메뉴 건너뛰기




Volumn 74, Issue , 2014, Pages 175-187

Inducible nitric oxide synthase mediates MG132 lethality in leukemic cells through mitochondrial depolarization

Author keywords

Apoptosis; Free radicals; Mitochondrial depolarization; Nitric oxide synthase; Proteasome inhibitor; Reactive oxygen nitrogen species

Indexed keywords

AMINOGUANIDINE; BENZYLOXYCARBONYLLEUCYLLEUCYLLEUCINAL; CASPASE; INDUCIBLE NITRIC OXIDE SYNTHASE; MANGANESE SUPEROXIDE DISMUTASE; NITRIC OXIDE; SUPEROXIDE; BENZYLOXYCARBONYLLEUCYL-LEUCYL-LEUCINE ALDEHYDE; CYCLIC GMP; CYSTEINE PROTEINASE INHIBITOR; LEUPEPTIN; PROTEASOME; SUPEROXIDE DISMUTASE;

EID: 84905048829     PISSN: 08915849     EISSN: 18734596     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2014.05.023     Document Type: Article
Times cited : (6)

References (69)
  • 1
    • 0032006110 scopus 로고    scopus 로고
    • Intracellular distribution of proteasomes
    • DOI 10.1016/S0952-7915(98)80040-X
    • A.J. Rivett Intracellular (Pubitemid 28112088)
    • (1998) Current Opinion in Immunology , vol.10 , Issue.1 , pp. 110-114
    • Rivett, A.J.1
  • 3
    • 79151480727 scopus 로고    scopus 로고
    • Ubiquitin-proteasome system and mitochondria - Reciprocity
    • N. Livnat-Levanon, and M.H. Glickman Ubiquitin-proteasome system and mitochondria - reciprocity Biochim. Biophys. Acta 1809 2011 80 87
    • (2011) Biochim. Biophys. Acta , vol.1809 , pp. 80-87
    • Livnat-Levanon, N.1    Glickman, M.H.2
  • 5
    • 67649402187 scopus 로고    scopus 로고
    • The Nrf2-antioxidant response element signaling pathway and its activation by oxidative stress
    • T. Nguyen, P. Nioi, and C.B. Pickett The Nrf2-antioxidant response element signaling pathway and its activation by oxidative stress J. Biol. Chem. 284 2009 13291 13295
    • (2009) J. Biol. Chem. , vol.284 , pp. 13291-13295
    • Nguyen, T.1    Nioi, P.2    Pickett, C.B.3
  • 9
    • 0032513215 scopus 로고    scopus 로고
    • Proteasome inhibitors activate stress kinases and induce Hsp72. Diverse effects on apoptosis
    • DOI 10.1074/jbc.273.11.6373
    • A.B. Meriin, V.L. Gabai, J. Yaglom, V.I. Shifrin, and M.Y. Sherman Proteasome inhibitors activate stress kinases and induce Hsp72: diverse effects on apoptosis J. Biol. Chem. 273 1998 6373 6379 (Pubitemid 28144729)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.11 , pp. 6373-6379
    • Meriin, A.B.1    Gabai, V.L.2    Yaglom, J.3    Shifrin, V.I.4    Sherman, M.Y.5
  • 10
    • 84856213846 scopus 로고    scopus 로고
    • The diverse and complex roles of NF-kappaB subunits in cancer
    • N.D. Perkins The diverse and complex roles of NF-kappaB subunits in cancer Nat. Rev. Cancer 12 2012 121 132
    • (2012) Nat. Rev. Cancer , vol.12 , pp. 121-132
    • Perkins, N.D.1
  • 11
    • 0032490670 scopus 로고    scopus 로고
    • Nuclear factor (NF)-κB-regulated X-chromosome-linked iap gene expression protects endothelial cells from tumor necrosis factor α-induced apoptosis
    • DOI 10.1084/jem.188.1.211
    • C. Stehlik, R. de Martin, I. Kumabashiri, J.A. Schmid, B.R. Binder, and J. Lipp Nuclear factor (NF)-kappaB-regulated X-chromosome-linked IAP gene expression protects endothelial cells from tumor necrosis factor alpha-induced apoptosis J. Exp. Med. 188 1998 211 216 (Pubitemid 28328620)
    • (1998) Journal of Experimental Medicine , vol.188 , Issue.1 , pp. 211-216
    • Stehlik, C.1    De Martin, R.2    Kumabashiri, I.3    Schmid, J.A.4    Binder, B.R.5    Lipp, J.6
  • 13
    • 0030692715 scopus 로고    scopus 로고
    • Tumor necrosis factor alpha and interleukin-1β regulate the murine manganese superoxide dismutase gene through a complex intronic enhancer involving C/EBP-β and NF-κB
    • P.L. Jones, D. Ping, and J.M. Boss Tumor necrosis factor alpha and interleukin-1beta regulate the murine manganese superoxide dismutase gene through a complex intronic enhancer involving C/EBP-beta and NF-kappaB Mol. Cell. Biol. 17 1997 6970 6981 (Pubitemid 27505927)
    • (1997) Molecular and Cellular Biology , vol.17 , Issue.12 , pp. 6970-6981
    • Jones, P.L.1    Ping, D.2    Boss, J.M.3
  • 14
    • 74849125276 scopus 로고    scopus 로고
    • The pharmacological NFkappaB inhibitors BAY117082 and MG132 induce cell arrest and apoptosis in leukemia cells through ROS-mitochondria pathway activation
    • A. Zanotto-Filho, A. Delgado-Canedo, R. Schroder, M. Becker, F. Klamt, and J.C. Moreira The pharmacological NFkappaB inhibitors BAY117082 and MG132 induce cell arrest and apoptosis in leukemia cells through ROS-mitochondria pathway activation Cancer Lett. 288 2010 192 203
    • (2010) Cancer Lett. , vol.288 , pp. 192-203
    • Zanotto-Filho, A.1    Delgado-Canedo, A.2    Schroder, R.3    Becker, M.4    Klamt, F.5    Moreira, J.C.6
  • 17
    • 84875539389 scopus 로고    scopus 로고
    • Proteasome inhibitor MG132 induces selective apoptosis in glioblastoma cells through inhibition of PI3K/Akt and NFkappaB pathways, mitochondrial dysfunction, and activation of p38-JNK1/2 signaling
    • A. Zanotto-Filho, E. Braganhol, A.M. Battastini, and J.C. Moreira Proteasome inhibitor MG132 induces selective apoptosis in glioblastoma cells through inhibition of PI3K/Akt and NFkappaB pathways, mitochondrial dysfunction, and activation of p38-JNK1/2 signaling Invest. New Drugs 30 2012 2252 2262
    • (2012) Invest. New Drugs , vol.30 , pp. 2252-2262
    • Zanotto-Filho, A.1    Braganhol, E.2    Battastini, A.M.3    Moreira, J.C.4
  • 18
    • 0037516876 scopus 로고    scopus 로고
    • Conformational change and mitochondrial translocation of Bax accompany proteasome inhibitor-induced apoptosis of chronic lymphocytic leukemic cells
    • DOI 10.1038/sj.onc.1206326
    • G. Dewson, R.T. Snowden, J.B. Almond, M.J. Dyer, and G.M. Cohen Conformational change and mitochondrial translocation of Bax accompany proteasome inhibitor-induced apoptosis of chronic lymphocytic leukemic cells Oncogene 22 2003 2643 2654 (Pubitemid 36605612)
    • (2003) Oncogene , vol.22 , Issue.17 , pp. 2643-2654
    • Dewson, G.1    Snowden, R.T.2    Almond, J.B.3    Dyer, M.J.S.4    Cohen, G.M.5
  • 20
    • 84859799949 scopus 로고    scopus 로고
    • Stress management at the ER: Regulators of ER stress-induced apoptosis
    • A.M. Gorman, S.J. Healy, R. Jager, and A. Samali Stress management at the ER: regulators of ER stress-induced apoptosis Pharmacol. Ther. 134 2012 306 316
    • (2012) Pharmacol. Ther. , vol.134 , pp. 306-316
    • Gorman, A.M.1    Healy, S.J.2    Jager, R.3    Samali, A.4
  • 22
    • 34547673497 scopus 로고    scopus 로고
    • Peroxynitrite: Biochemistry, pathophysiology and development of therapeutics
    • DOI 10.1038/nrd2222, PII NRD2222
    • C. Szabo, H. Ischiropoulos, and R. Radi Peroxynitrite: biochemistry, pathophysiology and development of therapeutics Nat. Rev. Drug Discovery 6 2007 662 680 (Pubitemid 47207751)
    • (2007) Nature Reviews Drug Discovery , vol.6 , Issue.8 , pp. 662-680
    • Szabo, C.1    Ischiropoulos, H.2    Radi, R.3
  • 23
    • 68249153842 scopus 로고    scopus 로고
    • The effect of MG132, a proteasome inhibitor on HeLa cells in relation to cell growth, reactive oxygen species and GSH
    • Y.H. Han, H.J. Moon, B.R. You, and W.H. Park The effect of MG132, a proteasome inhibitor on HeLa cells in relation to cell growth, reactive oxygen species and GSH Oncol. Rep. 22 2009 215 221
    • (2009) Oncol. Rep. , vol.22 , pp. 215-221
    • Han, Y.H.1    Moon, H.J.2    You, B.R.3    Park, W.H.4
  • 24
    • 77953834412 scopus 로고    scopus 로고
    • MG132 as a proteasome inhibitor induces cell growth inhibition and cell death in A549 lung cancer cells via influencing reactive oxygen species and GSH level
    • Y.H. Han, and W.H. Park MG132 as a proteasome inhibitor induces cell growth inhibition and cell death in A549 lung cancer cells via influencing reactive oxygen species and GSH level Hum. Exp. Toxicol. 29 2010 607 614
    • (2010) Hum. Exp. Toxicol. , vol.29 , pp. 607-614
    • Han, Y.H.1    Park, W.H.2
  • 25
    • 79956204057 scopus 로고    scopus 로고
    • Optimization of the tetrazolium dye (MTT) colorimetric assay for cellular growth and viability
    • P.W. Sylvester Optimization of the tetrazolium dye (MTT) colorimetric assay for cellular growth and viability Methods Mol. Biol. 716 2011 157 168
    • (2011) Methods Mol. Biol. , vol.716 , pp. 157-168
    • Sylvester, P.W.1
  • 26
    • 0032712575 scopus 로고    scopus 로고
    • Divided we stand: Tracking cell proliferation with carboxyfluorescein diacetate succinimidyl ester
    • A.B. Lyons Divided we stand: tracking cell proliferation with carboxyfluorescein diacetate succinimidyl ester Immunol. Cell Biol. 77 1999 509 515
    • (1999) Immunol. Cell Biol. , vol.77 , pp. 509-515
    • Lyons, A.B.1
  • 27
    • 39149116749 scopus 로고    scopus 로고
    • Multiparametric analysis of cells with different mitochondrial membrane potential during apoptosis by polychromatic flow cytometry
    • L. Troiano, R. Ferraresi, E. Lugli, E. Nemes, E. Roat, M. Nasi, M. Pinti, and A. Cossarizza Multiparametric analysis of cells with different mitochondrial membrane potential during apoptosis by polychromatic flow cytometry Nat. Protoc. 2 2007 2719 2727
    • (2007) Nat. Protoc. , vol.2 , pp. 2719-2727
    • Troiano, L.1    Ferraresi, R.2    Lugli, E.3    Nemes, E.4    Roat, E.5    Nasi, M.6    Pinti, M.7    Cossarizza, A.8
  • 29
    • 0034068601 scopus 로고    scopus 로고
    • Mitochondrial control of cell death
    • DOI 10.1038/74994
    • G. Kroemer, and J.C. Reed Mitochondrial control of cell death Nat. Med. 6 2000 513 519 (Pubitemid 30305900)
    • (2000) Nature Medicine , vol.6 , Issue.5 , pp. 513-519
    • Kroemer, G.1    Reed, J.C.2
  • 30
    • 33748789479 scopus 로고    scopus 로고
    • Mediators of endoplasmic reticulum stress-induced apoptosis
    • DOI 10.1038/sj.embor.7400779, PII 7400779
    • E. Szegezdi, S.E. Logue, A.M. Gorman, and A. Samali Mediators of endoplasmic reticulum stress-induced apoptosis EMBO Rep. 7 2006 880 885 (Pubitemid 44523966)
    • (2006) EMBO Reports , vol.7 , Issue.9 , pp. 880-885
    • Szegezdi, E.1    Logue, S.E.2    Gorman, A.M.3    Samali, A.4
  • 31
    • 84857116578 scopus 로고    scopus 로고
    • Reactive oxygen species (ROS) homeostasis and redox regulation in cellular signaling
    • P.D. Ray, B.W. Huang, and Y. Tsuji Reactive oxygen species (ROS) homeostasis and redox regulation in cellular signaling Cell. Signalling 24 2012 981 990
    • (2012) Cell. Signalling , vol.24 , pp. 981-990
    • Ray, P.D.1    Huang, B.W.2    Tsuji, Y.3
  • 33
    • 0030040255 scopus 로고    scopus 로고
    • Selective pharmacological inhibition of distinct nitric oxide synthase isoforms
    • DOI 10.1016/0006-2952(95)02099-3
    • G.J. Southan, and C. Szabo Selective pharmacological inhibition of distinct nitric oxide synthase isoforms Biochem. Pharmacol. 51 1996 383 394 (Pubitemid 26071171)
    • (1996) Biochemical Pharmacology , vol.51 , Issue.4 , pp. 383-394
    • Southan, G.J.1    Szabo, C.2
  • 35
    • 0033567065 scopus 로고    scopus 로고
    • Enzymatic function of nitric oxide synthases
    • DOI 10.1016/S0008-6363(99)00115-7, PII S0008636399001157
    • P.J. Andrew, and B. Mayer Enzymatic function of nitric oxide synthases Cardiovasc. Res. 43 1999 521 531 (Pubitemid 29369251)
    • (1999) Cardiovascular Research , vol.43 , Issue.3 , pp. 521-531
    • Andrew, P.J.1    Mayer, B.2
  • 36
    • 79958152853 scopus 로고    scopus 로고
    • Superoxide dismutase in redox biology: The roles of superoxide and hydrogen peroxide
    • G.R. Buettner Superoxide dismutase in redox biology: the roles of superoxide and hydrogen peroxide Anti-cancer Agents Med. Chem. 11 2011 341 346
    • (2011) Anti-cancer Agents Med. Chem. , vol.11 , pp. 341-346
    • Buettner, G.R.1
  • 37
    • 0036890524 scopus 로고    scopus 로고
    • Peroxynitrite reactions and formation in mitochondria
    • DOI 10.1016/S0891-5849(02)01111-5, PII S0891584902011115
    • R. Radi, A. Cassina, R. Hodara, C. Quijano, and L. Castro Peroxynitrite reactions and formation in mitochondria Free Radic. Biol. Med. 33 2002 1451 1464 (Pubitemid 35351588)
    • (2002) Free Radical Biology and Medicine , vol.33 , Issue.11 , pp. 1451-1464
    • Radi, R.1    Cassina, A.2    Hodara, R.3    Quijano, C.4    Castro, L.5
  • 38
    • 84874452686 scopus 로고    scopus 로고
    • Redox control of leukemia: From molecular mechanisms to therapeutic opportunities
    • M.E. Irwin, N. Rivera-Del Valle, and J. Chandra Redox control of leukemia: from molecular mechanisms to therapeutic opportunities Antioxid. Redox Signaling 18 2013 1349 1383
    • (2013) Antioxid. Redox Signaling , vol.18 , pp. 1349-1383
    • Irwin, M.E.1    Rivera-Del Valle, N.2    Chandra, J.3
  • 39
    • 0035968305 scopus 로고    scopus 로고
    • Inducible nitric-oxide synthase is regulated by the proteasome degradation pathway
    • A. Musial, and N.T. Eissa Inducible nitric-oxide synthase is regulated by the proteasome degradation pathway J. Biol. Chem. 276 2001 24268 24273
    • (2001) J. Biol. Chem. , vol.276 , pp. 24268-24273
    • Musial, A.1    Eissa, N.T.2
  • 40
    • 0042819604 scopus 로고    scopus 로고
    • Catalase is regulated by ubiquitination and proteosomal degradation. Role of the c-Abl and Arg tyrosine kinases
    • DOI 10.1021/bi035023f
    • C. Cao, Y. Leng, X. Liu, Y. Yi, P. Li, and D. Kufe Catalase is regulated by ubiquitination and proteosomal degradation: role of the c-Abl and Arg tyrosine kinases Biochemistry 42 2003 10348 10353 (Pubitemid 37071434)
    • (2003) Biochemistry , vol.42 , Issue.35 , pp. 10348-10353
    • Cao, C.1    Leng, Y.2    Liu, X.3    Yi, Y.4    Li, P.5    Kufe, D.6
  • 41
    • 0037442128 scopus 로고    scopus 로고
    • The mitochondrial network of human neutrophils: Role in chemotaxis, phagocytosis, respiratory burst activation, and commitment to apoptosis
    • G. Fossati, D.A. Moulding, D.G. Spiller, R.J. Moots, M.R. White, and S.W. Edwards The mitochondrial network of human neutrophils: role in chemotaxis, phagocytosis, respiratory burst activation, and commitment to apoptosis J. Immunol. 170 2003 1964 1972 (Pubitemid 36197416)
    • (2003) Journal of Immunology , vol.170 , Issue.4 , pp. 1964-1972
    • Fossati, G.1    Moulding, D.A.2    Spiller, D.G.3    Moots, R.J.4    White, M.R.H.5    Edwards, S.W.6
  • 42
    • 84883617963 scopus 로고    scopus 로고
    • Synergistic apoptosis of CML cells by buthionine sulfoximine and hydroxychavicol correlates with activation of AIF and GSH-ROS-JNK-ERK-iNOS pathway
    • A.A. Chowdhury, J. Chaudhuri, N. Biswas, A. Manna, S. Chatterjee, S.K. Mahato, U. Chaudhuri, P. Jaisankar, and S. Bandyopadhyay Synergistic apoptosis of CML cells by buthionine sulfoximine and hydroxychavicol correlates with activation of AIF and GSH-ROS-JNK-ERK-iNOS pathway PLoS One 8 2013 e73672
    • (2013) PLoS One , vol.8 , pp. 73672
    • Chowdhury, A.A.1    Chaudhuri, J.2    Biswas, N.3    Manna, A.4    Chatterjee, S.5    Mahato, S.K.6    Chaudhuri, U.7    Jaisankar, P.8    Bandyopadhyay, S.9
  • 44
    • 0033789703 scopus 로고    scopus 로고
    • The inhibitory potency and selectivity of arginine substrate site nitric-oxide synthase inhibitors is solely determined by their affinity toward the different isoenzymes
    • R. Boer, W.R. Ulrich, T. Klein, B. Mirau, S. Haas, and I. Baur The inhibitory potency and selectivity of arginine substrate site nitric-oxide synthase inhibitors is solely determined by their affinity toward the different isoenzymes Mol. Pharmacol. 58 2000 1026 1034
    • (2000) Mol. Pharmacol. , vol.58 , pp. 1026-1034
    • Boer, R.1    Ulrich, W.R.2    Klein, T.3    Mirau, B.4    Haas, S.5    Baur, I.6
  • 46
    • 2942593991 scopus 로고    scopus 로고
    • ROS stress in cancer cells and therapeutic implications
    • DOI 10.1016/j.drup.2004.01.004
    • H. Pelicano, D. Carney, and P. Huang ROS stress in cancer cells and therapeutic implications Drug Resist. Updates 7 2004 97 110 (Pubitemid 38736063)
    • (2004) Drug Resistance Updates , vol.7 , Issue.2 , pp. 97-110
    • Pelicano, H.1    Carney, D.2    Huang, P.3
  • 47
    • 33748146888 scopus 로고    scopus 로고
    • Selective killing of oncogenically transformed cells through a ROS-mediated mechanism by β-phenylethyl isothiocyanate
    • DOI 10.1016/j.ccr.2006.08.009, PII S1535610806002509
    • D. Trachootham, Y. Zhou, H. Zhang, Y. Demizu, Z. Chen, H. Pelicano, P.J. Chiao, G. Achanta, R.B. Arlinghaus, J. Liu, and P. Huang Selective killing of oncogenically transformed cells through a ROS-mediated mechanism by beta-phenylethyl isothiocyanate Cancer Cell 10 2006 241 252 (Pubitemid 44311067)
    • (2006) Cancer Cell , vol.10 , Issue.3 , pp. 241-252
    • Trachootham, D.1    Zhou, Y.2    Zhang, H.3    Demizu, Y.4    Chen, Z.5    Pelicano, H.6    Chiao, P.J.7    Achanta, G.8    Arlinghaus, R.B.9    Liu, J.10    Huang, P.11
  • 48
    • 0027360689 scopus 로고
    • Regulation of proteasome expression in developing and transformed cells
    • A. Ichihara, K. Tanaka, T. Andoh, and N. Shimbara Regulation of proteasome expression in developing and transformed cells Adv. Enzyme Regul. 33 1993 173 180
    • (1993) Adv. Enzyme Regul. , vol.33 , pp. 173-180
    • Ichihara, A.1    Tanaka, K.2    Andoh, T.3    Shimbara, N.4
  • 50
    • 84871510797 scopus 로고    scopus 로고
    • Therapeutic targeting of cancer cell cycle using proteasome inhibitors
    • N. Rastogi, and D.P. Mishra Therapeutic targeting of cancer cell cycle using proteasome inhibitors Cell Div. 7 2012 26
    • (2012) Cell Div. , vol.7 , pp. 26
    • Rastogi, N.1    Mishra, D.P.2
  • 51
    • 0033623487 scopus 로고    scopus 로고
    • Proteasome inhibitors induced caspase-dependent apoptosis and accumulation of p21WAF1/Cip1 in human immature leukemic cells
    • C. Naujokat, O. Sezer, H. Zinke, A. Leclere, S. Hauptmann, and K. Possinger Proteasome inhibitors induced caspase-dependent apoptosis and accumulation of p21WAF1/Cip1 in human immature leukemic cells Eur. J. Haematol. 65 2000 221 236
    • (2000) Eur. J. Haematol. , vol.65 , pp. 221-236
    • Naujokat, C.1    Sezer, O.2    Zinke, H.3    Leclere, A.4    Hauptmann, S.5    Possinger, K.6
  • 52
    • 0032563106 scopus 로고    scopus 로고
    • Domain swapping in inducible nitric-oxide synthase: Electron transfer occurs between flavin and heme groups located on adjacent subunits in the dimer
    • DOI 10.1074/jbc.273.30.18950
    • U. Siddhanta, A. Presta, B. Fan, D. Wolan, D.L. Rousseau, and D.J. Stuehr Domain swapping in inducible nitric-oxide synthase: electron transfer occurs between flavin and heme groups located on adjacent subunits in the dimer J. Biol. Chem. 273 1998 18950 18958 (Pubitemid 28366284)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.30 , pp. 18950-18958
    • Siddhanta, U.1    Presta, A.2    Fan, B.3    Wolan, D.4    Rousseau, D.L.5    Stuehr, D.J.6
  • 53
  • 54
    • 38549101188 scopus 로고    scopus 로고
    • Quality control of mitochondria: Protection against neurodegeneration and ageing
    • DOI 10.1038/sj.emboj.7601972, PII 7601972
    • T. Tatsuta, and T. Langer Quality control of mitochondria: protection against neurodegeneration and ageing EMBO J. 27 2008 306 314 (Pubitemid 351161660)
    • (2008) EMBO Journal , vol.27 , Issue.2 , pp. 306-314
    • Tatsuta, T.1    Langer, T.2
  • 55
    • 15944382742 scopus 로고    scopus 로고
    • Mitochondrial nitric oxide synthase
    • DOI 10.1016/j.tips.2005.02.005
    • P. Ghafourifar, and E. Cadenas Mitochondrial nitric oxide synthase Trends Pharmacol. Sci. 26 2005 190 195 (Pubitemid 40432654)
    • (2005) Trends in Pharmacological Sciences , vol.26 , Issue.4 , pp. 190-195
    • Ghafourifar, P.1    Cadenas, E.2
  • 56
    • 1342282382 scopus 로고    scopus 로고
    • Mitochondrial nitric oxide synthase
    • DOI 10.1016/j.mito.2003.10.001, PII S1567724903001788
    • P.S. Brookes Mitochondrial nitric oxide synthase Mitochondrion 3 2004 187 204 (Pubitemid 38263634)
    • (2004) Mitochondrion , vol.3 , Issue.4 , pp. 187-204
    • Brookes, P.S.1
  • 57
    • 84870545221 scopus 로고    scopus 로고
    • Strategic localization of heart mitochondrial NOS: A review of the evidence
    • T. Zaobornyj, and P. Ghafourifar Strategic localization of heart mitochondrial NOS: a review of the evidence Am. J. Physiol. Heart Circ. Physiol. 303 2012 H1283 H1293
    • (2012) Am. J. Physiol. Heart Circ. Physiol. , vol.303
    • Zaobornyj, T.1    Ghafourifar, P.2
  • 58
    • 33646118481 scopus 로고    scopus 로고
    • Mitochondrial metabolic states and membrane potential modulate mtNOS activity
    • L.B. Valdez, T. Zaobornyj, and A. Boveris Mitochondrial metabolic states and membrane potential modulate mtNOS activity Biochim. Biophys. Acta 1757 2006 166 172
    • (2006) Biochim. Biophys. Acta , vol.1757 , pp. 166-172
    • Valdez, L.B.1    Zaobornyj, T.2    Boveris, A.3
  • 59
    • 0142150051 scopus 로고    scopus 로고
    • Mitochondrial formation of reactive oxygen species
    • DOI 10.1113/jphysiol.2003.049478
    • J.F. Turrens Mitochondrial formation of reactive oxygen species J. Physiol. 552 2003 335 344 (Pubitemid 37321833)
    • (2003) Journal of Physiology , vol.552 , Issue.2 , pp. 335-344
    • Turrens, J.F.1
  • 60
    • 84859809125 scopus 로고    scopus 로고
    • Redox regulation of mitochondrial function
    • D.E. Handy, and J. Loscalzo Redox regulation of mitochondrial function Antioxid. Redox Signaling 16 2012 1323 1367
    • (2012) Antioxid. Redox Signaling , vol.16 , pp. 1323-1367
    • Handy, D.E.1    Loscalzo, J.2
  • 61
    • 0033828545 scopus 로고    scopus 로고
    • Mechanisms involved in the pro- and anti-apoptotic role of NO in human leukemia
    • J.P. Kolb Mechanisms involved in the pro- and anti-apoptotic role of NO in human leukemia Leukemia 14 2000 1685 1694
    • (2000) Leukemia , vol.14 , pp. 1685-1694
    • Kolb, J.P.1
  • 62
    • 76049083966 scopus 로고    scopus 로고
    • Reactive oxygen species, cellular redox systems, and apoptosis
    • M.L. Circu, and T.Y. Aw Reactive oxygen species, cellular redox systems, and apoptosis Free Radic. Biol. Med. 48 2010 749 762
    • (2010) Free Radic. Biol. Med. , vol.48 , pp. 749-762
    • Circu, M.L.1    Aw, T.Y.2
  • 63
    • 79960716413 scopus 로고    scopus 로고
    • Regulating mitochondrial outer membrane proteins by ubiquitination and proteasomal degradation
    • M. Karbowski, and R.J. Youle Regulating mitochondrial outer membrane proteins by ubiquitination and proteasomal degradation Curr. Opin. Cell Biol. 23 2011 476 482
    • (2011) Curr. Opin. Cell Biol. , vol.23 , pp. 476-482
    • Karbowski, M.1    Youle, R.J.2
  • 66
    • 77951219693 scopus 로고    scopus 로고
    • Nuclear factor kappaB- and specificity protein 1-dependent p53-mediated bi-directional regulation of the human manganese superoxide dismutase gene
    • S.K. Dhar, Y. Xu St, and D.K. Clair Nuclear factor kappaB- and specificity protein 1-dependent p53-mediated bi-directional regulation of the human manganese superoxide dismutase gene J. Biol. Chem. 285 2010 9835 9846
    • (2010) J. Biol. Chem. , vol.285 , pp. 9835-9846
    • Dhar, S.K.1    Xu St, Y.2    Clair, D.K.3
  • 67
    • 84861628788 scopus 로고    scopus 로고
    • Manganese superoxide dismutase regulation and cancer
    • S.K. Dhar St, and D.K. Clair Manganese superoxide dismutase regulation and cancer Free Radic. Biol. Med. 52 2012 2209 2222
    • (2012) Free Radic. Biol. Med. , vol.52 , pp. 2209-2222
    • Dhar St, S.K.1    Clair, D.K.2
  • 68
    • 0037040834 scopus 로고    scopus 로고
    • Sp1 transcription factor as a molecular target for nitric oxide- and cyclic nucleotide-mediated suppression of cGMP-dependent protein kinase-Iα expression in vascular smooth muscle cells
    • DOI 10.1161/hh0402.105898
    • H. Sellak, X. Yang, X. Cao, T. Cornwell, G.A. Soff, and T. Lincoln Sp1 transcription factor as a molecular target for nitric oxide- and cyclic nucleotide-mediated suppression of cGMP-dependent protein kinase-Ialpha expression in vascular smooth muscle cells Circ. Res. 90 2002 405 412 (Pubitemid 34633909)
    • (2002) Circulation Research , vol.90 , Issue.4 , pp. 405-412
    • Sellak, H.1    Yang, X.2    Cao, X.3    Cornwell, T.4    Soff, G.A.5    Lincoln, T.6
  • 69
    • 84879937580 scopus 로고    scopus 로고
    • Mitochondrial modulation decreases the bortezomib-resistance in multiple myeloma cells
    • I.S. Song, H.K. Kim, S.R. Lee, S.H. Jeong, N. Kim, K.S. Ko, B.D. Rhee, and J. Han Mitochondrial modulation decreases the bortezomib-resistance in multiple myeloma cells Int. J. Cancer 133 2013 1357 1367
    • (2013) Int. J. Cancer , vol.133 , pp. 1357-1367
    • Song, I.S.1    Kim, H.K.2    Lee, S.R.3    Jeong, S.H.4    Kim, N.5    Ko, K.S.6    Rhee, B.D.7    Han, J.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.