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標題: Doxorubicin引發tNOX表現量增加導致A549肺癌細胞移動情形增加
Doxorubicin-mediated transient tNOX up-regulation leading to enhanced cell migration in A549 lung cancer cells
作者: 蘇郁晴
Su, Yu-Ching
關鍵字: tNOX;腫瘤相關NADH氧化;doxorubicin;cell migration;細胞移動
出版社: 生物醫學研究所
引用: Bachur, N.R., Gordon, S.L., and Gee, M.V. (1977). Anthracycline antibiotic augmentation of microsomal electron transport and free radical formation. Mol Pharmacol 13, 901-910. Bachur, N.R., Yu, F., Johnson, R., Hickey, R., Wu, Y., and Malkas, L. (1992). Helicase inhibition by anthracycline anticancer agents. Mol Pharmacol 41, 993-998. Bates, D.A., and Winterbourn, C.C. (1982). Deoxyribose breakdown by the adriamycin semiquinone and H2O2: evidence for hydroxyl radical participation. FEBS Lett 145, 137-142. Brightman, A.O., Wang, J., Miu, R.K., Sun, I.L., Barr, R., Crane, F.L., and Morre, D.J. (1992). A growth factor- and hormone-stimulated NADH oxidase from rat liver plasma membrane. Biochim Biophys Acta 1105, 109-117. Bruno, M., Brightman, A.O., Lawrence, J., Werderitsh, D., Morre, D.M., and Morre, D.J. (1992). Stimulation of NADH oxidase activity from rat liver plasma membranes by growth factors and hormones is decreased or absent with hepatoma plasma membranes. Biochem J 284 ( Pt 3), 625-628. Chen, C.F., Huang, S., Liu, S.C., and Chueh, P.J. (2006). Effect of polyclonal antisera to recombinant tNOX protein on the growth of transformed cells. Biofactors 28, 119-133. Cho, N., Chueh, P.J., Kim, C., Caldwell, S., Morre, D.M., and Morre, D.J. (2002). Monoclonal antibody to a cancer-specific and drug-responsive hydroquinone (NADH) oxidase from the sera of cancer patients. Cancer Immunol Immunother 51, 121-129. Chueh, P.J., Kim, C., Cho, N., Morre, D.M., and Morre, D.J. (2002). Molecular cloning and characterization of a tumor-associated, growth-related, and time-keeping hydroquinone (NADH) oxidase (tNOX) of the HeLa cell surface. Biochemistry 41, 3732-3741. Chueh, P.J., Wu, L.Y., Morre, D.M., and Morre, D.J. (2004). tNOX is both necessary and sufficient as a cellular target for the anticancer actions of capsaicin and the green tea catechin (-)-epigallocatechin-3-gallate. Biofactors 20, 235-249. Cullinane, C., Cutts, S.M., van Rosmalen, A., and Phillips, D.R. (1994). Formation of adriamycin--DNA adducts in vitro. Nucleic Acids Res 22, 2296-2303. Doroshow, J.H. (1983). Anthracycline antibiotic-stimulated superoxide, hydrogen peroxide, and hydroxyl radical production by NADH dehydrogenase. Cancer Res 43, 4543-4551. Feinstein, E., Canaani, E., and Weiner, L.M. (1993). Dependence of nucleic acid degradation on in situ free-radical production by adriamycin. Biochemistry 32, 13156-13161. Fornari, F.A., Jr., Jarvis, D.W., Grant, S., Orr, M.S., Randolph, J.K., White, F.K., and Gewirtz, D.A. (1996). Growth arrest and non-apoptotic cell death associated with the suppression of c-myc expression in MCF-7 breast tumor cells following acute exposure to doxorubicin. Biochem Pharmacol 51, 931-940. Fornari, F.A., Randolph, J.K., Yalowich, J.C., Ritke, M.K., and Gewirtz, D.A. (1994). Interference by doxorubicin with DNA unwinding in MCF-7 breast tumor cells. Mol Pharmacol 45, 649-656. Fritzsche, H., Wahnert, U., Chaires, J.B., Dattagupta, N., Schlessinger, F.B., and Crothers, D.M. (1987). Anthracycline antibiotics. Interaction with DNA and nucleosomes and inhibition of DNA synthesis. Biochemistry 26, 1996-2000. Fukuda, F., Kitada, M., Horie, T., and Awazu, S. (1992). Evaluation of adriamycin-induced lipid peroxidation. Biochem Pharmacol 44, 755-760. Gewirtz, D.A. (1999). A critical evaluation of the mechanisms of action proposed for the antitumor effects of the anthracycline antibiotics adriamycin and daunorubicin. Biochem Pharmacol 57, 727-741. Godbout, J.P., Pesavento, J., Hartman, M.E., Manson, S.R., and Freund, G.G. (2002). Methylglyoxal enhances cisplatin-induced cytotoxicity by activating protein kinase Cdelta. J Biol Chem 277, 2554-2561. Goormaghtigh, E., and Ruysschaert, J.M. (1984). Anthracycline glycoside-membrane interactions. Biochim Biophys Acta 779, 271-288. Griffin-Green, E.A., Zaleska, M.M., and Erecinska, M. (1988). Adriamycin-induced lipid peroxidation in mitochondria and microsomes. Biochem Pharmacol 37, 3071-3077. Gutteridge, J.M., and Quinlan, G.J. (1985). Free radical damage to deoxyribose by anthracycline, aureolic acid and aminoquinone antitumour antibiotics. An essential requirement for iron, semiquinones and hydrogen peroxide. Biochem Pharmacol 34, 4099-4103. Kim, S.H., and Kim, J.H. (1972). Lethal effect of adriamycin on the division cycle of HeLa cells. Cancer Res 32, 323-325. Konopa, J. (1988). G2 block induced by DNA crosslinking agents and its possible consequences. Biochem Pharmacol 37, 2303-2309. Ling, Y.H., Priebe, W., and Perez-Soler, R. (1993). Apoptosis induced by anthracycline antibiotics in P388 parent and multidrug-resistant cells. Cancer Res 53, 1845-1852. Liu, S.C., Yang, J.J., Shao, K.N., and Chueh, P.J. (2008). RNA interference targeting tNOX attenuates cell migration via a mechanism that involves membrane association of Rac. Biochem Biophys Res Commun 365, 672-677. Mao, L.C., Wang, H.M., Lin, Y.Y., Chang, T.K., Hsin, Y.H., and Chueh, P.J. (2008). Stress-induced down-regulation of tumor-associated NADH oxidase during apoptosis in transformed cells. FEBS Lett 582, 3445-3450. Minotti, G., Menna, P., Salvatorelli, E., Cairo, G., and Gianni, L. (2004). Anthracyclines: molecular advances and pharmacologic developments in antitumor activity and cardiotoxicity. Pharmacol Rev 56, 185-229. Molinari, A., Calcabrini, A., Crateri, P., and Arancia, G. (1990). Interaction of anthracyclinic antibiotics with cytoskeletal components of cultured carcinoma cells (CG5). Exp Mol Pathol 53, 11-33. Momparler, R.L., Karon, M., Siegel, S.E., and Avila, F. (1976). Effect of adriamycin on DNA, RNA, and protein synthesis in cell-free systems and intact cells. Cancer Res 36, 2891-2895. Morre, D.J., Bridge, A., Wu, L.Y., and Morre, D.M. (2000). Preferential inhibition by (-)-epigallocatechin-3-gallate of the cell surface NADH oxidase and growth of transformed cells in culture. Biochem Pharmacol 60, 937-946. Morre, D.J., Caldwell, S., Mayorga, A., Wu, L.Y., and Morre, D.M. (1997a). NADH oxidase activity from sera altered by capsaicin is widely distributed among cancer patients. Arch Biochem Biophys 342, 224-230. Morre, D.J., Chueh, P.J., and Morre, D.M. (1995a). Capsaicin inhibits preferentially the NADH oxidase and growth of transformed cells in culture. Proc Natl Acad Sci U S A 92, 1831-1835. Morre, D.J., Crane, F.L., Eriksson, L.C., Low, H., and Morre, D.M. (1991). NADH oxidase of liver plasma membrane stimulated by diferric transferrin and neoplastic transformation induced by the carcinogen 2-acetylaminofluorene. Biochim Biophys Acta 1057, 140-146. Morre, D.J., Kim, C., Paulik, M., Morre, D.M., and Faulk, W.P. (1997b). Is the drug-responsive NADH oxidase of the cancer cell plasma membrane a molecular target for adriamycin? J Bioenerg Biomembr 29, 269-280. Morre, D.J., and Morre, D.M. (2003). Cell surface NADH oxidases (ECTO-NOX proteins) with roles in cancer, cellular time-keeping, growth, aging and neurodegenerative diseases. Free Radic Res 37, 795-808. Morre, D.J., and Reust, T. (1997). A circulating form of NADH oxidase activity responsive to the antitumor sulfonylurea N-4-(methylphenylsulfonyl)-N''-(4-chlorophenyl)urea (LY181984) specific to sera from cancer patients. J Bioenerg Biomembr 29, 281-289. Morre, D.J., Wilkinson, F.E., Kim, C., Cho, N., Lawrence, J., Morre, D.M., and McClure, D. (1996). Antitumor sulfonylurea-inhibited NADH oxidase of cultured HeLa cells shed into media. Biochim Biophys Acta 1280, 197-206. Morre, D.J., Wilkinson, F.E., Lawrence, J., Cho, N., and Paulik, M. (1995b). Identification of antitumor sulfonylurea binding proteins of HeLa plasma membranes. Biochim Biophys Acta 1236, 237-243. Morre, D.J., Wu, L.Y., and Morre, D.M. (1995c). The antitumor sulfonylurea N-(4-methylphenylsulfonyl)-N''-(4-chlorophenyl) urea (LY181984) inhibits NADH oxidase activity of HeLa plasma membranes. Biochim Biophys Acta 1240, 11-17. Munger, C., Ellis, A., Woods, K., Randolph, J., Yanovich, S., and Gewirtz, D. (1988). Evidence for inhibition of growth related to compromised DNA synthesis in the interaction of daunorubicin with H-35 rat hepatoma. Cancer Res 48, 2404-2411. Phillips, D.R., White, R.J., and Cullinane, C. (1989). DNA sequence-specific adducts of adriamycin and mitomycin C. FEBS Lett 246, 233-240. Rao, A.P., and Rao, P.N. (1976). The cause of G2-arrest in Chinese hamster ovary cells treated with anticancer drugs. J Natl Cancer Inst 57, 1139-1143. Reyland, M.E., Anderson, S.M., Matassa, A.A., Barzen, K.A., and Quissell, D.O. (1999). Protein kinase C delta is essential for etoposide-induced apoptosis in salivary gland acinar cells. J Biol Chem 274, 19115-19123. Rogers, K.E., Carr, B.I., and Tokes, Z.A. (1983). Cell surface-mediated cytotoxicity of polymer-bound Adriamycin against drug-resistant hepatocytes. Cancer Res 43, 2741-2748. Singal, P.K., and Iliskovic, N. (1998). Doxorubicin-induced cardiomyopathy. N Engl J Med 339, 900-905. Sinha, B.K. (1989). Free radicals in anticancer drug pharmacology. Chem Biol Interact 69, 293-317. Sinha, B.K., Mimnaugh, E.G., Rajagopalan, S., and Myers, C.E. (1989). Adriamycin activation and oxygen free radical formation in human breast tumor cells: protective role of glutathione peroxidase in adriamycin resistance. Cancer Res 49, 3844-3848. Skladanowski, A., and Konopa, J. (1993). Adriamycin and daunomycin induce programmed cell death (apoptosis) in tumour cells. Biochem Pharmacol 46, 375-382. Skladanowski, A., and Konopa, J. (1994a). Interstrand DNA crosslinking induced by anthracyclines in tumour cells. Biochem Pharmacol 47, 2269-2278. Skladanowski, A., and Konopa, J. (1994b). Relevance of interstrand DNA crosslinking induced by anthracyclines for their biological activity. Biochem Pharmacol 47, 2279-2287. Sun, I.L., Sun, E.E., Crane, F.L., Morre, D.J., Lindgren, A., and Low, H. (1992). Requirement for coenzyme Q in plasma membrane electron transport. Proc Natl Acad Sci U S A 89, 11126-11130. Tanaka, M., and Yoshida, S. (1980). Mechanism of the inhibition of calf thymus DNA polymerases alpha and beta by daunomycin and adriamycin. J Biochem 87, 911-918. Tewey, K.M., Chen, G.L., Nelson, E.M., and Liu, L.F. (1984a). Intercalative antitumor drugs interfere with the breakage-reunion reaction of mammalian DNA topoisomerase II. J Biol Chem 259, 9182-9187. Tewey, K.M., Rowe, T.C., Yang, L., Halligan, B.D., and Liu, L.F. (1984b). Adriamycin-induced DNA damage mediated by mammalian DNA topoisomerase II. Science 226, 466-468. Tokes, Z.A., Rogers, K.E., and Rembaum, A. (1982). Synthesis of adriamycin-coupled polyglutaraldehyde microspheres and evaluation of their cytostatic activity. Proc Natl Acad Sci U S A 79, 2026-2030. Triton, T.R., and Yee, G. (1982). The anticancer agent adriamycin can be actively cytotoxic without entering cells. Science 217, 248-250. Yagiz, K., Morre, D.J., and Morre, D.M. (2006). Transgenic mouse line overexpressing the cancer-specific tNOX protein has an enhanced growth and acquired drug-response phenotype. J Nutr Biochem 17, 750-759. Zaleskis, G., Berleth, E., Verstovsek, S., Ehrke, M.J., and Mihich, E. (1994). Doxorubicin-induced DNA degradation in murine thymocytes. Mol Pharmacol 46, 901-908.
tNOX (tumor-associated NADH oxidase)是屬於一種與細胞生長有關的膜外-NADH氧化

tNOX (tumor-associated NADH oxidase) belongs to an ECTO-NOX family of growth-related NADH oxidases. Since over-expressing tNOX leads to cells transforming, enhanced invasion ability and exhibited more responsive to anticancer drugs. On the other hand, HeLa cell growth and migration are reduced by tNOX-knockdown utilizing RNA interference technique, implying that tNOX is associated with transformed cells proliferation, migration and invasive ability. Doxorubicin (adriamycin), a long-time use in clinical cancer treatment, has been demonstrated to be a target of tNOX. Here, we confirmed that the expression of tNOX is inhibited by doxorubicin treatments at both protein and RNA levels. Interestingly, the expression of tNOX is transiently enhanced by short-time exposure of lower concentrations of doxorubicin in association with increased A549 cells migration and proliferation, suggesting that the level of tNOX expression is important for aggressive cancer cell phenotypes. To explore tNOX function more deeply, we found a serine504 mutation on tNOX exhibits enhanced tNOX function in cell proliferation, migration and different responses against doxorubicin treatment compared to wild type tNOX.
其他識別: U0005-1107201111303900
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