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Volumn 42, Issue 4, 2014, Pages 934-938

ROS signalling, NADPH oxidases and cancer

Author keywords

Cancer; NADPH oxidase (Nox); Reactive oxygen species (ROS); Signalling

Indexed keywords

CYCLIC AMP; HYDROGEN PEROXIDE; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE;

EID: 84905858696     PISSN: 03005127     EISSN: 14708752     Source Type: Journal    
DOI: 10.1042/BST20140060     Document Type: Conference Paper
Times cited : (69)

References (50)
  • 1
    • 33846794822 scopus 로고    scopus 로고
    • The NOX family of ROS-generating NADPH oxidases: Physiology and pathophysiology
    • Bedard, K. and Krause, K. (2007) The NOX family of ROS-generating NADPH oxidases: physiology and pathophysiology. Physiol. Rev. 87, 245-313
    • (2007) Physiol. Rev. , vol.87 , pp. 245-313
    • Bedard, K.1    Krause, K.2
  • 2
    • 68749117502 scopus 로고    scopus 로고
    • Bcr-Abl-mediated redox regulation of the PI3K/AKT pathway
    • Naughton, R., Quiney, C., Turner, S.D. and Cotter, T.G. (2009) Bcr-Abl-mediated redox regulation of the PI3K/AKT pathway. Leukemia 23, 1432-1440
    • (2009) Leukemia , vol.23 , pp. 1432-1440
    • Naughton, R.1    Quiney, C.2    Turner, S.D.3    Cotter, T.G.4
  • 5
    • 1342281664 scopus 로고    scopus 로고
    • P22phox-derived superoxide mediates enhanced proliferative capacity of diabetic vascular smooth muscle cells
    • Jeong, H.Y., Jeong, H.Y. and Kim, C.D. (2004) p22phox-derived superoxide mediates enhanced proliferative capacity of diabetic vascular smooth muscle cells. Diabetes Res. Clin. Pract. 64, 1-10
    • (2004) Diabetes Res. Clin. Pract. , vol.64 , pp. 1-10
    • Jeong, H.Y.1    Jeong, H.Y.2    Kim, C.D.3
  • 6
    • 4944225786 scopus 로고    scopus 로고
    • Vascular cell adhesion molecule 1 (VCAM-1) activation of endothelial cell matrix metalloproteinases: Role of reactive oxygen species
    • Deem, T.L. and Cook-Mills, J.M. (2004) Vascular cell adhesion molecule 1 (VCAM-1) activation of endothelial cell matrix metalloproteinases: role of reactive oxygen species. Blood 104, 2385-2393
    • (2004) Blood , vol.104 , pp. 2385-2393
    • Deem, T.L.1    Cook-Mills, J.M.2
  • 7
    • 33745217132 scopus 로고    scopus 로고
    • Redox signaling in angiogenesis: Role of NADPH oxidase
    • Ushio-Fukai, M. (2006) Redox signaling in angiogenesis: role of NADPH oxidase. Cardiovasc. Res. 71, 226-235
    • (2006) Cardiovasc. Res. , vol.71 , pp. 226-235
    • Ushio-Fukai, M.1
  • 9
    • 78049300452 scopus 로고    scopus 로고
    • Modulation of gene expression and tumor cell growth by redox modification of STAT3
    • Li, L., Cheung, S.-H., Evans, E.L. and Shaw, P.E. (2010) Modulation of gene expression and tumor cell growth by redox modification of STAT3. Cancer Res. 70, 8222-8232
    • (2010) Cancer Res. , vol.70 , pp. 8222-8232
    • Li, L.1    Cheung, S.-H.2    Evans, E.L.3    Shaw, P.E.4
  • 11
    • 79751534683 scopus 로고    scopus 로고
    • NADPH oxidases regulate cell growth and migration in myeloid cells transformed by oncogenic tyrosine kinases
    • Reddy, M.M., Fernandes, M.S., Salgia, R., Levine, R.L., Griffin, J.D. and Sattler, M. (2011) NADPH oxidases regulate cell growth and migration in myeloid cells transformed by oncogenic tyrosine kinases. Leukemia 25, 281-289
    • (2011) Leukemia , vol.25 , pp. 281-289
    • Reddy, M.M.1    Fernandes, M.S.2    Salgia, R.3    Levine, R.L.4    Griffin, J.D.5    Sattler, M.6
  • 13
    • 0038799736 scopus 로고    scopus 로고
    • Oxidative DNA damage: Mechanisms, mutation, and disease
    • Cooke, M.S., Evans, M.D., Dizdaroglu, M. and Lunec, J. (2003) Oxidative DNA damage: mechanisms, mutation, and disease. FASEB J. 17, 1195-1214
    • (2003) FASEB J. , vol.17 , pp. 1195-1214
    • Cooke, M.S.1    Evans, M.D.2    Dizdaroglu, M.3    Lunec, J.4
  • 14
    • 2442693092 scopus 로고    scopus 로고
    • The superoxide-generating oxidase Nox1 is functionally required for Ras oncogene transformation
    • Mitsushita, J., Lambeth, J.D. and Kamata, T. (2004) The superoxide-generating oxidase Nox1 is functionally required for Ras oncogene transformation. Cancer Res. 64, 3580-3585
    • (2004) Cancer Res. , vol.64 , pp. 3580-3585
    • Mitsushita, J.1    Lambeth, J.D.2    Kamata, T.3
  • 15
    • 15044362438 scopus 로고    scopus 로고
    • Intracellular messenger function of hydrogen peroxide and its regulation by peroxiredoxins
    • 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
    • (2005) Curr. Opin. Cell Biol. , vol.17 , pp. 183-189
    • Rhee, S.G.1    Kang, S.W.2    Jeong, W.3    Chang, T.-S.4    Yang, K.-S.5    Woo, H.A.6
  • 16
    • 84876890840 scopus 로고    scopus 로고
    • Redox regulation of protein kinases
    • Corcoran, A. and Cotter, T.G. (2013) Redox regulation of protein kinases. FEBS J. 280, 1944-1965
    • (2013) FEBS J. , vol.280 , pp. 1944-1965
    • Corcoran, A.1    Cotter, T.G.2
  • 17
    • 0036291166 scopus 로고    scopus 로고
    • Regulation of protein phosphatase 2A by hydrogen peroxide and glutathionylation
    • Rao, R.K. and Clayton, L.W. (2002) Regulation of protein phosphatase 2A by hydrogen peroxide and glutathionylation. Biochem. Biophys. Res. Commun. 293, 610-616
    • (2002) Biochem. Biophys. Res. Commun. , vol.293 , pp. 610-616
    • Rao, R.K.1    Clayton, L.W.2
  • 18
    • 0042163035 scopus 로고    scopus 로고
    • Reversible inhibition of the protein phosphatase 1 by hydrogen peroxide: Potential regulation of eIF2 phosphorylation in differentiated PC12 cells
    • O'Loghlen, A., Pérez-Morgado, M.I., Salinas, M. and Martín, M.E. (2003) Reversible inhibition of the protein phosphatase 1 by hydrogen peroxide: potential regulation of eIF2? phosphorylation in differentiated PC12 cells. Arch. Biochem. Biophys. 417, 194-202
    • (2003) Arch. Biochem. Biophys. , vol.417 , pp. 194-202
    • O'loghlen, A.1    Pérez-Morgado, M.I.2    Salinas, M.3    Martín, M.E.4
  • 19
    • 0028973482 scopus 로고
    • Requirement for generation of H2O2 for platelet-derived growth factor signal transduction
    • Sundaresan, M., Yu, Z.X., Ferrans, V.J., Irani, K. and Finkel, T. (1995) Requirement for generation of H2O2 for platelet-derived growth factor signal transduction. Science 270, 296-299
    • (1995) Science , vol.270 , pp. 296-299
    • Sundaresan, M.1    Yu, Z.X.2    Ferrans, V.J.3    Irani, K.4    Finkel, T.5
  • 20
    • 15144343374 scopus 로고    scopus 로고
    • Epidermal growth factor (EGF)-induced generation of hydrogen peroxide: Role in EGF receptor-mediated tyrosine phosphorylation
    • Bae, Y.S., Kang, S.W., Seo, M.S., Baines, I.C., Tekle, E., Chock, P.B. and Rhee, S.G. (1997) Epidermal growth factor (EGF)-induced generation of hydrogen peroxide: role in EGF receptor-mediated tyrosine phosphorylation. J. Biol. Chem. 272, 217-221
    • (1997) J. Biol. Chem. , vol.272 , pp. 217-221
    • Bae, Y.S.1    Kang, S.W.2    Seo, M.S.3    Baines, I.C.4    Tekle, E.5    Chock, P.B.6    Rhee, S.G.7
  • 21
    • 33748466565 scopus 로고    scopus 로고
    • Specificity in reactive oxidant signaling: Think globally, act locally
    • Terada, L.S. (2006) Specificity in reactive oxidant signaling: think globally, act locally. J. Cell Biol. 174, 615-623
    • (2006) J. Cell Biol. , vol.174 , pp. 615-623
    • Terada, L.S.1
  • 22
    • 65349157681 scopus 로고    scopus 로고
    • Compartmentalization of redox signaling through NADPH oxidase-derived ROS
    • Ushio-Fukai, M. (2009) Compartmentalization of redox signaling through NADPH oxidase-derived ROS. Antioxid. Redox Signal. 11, 1289-1299
    • (2009) Antioxid. Redox Signal. , vol.11 , pp. 1289-1299
    • Ushio-Fukai, M.1
  • 23
    • 84856940017 scopus 로고    scopus 로고
    • Peroxiredoxin functions as a peroxidase and a regulator and sensor of local peroxides
    • 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
    • (2012) J. Biol. Chem. , vol.287 , pp. 4403-4410
    • Rhee, S.G.1    Woo, H.A.2    Kil, I.S.3    Bae, S.H.4
  • 24
    • 0242668686 scopus 로고    scopus 로고
    • Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling
    • Wood, Z.A., Poole, L.B. and Karplus, P.A. (2003) Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling. Science 300, 650-653
    • (2003) Science , vol.300 , pp. 650-653
    • Wood, Z.A.1    Poole, L.B.2    Karplus, P.A.3
  • 25
    • 76749102420 scopus 로고    scopus 로고
    • Inactivation of peroxiredoxin i by phosphorylation allows localized H2O2 accumulation for cell signaling
    • Woo, H.A., Yim, S.H., Shin, D.H., Kang, D., Yu, D.-Y. and Rhee, S.G. (2010) Inactivation of peroxiredoxin I by phosphorylation allows localized H2O2 accumulation for cell signaling. Cell 140, 517-528
    • (2010) Cell , vol.140 , pp. 517-528
    • Woo, H.A.1    Yim, S.H.2    Shin, D.H.3    Kang, D.4    Yu, D.-Y.5    Rhee, S.G.6
  • 26
    • 33750926794 scopus 로고    scopus 로고
    • Role of Nox family NADPH oxidases in host defense
    • Leto, T.L. and Geiszt, M. (2006) Role of Nox family NADPH oxidases in host defense. Antioxid. Redox Signal. 8, 1549-1561
    • (2006) Antioxid. Redox Signal. , vol.8 , pp. 1549-1561
    • Leto, T.L.1    Geiszt, M.2
  • 27
    • 0025904386 scopus 로고
    • Identification of a superoxide-generating NADPH oxidase system in human fibroblasts
    • Meier, B., Cross, A.R., Hancock, J.T., Kaup, F.J. and Jones, O.T. (1991) Identification of a superoxide-generating NADPH oxidase system in human fibroblasts. Biochem. J. 275, 241-245
    • (1991) Biochem. J. , vol.275 , pp. 241-245
    • Meier, B.1    Cross, A.R.2    Hancock, J.T.3    Kaup, F.J.4    Jones, O.T.5
  • 28
    • 0028365310 scopus 로고
    • Angiotensin II stimulates NADH and NADPH oxidase activity in cultured vascular smooth muscle cells
    • Griendling, K.K., Minieri, C.A., Ollerenshaw, J.D. and Alexander, R.W. (1994) Angiotensin II stimulates NADH and NADPH oxidase activity in cultured vascular smooth muscle cells. Circ. Res. 74, 1141-1148
    • (1994) Circ. Res. , vol.74 , pp. 1141-1148
    • Griendling, K.K.1    Minieri, C.A.2    Ollerenshaw, J.D.3    Alexander, R.W.4
  • 29
    • 0034617071 scopus 로고    scopus 로고
    • A gp91phox containing NADPH oxidase selectively expressed in endothelial cells is a major source of oxygen radical generation in the arterial wall
    • Görlach, A., Brandes, R.P., Nguyen, K., Amidi, M., Dehghani, F. and Busse, R. (2000) A gp91phox containing NADPH oxidase selectively expressed in endothelial cells is a major source of oxygen radical generation in the arterial wall. Circ. Res. 87, 26-32
    • (2000) Circ. Res. , vol.87 , pp. 26-32
    • Görlach, A.1    Brandes, R.P.2    Nguyen, K.3    Amidi, M.4    Dehghani, F.5    Busse, R.6
  • 32
    • 22844440003 scopus 로고    scopus 로고
    • Involvement of NADPH oxidase isoforms and Src family kinases in CD95-dependent hepatocyte apoptosis
    • Reinehr, R., Becker, S., Eberle, A., Grether-Beck, S. and Häussinger, D. (2005) Involvement of NADPH oxidase isoforms and Src family kinases in CD95-dependent hepatocyte apoptosis. J. Biol. Chem. 280, 27179-27194
    • (2005) J. Biol. Chem. , vol.280 , pp. 27179-27194
    • Reinehr, R.1    Becker, S.2    Eberle, A.3    Grether-Beck, S.4    Häussinger, D.5
  • 33
    • 44949106317 scopus 로고    scopus 로고
    • Structure, regulation and evolution of Nox-family NADPH oxidases that produce reactive oxygen species
    • Sumimoto, H. (2008) Structure, regulation and evolution of Nox-family NADPH oxidases that produce reactive oxygen species. FEBS J. 275, 3249-3277
    • (2008) FEBS J. , vol.275 , pp. 3249-3277
    • Sumimoto, H.1
  • 35
    • 73449129394 scopus 로고    scopus 로고
    • Hydrogen peroxide as a cell-survival signaling molecule
    • Groeger, G., Quiney, C. and Cotter, T.G. (2009) Hydrogen peroxide as a cell-survival signaling molecule. Antioxid. Redox Signal. 11, 2655-2671
    • (2009) Antioxid. Redox Signal. , vol.11 , pp. 2655-2671
    • Groeger, G.1    Quiney, C.2    Cotter, T.G.3
  • 38
    • 84858597029 scopus 로고    scopus 로고
    • Constitutive NADPH oxidase 4 activity resides in the composition of the B-loop and the penultimate C terminus
    • von Löhneysen, K., Noack, D., Hayes, P., Friedman, J.S. and Knaus, U.G. (2012) Constitutive NADPH oxidase 4 activity resides in the composition of the B-loop and the penultimate C terminus. J. Biol. Chem. 287, 8737-8745
    • (2012) J. Biol. Chem. , vol.287 , pp. 8737-8745
    • Von Löhneysen, K.1    Noack, D.2    Hayes, P.3    Friedman, J.S.4    Knaus, U.G.5
  • 39
    • 84872418752 scopus 로고    scopus 로고
    • Imatinib and Nilotinib inhibit Bcr-Abl-induced ROS through targeted degradation of the NADPH oxidase subunit p22phox
    • Landry, W.D., Woolley, J.F. and Cotter, T.G. (2013) Imatinib and Nilotinib inhibit Bcr-Abl-induced ROS through targeted degradation of the NADPH oxidase subunit p22phox. Leukemia 37, 183-189
    • (2013) Leukemia , vol.37 , pp. 183-189
    • Landry, W.D.1    Woolley, J.F.2    Cotter, T.G.3
  • 40
    • 0034562783 scopus 로고    scopus 로고
    • Reactive oxygen species and acute renal failure
    • Nath, K.A. and Norby, S.M. (2000) Reactive oxygen species and acute renal failure. Am. J. Med. 109, 665-678
    • (2000) Am. J. Med. , vol.109 , pp. 665-678
    • Nath, K.A.1    Norby, S.M.2
  • 41
    • 0037027485 scopus 로고    scopus 로고
    • Perivascular superoxide anion contributes to impairment of endothelium-dependent relaxation: Role of gp91phox
    • Rey, F.E., Li, X.-C., Carretero, O.A., Garvin, J.L. and Pagano, P.J. (2002) Perivascular superoxide anion contributes to impairment of endothelium-dependent relaxation: role of gp91phox. Circulation 106, 2497-502
    • (2002) Circulation , vol.106 , pp. 2497-2502
    • Rey, F.E.1    Li, X.-C.2    Carretero, O.A.3    Garvin, J.L.4    Pagano, P.J.5
  • 43
    • 0042864155 scopus 로고    scopus 로고
    • Increased expression of NAD(P)H oxidase subunits, NOX4 and p22phox, in the kidney of streptozotocin-induced diabetic rats and its reversibity by interventive insulin treatment
    • Etoh, T., Inoguchi, T., Kakimoto, M., Sonoda, N., Kobayashi, K., Kuroda, J., Sumimoto, H. and Nawata, H. (2003) Increased expression of NAD(P)H oxidase subunits, NOX4 and p22phox, in the kidney of streptozotocin-induced diabetic rats and its reversibity by interventive insulin treatment. Diabetologia 46, 1428-1437
    • (2003) Diabetologia , vol.46 , pp. 1428-1437
    • Etoh, T.1    Inoguchi, T.2    Kakimoto, M.3    Sonoda, N.4    Kobayashi, K.5    Kuroda, J.6    Sumimoto, H.7    Nawata, H.8
  • 44
    • 33751182650 scopus 로고    scopus 로고
    • Atorvastatin protects against cerebral infarction via inhibition of NADPH oxidase-derived superoxide in ischemic stroke
    • Hong, H., Zeng, J.-S., Kreulen, D.L., Kaufman, D.I. and Chen, A.F. (2006) Atorvastatin protects against cerebral infarction via inhibition of NADPH oxidase-derived superoxide in ischemic stroke. Am. J. Physiol. Heart Circ. Physiol. 291, H2210-H2215
    • (2006) Am. J. Physiol. Heart Circ. Physiol. , vol.291
    • Hong, H.1    Zeng, J.-S.2    Kreulen, D.L.3    Kaufman, D.I.4    Chen, A.F.5
  • 47
    • 84861854211 scopus 로고    scopus 로고
    • NADPH oxidases: Novel therapeutic targets for neurodegenerative diseases
    • Gao, H.-M., Zhou, H. and Hong, J.-S. (2012) NADPH oxidases: novel therapeutic targets for neurodegenerative diseases. Trends Pharmacol. Sci. 33, 295-303
    • (2012) Trends Pharmacol. Sci. , vol.33 , pp. 295-303
    • Gao, H.-M.1    Zhou, H.2    Hong, J.-S.3
  • 48
    • 84866425239 scopus 로고    scopus 로고
    • Aiding and abetting roles of NOX oxidases in cellular transformation
    • Block, K. and Gorin, Y. (2012) Aiding and abetting roles of NOX oxidases in cellular transformation. Nat. Rev. Cancer 12, 627-637
    • (2012) Nat. Rev. Cancer , vol.12 , pp. 627-637
    • Block, K.1    Gorin, Y.2
  • 49
    • 84863743170 scopus 로고    scopus 로고
    • H2O2 production downstream of FLT3 is mediated by p22phox in the endoplasmic reticulum and is required for STAT5 signalling
    • Woolley, J.F., Naughton, R., Stanicka, J., Gough, D.R., Bhatt, L., Dickinson, B.C., Chang, C.J. and Cotter, T.G. (2012) H2O2 production downstream of FLT3 is mediated by p22phox in the endoplasmic reticulum and is required for STAT5 signalling. PLoS ONE 7, e34050
    • (2012) PLoS ONE , vol.7
    • Woolley, J.F.1    Naughton, R.2    Stanicka, J.3    Gough, D.R.4    Bhatt, L.5    Dickinson, B.C.6    Chang, C.J.7    Cotter, T.G.8
  • 50
    • 35649021332 scopus 로고    scopus 로고
    • NADPH oxidase promotes pancreatic cancer cell survival via inhibiting JAK2 dephosphorylation by tyrosine phosphatases
    • Lee, J.K., Edderkaoui, M., Truong, P., Ohno, I., Jang, K.-T., Berti, A., Pandol, S.J. and Gukovskaya, A.S. (2007) NADPH oxidase promotes pancreatic cancer cell survival via inhibiting JAK2 dephosphorylation by tyrosine phosphatases. Gastroenterology 133, 1637-1648
    • (2007) Gastroenterology , vol.133 , pp. 1637-1648
    • Lee, J.K.1    Edderkaoui, M.2    Truong, P.3    Ohno, I.4    Jang, K.-T.5    Berti, A.6    Pandol, S.J.7    Gukovskaya, A.S.8


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