An Alternatively Spliced Form of NQO1 (DT-Diaphorase) Messenger RNA Lacking the Putative Quinone Substrate Binding Site Is Present in Human Normal and Tumor Tissues

Cancer Research

Volumn 55, Issue 12, 1995, Pages 2542-2547

  Gasdaska, Pamela Y ^a   Fisher, Hugh ^a   Powis, Garth ^a  

^a UNIVERSITY OF ARIZONA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

2,6 DICHLOROPHENOLINDOPHENOL; BENZOQUINONE EPOXIDE; COMPLEMENTARY DNA; DIAZIQUONE; MENADIONE; MESSENGER RNA; METHYLBENZOQUINONE; METHYLENE BLUE; MITOXANTRONE; POLYCLONAL ANTIBODY; POTASSIUM FERRICYANIDE; QUINONE DERIVATIVE; RECOMBINANT PROTEIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE (PHOSPHATE) DEHYDROGENASE (QUINONE); UNCLASSIFIED DRUG;

ALTERNATIVE RNA SPLICING; ARTICLE; COLON TUMOR; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME SUBSTRATE; HUMAN; HUMAN CELL; HUMAN TISSUE; LUNG TUMOR; PRIORITY JOURNAL; TUMOR CELL LINE;

ADENOCARCINOMA; ALTERNATIVE SPLICING; BASE SEQUENCE; BINDING SITES; BLOTTING, NORTHERN; CELL LINE; COLON; COLONIC NEOPLASMS; COMPARATIVE STUDY; DNA PRIMERS; DNA, COMPLEMENTARY; HUMAN; LUNG; LUNG NEOPLASMS; MOLECULAR SEQUENCE DATA; NAD(P)H DEHYDROGENASE (QUINONE); POLYMERASE CHAIN REACTION; QUINONES; REFERENCE VALUES; RNA, MESSENGER; SUBSTRATE SPECIFICITY; SUPPORT, NON-U.S. GOV'T; SUPPORT, U.S. GOV'T, P.H.S.; TUMOR CELLS, CULTURED;

EID: 0029058447     PISSN: 00085472     EISSN: 15387445     Source Type: Journal    
DOI: None     Document Type: Article

References (40)

1. Ernster, L. DT-diaphorase. Methods Enzymol., 10: 309–317, 1967.
2. Edwards, Y. H., Potter, J., and Hopkinson, D. A. Human FAD-dependent NAD(P)H diaphorase. Biochem. J., 757: 429–436, 1980.
3. Talalay, P., and Benson, A. M. Elevation of quinone reductase activity by anticarci-nogenic antioxidants. Adv. Enzyme Regul., 20: 287–300, 1982.
4. Beyer, R. E., Segúra-Aguilar, J. E., and Ernster, L. The anticancer enzyme DT diaphorase is induced selectively in liver during ascites hepatoma growth. Anticancer Res., 8: 233–238, 1988.
5. Hommes, F. A., Havinga, H., and Everts, R. S. Induction of DT-diaphorase by benzo(a)pyrene in rat liver. Arch. Biochem. Biophys., 197: 236–243, 1979.
6. Siegel, D., Gibson, N. W., Preusch, P. C., and Ross, D. Metabolism of mitomycin C by DT-diaphorase: role in mitomycin C-induced DNA damage and cytotoxicity in human colon carcinoma cells. Cancer Res., 50: 7483–7489, 1990.
7. Siegel, D., Gibson, N. W., Preusch, P. C., and Ross, D. Metabolism of diaziquone by NAD(P)H:(quinone acceptor) oxidoreductase (DT-diaphorase): role in diaziquone-induced DNA damage and cytotoxicity in human colon carcinoma cells. Cancer Res., 50: 7293–7300, 1990.
8. Walton, M. I., Smith, P. J., and Workman, P. The role of NAD(P)H:quinone reductase (EC 1.6.99.2. DT-diaphorase) in the reductive bioactivation of the novel indoloqui-none antitumor agent E09. Cancer Commun., 3: 199–206, 1991.
9. Knox, R. J., Boland, M. P., Friedlos, F., Coles, B., Southan, C., and Roberts, J. J. The nitroreductase enzyme in Walker cells that activates 5-(aziridin-l-yl)-2–4-dinitroben-zamide (CB 1954) to 5-(aziridin-l-yl)-4-hydroxylamino-2-nitrobcnzamide is a form of NAD(P)H dehydrogenase (quinone) (EC 1.6.99.2.). Biochem. Pharmacol., 37: 4671–4677, 1988.
10. Beyer, R. E., Segúra-Aguilar, J., Lind, C., and Castro, V. M. DT diaphorase activity in various cells in culture with emphasis on induction in ascites hepatoma cells. Chem. Scr., 27: 145–150, 1987.
11. Malkinson, A. M., Siegel, D., Forrest, G. L., Gasdar, A. F., Oie, H.I.C., Chan, D. C., Bunn, P. A., Mabry, M., Dykes, D. J., Harrison, S. D., Jr., and Ross, D. Elevated DT-diaphorase activity and messenger RNA content in human non-small cell lung carcinoma: relationship to the response of lung tumor xenografts to mitomycin C. Cancer Res., 52: 4752–4757, 1992.
12. Ross, D., Siegel, D., Beall, H., Prakash, A. S., Mulcahy, R. T., and Gibson, N. W. DT-diaphorase in activation and detoxification of quinones. Cancer Metastasis Rev., 12: 83–101, 1993.
13. Workman, P., and Stratford, I. J. The experimental development of bioreductive drugs and their role in cancer therapy. Cancer and Metastasis Rev., 12: 73–82, 1993.
14. Rauth, A. M., Marshall, R. S., and Kuehl, B. L. Cellular approaches to bioreductive drug mechanisms. Cancer Metastasis Rev., 12: 153–164, 1993.
15. Riley, R. J., and Workman, P. DT-diaphorase and cancer chemotherapy. Biochem. Pharmacol., 43: 1657–1669, 1992.
16. Workman, P., Walton, M. I., Powis, G., and Schlager, J. J. DT-diaphorase: questionable role in mitomycin C resistance, but a target for novel bioreductive drugs? Br. J. Cancer, 60: 800–802, 1989.
17. Jaiswal, A. K., McBride, O. W., Adesnik, M., and Nebert, D. W. Human dioxin-inducible cytosolic NAD(P)H:menadione oxidoreductase. J. Biol. Chem., 27: 13572–13578, 1988.
18. 1) gene structure and induction by dioxin. Biochemistry, 30: 10647–10655, 1991.
19. 2) corresponding to a second member of the NAD(P)H:quinone oxidoreductase gene family. Extensive polymorphism at the NQO gene locus on chromosome 6. Biochemistry, 29: 1899–1906, 1990.
20. Gasdaska, P. Y., Powis, G., Hyman, P., and Fisher, H. Cigarette smoking is a determinant of DT-diaphorase gene expression in human non-small cell lung carcinoma. Cancer Res., 53: 5458–5461, 1993.
21. Smith, C. W., Patton, J. G., and Nadal-Ginard, B. Alternative splicing in the control of gene expression. Annu. Rev. Genet., 23: 527–577, 1989.
22. Bingham, P. M., Chou, T-B., Mims, I., and Zachar, Z. On/off regulation of gene expression at the level of splicing. Trends Genet., 4: 134–138, 1988.
23. Brunmark, A., Cadenas, E., Lind, C., Segúra-Aguilar, J., and Ernster, L. DT-Diapho-rase-catalyzed two-electron reduction of quinone epoxides. Free Rad. Biol, ed., 3: 181–188, 1987.
24. Davis, L. G., Dibner, M. D., and Battey, J. F. Preparation and analysis of RNA from eukaryotic cells. In: Basic Methods in Molecular Biology, pp. 129–156. New York: Elsevier, 1980.
25. Innis, M. A., Gelfand, D. H., Sninsky, J. J., and White, T. J. PCR Protocols-A Guide to Methods and Applications, p. 14. San Diego: Academic Press, Inc., 1991.
26. Sanger, F. S., Nicklen, S., and Coulson, A. R. DNA sequencing with chain-terminating inhibitors (DNA polymerase/nucleotide sequences/bacteriophase × 174). Proc. Natl. Acad. Sci. USA, 74: 5463–5467, 1977.
27. 6-methylguanine DNA methyltransferase (MGMT) mRNA levels in Mer+ and Mer- human tumor cell lines containing the MGMT gene by the polymerase chain reaction technique. Cancer Commun., 2: 13–20, 1990.
28. Studier, W. F., Rosenberger, A., Dunn, J., and Dubendorff, J. Use of T7 RNA polymerase to direct expression of cloned genes. Methods Enzymol., 185: 60–89, 1990.
29. Ma, Q., Wang, R., Yang, C. S., and Lu, A. Y. H. Expression of mammalian DT-diaphorase in Escherichia coli: purification and characterization of the expressed protein. Arch. Biochem. Biophys., 283: 311–317, 1990.
30. Schlager, J. J., and Powis, G. Mitomycin C is not metabolized by but is an inhibitor of human kidney NAD(P)H:(quinone-acceptor) oxidoreductase. Cancer Chemother. Pharmacol., 22: 126–130, 1988.
31. Beall, H. D., Mulcahy, R. T., Siegel, D., Traver, R. D., Gibson, N. W., and Ross, D. Metabolism of bioreductive antitumor compounds by purified rat and human DT-diaphorases. Cancer Res., 54: 3196–3201, 1994.
32. Ma, Q., Cui, K., Wang, R. W., Lu, A. Y. H., and Yang, C. S. Site-directed mutagenesis of rat liver NAD(P)H:quinone oxidoreductase: roles of lysine 76 and cysteine 179. Arch. Biochem. Biophys., 294: 434–439, 1992.
33. Forrest, G. L., Qian, J., Ma, J-X., Kaplan, W. D., Akman, S., Dorshow, J., and Chen, S. Rat liver NAD(P)H:quinone oxidoreductase: cDNA expression and site-directed mutagenesis. Biochem. Biophys. Res. Commun., 169: 1087–1093, 1990.
34. Ma, Q., Cui, K., Xiao, F., Lu, A. Y. H., and Yang, C. S. Identification of a glycine-rich sequence as an NAD(P)H-binding site and tyrosine 128 as a dicumarol-binding site in rat liver NAD(P)H:quinone oxidoreductase by site-directed mutagenesis. J. Biol. Chem., 267: 22298–22304, 1992.
35. Chen, H-H., Ma, J-X., Forrest, G. L., Deng, P. S. K., Martino, P. A., Lee, T., and Chen, S. Expression of rat liver NAD(P)H:quinone-acceptor oxidoreductase in Escherichia coli and mutagenesis in vitro at Arg 177. Biochem. J., 284: 855–860, 1992.
36. Traver, R. D., Horikoshi, T., Danenberg, K. D., Stadlbauer, T. H. W., Danenberg, P. V., Ross, D., and Gibson, N. W. NAD(P)H:quinone oxidoreductase gene expression in human colon carcinoma cells: characterization of a mutation which modulated DT-diaphorase activity and mitomycin sensitivity. Cancer Res., 52: 797–802, 1992.
37. Powis, G., Lee-See, K., Santone, K. S., Melder, D. C., and Hodnett, E. M. Quinone-imines as substrates for quinone reductase (NAD(P)H:(quinone-acceptor) oxidoreductase) and the effect of dicumarol on their cytotoxicity. Biochem. Pharmacol., 36: 2473–2479, 1987.
38. De Flora, S., Morelli, A., Basso, C., Romano, M., Serra, D., and De Flora, A. Prominent role of DT-diaphorase as a cellular mechanism reducing chromium(VI) and reverting its mutagenicity. Cancer Res., 45: 3188–3196, 1985.
39. Schlager, J. J., and Powis, G. Cytosolic NAD(P)H:(Quinone acceptor)oxidoreductase in human normal and tumor tissue: Effects of cigarette smoking and alcohol. Int. J. Cancer, 45: 403–409, 1990.
40. Talalay, P., and Benson, A. M. Elevation of quinone reductase activity by anticarci-nogenic antioxidants. Adv. Enzyme Regul., 20: 287–300, 1982.