacol. 64 (2002) 1597-1603
20. Bock K.W., Lilienblum W., and Pfeil H. Conversion of benzo[a]pyrene-3,6-quinone to quinol glucuronides with rat liver microsomes or purified NADPH-cytochrome c reductase and UDP-glucuronosyltransferase. FEBS Lett. 121 (1980) 269-272
21. Lind C. Formation of benzo[a]pyrene-3,6-quinol mono- and diglucuronides in rat liver microsomes. Arch. Biochem. Biophys. 240 (1985) 226-235
22. Lind C. Relationship between the rate of reduction of benzo[a]pyrene-3,6-quinone and the formation of benzo[a]pyrene-3,6-quinol glucuronides in rat liver microsomes. Biochem. Pharmacol. 34 (1985) 895-897