SOD2 to SOD1 switch in breast cancer

Journal of Biological Chemistry

Volumn 289, Issue 9, 2014, Pages 5412-5416

  Papa, Luena ^a   Hahn, Mary ^a   Marsh, Ellen L ^b   Evans, Bradley S ^b   Germain, Doris ^a  

^a MOUNT SINAI SCHOOL OF MEDICINE   (United States)

^b DONALD DANFORTH PLANT SCIENCE CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BREAST CANCER CELLS; CELLULAR COMPARTMENTS; DOWN-REGULATION; EPITHELIAL-MESENCHYMAL TRANSITION; INTERMEMBRANE SPACE; IRREVERSIBLE DAMAGE; OVER-EXPRESSION; REACTIVE OXYGEN SPECIES;

ANTIOXIDANTS; CELL CULTURE; DISEASES; MITOCHONDRIA; ONCOGENIC VIRUSES;

OXYGEN;

COPPER ZINC SUPEROXIDE DISMUTASE; MANGANESE SUPEROXIDE DISMUTASE; REACTIVE OXYGEN METABOLITE;

ANIMAL TISSUE; ARTICLE; BREAST CANCER; CANCER CELL CULTURE; CONTROLLED STUDY; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME INHIBITION; ENZYME LOCALIZATION; FEMALE; HUMAN; HUMAN TISSUE; MITOCHONDRION; MOUSE; NONHUMAN; ONCOGENE RAS; PRIORITY JOURNAL; PROTEIN EXPRESSION;

CANCER; GLUCOSE METABOLISM; MITOCHONDRIA; REACTIVE OXYGEN SPECIES (ROS); ROS; SUPEROXIDE DISMUTASE (SOD);

BREAST NEOPLASMS; CELL LINE, TUMOR; DOWN-REGULATION; ENZYME INHIBITORS; EPITHELIAL-MESENCHYMAL TRANSITION; FEMALE; GENE EXPRESSION REGULATION, ENZYMOLOGIC; GENE EXPRESSION REGULATION, NEOPLASTIC; HUMANS; NEOPLASM PROTEINS; SIRTUIN 3; SUPEROXIDE DISMUTASE; SUPEROXIDES;

EID: 84896841594     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.C113.526475     Document Type: Article

References (17)

1. Tao, R., Coleman, M. C., Pennington, J. D., Ozden, O., Park, S. H., Jiang, H., Kim, H. S., Flynn, C. R., Hill, S., Hayes McDonald, W., Olivier, A. K., Spitz, D. R., and Gius, D. (2010) Sirt3-mediated deacetylation of evolutionarily conserved lysine 122 regulates MnSOD activity in response to stress. Mol. Cell 40, 893-904
2. Lu, W., Ogasawara, M. A., and Huang, P. (2007) Models of reactive oxygen species in cancer. Drug Discov. Today Dis. Models 4, 67-73
3. Bellot, G. L., Liu, D., and Pervaiz, S. (2013) ROS, autophagy, mitochondria and cancer: Ras, the hidden master? Mitochondrion 13, 155-162
4. Finley, L. W., Carracedo, A., Lee, J., Souza, A., Egia, A., Zhang, J., Teruya-Feldstein, J., Moreira, P. I., Cardoso, S. M., Clish, C. B., Pandolfi, P. P., and Haigis, M. C. (2011) SIRT3 opposes reprogramming of cancer cell metabolism through HIF1a destabilization. Cancer Cell 19, 416-428
5. Radke, S., Pirkmaier, A., and Germain, D. (2005) Differential expression of the F-box proteins Skp2 and Skp2B in breast cancer. Oncogene 24, 3448-3458 (Pubitemid 40756246)
6. Zielonka, J., Hardy, M., and Kalyanaraman, B. (2009) HPLC study of oxidation products of hydroethidine in chemical and biological systems: ramifications in superoxide measurements. Free Radic. Biol. Med. 46, 329-338
7. Somwar, R., Erdjument-Bromage, H., Larsson, E., Shum, D., Lockwood, W. W., Yang, G., Sander, C., Ouerfelli, O., Tempst, P. J., Djaballah, H., and Varmus, H. E. (2011) Superoxide dismutase 1 (SOD1) is a target for a small molecule identified in a screen for inhibitors of the growth of lung adenocarcinoma cell lines. Proc. Natl. Acad. Sci. U.S.A. 108, 16375-16380
8. Zielonka, J., and Kalyanaraman, B. (2010) Hydroethidine- and MitoSOX-derived red fluorescence is not a reliable indicator of intracellular superoxide formation: another inconvenient truth. Free Radic. Biol. Med. 48, 983-1001
9. Rosen, D. R., Siddique, T., Patterson, D., Figlewicz, D. A., Sapp, P., Hentati, A., Donaldson, D., Goto, J., O'Regan, J. P., Deng, H. X., et al. (1993) Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis. Nature 362, 59-62 (Pubitemid 23087289)
10. Higgins, C. M., Jung, C., Ding, H., and Xu, Z. (2002) Mutant Cu, Zn superoxide dismutase that causes motoneuron degeneration is present in mitochondria in the CNS. J. Neurosci. 22, RC215
11. Jaarsma, D., Rognoni, F., van Duijn, W., Verspaget, H. W., Haasdijk, E. D., and Holstege, J. C. (2001) CuZn superoxide dismutase (SOD1) accumulates in vacuolated mitochondria in transgenic mice expressing amyotrophic lateral sclerosis-linked SOD1 mutations. Acta Neuropathol. 102, 293-305 (Pubitemid 32894698)
12. Mattiazzi, M., D'Aurelio, M., Gajewski, C. D., Martushova, K., Kiaei, M., Beal, M. F., and Manfredi, G. (2002) Mutated human SOD1 causes dysfunction of oxidative phosphorylation in mitochondria of transgenic mice. J. Biol. Chem. 277, 29626-29633 (Pubitemid 41079252)
13. Okado-Matsumoto, A., and Fridovich, I. (2001) Subcellular distribution of superoxide dismutases (SOD) in rat liver: Cu, Zn-SOD in mitochondria. J. Biol. Chem. 276, 38388-38393
14. Fischer, L. R., Igoudjil, A., Magrané, J., Li, Y., Hansen, J. M., Manfredi, G., and Glass, J. D. (2011) SOD1 targeted to the mitochondrial intermembrane space prevents motor neuropathy in the Sod1 knockout mouse. Brain 134, 196-209
15. Kim, H. S., Patel, K., Muldoon-Jacobs, K., Bisht, K. S., Aykin-Burns, N., Pennington, J. D., van der Meer, R., Nguyen, P., Savage, J., Owens, K. M., Vassilopoulos, A., Ozden, O., Park, S. H., Singh, K. K., Abdulkadir, S. A., Spitz, D. R., Deng, C. X., and Gius, D. (2010) SIRT3 is a mitochondria-localized tumor suppressor required for maintenance of mitochondrial integrity and metabolism during stress. Cancer Cell 17, 41-52
16. Hazan, R. B., Qiao, R., Keren, R., Badano, I., and Suyama, K. (2004) Cadherin switch in tumor progression. Ann. N.Y. Acad. Sci. 1014, 155-163 (Pubitemid 38594801)
17. Papa, L., and Germain, D. (2014) Sirt3 regulates the mitochondrial unfolded protein response. Mol. Cell. Biol. 34, 699-710