Copper modifies liver microsomal UDP-glucuronyltransferase activity through different and opposite mechanisms

Chemico-Biological Interactions

Volumn 167, Issue 1, 2007, Pages 1-11

  Letelier, María Eugenia ^a   Lagos, Fernando ^a   Faúndez, Mario ^a   Miranda, Dante ^a   Montoya, Margarita ^a   Aracena Parks, Paula ^a   González Lira, Víctor ^a  

^a UNIVERSITY OF CHILE   (Chile)

Author keywords

UGT Cu; UGT Cu ascorbate; UGT inhibition activation

Indexed keywords

2,4 DITHIOTHREITOL; ASCORBIC ACID; BINDING PROTEIN; COPPER; COPPER ASCORBATE; DITHIOTHREITOL; EDETIC ACID; FERROUS ASCORBATE; GLUCURONOSYLTRANSFERASE; IRON; REACTIVE OXYGEN METABOLITE; REDUCING AGENT; UNCLASSIFIED DRUG;

ANIMAL TISSUE; ARTICLE; CATALYSIS; CATALYST; CONCENTRATION RESPONSE; ENZYME ACTIVATION; ENZYME ACTIVITY; FENTON REACTION; INCUBATION TIME; LIVER MICROSOME; MALE; METAL BINDING; NONHUMAN; OXIDATION; RAT; TIME;

ANIMALS; ASCORBIC ACID; CHELATING AGENTS; COPPER; EDETIC ACID; GLUCURONOSYLTRANSFERASE; MALE; MICROSOMES, LIVER; OCTOXYNOL; RATS; RATS, SPRAGUE-DAWLEY; SULFHYDRYL COMPOUNDS;

RATTUS;

EID: 33947230114     PISSN: 00092797     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbi.2006.12.010     Document Type: Article

References (37)

1. Ghosh S.S., Lu Y., Lee S.W., Wang X., Guha C., Roy-Chowdhury J., and Roy-Chowdhury N. Role of cysteine residues in the function of human UDP glucuronosyltransferase isoform 1A1 (UGT1A1). Biochem. J. 392 (2005) 685-692
2. Kasper C.B., and Henton D. Glucuronidation. In: Jacoby W.B. (Ed). Enzymatic Basis of Detoxication Vol. II (1980), Academic Press, New York, NY, USA 3-36
3. Senay C., Jedlitschky G., Terrier N., Burchell B., Magdalou J., and Fournel-Gigleux S. The importance of cysteine 126 in the human liver UDP-glucuronosyltransferase UGT1A6. Biochim. Biophys. Acta (BBA): Protein Struct. Mol. Enzymol. 1597 1 (2002) 90-96
4. Sánchez E., and Tephly T.R. Activation of hepatic microsomal glucuronyl transferase by bilirubin. Life Sci. 13 11 (1973) 1483-1490
5. Martin S.T., and Black S.D. Detergent effects in rabbit liver microsomal UDP-glucuronosyltransferase studied by means of a continuous spectrophotometric assay with p-nitrophenol. Biochem. Biophys. Res. Commun. 200 2 (1994) 1093-1098
6. Bentley D., Wood G., and Graham A. Effects of lipid peroxidation on the activity of microsomal UDP-glucuronosyltransferase. Med. Biol. 57 5 (1979) 274-280
7. Dannenberg A.J., Kavencasky J., Scarlata A., and Zakim D. Organization of microsomal UDP-glucuronosyl transferase. Activation by treatment at high pressure. Biochemistry 29 25 (1990) 5961-5967
8. Fulceri R., Bánhegy G., Gamberucci A., Giunti R., Mandl J., and Benedetti A. Evidence for the intraluminal positioning of p-nitrophenol UDP-glucuronosyltransferase activity in rat liver microsomal vesicles. Arch. Biochem. Biophys. 309 1 (1994) 43-46
9. De Groot H., Noll T., and Tolle T. Loss of latent activity of liver microsomal membrane enzymes evoked by lipid peroxidation of nucleoside diphosphatase, glucose-6-phosphatase and UDP glucuronyltransferase. Biochim. Biophys. Acta 815 1 (1985) 91-96
10. Lear L., Nation R.L., and Stupans I. Influence of morphine concentration on detergent activation of rat liver morphine-UDP-glucuronosyltransferase. Biochem. Pharmacol. 42 (1991) 55-60
11. Letelier M.E., Pimentel A., Pino P., Lepe A.M., Faúndez M., Aracena P., and Speisky H. Microsomal UDP-glucuronyltransferase from rat liver. Oxidative activation. Basic Clin. Pharmacol. Toxicol. 96 6 (2005) 480-486
12. Letelier M.E., Lepe A.M., Faúndez M., Salazar J., Marín R., Aracena P., and Speisky H. Possible mechanisms underlying copper-induced damage in biological membranes leading to cellular toxicity. Chem. Biol. Interact. 151 2 (2005) 71-82
13. Lawrence A.J., Michalkiewicz A., Morley J.S., Mackinnon K., and Billington D. Differential inhibition of hepatic morphine UDP-glucuronosyltransferases by metal ions. Biochem. Pharmacol. 43 11 (1992) 2335-2341
14. Watanabe A., Wakabayashi H., Kuwabara Y., Yamamoto H., Hattori S., and Tsuji T. Liver bilirubin UDP-glucuronosyltransferase activity in chronic nonhemolytic unconjugated hyperbilirubinemia of adults. J. Res. Exp. Med. 197 6 (May, 1998) 329-336
15. Denissenko M., Pao A., and Tang M. Preferential formation of benzo(a)pyrene adducts at lung cancer mutational hotspots in P53. Science 274 (1996) 430-432
16. Liehr J.G. Is estradiol a genotoxic mutagenic carcinogen?. Endocr. Rev. 21 (2000) 40-54
17. Shimada T., Hayes C., and Yamazaki H. Activation of chemically diverse procarcinogens by human cytochrome P450-1B1. Cancer Res. 56 (1996) 2979-2984
18. Lowry O.H., Rosenbrough N.J., Farr R.J., and Randall A.L. Protein measurement with the Folin phenol reagent. J. Biol. Chem. 193 1 (1951) 265-275
19. Hatano R., Ebara M., Fukuda H., Yoshikawa M., Sugiura N., Kondo F., Yukawa M., and Saisho H. Fatty liver, chronic hepatitis C and hepatocellular carcinoma. Accumulation of copper in the liver and hepatic injury in chronic hepatitis. C. J. Gastroenterol. Hepatol. 15 (2000) 786-791
20. Bhave S.A., Pandi A.N., Pradhan A.M., Sidhaye D.G., Kantarjian A., Williams A., Talbot I.C., and Tanner M.S. Liver disease in India. Arch. Dis. Child 57 12 (1982) 922-928
21. Tanner M.S. Role of copper in Indian childhood cirrhosis. Am. J. Clin. Nutr. 67 (1998) 1074-1081
22. Chutan H.K., Gupta P.S., Gulati S., and Gupta D.N. Acute copper sulphate poisoning. Am. J. Med. 39 5 (1965) 849-854
23. Suciu I., Prodan L., Lazar V., Ilea E., Cocirla A., Olinici L., Paduraru A., Zagreanu O., Lengyel P., Gyorffi L., and Andru D. Research on copper poisoning. Med. Lav. 72 3 (1981) 190-197
24. Aparna Jain M.C., Nazneen Parveen M., Khan N.U., Parish J.H., and Hadi S.M. Reactivities of flavonoids with different hydroxyl substituents for the cleavage of DNA in the presence of Cu(II). Phytother. Res. 13 7 (1999) 609-612
25. Sánchez E., Del Villar E., Letelier M.E., and Vega P. Dual effects of mersalyl on UDP-glucuronyltransferase activities in rat liver microsomes. IRCS Med. Sci. 9 (1981) 1049-1050
26. Ikushiro S., Yoshikazu E., and Iyanagi T. Activation of glucuronidation through reduction of a disulfide bond in rat UDP-glucuronosyltransferase 1A6. Biochemistry 41 (2002) 12813-12820
27. Harris E.D. Copper transport: an overview. Proc. Soc. Exp. Biol. Med. 196 (1991) 130-140
28. 2. J. Free Radic. Biol. Med. 2 (1986) 3-11
29. Eaton D., and Toal B. Evaluation of the Cd/hemoglobin affinity assay for the rapid determination of metallothionein in biological tissues. Toxicol. Appl. Pharmacol. 66 1 (1982) 134-142
30. Hellman N.E., and Gitlin J.D. Ceruloplasmin metabolism and function. Annu. Rev. Nutr. 22 (2002) 439-458
31. Palmiter R.D. The elusive function of metallothioneins. Proc. Natl. Acad. Sci. 95 (1998) 8428-8430
32. Roelofsen H., Wolters H., Van Luyn M.J., Miura N., Kuipers F., and Vonk R.J. Copper-induced apical trafficking of ATP7B in polarized hepatoma cells provides a mechanism of biliary copper excretion. Gastroenterology 119 (2000) 782-793
33. Huffman D.L., and O'Halloran T.V. Function, structure, and mechanism of intracellular copper trafficking proteins. Annu. Rev. Biochem. 10 (2001) 677-701
34. Myers B.M., Prendergast F.G., Holman R., Kuntz S.M., and Larusso N.F. Alterations in hepatocyte lysosomes in experimental hepatic copper overload in rats. Gastroenterology 105 6 (1993) 1814-1823
35. Sokol R.J., Deveraux M.W., O'Brien K., Khandwala R.A., and Loehr J.P. Abnormal hepatic mitochondrial respiration and cytochrome C oxidase activity in rats with long-term copper overload. Gastroenterology 105 1 (1993) 178-187
36. Aburto E.M., Cribb A.E., Fuentealba I.C., Ikede B.O., Kibenge F.S., and Markham F. Morphological and biochemical assessment of the liver response to excess dietary copper in Fischer 344 rats. Can. J. Vet. Res. 65 2 (2001) 97-103
37. Letelier M.E., Izquierdo P., Godoy L., Lepe A.M., and Faúndez M. Liver microsomal biotransformation of nitro-aryl drugs: a mechanism for potential oxidative stress induction. J. Appl. Toxicol. 24 6 (2004) 519-525