References
- Agrawal-Singh, S., Isken, F., Agelopoulos, K., Klein, H.U., Thoennissen, N.H., Koehler, G., Hascher, A., Bäumer, N., Berdel, W.E., Thiede, C., et al. (2012). Genome-wide analysis of histone H3 acetylation patterns in AML identifies PRDX2 as an epigenetically silenced tumor suppressor gene. Blood 119, 2346-2357. https://doi.org/10.1182/blood-2011-06-358705
- Bae, S.H., Sung, S.H., Lee, H.E., Kang, H.T., Lee, S.K., Oh, S.Y., Woo, H.A., Kil, I.S., and Rhee, S.G. (2012). Peroxiredoxin III and sulfiredoxin together protect mice from pyrazole-induced oxidative liver injury. Antioxid. Redox Signal. 17, 1351-1361. https://doi.org/10.1089/ars.2011.4334
- Chou, W.C., Jie, C., Kenedy, A.A., Jones, R.J., Trush, M.A., and Dang, C.V. (2004). Role of NADPH oxidase in arsenic-induced reactive oxygen species formation and cytotoxicity in myeloid leukemia cells. Proc. Natl. Acad. Sci. U. S. A. 101, 4578-4583. https://doi.org/10.1073/pnas.0306687101
- Coe, E. and Schimmer, A.D. (2008). Catalase activity and arsenic sensitivity in acute leukemia. Leuk. Lymphoma 49, 1976-1981. https://doi.org/10.1080/10428190802353617
- Cox, A.G., Winterbourn, C.C., and Hampton, M.B. (2010). Mitochondrial peroxiredoxin involvement in antioxidant defence and redox signalling. Biochem. J. 425, 313-325. https://doi.org/10.1042/BJ20091541
- de Thé, H. and Chen, Z. (2010). Acute promyelocytic leukaemia: novel insights into the mechanisms of cure. Nat. Rev. Cancer 10, 775-783. https://doi.org/10.1038/nrc2943
- George, B., Mathews, V., Poonkuzhali, B., Shaji, R.V., Srivastava, A., and Chandy, M. (2004). Treatment of children with newly diagnosed acute promyelocytic leukemia with arsenic trioxide: a single center experience. Leukemia 18, 1587-1590. https://doi.org/10.1038/sj.leu.2403480
- 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. https://doi.org/10.1016/S0006-2952(98)00307-4
- Ghavamzadeh, A., Alimoghaddam, K., Ghaffari, S.H., Rostami, S., Jahani, M., Hosseini, R., Mossavi, A., Baybordi, E., Khodabadeh, A, Iravani, M., et al. (2006). Treatment of acute promyelocytic leukemia with arsenic trioxide without ATRA and/or chemotherapy. Ann. Oncol. 17, 131-134. https://doi.org/10.1093/annonc/mdj019
- Groninger, E., Meeuwsen-De Boer, G.J., De Graaf, S.S., Kamps, W.A., and De Bont, E.S. (2002). Vincristine induced apoptosis in acute lymphoblastic leukaemia cells: a mitochondrial controlled pathway regulated by reactive oxygen species? Int. J. Oncol. 21, 1339-1345.
- Hole, P.S., Darley, R.L., and Tonks, A. (2011). Do reactive oxygen species play a role in myeloid leukemias? Blood 117, 5816-5826. https://doi.org/10.1182/blood-2011-01-326025
- Hu, J., Liu, Y.F., Wu, C.F., Xu, F., Shen, Z.X., Zhu, Y.M., Li, J.M., Tang, W, Zhao, W.L., Wu, W., et al. (2009). Long-term efficacy and safety of all-trans retinoic acid/arsenic trioxide-based therapy in newly diagnosed acute promyelocytic leukemia. Proc. Natl. Acad. Sci. U. S. A. 106, 3342-3347. https://doi.org/10.1073/pnas.0813280106
- Huang, W., Cash, N., Wen, L., Szatmary, P., Mukherjee, R., Armstrong, J., Chvanov, M., Tepikin, A.V., Murphy, M.P., Sutton, R., et al. (2015). Effects of the mitochondria-targeted antioxidant mitoquinone in murine acute pancreatitis. Mediators Inflamm. 2015, 1-13.
- Iacobini, M., Menichelli, A., Palumbo, G., Multari, G., Werner, B., and Del Principe, D. (2001). Involvement of oxygen radicals in cytarabine- induced apoptosis in human polymorphonuclear cells. Biochem. Pharmacol. 61, 1033-1040. https://doi.org/10.1016/S0006-2952(01)00548-2
- Irwin, M.E., Rivera-Del Valle, N., and Chandra, J. (2013). Redox control of leukemia: from molecular mechanisms to therapeutic opportunities. Antioxid. Redox Signal. 18, 1349-1383. https://doi.org/10.1089/ars.2011.4258
- Jing, Y., Dai, J., Chalmers-Redman, R.M., Tatton, W.G., and Waxman, S. (1999). Arsenic trioxide selectively induces acute promyelocytic leukemia cell apoptosis via a hydrogen peroxide-dependent pathway. Blood 94, 2102-2111. https://doi.org/10.1182/blood.V94.6.2102
-
Kang, S.W., Chae, H.Z., Seo, M.S., Kim, K., Baines, I.C., and Rhee, S.G. (1998). Mammalian peroxiredoxin isoforms can reduce hydrogen peroxide generated in response to growth factors and tumor necrosis
$factor-{\alpha}$ . J. Biol. Chem. 273, 6297-6302. https://doi.org/10.1074/jbc.273.11.6297 - Kang, S.W., Rhee, S.G., Chang, T.S., Jeong, W., and Choi, M.H. (2005). 2-Cys peroxiredoxin function in intracellular signal transduction: therapeutic implications. Trends Mol. Med. 11, 571-578. https://doi.org/10.1016/j.molmed.2005.10.006
- Kanno, S., Higurashi, A., Watanabe, Y., Shouji, A., Asou, K., and Ishikawa, M. (2004). Susceptibility to cytosine arabinoside (Ara-C)- induced cytotoxicity in human leukemia cell lines. Toxicol. Lett. 152, 149-158. https://doi.org/10.1016/j.toxlet.2004.04.014
- Kearns, P.R., Pieters, R., Rottier, M.M., Pearson, A.D., and Hall, A.G. (2001). Raised blast glutathione levels are associated with an increased risk of relapse in childhood acute lymphocytic leukemia. Blood 97, 393-398. https://doi.org/10.1182/blood.V97.2.393
- Lee, S.R., Kim, J.R., Kwon, K.S., Yoon, H.W., Levie, R.L., Ginsburg, A., and Rhee, S.G. (1999). Molecular cloning and characterization of a mitochondrial selenocysteine-containing thioredoxin reductase from rat liver. J. Biol. Chem. 274, 4722-4734. https://doi.org/10.1074/jbc.274.8.4722
- Li, N., Ragheb, K., Lawler, G., Sturgis, J., Rajwa, B., Melendez, J.A., and Robinson, J.P. (2003). Mitochondrial complex I inhibitor rotenone induces apoptosis through enhancing mitochondrial reactive oxygen species production. J. Biol. Chem. 278, 8516-8525. https://doi.org/10.1074/jbc.M210432200
- Liu, S.X., Davidson, M.M., Tang, X., Walker, W.F., Athar, M., Ivanov, V., and Hei, T.K. (2005). Mitochondrial damage mediates genotoxicity of arsenic in mammalian cells. Cancer Res. 65, 3236-3242. https://doi.org/10.1158/0008-5472.CAN-05-0424
- Lu, J., Chew, E.H., and Holmgren, A. (2007). Targeting thioredoxin reductase is a basis for cancer therapy by arsenic trioxide. Proc. Natl. Acad. Sci. U. S. A. 104, 12288-12293. https://doi.org/10.1073/pnas.0701549104
- Maraldi, T., Prata, C., Fiorentini, D., Zambonin, L., Landi, L., and Hakim, G. (2009). Induction of apoptosis in a human leukemic cell line via reactive oxygen species modulation by antioxidants. Free Radic. Biol. Med. 46, 244-252. https://doi.org/10.1016/j.freeradbiomed.2008.10.027
- Mathews, V., George, B., Chendamarai, E., Lakshmi, K.M., Desire, S., Balasubramanian, P., Viswabandya, A., Thirugnanam, R., Abraham, A., Shaji, R.V., et al. (2010). Single-agent arsenic trioxide in the treatment of newly diagnosed acute promyelocytic leukemia: long-term follow-up data. J. Clin. Oncol. 28, 3866-3871. https://doi.org/10.1200/JCO.2010.28.5031
- Maung, Z.T., Hogarth, L., Reid, M.M., Proctor, S.J., Hamilton, P.J., and Hall, A.G. (1994). Raised intracellular glutathione levels correlate with in vitro resistance to cytotoxic drugs in leukaemic cells from patients with acute lymphoblastic leukemia. Leukemia 8, 1487-1491.
- Mi, J.Q., Li, J.M., Shen, Z.X., Chen, S.J., and Chen, Z. (2012). How to manage acute promyelocytic leukemia. Leukemia 26, 1743-1751. https://doi.org/10.1038/leu.2012.57
- Noh, Y.H., Baek, J.Y., Jeong, W., Rhee, S.G., and Chang, T.S. (2009). Sulfiredoxin translocation into mitochondria plays a crucial role in reducing hyperoxidized peroxiredoxin III. J. Biol. Chem. 284, 8470- 8477. https://doi.org/10.1074/jbc.M808981200
- Partridge, M.A., Huang, S.X., Hernandez-Rosa, E., Davidson, M.M., and Hei, T.K. (2007). Arsenic induced mitochondrial DNA damage and altered mitochondrial oxidative function: implications for genotoxic mechanisms in mammalian cells. Cancer Res. 67, 5239-5247. https://doi.org/10.1158/0008-5472.CAN-07-0074
- Pelicano, H., Feng, L., Zhou, Y., Carew, J.S., Hileman, E.O., Plunkett, W., Keating, M.J., and Huang, P. (2003). Inhibition of mitochondrial respiration: a novel strategy to enhance drug-induced apoptosis in human leukemia cells by a reactive oxygen species-mediated mechanism. J. Biol. Chem. 278, 37832-37839. https://doi.org/10.1074/jbc.M301546200
- Potmesil, M., Israel, M., and Silber, R. (1984). Two mechanisms of adriamycin-DNA interaction in L1210 cells. Biochem. Pharmacol. 33, 3137-3142. https://doi.org/10.1016/0006-2952(84)90069-8
- Ravandi, F., Estey, E., Jones, D., Faderl, S., O'Brien, S., Fiorentino, J., Pierce, S., Blamble, D., Estrov, Z., Wierda, W., et al. (2009). Effective treatment of acute promyelocytic leukemia with all-trans- retinoic acid, arsenic trioxide, and gemtuzumab ozogamicin. J. Clin. Oncol. 27, 504-510. https://doi.org/10.1200/JCO.2008.18.6130
- Rhee, S.G., Kang, S.W., Jeong, W., Chang, T.S., Yang, K.S., and Woo, H.A. (2005). Intracellular messenger function of hydrogen peroxide and its regulation by peroxiredoxins. Curr. Opin. Cell Biol. 17, 183-189. https://doi.org/10.1016/j.ceb.2005.02.004
- Rhee, S.G., Woo, H.A., Kil, I.S., and Bae, S.H. (2012). Peroxiredoxin functions as a peroxidase and a regulator and sensor of local peroxides. J. Biol. Chem. 287, 4403-4410. https://doi.org/10.1074/jbc.R111.283432
- Sallmyr, A., Fan, J., and Rassool, F.V. (2008). Genomic instability in myeloid malignancies: increased reactive oxygen species (ROS), DNA double strand breaks (DSBs) and error-prone repair. Cancer Lett. 270, 1-9. https://doi.org/10.1016/j.canlet.2008.03.036
- Sanz, M.A., Fenaux, P., and Lo Coco, F. (2005). Arsenic trioxide in the treatment of acute promyelocytic leukemia. A review of current evidence. Haematologica 90, 1231-1235.
- Soignet, S.L., Frankel, S.R., Douer, D., Tallman, M.S., Kantarjian, H., Calleja, E., Stone, R.M., Kalaycio, M., Scheinberg, D.A., Steinherz, P., et al. (2001). United States multicenter study of arsenic trioxide in relapsed acute promyelocytic leukemia. J. Clin. Oncol. 19, 3852-3860. https://doi.org/10.1200/JCO.2001.19.18.3852
- Soignet, S.L., Maslak, P., Wang, Z.G., Jhanwar, S., Calleja, E., Darnashti, L.J., Corso, D., DeBlasio, A., Gabrilove, J., Scheinberg, D.A., et al. (1998). Complete remission after treatment of acute promyelocytic leukemia with arsenic trioxide. N. Engl. J. Med. 339, 1341-1348. https://doi.org/10.1056/NEJM199811053391901
- Sumi, D., Shinkai, Y., and Kumagai, Y. (2010). Signal transduction pathways and transcription factors triggered by arsenic trioxide in leukemia cells. Toxicol. Appl. Pharmacol. 244, 385-392. https://doi.org/10.1016/j.taap.2010.02.012
- Vivas-Mejía, P.E., Ozpolat, B., Chen, X., and Lopez-Berestein, G. (2009). Downregulation of the c-MYC target gene, peroxiredoxin III, contributes to arsenic trioxide-induced apoptosis in acute promyelocytic leukemia. Int. J. Cancer 125, 264-275. https://doi.org/10.1002/ijc.24341
- Wen, S.T. and Van Etten, R.A. (1997). The PAG gene product, a stressinduced protein with antioxidant properties, is an Abl SH3-inding protein and a physiological inhibitor of c-Abl tyrosine kinase activity. Genes Dev. 11, 2456-2467. https://doi.org/10.1101/gad.11.19.2456
- Woo, H.A., Jeong, W., Chang, T.S., Park, K.J., Park, S.J., Yang, J.S., and Rhee, S.G. (2005). Reduction of cysteine sulfinic acid by sulfiredoxin is specific to 2-cys peroxiredoxins. J. Biol. Chem. 280, 3125-3128. https://doi.org/10.1074/jbc.C400496200
- Zhang, P., Liu, B., Kang, S.W., Seo, M.S., Rhee, S.G., and Obeid, L.M. (1997). Thioredoxin peroxidase is a novel inhibitor of apoptosis with a mechanism distinct from that of Bcl-2. J. Biol. Chem. 272, 30615-30618. https://doi.org/10.1074/jbc.272.49.30615
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