메뉴 건너뛰기




Volumn 13, Issue 9, 2012, Pages 10697-10721

Cell signaling through protein kinase C oxidation and activation

Author keywords

Cell signaling; Protein kinase c; Reactive oxygen species

Indexed keywords

ACTIVATING TRANSCRIPTION FACTOR 1; ANGIOTENSIN II; CALCIUM ION; GUANOSINE TRIPHOSPHATASE; PHOSPHATIDYLINOSITOL 3 KINASE; PHOSPHOINOSITIDE DEPENDENT PROTEIN KINASE 1; PHOSPHOLIPASE C; PROTEIN KINASE C; PROTEIN KINASE C BETA; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE 1; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE 4;

EID: 84866914984     PISSN: 16616596     EISSN: 14220067     Source Type: Journal    
DOI: 10.3390/ijms130910697     Document Type: Review
Times cited : (200)

References (177)
  • 1
    • 33845478569 scopus 로고    scopus 로고
    • Proteomic analysis of phosphorylation, oxidation and nitrosylation in signal transduction
    • Spickett, C.M.; Pitt, A.R.; Morrice, N.; Kolch, W. Proteomic analysis of phosphorylation, oxidation and nitrosylation in signal transduction. Biochim. Biophys. Acta 2006, 1764, 1823-1841.
    • (2006) Biochim. Biophys. Acta , vol.1764 , pp. 1823-1841
    • Spickett, C.M.1    Pitt, A.R.2    Morrice, N.3    Kolch, W.4
  • 2
    • 20444400257 scopus 로고    scopus 로고
    • Redox redux: Revisiting PTPs and the control of cell signaling
    • Tonks, N.K. Redox redux: Revisiting PTPs and the control of cell signaling. Cell 2005, 121, 667-670.
    • (2005) Cell , vol.121 , pp. 667-670
    • Tonks, N.K.1
  • 6
    • 79952311582 scopus 로고    scopus 로고
    • Ecto-phosphatase in protozoan parasites: Possible roles in nutrition, growth and ROS sensing
    • Cosentino-Gomes, D.; Meyer-Fernandes, J.R. Ecto-phosphatase in protozoan parasites: Possible roles in nutrition, growth and ROS sensing. J. Bioenerg. Biomembr. 2011, 43, 89-92.
    • (2011) J. Bioenerg. Biomembr , vol.43 , pp. 89-92
    • Cosentino-Gomes, D.1    Meyer-Fernandes, J.R.2
  • 7
    • 79961191673 scopus 로고    scopus 로고
    • Redox regulation of protein kinases as a modulator of vascular function
    • Knock, G.A.; Ward, J.P.T. Redox regulation of protein kinases as a modulator of vascular function. Antioxid. Redox Signal. 2011, 15, 1531-1547.
    • (2011) Antioxid. Redox Signal , vol.15 , pp. 1531-1547
    • Knock, G.A.1    Ward, J.P.T.2
  • 8
    • 0026451081 scopus 로고
    • Intracellular signaling by hydrolysis of phospholipids and activation of protein kinase C
    • Nishizuka, Y. Intracellular signaling by hydrolysis of phospholipids and activation of protein kinase C. Science 1992, 258, 607-614.
    • (1992) Science , vol.258 , pp. 607-614
    • Nishizuka, Y.1
  • 9
    • 0029060391 scopus 로고
    • Protein Kinase C and lipid signaling for sustained cellular responses
    • Nishizuka, Y. Protein Kinase C and lipid signaling for sustained cellular responses. FASEB J. 1995, 9, 486-496.
    • (1995) FASEB J , vol.9 , pp. 486-496
    • Nishizuka, Y.1
  • 10
    • 80053268287 scopus 로고    scopus 로고
    • PKC-delta and PKC-epsilon: Foes of the same family or strangers?
    • Duquesnes, N.; Lezoualc'h, F.; Crozatier, B. PKC-delta and PKC-epsilon: Foes of the same family or strangers? J. Mol. Cell. Cardiol. 2011, 51, 665-673.
    • (2011) J. Mol. Cell. Cardiol , vol.51 , pp. 665-673
    • Duquesnes, N.1    Lezoualc'h, F.2    Crozatier, B.3
  • 12
    • 0024412493 scopus 로고
    • The protein kinase C family: Heterogeneity and its implications
    • Kikkawa, U.; Kishimoto, A.; Nishizuka, Y. The protein kinase C family: Heterogeneity and its implications. Annu. Rev. Biochem. 1989, 58, 31-44.
    • (1989) Annu. Rev. Biochem , vol.58 , pp. 31-44
    • Kikkawa, U.1    Kishimoto, A.2    Nishizuka, Y.3
  • 13
    • 0028832593 scopus 로고
    • Spectroscopic characterization of specific phorbol ester binding to PKC-receptor sites in membranes in situ
    • Svetek, J.; Schara, M.; Pecar, S.; Hergenhahn, M.; Hecker, E. Spectroscopic characterization of specific phorbol ester binding to PKC-receptor sites in membranes in situ. Carcinogenises 1995, 10, 2589-2592.
    • (1995) Carcinogenises , vol.10 , pp. 2589-2592
    • Svetek, J.1    Schara, M.2    Pecar, S.3    Hergenhahn, M.4    Hecker, E.5
  • 17
    • 33744926666 scopus 로고    scopus 로고
    • PKD at the crossroads of DAG and PKC signaling
    • Wang, Q.J. PKD at the crossroads of DAG and PKC signaling. Trends Pharmacol. Sci. 2006, 27, 317-323.
    • (2006) Trends Pharmacol. Sci , vol.27 , pp. 317-323
    • Wang, Q.J.1
  • 18
    • 0034644523 scopus 로고    scopus 로고
    • Cellular signaling: Pivoting around PDK-1
    • Toker, A.; Newton, A.C. Cellular signaling: Pivoting around PDK-1. Cell 2000, 2, 185-188.
    • (2000) Cell , vol.2 , pp. 185-188
    • Toker, A.1    Newton, A.C.2
  • 20
    • 0037337159 scopus 로고    scopus 로고
    • Regulation of the ABC kinases by phosphorylation: Protein kinase C as a paradigm
    • Newton, A.C. Regulation of the ABC kinases by phosphorylation: Protein kinase C as a paradigm. Biochem. J. 2003, 2, 361-371.
    • (2003) Biochem. J , vol.2 , pp. 361-371
    • Newton, A.C.1
  • 21
    • 55949109631 scopus 로고    scopus 로고
    • Structural basis of protein kinase C isoform function
    • Steinberg, S.F. Structural basis of protein kinase C isoform function. Physiol. Rev. 2008, 4, 1341-1378.
    • (2008) Physiol. Rev , vol.4 , pp. 1341-1378
    • Steinberg, S.F.1
  • 22
    • 0032582525 scopus 로고    scopus 로고
    • Protein kinase C as a molecular machine for decoding calcium and diacylglycerol signals
    • Oancea, E.; Meyer, T. Protein kinase C as a molecular machine for decoding calcium and diacylglycerol signals. Cell 1998, 3, 307-318.
    • (1998) Cell , vol.3 , pp. 307-318
    • Oancea, E.1    Meyer, T.2
  • 23
    • 0034190297 scopus 로고    scopus 로고
    • Protein kinase C signaling and oxidative stress
    • Gopalakrishna, R.; Jaken, S. Protein kinase C signaling and oxidative stress. Free. Radic. Biol. Med. 2000, 9, 1349-1361.
    • (2000) Free. Radic. Biol. Med , vol.9 , pp. 1349-1361
    • Gopalakrishna, R.1    Jaken, S.2
  • 24
    • 0036183299 scopus 로고    scopus 로고
    • The family of protein kinase C and membrane lipid mediators
    • Saito, N.; Kikkawa, U.; Nishizuka, Y. The family of protein kinase C and membrane lipid mediators. J. Diabetes Complic. 2002, 1, 4-8.
    • (2002) J. Diabetes Complic , vol.1 , pp. 4-8
    • Saito, N.1    Kikkawa, U.2    Nishizuka, Y.3
  • 26
    • 33845480287 scopus 로고    scopus 로고
    • Protein tyrosine phosphorylation and reversible oxidation: Two cross-talking posttranslation modifications
    • Chiarugi, P.; Buricchi, F. Protein tyrosine phosphorylation and reversible oxidation: Two cross-talking posttranslation modifications. Antioxid. Redox Signal. 2007, 1, 1-24.
    • (2007) Antioxid. Redox Signal , vol.1 , pp. 1-24
    • Chiarugi, P.1    Buricchi, F.2
  • 29
    • 0031964645 scopus 로고    scopus 로고
    • Anchoring proteins for protein kinase C: A means for isozyme selectivity
    • Mochly-Rosen, D.; Gordon, A.S. Anchoring proteins for protein kinase C: A means for isozyme selectivity. FASEB J. 1998, 1, 35-42.
    • (1998) FASEB J , vol.1 , pp. 35-42
    • Mochly-Rosen, D.1    Gordon, A.S.2
  • 30
    • 0027322679 scopus 로고
    • Protein kinase C isoenzymes: Divergence in signal transduction?
    • Hug, H.; Sarre T.F. Protein kinase C isoenzymes: Divergence in signal transduction? Biochem. J. 1993, 2, 329-343.
    • (1993) Biochem. J , vol.2 , pp. 329-343
    • Hug, H.1    Sarre, T.F.2
  • 32
    • 39449125539 scopus 로고    scopus 로고
    • Immunogold electron microscopic demonstration of distinct submembranous localization of theactivated γPKC depending on the stimulation
    • Oyasu, M.; Fujimiya, M.; Kashiwagi, K.; Ohmori, S.; Imaeda, H.; Saito, N. Immunogold electron microscopic demonstration of distinct submembranous localization of theactivated γPKC depending on the stimulation. J. Histochem. Cytochem. 2008, 56, 253-265.
    • (2008) J. Histochem. Cytochem , vol.56 , pp. 253-265
    • Oyasu, M.1    Fujimiya, M.2    Kashiwagi, K.3    Ohmori, S.4    Imaeda, H.5    Saito, N.6
  • 33
    • 36649003474 scopus 로고    scopus 로고
    • Dietary long-chain n-3 fatty acids modify blood and cardiac phospholipids and reduce protein kinase-C-delta and protein kinase-C-epsilon translocation
    • Judé, S.; Martel, E.; Vincent, F.; Besson, P.; Couet, C.; Ogilvie, G.K.; Pinault, M.; De Chalendar, C.; Bougnoux, P.; Richard, S. et al. Dietary long-chain n-3 fatty acids modify blood and cardiac phospholipids and reduce protein kinase-C-delta and protein kinase-C-epsilon translocation. Br. J. Nutr. 2007, 6, 1143-1151.
    • (2007) Br. J. Nutr , vol.6 , pp. 1143-1151
    • Judé, S.1    Martel, E.2    Vincent, F.3    Besson, P.4    Couet, C.5    Ogilvie, G.K.6    Pinault, M.7    de Chalendar, C.8    Bougnoux, P.9    Richard, S.10
  • 34
    • 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.; Rhee, S.G. Epidermal growth factor (EGF)-induced generation of hydrogen peroxide. Role in EGF receptor-mediated tyrosine phosphorylation. J. Biol. Chem. 1997, 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
  • 35
    • 17644371347 scopus 로고    scopus 로고
    • Functions and mechanisms of redox regulation of cysteine-based phosphatases
    • Salmeen, A.; Barford, D. Functions and mechanisms of redox regulation of cysteine-based phosphatases. Antioxid. Redox Signal. 2005, 7, 560-577.
    • (2005) Antioxid. Redox Signal , vol.7 , pp. 560-577
    • Salmeen, A.1    Barford, D.2
  • 37
    • 70349341899 scopus 로고    scopus 로고
    • Downstream targets and intracellular compartmentalization in Nox Signaling
    • Chen, K.; Craige, S.E.; Keaney, J.F., Jr. Downstream targets and intracellular compartmentalization in Nox Signaling. Antioxid. Redox Signal. 2009, 11, 2467-2480.
    • (2009) Antioxid. Redox Signal , vol.11 , pp. 2467-2480
    • Chen, K.1    Craige, S.E.2    Keaney Jr., J.F.3
  • 38
    • 0031953114 scopus 로고    scopus 로고
    • The evolutionarily conserved zinc finger motif in the largest subunit of human replication protein A is required for DNA replication and mismatch repair but not for nucleotide excision repair
    • Lin, Y.L.; Shivji, M.K.; Chen, C.; Kolodner, R.; Wood, R.D.; Dutta, A. The evolutionarily conserved zinc finger motif in the largest subunit of human replication protein A is required for DNA replication and mismatch repair but not for nucleotide excision repair. J. Biol. Chem. 1998, 3, 1453-1461.
    • (1998) J. Biol. Chem , vol.3 , pp. 1453-1461
    • Lin, Y.L.1    Shivji, M.K.2    Chen, C.3    Kolodner, R.4    Wood, R.D.5    Dutta, A.6
  • 40
    • 4844224721 scopus 로고    scopus 로고
    • Activation loop phosphorylation controls protein kinase D-dependent activation of nuclear factor kappaB
    • Storz, P.; Döppler, H.; Toker, A. Activation loop phosphorylation controls protein kinase D-dependent activation of nuclear factor kappaB. Mol. Pharmacol. 2004, 66, 870-879.
    • (2004) Mol. Pharmacol , vol.66 , pp. 870-879
    • Storz, P.1    Döppler, H.2    Toker, A.3
  • 41
    • 1642379541 scopus 로고    scopus 로고
    • Protein kinase Cdelta selectively regulates protein kinase D-dependent activation of NF-kappaB in oxidative stress signaling
    • Storz, P.; Döppler, H.; Toker, A. Protein kinase Cdelta selectively regulates protein kinase D-dependent activation of NF-kappaB in oxidative stress signaling. Mol. Cell. Biol. 2004, 24, 2614-2626.
    • (2004) Mol. Cell. Biol , vol.24 , pp. 2614-2626
    • Storz, P.1    Döppler, H.2    Toker, A.3
  • 42
    • 0037413711 scopus 로고    scopus 로고
    • Protein kinase D mediates a stress-induced NF-kappaB activation and survival pathway
    • Storz, P.; Toker, A. Protein kinase D mediates a stress-induced NF-kappaB activation and survival pathway. EMBO J. 2003, 22, 109-120.
    • (2003) EMBO J , vol.22 , pp. 109-120
    • Storz, P.1    Toker, A.2
  • 43
    • 0029765443 scopus 로고    scopus 로고
    • Role of uncoupled and non-coupled oxidations in maintenance of safely low levels of oxygen and its one-electron reductants
    • Skulachev, V.P. Role of uncoupled and non-coupled oxidations in maintenance of safely low levels of oxygen and its one-electron reductants. Q. Rev. Biophys. 1996, 29, 169-202.
    • (1996) Q. Rev. Biophys , vol.29 , pp. 169-202
    • Skulachev, V.P.1
  • 44
    • 4544354262 scopus 로고    scopus 로고
    • Inhibitors of the quinone-binding site allow rapid superoxide production from mitochondrial NADH: Ubiquinone oxidoreductase (complex I)
    • Lambert, A.J.; Brand, M.D. Inhibitors of the quinone-binding site allow rapid superoxide production from mitochondrial NADH: Ubiquinone oxidoreductase (complex I). J. Biol. Chem. 2004, 17, 39414-39420.
    • (2004) J. Biol. Chem , vol.17 , pp. 39414-39420
    • Lambert, A.J.1    Brand, M.D.2
  • 45
    • 78650869592 scopus 로고    scopus 로고
    • Mitochondrial ROS generation and its regulation: Mechanisms involved in H2O2 signaling
    • Rigoulet, M.; Yoboue, E.D.; Devin, A. Mitochondrial ROS generation and its regulation: Mechanisms involved in H2O2 signaling. Antioxid. Redox Signal. 2011, 1, 459-468.
    • (2011) Antioxid. Redox Signal , vol.1 , pp. 459-468
    • Rigoulet, M.1    Yoboue, E.D.2    Devin, A.3
  • 46
    • 0032538457 scopus 로고    scopus 로고
    • Selective role for beta-protein kinase C in signaling for O-2 generation but not degranulation or adherence in differentiated HL60 cells
    • Korchak, H.M.; Rossi, M.W.; Kilpatrick, L.E. Selective role for beta-protein kinase C in signaling for O-2 generation but not degranulation or adherence in differentiated HL60 cells. J. Biol. Chem. 1998, 16, 27292-27299.
    • (1998) J. Biol. Chem , vol.16 , pp. 27292-27299
    • Korchak, H.M.1    Rossi, M.W.2    Kilpatrick, L.E.3
  • 47
    • 33748188519 scopus 로고    scopus 로고
    • Modulation of mitochondrial metabolic function by phorbol 12-myristate 13-acetate through increased mitochondrial translocation of protein kinase Calpha in C2C12 myocytes
    • Wang, Y.; Biswas, G.; Prabu, S.K.; Avadhani, N.G. Modulation of mitochondrial metabolic function by phorbol 12-myristate 13-acetate through increased mitochondrial translocation of protein kinase Calpha in C2C12 myocytes. Biochem. Pharmacol. 2006, 28, 881-892.
    • (2006) Biochem. Pharmacol , vol.28 , pp. 881-892
    • Wang, Y.1    Biswas, G.2    Prabu, S.K.3    Avadhani, N.G.4
  • 48
    • 33645452703 scopus 로고    scopus 로고
    • Chondrocyte cell death mediated by reactive oxygen species-dependent activation of PKC-betaI
    • DelCarlo, M.; Loeser, R.F. Chondrocyte cell death mediated by reactive oxygen species-dependent activation of PKC-betaI. Am. J. Physiol. Cell Physiol. 2006, 290, 802-811.
    • (2006) Am. J. Physiol. Cell Physiol , vol.290 , pp. 802-811
    • Delcarlo, M.1    Loeser, R.F.2
  • 49
    • 0022803784 scopus 로고
    • Characterization and distribution of protein kinase C in ovarian tissue
    • Noland, T.A., Jr.; Dimino, M.J. Characterization and distribution of protein kinase C in ovarian tissue. Biol. Reprod. 1986, 35, 863-872.
    • (1986) Biol. Reprod , vol.35 , pp. 863-872
    • Noland Jr., T.A.1    Dimino, M.J.2
  • 50
    • 0033233483 scopus 로고    scopus 로고
    • Protein kinase C delta targets mitochondria, alters mitochondrial membrane potential, and induces apoptosis in normal and neoplastic keratinocytes when overexpressed by an adenoviral vector
    • Li, L.; Lorenzo, P.S.; Bogi, K.; Blumberg, P.M.; Yuspa, S.H. Protein kinase C delta targets mitochondria, alters mitochondrial membrane potential, and induces apoptosis in normal and neoplastic keratinocytes when overexpressed by an adenoviral vector. Mol. Cell. Biol. 1999, 12, 8547-8558.
    • (1999) Mol. Cell. Biol , vol.12 , pp. 8547-8558
    • Li, L.1    Lorenzo, P.S.2    Bogi, K.3    Blumberg, P.M.4    Yuspa, S.H.5
  • 51
    • 0034698182 scopus 로고    scopus 로고
    • Mitochondrial translocation of protein kinase C deltain phorbol ester-induced cytochrome c release and apoptosis
    • Majumder, P.K.; Pandey, P.; Sun, X.; Cheng, K.; Datta, R.; Saxena, S.; Kharbanda, S.; Kufe, D. Mitochondrial translocation of protein kinase C deltain phorbol ester-induced cytochrome c release and apoptosis. J. Biol. Chem. 2000, 21, 21793-21796.
    • (2000) J. Biol. Chem , vol.21 , pp. 21793-21796
    • Majumder, P.K.1    Pandey, P.2    Sun, X.3    Cheng, K.4    Datta, R.5    Saxena, S.6    Kharbanda, S.7    Kufe, D.8
  • 53
    • 0037040343 scopus 로고    scopus 로고
    • Mitochondrial PKCepsilon and MAPK form signaling modules in the murine heart: Enhanced mitochondrial PKCepsilon-MAPK interactions and differential MAPK activation in PKCepsilon-induced cardioprotection
    • Baines, C.P.; Zhang, J.; Wang, G.W.; Zheng, Y.T.; Xiu, J.X.; Cardwell, E.M.; Bolli, R.; Ping, P. Mitochondrial PKCepsilon and MAPK form signaling modules in the murine heart: Enhanced mitochondrial PKCepsilon-MAPK interactions and differential MAPK activation in PKCepsilon-induced cardioprotection. Circ. Res. 2002, 8, 390-397.
    • (2002) Circ. Res , vol.8 , pp. 390-397
    • Baines, C.P.1    Zhang, J.2    Wang, G.W.3    Zheng, Y.T.4    Xiu, J.X.5    Cardwell, E.M.6    Bolli, R.7    Ping, P.8
  • 54
    • 80052046723 scopus 로고    scopus 로고
    • Interruption of mitochondrial complex IV activity and cytochrome c expression activated O2--mediated cell survival in silibinin-treated human melanoma A375-S2 cells via IGF-1R-PI3K-Akt and IGF-1R-PLC γ-PKC pathways
    • Jiang, Y.Y.; Huang, H.; Wang, H.J.; Wu, D.; Yang, R.; Tashiro, S.; Onodera, S.; Ikejima, T. Interruption of mitochondrial complex IV activity and cytochrome c expression activated O2--mediated cell survival in silibinin-treated human melanoma A375-S2 cells via IGF-1R-PI3K-Akt and IGF-1R-PLC γ-PKC pathways. Eur. J. Pharmacol. 2011, 668, 78-87.
    • (2011) Eur. J. Pharmacol , vol.668 , pp. 78-87
    • Jiang, Y.Y.1    Huang, H.2    Wang, H.J.3    Wu, D.4    Yang, R.5    Tashiro, S.6    Onodera, S.7    Ikejima, T.8
  • 55
    • 0035856980 scopus 로고    scopus 로고
    • Biochemistry and molecular cell biology of diabetic complications
    • Brownlee, M. Biochemistry and molecular cell biology of diabetic complications. Nature 2001, 13, 813-820.
    • (2001) Nature , vol.13 , pp. 813-820
    • Brownlee, M.1
  • 56
    • 33645765312 scopus 로고    scopus 로고
    • Diabetes and mitochondrial function: Role of hyperglycemia and oxidative stress
    • Rolo, A.P.; Palmeira, C.M. Diabetes and mitochondrial function: Role of hyperglycemia and oxidative stress. Toxicol. Appl. Pharmacol. 2006, 15, 167-178.
    • (2006) Toxicol. Appl. Pharmacol , vol.15 , pp. 167-178
    • Rolo, A.P.1    Palmeira, C.M.2
  • 58
    • 33750688219 scopus 로고    scopus 로고
    • Mitochondrial ROS-PKC epsilon signaling axis is uniquely involved in hypoxic increase in [Ca2+] in pulmonary artery smooth muscle cells
    • Rathore, R.; Zheng, Y.M.; Li, X.Q.; Wang, Q.S.; Liu, Q.H.; Ginnan, R.; Singer, H.A.; Ho, Y.S.; Wang, Y.X. Mitochondrial ROS-PKC epsilon signaling axis is uniquely involved in hypoxic increase in [Ca2+] in pulmonary artery smooth muscle cells. Biochem. Biophys. Res. Commun. 2006, 351, 784-790.
    • (2006) Biochem. Biophys. Res. Commun , vol.351 , pp. 784-790
    • Rathore, R.1    Zheng, Y.M.2    Li, X.Q.3    Wang, Q.S.4    Liu, Q.H.5    Ginnan, R.6    Singer, H.A.7    Ho, Y.S.8    Wang, Y.X.9
  • 59
    • 77958609724 scopus 로고    scopus 로고
    • Protective role of taurine against arsenic-induced mitochondria-dependent hepatic apoptosis via the inhibition of PKCdelta-JNK pathway
    • Das, J.; Ghosh, J.; Manna, P.; Sil, P.C. Protective role of taurine against arsenic-induced mitochondria-dependent hepatic apoptosis via the inhibition of PKCdelta-JNK pathway. PloS One 2010, 5, e12602.
    • (2010) PloS One , vol.5
    • Das, J.1    Ghosh, J.2    Manna, P.3    Sil, P.C.4
  • 60
    • 36849048813 scopus 로고    scopus 로고
    • Delayed activation of PKCdelta and NFkappaB and higher radioprotection in splenic lymphocytes by copper (II)-Curcumin (1:1) complex as compared to curcumin
    • Kunwar, A.; Narang, H.; Priyadarsini, K.I.; Krishna, M.; Pandey, R.; Sainis, K.B. Delayed activation of PKCdelta and NFkappaB and higher radioprotection in splenic lymphocytes by copper (II)-Curcumin (1:1) complex as compared to curcumin. J. Cell. Biochem. 2007, 102, 1214-1224.
    • (2007) J. Cell. Biochem , vol.102 , pp. 1214-1224
    • Kunwar, A.1    Narang, H.2    Priyadarsini, K.I.3    Krishna, M.4    Pandey, R.5    Sainis, K.B.6
  • 61
    • 19944399432 scopus 로고    scopus 로고
    • The concept of anaesthetic-induced cardioprotection: Mechanisms of action
    • Weber, N.C.; Schlack, W. The concept of anaesthetic-induced cardioprotection: Mechanisms of action. Best. Pract. Res. Clin. Anaesthesiol. 2005, 19, 429-443.
    • (2005) Best. Pract. Res. Clin. Anaesthesiol , vol.19 , pp. 429-443
    • Weber, N.C.1    Schlack, W.2
  • 63
    • 33646540442 scopus 로고    scopus 로고
    • N-(4-hydroxyphenyl) retinamide-induced apoptosis triggered by reactive oxygen species is mediated by activation of MAPKs in head and neck squamous carcinoma cells
    • Kim, H.J.; Chakravarti, N.; Oridate, N.; Choe, C.; Claret, F.X.; Lotan, R. N-(4-hydroxyphenyl) retinamide-induced apoptosis triggered by reactive oxygen species is mediated by activation of MAPKs in head and neck squamous carcinoma cells. Oncogene 2006, 25, 2785-2794.
    • (2006) Oncogene , vol.25 , pp. 2785-2794
    • Kim, H.J.1    Chakravarti, N.2    Oridate, N.3    Choe, C.4    Claret, F.X.5    Lotan, R.6
  • 64
    • 0031953147 scopus 로고    scopus 로고
    • Cyclic strain-induced reactive oxygen species involved in ICAM-1 gene induction in endothelial cells
    • Cheng, J.J.; Wung, B.S.; Chao, Y.J.; Wang, D.L. Cyclic strain-induced reactive oxygen species involved in ICAM-1 gene induction in endothelial cells. Hypertension 1998, 31, 125-130.
    • (1998) Hypertension , vol.31 , pp. 125-130
    • Cheng, J.J.1    Wung, B.S.2    Chao, Y.J.3    Wang, D.L.4
  • 65
    • 0030996930 scopus 로고    scopus 로고
    • Cyclic strain-induced monocyte chemotactic protein-1 gene expression in endothelial cells involves reactive oxygen species activation of activator protein 1
    • Wung, B.S.; Cheng, J.J.; Hsieh, H.J.; Shyy, Y.J.; Wang, D.L. Cyclic strain-induced monocyte chemotactic protein-1 gene expression in endothelial cells involves reactive oxygen species activation of activator protein 1. Circ. Res. 1997, 81, 1-7.
    • (1997) Circ. Res , vol.81 , pp. 1-7
    • Wung, B.S.1    Cheng, J.J.2    Hsieh, H.J.3    Shyy, Y.J.4    Wang, D.L.5
  • 66
    • 4143055746 scopus 로고    scopus 로고
    • Mitochondrial requirement for endothelial responses to cyclic strain: Implications for mechanotransduction
    • Ali, M.H.; Pearlstein, D.P.; Mathieu, C.E.; Schumacker, P.T. Mitochondrial requirement for endothelial responses to cyclic strain: Implications for mechanotransduction. Am. J. Physiol. Lung Cell. Mol. Physiol. 2004, 287, 486-496.
    • (2004) Am. J. Physiol. Lung Cell. Mol. Physiol , vol.287 , pp. 486-496
    • Ali, M.H.1    Pearlstein, D.P.2    Mathieu, C.E.3    Schumacker, P.T.4
  • 67
    • 33745728365 scopus 로고    scopus 로고
    • Stretch-induced phosphorylation of focal adhesion kinase in endothelial cells: Role of mitochondrial oxidants
    • Ali, M.H.; Mungai, P.T.; Schumacker, P.T. Stretch-induced phosphorylation of focal adhesion kinase in endothelial cells: Role of mitochondrial oxidants. Am. J. Physiol. Lung Cell. Mol. Physiol. 2006, 291, 38-45.
    • (2006) Am. J. Physiol. Lung Cell. Mol. Physiol , vol.291 , pp. 38-45
    • Ali, M.H.1    Mungai, P.T.2    Schumacker, P.T.3
  • 68
    • 0037129803 scopus 로고    scopus 로고
    • Phosphorylation of p47phox sites by PKC alpha, betaII, delta, and zeta: Effect on binding to p22phox and on NADPH oxidase activation
    • Fontayne, A.; Dang, P.M.; Gougerot-Pocidalo, M.A.; El-Benna, J. Phosphorylation of p47phox sites by PKC alpha, betaII, delta, and zeta: Effect on binding to p22phox and on NADPH oxidase activation. Biochemistry 2002, 18, 7743-7750.
    • (2002) Biochemistry , vol.18 , pp. 7743-7750
    • Fontayne, A.1    Dang, P.M.2    Gougerot-Pocidalo, M.A.3    El-Benna, J.4
  • 69
    • 1542406446 scopus 로고    scopus 로고
    • Nox enzymes and the biology of reactive oxygen
    • Lambeth, J.D. Nox enzymes and the biology of reactive oxygen. Nat. Rev. Immunol. 2004, 4, 181-189.
    • (2004) Nat. Rev. Immunol , vol.4 , pp. 181-189
    • Lambeth, J.D.1
  • 70
    • 0028142461 scopus 로고
    • The phosphorylation of the respiratory burst oxidase component p47phox during neutrophil activation. Phosphorylation of sites recognized by protein kinase C and by proline-directed kinases
    • El Benna, J.; Faust, L.P.; Babior, B.M. The phosphorylation of the respiratory burst oxidase component p47phox during neutrophil activation. Phosphorylation of sites recognized by protein kinase C and by proline-directed kinases. J. Biol. Chem. 1994, 23, 23431-234316.
    • (1994) J. Biol. Chem , vol.23 , pp. 23431-234316
    • El Benna, J.1    Faust, L.P.2    Babior, B.M.3
  • 71
    • 65949102522 scopus 로고    scopus 로고
    • P47phox, the phagocyte NADPH oxidase/Nox2 organizer: Structure, phosphorylation and implication in diseases
    • El-Benna, J.; Dang, P.M.; Gougerot-Pocidalo, M.A.; Marie, J.C.; Braut-Boucher, F. p47phox, the phagocyte NADPH oxidase/Nox2 organizer: Structure, phosphorylation and implication in diseases. Exp. Mol. Med. 2009, 30, 217-225.
    • (2009) Exp. Mol. Med , vol.30 , pp. 217-225
    • El-Benna, J.1    Dang, P.M.2    Gougerot-Pocidalo, M.A.3    Marie, J.C.4    Braut-Boucher, F.5
  • 72
    • 0028978633 scopus 로고
    • The phosphorylation targets of p47phox, a subunit of the respiratory burst oxidase. Functions of the individual target serines as evaluated by site-directed mutagenesis
    • Faust, L.R.; El Benna, J.; Babior, B.M.; Chanock, S.J. The phosphorylation targets of p47phox, a subunit of the respiratory burst oxidase. Functions of the individual target serines as evaluated by site-directed mutagenesis. J. Clin. Invest. 1995, 96, 1499-1505.
    • (1995) J. Clin. Invest , vol.96 , pp. 1499-1505
    • Faust, L.R.1    El Benna, J.2    Babior, B.M.3    Chanock, S.J.4
  • 73
    • 4744349398 scopus 로고    scopus 로고
    • Structure and regulation of the neutrophil respiratory burst oxidase: Comparison with nonphagocyte oxidases
    • Quinn, M.T.; Gauss, K.A. Structure and regulation of the neutrophil respiratory burst oxidase: Comparison with nonphagocyte oxidases. J. Leukoc. Biol. 2004, 76, 76760-76781.
    • (2004) J. Leukoc. Biol , vol.76 , pp. 76760-76781
    • Quinn, M.T.1    Gauss, K.A.2
  • 74
    • 36849064316 scopus 로고    scopus 로고
    • Molecular evolution of Phox-related regulatory subunits for NADPH oxidase enzymes
    • Kawahara, T.; Lambeth J.D. Molecular evolution of Phox-related regulatory subunits for NADPH oxidase enzymes. BMC Evol. Biol. 2007, 7, 178.
    • (2007) BMC Evol. Biol , vol.7 , pp. 178
    • Kawahara, T.1    Lambeth, J.D.2
  • 76
    • 50849098818 scopus 로고    scopus 로고
    • Activation of microglia with zymosan promotes excitatory amino acid release via volume-regulated anion channels: The role of NADPH oxidases
    • Harrigan, T.J.; Abdullaev, I.F.; Jourd'heuil, D.; Mongin, A.A. Activation of microglia with zymosan promotes excitatory amino acid release via volume-regulated anion channels: The role of NADPH oxidases. J. Neurochem. 2008, 106, 2449-2462.
    • (2008) J. Neurochem , vol.106 , pp. 2449-2462
    • Harrigan, T.J.1    Abdullaev, I.F.2    Jourd'heuil, D.3    Mongin, A.A.4
  • 77
    • 15944372262 scopus 로고    scopus 로고
    • Activation and assembly of the NADPH oxidase: A structural perspective
    • Groemping, Y.; Rittinger, K. Activation and assembly of the NADPH oxidase: A structural perspective. Biochem. J. 2005, 15, 401-416.
    • (2005) Biochem. J , vol.15 , pp. 401-416
    • Groemping, Y.1    Rittinger, K.2
  • 78
    • 0023937220 scopus 로고
    • Relationship of protein phosphorylation to the activation of the respiratory burst in human neutrophils. Defects in the phosphorylation of a group of closely related 48-kDa proteins in two forms of chronic granulomatous disease
    • Okamura, N.; Curnutte, J.T.; Roberts, R.L.; Babior, B.M. Relationship of protein phosphorylation to the activation of the respiratory burst in human neutrophils. Defects in the phosphorylation of a group of closely related 48-kDa proteins in two forms of chronic granulomatous disease. J. Biol. Chem. 1988, 15, 6777-6782.
    • (1988) J. Biol. Chem , vol.15 , pp. 6777-6782
    • Okamura, N.1    Curnutte, J.T.2    Roberts, R.L.3    Babior, B.M.4
  • 79
    • 26244444476 scopus 로고    scopus 로고
    • Functional analysis of Nox4 reveals unique characteristics compared to other NADPH oxidases
    • Martyn, K.D.; Frederick, L.M.; von Loehneysen, K.; Dinauer, M.C.; Knaus, U.G. Functional analysis of Nox4 reveals unique characteristics compared to other NADPH oxidases. Cell. Signal. 2006, 18, 69-82.
    • (2006) Cell. Signal , vol.18 , pp. 69-82
    • Martyn, K.D.1    Frederick, L.M.2    von Loehneysen, K.3    Dinauer, M.C.4    Knaus, U.G.5
  • 80
    • 70349316712 scopus 로고    scopus 로고
    • Nox5 and the regulation of cellular function
    • Fulton D.J. Nox5 and the regulation of cellular function. Antioxid Redox Signal. 2009, 11, 2443-2452.
    • (2009) Antioxid Redox Signal , vol.11 , pp. 2443-2452
    • Fulton, D.J.1
  • 81
    • 77954354755 scopus 로고    scopus 로고
    • Angiotensin II stimulates thick ascending limb superoxide production via protein kinase C(α)-dependent NADPH oxidase activation
    • Herrera, M.; Silva, G.B.; Garvin, J.L. Angiotensin II stimulates thick ascending limb superoxide production via protein kinase C(α)-dependent NADPH oxidase activation. J. Biol. Chem. 2010, 285, 21323-21328.
    • (2010) J. Biol. Chem , vol.285 , pp. 21323-21328
    • Herrera, M.1    Silva, G.B.2    Garvin, J.L.3
  • 83
    • 0034889593 scopus 로고    scopus 로고
    • Negative regulation of ligand-initiated Ca2+ uptake by PKC-beta II in differentiated HL60 cells
    • Korchak, H.M.; Corkey, B.E.; Yaney, G.C.; Kilpatrick, L.E. Negative regulation of ligand-initiated Ca2+ uptake by PKC-beta II in differentiated HL60 cells. Am. J. Physiol. Cell Physiol. 2001, 281, 514-523.
    • (2001) Am. J. Physiol. Cell Physiol , vol.281 , pp. 514-523
    • Korchak, H.M.1    Corkey, B.E.2    Yaney, G.C.3    Kilpatrick, L.E.4
  • 84
    • 0027526348 scopus 로고
    • Protein kinase C isotypes and signal-transduction in human neutrophils: Selective substrate specificity of calcium-dependent beta-PKC and novel calcium-independent nPKC
    • Majumdar, S.; Kane, L.H.; Rossi, M.W.; Volpp, B.D.; Nauseef, W.M.; Korchak, H.M. Protein kinase C isotypes and signal-transduction in human neutrophils: Selective substrate specificity of calcium-dependent beta-PKC and novel calcium-independent nPKC. Biochim. Biophys. Acta 1993, 16, 276-286.
    • (1993) Biochim. Biophys. Acta , vol.16 , pp. 276-286
    • Majumdar, S.1    Kane, L.H.2    Rossi, M.W.3    Volpp, B.D.4    Nauseef, W.M.5    Korchak, H.M.6
  • 85
    • 33747262660 scopus 로고    scopus 로고
    • Homocysteine stimulates phosphorylation of NADPH oxidase p47phox and p67phox subunits in monocytes via protein kinase C beta activation
    • Siow, Y.L.; Au-Yeung, K.K.; Woo, C.W.; O, K. Homocysteine stimulates phosphorylation of NADPH oxidase p47phox and p67phox subunits in monocytes via protein kinase C beta activation. Biochem. J. 2006, 15, 73-82.
    • (2006) Biochem. J , vol.15 , pp. 73-82
    • Siow, Y.L.1    Au-Yeung, K.K.2    Woo, C.W.3
  • 86
    • 0037248553 scopus 로고    scopus 로고
    • A novel assay system implicates PtdIns(3,4)P(2), PtdIns(3)P, and PKC delta in intracellular production of reactive oxygen species by the NADPH oxidase
    • Brown, G.E.; Stewart, M.Q.; Liu, H.; Ha, V.L.; Yaffe, M.B. A novel assay system implicates PtdIns(3,4)P(2), PtdIns(3)P, and PKC delta in intracellular production of reactive oxygen species by the NADPH oxidase. Mol. Cell 2003, 11, 35-47.
    • (2003) Mol. Cell , vol.11 , pp. 35-47
    • Brown, G.E.1    Stewart, M.Q.2    Liu, H.3    Ha, V.L.4    Yaffe, M.B.5
  • 87
    • 38849142607 scopus 로고    scopus 로고
    • A critical role of protein kinase C delta activation loop phosphorylation in formyl-methionyl-leucyl-phenylalanine-induced phosphorylation of p47(phox) and rapid activation of nicotinamide adenine dinucleotide phosphate oxidase
    • Cheng, N.; He, R.; Tian, J.; Dinauer, M.C.; Ye, R.D. A critical role of protein kinase C delta activation loop phosphorylation in formyl-methionyl-leucyl-phenylalanine-induced phosphorylation of p47(phox) and rapid activation of nicotinamide adenine dinucleotide phosphate oxidase. J. Immunol. 2007, 1179, 7720-7728.
    • (2007) J. Immunol , vol.1179 , pp. 7720-7728
    • Cheng, N.1    He, R.2    Tian, J.3    Dinauer, M.C.4    Ye, R.D.5
  • 89
    • 53449086013 scopus 로고    scopus 로고
    • Hypoxia activates NADPH oxidase to increase [ROS]i and [Ca2+]i through the mitochondrial ROS-PKCepsilon signaling axis in pulmonary artery smooth muscle cells
    • Rathore, R.; Zheng, Y.M.; Niu, C.F.; Liu, Q.H.; Korde, A.; Ho, Y.S.; Wang, Y.X. Hypoxia activates NADPH oxidase to increase [ROS]i and [Ca2+]i through the mitochondrial ROS-PKCepsilon signaling axis in pulmonary artery smooth muscle cells. Free Radic. Biol. Med. 2008, 1, 1223-1231.
    • (2008) Free Radic. Biol. Med , vol.1 , pp. 1223-1231
    • Rathore, R.1    Zheng, Y.M.2    Niu, C.F.3    Liu, Q.H.4    Korde, A.5    Ho, Y.S.6    Wang, Y.X.7
  • 91
    • 0035863923 scopus 로고    scopus 로고
    • Protein kinase C zeta phosphorylates a subset of selective sites of the NADPH oxidase component p47phox and participates in formyl peptide-mediated neutrophil respiratory burst
    • Dang, P.M.; Fontayne, A.; Hakim, J.; El Benna, J.; Périanin, A. Protein kinase C zeta phosphorylates a subset of selective sites of the NADPH oxidase component p47phox and participates in formyl peptide-mediated neutrophil respiratory burst. J. Immunol. 2001, 15, 1206-1213.
    • (2001) J. Immunol , vol.15 , pp. 1206-1213
    • Dang, P.M.1    Fontayne, A.2    Hakim, J.3    El Benna, J.4    Périanin, A.5
  • 93
    • 84864124443 scopus 로고    scopus 로고
    • Small interfering RNA-mediated knockdown of protein kinase C zeta attenuates domoic acid-induced cognitive deficits in mice
    • doi:10.1093/toxsci/kfs124
    • Wu, D.M.; Lu, J.; Zheng, Y.L.; Zhang, Y.Q.; Hu, B.; Cheng, W.; Zhang, Z.F.; Li, M.Q. Small interfering RNA-mediated knockdown of protein kinase C zeta attenuates domoic acid-induced cognitive deficits in mice. Toxicol. Sci. 2012, doi:10.1093/toxsci/kfs124.
    • (2012) Toxicol. Sci
    • Wu, D.M.1    Lu, J.2    Zheng, Y.L.3    Zhang, Y.Q.4    Hu, B.5    Cheng, W.6    Zhang, Z.F.7    Li, M.Q.8
  • 94
    • 79251550763 scopus 로고    scopus 로고
    • Lipopolysaccharide-induced cytokine expression in alveolar epithelial cells: Role of PKCζ-mediated p47phox phosphorylation
    • Leverence, J.T.; Medhora, M.; Konduri, G.G.; Sampath, V. Lipopolysaccharide-induced cytokine expression in alveolar epithelial cells: Role of PKCζ-mediated p47phox phosphorylation. Chem. Biol. Interact. 2011, 15, 72-81.
    • (2011) Chem. Biol. Interact , vol.15 , pp. 72-81
    • Leverence, J.T.1    Medhora, M.2    Konduri, G.G.3    Sampath, V.4
  • 95
    • 0029983262 scopus 로고    scopus 로고
    • Phosphorylation of the respiratory burst oxidase subunit p47phox as determined by two-dimensional phosphopeptide mapping. Phosphorylation by protein kinase C, protein kinase A, and a mitogen-activated protein kinase
    • El Benna, J.; Faust, R.P.; Johnson, J.L.; Babior, B.M. Phosphorylation of the respiratory burst oxidase subunit p47phox as determined by two-dimensional phosphopeptide mapping. Phosphorylation by protein kinase C, protein kinase A, and a mitogen-activated protein kinase. J. Biol. Chem. 1996, 15, 6374-6378.
    • (1996) J. Biol. Chem , vol.15 , pp. 6374-6378
    • El Benna, J.1    Faust, R.P.2    Johnson, J.L.3    Babior, B.M.4
  • 96
    • 0023735432 scopus 로고
    • The 47-kDa protein involved in the NADPH:O2 oxidoreductase activity of human neutrophils is phosphorylated by cyclic AMP-dependent protein kinase without induction of a respiratory burst
    • Kramer, I.M.; van der Bend, R.L.; Verhoeven, A.J.; Roos, D. The 47-kDa protein involved in the NADPH:O2 oxidoreductase activity of human neutrophils is phosphorylated by cyclic AMP-dependent protein kinase without induction of a respiratory burst. Biochim. Biophys. Acta 1988, 16, 189-196.
    • (1988) Biochim. Biophys. Acta , vol.16 , pp. 189-196
    • Kramer, I.M.1    van der Bend, R.L.2    Verhoeven, A.J.3    Roos, D.4
  • 97
    • 0030588188 scopus 로고    scopus 로고
    • Activation of p38 in stimulated human neutrophils: Phosphorylation of the oxidase component p47phox by p38 and ERK but not by JNK
    • El Benna, J.; Han, J.; Park, J.W.; Schmid, E.; Ulevitch, R.J.; Babior, B.M. Activation of p38 in stimulated human neutrophils: Phosphorylation of the oxidase component p47phox by p38 and ERK but not by JNK. Arch. Biochem. Biophys. 1996, 15, 395-400.
    • (1996) Arch. Biochem. Biophys , vol.15 , pp. 395-400
    • El Benna, J.1    Han, J.2    Park, J.W.3    Schmid, E.4    Ulevitch, R.J.5    Babior, B.M.6
  • 98
    • 0034327804 scopus 로고    scopus 로고
    • The mitogen-activated protein kinase extracellular signal-regulated kinase 1/2 pathway is involved in formyl-methionyl-leucyl-phenylalanine-induced p47phox phosphorylation in human neutrophils
    • Dewas, C.; Fay, M.; Gougerot-Pocidalo, M.A.; El-Benna, J. The mitogen-activated protein kinase extracellular signal-regulated kinase 1/2 pathway is involved in formyl-methionyl-leucyl-phenylalanine-induced p47phox phosphorylation in human neutrophils. J. Immunol. 2000, 165, 5238-5244.
    • (2000) J. Immunol , vol.165 , pp. 5238-5244
    • Dewas, C.1    Fay, M.2    Gougerot-Pocidalo, M.A.3    El-Benna, J.4
  • 99
    • 0035884196 scopus 로고    scopus 로고
    • Phosphorylation of the leucocyte NADPH oxidase subunit p47(phox) by casein kinase 2: Conformation-dependent phosphorylation and modulation of oxidase activity
    • Park, H.S.; Lee, S.M.; Lee, J.H.; Kim, Y.S.; Bae, Y.S.; Park, J.W. Phosphorylation of the leucocyte NADPH oxidase subunit p47(phox) by casein kinase 2: Conformation-dependent phosphorylation and modulation of oxidase activity. Biochem. J. 2001, 15, 783-790.
    • (2001) Biochem. J , vol.15 , pp. 783-790
    • Park, H.S.1    Lee, S.M.2    Lee, J.H.3    Kim, Y.S.4    Bae, Y.S.5    Park, J.W.6
  • 100
    • 0037883614 scopus 로고    scopus 로고
    • Akt phosphorylates p47phox and mediates respiratory burst activity in human neutrophils
    • Chen, Q.; Powell, D.W.; Rane, M.J.; Singh, S.; Butt, W.; Klein, J.B.; McLeish, K.R. Akt phosphorylates p47phox and mediates respiratory burst activity in human neutrophils. J. Immunol. 2003, 15, 5302-5308.
    • (2003) J. Immunol , vol.15 , pp. 5302-5308
    • Chen, Q.1    Powell, D.W.2    Rane, M.J.3    Singh, S.4    Butt, W.5    Klein, J.B.6    McLeish, K.R.7
  • 102
    • 28444488929 scopus 로고    scopus 로고
    • P21-activated kinase (Pak) regulates NADPH oxidase activation in human neutrophils
    • Martyn, K.D.; Kim, M.J.; Quinn, M.T.; Dinauer, M.C.; Knaus, U.G. p21-activated kinase (Pak) regulates NADPH oxidase activation in human neutrophils. Blood 2005, 1, 3962-3969.
    • (2005) Blood , vol.1 , pp. 3962-3969
    • Martyn, K.D.1    Kim, M.J.2    Quinn, M.T.3    Dinauer, M.C.4    Knaus, U.G.5
  • 103
    • 0030950647 scopus 로고    scopus 로고
    • Phosphatidic acid-mediated phosphorylation of the NADPH oxidase component p47-phox. Evidence that phosphatidic acid may activate a novel protein kinase
    • Waite, K.A.; Wallin, R.; Qualliotine-Mann, D.; McPhail, L.C. Phosphatidic acid-mediated phosphorylation of the NADPH oxidase component p47-phox. Evidence that phosphatidic acid may activate a novel protein kinase. J. Biol. Chem. 1997, 13, 15569-15578.
    • (1997) J. Biol. Chem , vol.13 , pp. 15569-15578
    • Waite, K.A.1    Wallin, R.2    Qualliotine-Mann, D.3    McPhail, L.C.4
  • 104
    • 20144378137 scopus 로고    scopus 로고
    • Src-mediated tyrosine phosphorylation of p47phox in hyperoxia-induced activation of NADPH oxidase and generation of reactive oxygen species in lung endothelial cells
    • Chowdhury, A.K.; Watkins, T.; Parinandi, N.L.; Saatian, B.; Kleinberg, M.E.; Usatyuk, P.V.; Natarajan, V. Src-mediated tyrosine phosphorylation of p47phox in hyperoxia-induced activation of NADPH oxidase and generation of reactive oxygen species in lung endothelial cells. J. Biol. Chem. 2005, 27, 20700-20711.
    • (2005) J. Biol. Chem , vol.27 , pp. 20700-20711
    • Chowdhury, A.K.1    Watkins, T.2    Parinandi, N.L.3    Saatian, B.4    Kleinberg, M.E.5    Usatyuk, P.V.6    Natarajan, V.7
  • 105
    • 62649089147 scopus 로고    scopus 로고
    • The inflammatory response in the MPTP model of Parkinson's disease is mediated by brain angiotensin: Relevance to progression of the disease
    • Joglar, B.; Rodriguez-Pallares, J.; Rodriguez-Perez, A.I.; Rey, P.; Guerra, M.J.; Labandeira-Garcia, J.L. The inflammatory response in the MPTP model of Parkinson's disease is mediated by brain angiotensin: Relevance to progression of the disease. J. Neurochem. 2009, 109, 656-669.
    • (2009) J. Neurochem , vol.109 , pp. 656-669
    • Joglar, B.1    Rodriguez-Pallares, J.2    Rodriguez-Perez, A.I.3    Rey, P.4    Guerra, M.J.5    Labandeira-Garcia, J.L.6
  • 106
    • 34249655705 scopus 로고    scopus 로고
    • Angiotensin II increases expression of alpha1C subunit of L-type calcium channel through a reactive oxygen species and cAMP response element-binding protein-dependent pathway in HL-1 myocytes
    • Tsai, C.T.; Wang, D.L.; Chen, W.P.; Hwang, J.J.; Hsieh, C.S.; Hsu, K.L.; Tseng, C.D.; Lai, L.P.; Tseng, Y.Z.; Chiang, F.T. et al. Angiotensin II increases expression of alpha1C subunit of L-type calcium channel through a reactive oxygen species and cAMP response element-binding protein-dependent pathway in HL-1 myocytes. Circ. Res. 2007, 25, 1476-1485.
    • (2007) Circ. Res , vol.25 , pp. 1476-1485
    • Tsai, C.T.1    Wang, D.L.2    Chen, W.P.3    Hwang, J.J.4    Hsieh, C.S.5    Hsu, K.L.6    Tseng, C.D.7    Lai, L.P.8    Tseng, Y.Z.9    Chiang, F.T.10
  • 107
    • 0033765672 scopus 로고    scopus 로고
    • High glucose level and free fatty acid stimulate reactive oxygen species production through protein kinase C-Dependent activation of NAD(P)H oxidase in cultured vascular cells
    • Inoguchi, T.; Li, P.; Umeda, F.; Yu, H.Y.; Kakimoto, M.; Imamura, M.; Aoki, T.; Etoh, T.; Hashimoto, T.; Naruse, M. et al. High glucose level and free fatty acid stimulate reactive oxygen species production through protein kinase C-Dependent activation of NAD(P)H oxidase in cultured vascular cells. Diabetes 2000, 49, 1939-1945.
    • (2000) Diabetes , vol.49 , pp. 1939-1945
    • Inoguchi, T.1    Li, P.2    Umeda, F.3    Yu, H.Y.4    Kakimoto, M.5    Imamura, M.6    Aoki, T.7    Etoh, T.8    Hashimoto, T.9    Naruse, M.10
  • 108
    • 60649120010 scopus 로고    scopus 로고
    • C-reactive protein stimulates superoxide anion release and tissue factor activity in vivo
    • Devaraj, S.; Dasu, M.R.; Singh, U.; Rao, L.V.; Jialal, I. C-reactive protein stimulates superoxide anion release and tissue factor activity in vivo. Atherosclerosis 2009, 203, 67-74.
    • (2009) Atherosclerosis , vol.203 , pp. 67-74
    • Devaraj, S.1    Dasu, M.R.2    Singh, U.3    Rao, L.V.4    Jialal, I.5
  • 111
    • 34247855829 scopus 로고    scopus 로고
    • Effect of endothelin on sodium/hydrogen exchanger activity of human monocytes and atherosclerosis-related functions
    • Koliakos, G.; Befani, C.; Paletas, K.; Kaloyianni, M. Effect of endothelin on sodium/hydrogen exchanger activity of human monocytes and atherosclerosis-related functions. Ann. N. Y. Acad. Sci. 2007, 1095, 274-291.
    • (2007) Ann. N. Y. Acad. Sci , vol.1095 , pp. 274-291
    • Koliakos, G.1    Befani, C.2    Paletas, K.3    Kaloyianni, M.4
  • 113
    • 74949119895 scopus 로고    scopus 로고
    • Protein kinase C-dependent NAD(P)H oxidase activation induced by type 1 diabetes in renal medullary thick ascending limb
    • Yang, J.; Lane, P.H.; Pollock, J.S.; Carmines, P.K. Protein kinase C-dependent NAD(P)H oxidase activation induced by type 1 diabetes in renal medullary thick ascending limb. Hypertension 2010, 55, 468-473.
    • (2010) Hypertension , vol.55 , pp. 468-473
    • Yang, J.1    Lane, P.H.2    Pollock, J.S.3    Carmines, P.K.4
  • 116
    • 28544448737 scopus 로고    scopus 로고
    • Reactive oxygen species amplify glucose signalling in renal cells cultured under high glucose and in diabetic kidney
    • Ha, H.; Lee, H.B. Reactive oxygen species amplify glucose signalling in renal cells cultured under high glucose and in diabetic kidney. Nephrology (Carlton) 2005, 10, S7-S10.
    • (2005) Nephrology (Carlton) , vol.10
    • Ha, H.1    Lee, H.B.2
  • 117
    • 79955015016 scopus 로고    scopus 로고
    • Tumor-induced endothelial cell apoptosis: Roles of NAD(P)H oxidase-derived reactive oxygen species
    • Lin, R.Z.; Wang, T.P.; Hung, R.J.; Chuang, Y.J.; Chien, C.C.; Chang, H.Y. Tumor-induced endothelial cell apoptosis: Roles of NAD(P)H oxidase-derived reactive oxygen species. J. Cell. Physiol. 2011, 226, 1750-1762.
    • (2011) J. Cell. Physiol , vol.226 , pp. 1750-1762
    • Lin, R.Z.1    Wang, T.P.2    Hung, R.J.3    Chuang, Y.J.4    Chien, C.C.5    Chang, H.Y.6
  • 118
    • 60549097414 scopus 로고    scopus 로고
    • Advanced oxidation protein products induce mesangial cell perturbation through PKC-dependent activation of NADPH oxidase
    • Wei, X.F.; Zhou, Q.G.; Hou, F.F.; Liu, B.Y.; Liang, M. Advanced oxidation protein products induce mesangial cell perturbation through PKC-dependent activation of NADPH oxidase. Am. J. Physiol. Ren. Physiol. 2009, 296, 427-437.
    • (2009) Am. J. Physiol. Ren. Physiol , vol.296 , pp. 427-437
    • Wei, X.F.1    Zhou, Q.G.2    Hou, F.F.3    Liu, B.Y.4    Liang, M.5
  • 119
    • 0034725652 scopus 로고    scopus 로고
    • Reactive oxygen species as mediators of angiotensin II signaling
    • Griendling, K.K.; Ushio-Fukai, M. Reactive oxygen species as mediators of angiotensin II signaling. Regul. Pept. 2000, 28, 21-27.
    • (2000) Regul. Pept , vol.28 , pp. 21-27
    • Griendling, K.K.1    Ushio-Fukai, M.2
  • 120
    • 0037076798 scopus 로고    scopus 로고
    • Expression of a functionally active gp91phox-containing neutrophil-type NAD(P)H oxidase in smooth muscle cells from human resistance arteries: Regulation by angiotensin II
    • Touyz, R.M.; Chen, X.; Tabet, F.; Yao, G.; He, G.; Quinn, M.T.; Pagano, P.J.; Schiffrin, E.L. Expression of a functionally active gp91phox-containing neutrophil-type NAD(P)H oxidase in smooth muscle cells from human resistance arteries: Regulation by angiotensin II. Circ. Res. 2002, 90, 1205-1213.
    • (2002) Circ. Res , vol.90 , pp. 1205-1213
    • Touyz, R.M.1    Chen, X.2    Tabet, F.3    Yao, G.4    He, G.5    Quinn, M.T.6    Pagano, P.J.7    Schiffrin, E.L.8
  • 122
    • 79960012285 scopus 로고    scopus 로고
    • Activation of Src-ATF1 pathway is involved in upregulation of Nox1, a catalytic subunit of NADPH oxidase, by aldosterone
    • Shi, G.; Fu, Y.; Jiang, W.; Yin, A.; Feng, M.; Wu, Y.; Kawai, Y.; Miyamori, I.; Fan, C.; Activation of Src-ATF1 pathway is involved in upregulation of Nox1, a catalytic subunit of NADPH oxidase, by aldosterone. Endocr. J. 2011, 58, 491-499.
    • (2011) Endocr. J , vol.58 , pp. 491-499
    • Shi, G.1    Fu, Y.2    Jiang, W.3    Yin, A.4    Feng, M.5    Wu, Y.6    Kawai, Y.7    Miyamori, I.8    Fan, C.9
  • 123
    • 0035844030 scopus 로고    scopus 로고
    • Novel gp91(phox) homologues in vascular smooth muscle cells: Nox1 mediates angiotensin II-induced superoxide formation and redox-sensitive signaling pathways
    • Lassègue, B.; Sorescu, D.; Szöcs, K.; Yin, Q.; Akers, M.; Zhang, Y.; Grant, S.L.; Lambeth, J.D.; Griendling, K.K. Novel gp91(phox) homologues in vascular smooth muscle cells: Nox1 mediates angiotensin II-induced superoxide formation and redox-sensitive signaling pathways. Circ. Res. 2001, 88, 888-894.
    • (2001) Circ. Res , vol.88 , pp. 888-894
    • Lassègue, B.1    Sorescu, D.2    Szöcs, K.3    Yin, Q.4    Akers, M.5    Zhang, Y.6    Grant, S.L.7    Lambeth, J.D.8    Griendling, K.K.9
  • 124
    • 0035584538 scopus 로고    scopus 로고
    • Upregulation of the vascular NAD(P)H-oxidase isoforms Nox1 and Nox4 by the renin-angiotensin system in vitro and in vivo
    • Wingler, K.; Wünsch, S.; Kreutz, R.; Rothermund, L.; Paul, M.; Schmidt, H.H. Upregulation of the vascular NAD(P)H-oxidase isoforms Nox1 and Nox4 by the renin-angiotensin system in vitro and in vivo. Free Radic. Biol. Med. 2001, 31, 1456-1464.
    • (2001) Free Radic. Biol. Med , vol.31 , pp. 1456-1464
    • Wingler, K.1    Wünsch, S.2    Kreutz, R.3    Rothermund, L.4    Paul, M.5    Schmidt, H.H.6
  • 125
    • 77950678652 scopus 로고    scopus 로고
    • Protein kinase C-delta is involved in induction of Nox1 gene expression by aldosterone in rat vascular smooth muscle cells
    • Wei, H.; Mi, X.; Ji, L.; Yang, L.; Xia, Q.; Wei, Y.; Miyamori, I.; Fan, C. Protein kinase C-delta is involved in induction of Nox1 gene expression by aldosterone in rat vascular smooth muscle cells. Biochemistry (Mosc) 2010, 75, 304-309.
    • (2010) Biochemistry (Mosc) , vol.75 , pp. 304-309
    • Wei, H.1    Mi, X.2    Ji, L.3    Yang, L.4    Xia, Q.5    Wei, Y.6    Miyamori, I.7    Fan, C.8
  • 126
    • 25844507931 scopus 로고    scopus 로고
    • PKCdelta mediates up-regulation of Nox1, a catalytic subunit of NADPH oxidase, via transactivation of the EGF receptor: Possible involvement of PKCdelta in vascular hypertrophy
    • Fan, C.Y.; Katsuyama, M.; Yabe-Nishimura, C. PKCdelta mediates up-regulation of Nox1, a catalytic subunit of NADPH oxidase, via transactivation of the EGF receptor: Possible involvement of PKCdelta in vascular hypertrophy. Biochem. J. 2005, 390, 761-767.
    • (2005) Biochem. J , vol.390 , pp. 761-767
    • Fan, C.Y.1    Katsuyama, M.2    Yabe-Nishimura, C.3
  • 127
    • 63049123598 scopus 로고    scopus 로고
    • Insulin-induced NADPH oxidase activation promotes proliferation and matrix metalloproteinase activation in monocytes/macrophages
    • San José, G.; Bidegain, J.; Robador, P.A.; Díez, J.; Fortuño, A.; Zalba, G. Insulin-induced NADPH oxidase activation promotes proliferation and matrix metalloproteinase activation in monocytes/macrophages. Free Radic. Biol. Med. 2009, 46, 1058-1067.
    • (2009) Free Radic. Biol. Med , vol.46 , pp. 1058-1067
    • San, J.G.1    Bidegain, J.2    Robador, P.A.3    Díez, J.4    Fortuño, A.5    Zalba, G.6
  • 129
    • 1342304048 scopus 로고    scopus 로고
    • The NAD(P)H oxidase homolog Nox4 modulates insulin-stimulated generation of H2O2 and plays an integral role in insulin signal transduction
    • Mahadev, K.; Motoshima, H.; Wu, X.; Ruddy, J.M.; Arnold, R.S.; Cheng, G.; Lambeth, J.D.; Goldstein, B.J. The NAD(P)H oxidase homolog Nox4 modulates insulin-stimulated generation of H2O2 and plays an integral role in insulin signal transduction. Mol. Cell. Biol. 2004, 24, 1844-1854.
    • (2004) Mol. Cell. Biol , vol.24 , pp. 1844-1854
    • Mahadev, K.1    Motoshima, H.2    Wu, X.3    Ruddy, J.M.4    Arnold, R.S.5    Cheng, G.6    Lambeth, J.D.7    Goldstein, B.J.8
  • 131
    • 17644378052 scopus 로고    scopus 로고
    • H2O2 activates Nox4 through PLA2-dependent arachidonic acid production in adult cardiac fibroblasts
    • Colston, J.T.; de la Rosa, S.D.; Strader, J.R.; Anderson, M.A.; Freeman, G.L. H2O2 activates Nox4 through PLA2-dependent arachidonic acid production in adult cardiac fibroblasts. FEBS Lett. 2005, 579, 2533-2540.
    • (2005) FEBS Lett , vol.579 , pp. 2533-2540
    • Colston, J.T.1    de la Rosa, S.D.2    Strader, J.R.3    Anderson, M.A.4    Freeman, G.L.5
  • 132
    • 3142736370 scopus 로고    scopus 로고
    • Angiotensin II-induced ERK1/ERK2 activation and protein synthesis are redox-dependent in glomerular mesangial cells
    • Gorin, Y.; Ricono, J.M.; Wagner, B.; Kim, N.H.; Bhandari, B.; Choudhury, G.G.; Abboud, H.E. Angiotensin II-induced ERK1/ERK2 activation and protein synthesis are redox-dependent in glomerular mesangial cells. Biochem. J. 2004, 381, 231-239.
    • (2004) Biochem. J , vol.381 , pp. 231-239
    • Gorin, Y.1    Ricono, J.M.2    Wagner, B.3    Kim, N.H.4    Bhandari, B.5    Choudhury, G.G.6    Abboud, H.E.7
  • 134
    • 84859620774 scopus 로고    scopus 로고
    • Angiotensin II plays a critical role in alcohol-induced cardiac nitrative damage, cell death, remodeling, and cardiomyopathy in a protein kinase C/nicotinamide adenine dinucleotide phosphate oxidase-dependent manner
    • Tan, Y.; Li, X.; Prabhu, S.D.; Brittian, K.R.; Chen, Q.; Yin, X.; McClain, C.J.; Zhou, Z.; Cai, L. Angiotensin II plays a critical role in alcohol-induced cardiac nitrative damage, cell death, remodeling, and cardiomyopathy in a protein kinase C/nicotinamide adenine dinucleotide phosphate oxidase-dependent manner. J. Am. Coll. Cardiol. 2012, 59, 1477-1486.
    • (2012) J. Am. Coll. Cardiol , vol.59 , pp. 1477-1486
    • Tan, Y.1    Li, X.2    Prabhu, S.D.3    Brittian, K.R.4    Chen, Q.5    Yin, X.6    McClain, C.J.7    Zhou, Z.8    Cai, L.9
  • 135
    • 84863238020 scopus 로고    scopus 로고
    • Angiotensin II stimulates epithelial sodium channels in the cortical collecting duct of the rat kidney
    • Sun, P.; Yue, P.; Wang, W.H. Angiotensin II stimulates epithelial sodium channels in the cortical collecting duct of the rat kidney. Am. J. Physiol. Ren. Physiol. 2012, 302, 679-687.
    • (2012) Am. J. Physiol. Ren. Physiol , vol.302 , pp. 679-687
    • Sun, P.1    Yue, P.2    Wang, W.H.3
  • 136
    • 33747427339 scopus 로고    scopus 로고
    • Superoxide stimulates NaCl absorption in the thick ascending limb via activation of protein kinase C
    • Silva, G.B.; Ortiz, P.A.; Hong, N.J.; Garvin, J.L. Superoxide stimulates NaCl absorption in the thick ascending limb via activation of protein kinase C. Hypertension 2006, 48, 467-472.
    • (2006) Hypertension , vol.48 , pp. 467-472
    • Silva, G.B.1    Ortiz, P.A.2    Hong, N.J.3    Garvin, J.L.4
  • 137
    • 79960062769 scopus 로고    scopus 로고
    • Fibrotic response induced by angiotensin-II requires NAD(P)H oxidase-induced reactive oxygen species (ROS) in skeletal muscle cells
    • Cabello-Verrugio, C.; Acuña, M.J.; Morales, M.G.; Becerra, A.; Simon, F.; Brandan, E. Fibrotic response induced by angiotensin-II requires NAD(P)H oxidase-induced reactive oxygen species (ROS) in skeletal muscle cells. Biochem. Biophys. Res. Commun. 2011, 8, 665-670.
    • (2011) Biochem. Biophys. Res. Commun , vol.8 , pp. 665-670
    • Cabello-Verrugio, C.1    Acuña, M.J.2    Morales, M.G.3    Becerra, A.4    Simon, F.5    Brandan, E.6
  • 139
    • 0026612790 scopus 로고
    • The role of angiotensin, AT1 and AT2 receptors in the pressor, drinking and vasopressin responses to central angiotensin
    • Hogarty, D.C.; Speakman, E.A.; Puig, V.; Phillips, M.I. The role of angiotensin, AT1 and AT2 receptors in the pressor, drinking and vasopressin responses to central angiotensin. Brain Res. 1992, 586, 289-294.
    • (1992) Brain Res , vol.586 , pp. 289-294
    • Hogarty, D.C.1    Speakman, E.A.2    Puig, V.3    Phillips, M.I.4
  • 140
    • 0032583132 scopus 로고    scopus 로고
    • Angiotensin II in central nervous system physiology
    • Phillips, M.I.; Sumners, C. Angiotensin II in central nervous system physiology. Regul. Pept. 1998, 78, 1-11.
    • (1998) Regul. Pept , vol.78 , pp. 1-11
    • Phillips, M.I.1    Sumners, C.2
  • 142
    • 80051933965 scopus 로고    scopus 로고
    • Dual function of protein kinase C (PKC) in 12-O-tetradecanoylphorbol-13-acetate (TPA)-induced manganese superoxide dismutase (MnSOD) expression: Activation of CREB and FOXO3a by PKC-alpha phosphorylation and by PKC-mediated inactivation of Akt, respectively
    • Chung, Y.W.; Kim, H.K.; Kim, I.Y.; Yim, M.B.; Chock, P.B. Dual function of protein kinase C (PKC) in 12-O-tetradecanoylphorbol-13-acetate (TPA)-induced manganese superoxide dismutase (MnSOD) expression: Activation of CREB and FOXO3a by PKC-alpha phosphorylation and by PKC-mediated inactivation of Akt, respectively. J. Biol. Chem. 2011, 286, 29681-29690.
    • (2011) J. Biol. Chem , vol.286 , pp. 29681-29690
    • Chung, Y.W.1    Kim, H.K.2    Kim, I.Y.3    Yim, M.B.4    Chock, P.B.5
  • 143
    • 78651282774 scopus 로고    scopus 로고
    • Extracellular-superoxide dismutase expression during monocytic differentiation of U937 cells
    • Kamiya, T.; Makino, J.; Hara, H.; Inagaki, N.; Adachi, T. Extracellular-superoxide dismutase expression during monocytic differentiation of U937 cells. J. Cell. Biochem. 2011, 112, 244-255.
    • (2011) J. Cell. Biochem , vol.112 , pp. 244-255
    • Kamiya, T.1    Makino, J.2    Hara, H.3    Inagaki, N.4    Adachi, T.5
  • 144
    • 84862811283 scopus 로고    scopus 로고
    • Inhibition of protein kinase C β(2) prevents tumor necrosis factor-α-induced apoptosis and oxidative stress in endothelial cells: The role of NADPH oxidase subunits
    • Deng, B.; Xie, S.; Wang, J.; Xia, Z.; Nie, R. Inhibition of protein kinase C β(2) prevents tumor necrosis factor-α-induced apoptosis and oxidative stress in endothelial cells: The role of NADPH oxidase subunits. J. Vasc. Res. 2012, 49, 144-159.
    • (2012) J. Vasc. Res , vol.49 , pp. 144-159
    • Deng, B.1    Xie, S.2    Wang, J.3    Xia, Z.4    Nie, R.5
  • 145
    • 79955060332 scopus 로고    scopus 로고
    • Molecular regulation of NADPH oxidase 5 via the MAPK pathway
    • Pandey, D.; Fulton, D.J. Molecular regulation of NADPH oxidase 5 via the MAPK pathway. Am. J. Physiol. Heart Circ. Physiol. 2011, 300, 1336-1344.
    • (2011) Am. J. Physiol. Heart Circ. Physiol , vol.300 , pp. 1336-1344
    • Pandey, D.1    Fulton, D.J.2
  • 147
    • 33847697219 scopus 로고    scopus 로고
    • Novel mechanism of activation of NADPH oxidase 5. Calcium sensitization via phosphorylation
    • Jagnandan, D.; Church, J.E.; Banfi, B.; Stuehr, D.J.; Marrero, M.B.; Fulton, D.J. Novel mechanism of activation of NADPH oxidase 5. Calcium sensitization via phosphorylation. J. Biol. Chem. 2007, 282, 6494-6507.
    • (2007) J. Biol. Chem , vol.282 , pp. 6494-6507
    • Jagnandan, D.1    Church, J.E.2    Banfi, B.3    Stuehr, D.J.4    Marrero, M.B.5    Fulton, D.J.6
  • 149
    • 0030963249 scopus 로고    scopus 로고
    • Activation of the leukocyte NADPH oxidase subunit p47phox by protein kinase C. A phosphorylation-dependent change in the conformation of the C-terminal end of p47phox
    • Park, J.W.; Babior, B.M. Activation of the leukocyte NADPH oxidase subunit p47phox by protein kinase C. A phosphorylation-dependent change in the conformation of the C-terminal end of p47phox. Biochemistry 1997, 36, 7474-7480.
    • (1997) Biochemistry , vol.36 , pp. 7474-7480
    • Park, J.W.1    Babior, B.M.2
  • 150
    • 0027163225 scopus 로고
    • Activation of neutrophil leukocytes: Chemoattractant receptors and respiratory burst
    • Baggiolini, M.; Boulay, F.; Badwey, J.A.; Curnutte, J.T. Activation of neutrophil leukocytes: Chemoattractant receptors and respiratory burst. FASEB J. 1993, 7, 1004-1010.
    • (1993) FASEB J , vol.7 , pp. 1004-1010
    • Baggiolini, M.1    Boulay, F.2    Badwey, J.A.3    Curnutte, J.T.4
  • 152
    • 0026040577 scopus 로고
    • The polyphosphoinositide cycle exists in the nuclei of Swiss 3T3 cells under the control of a receptor (for IGF-I) in the plasma membrane, and stimulation of the cycle increases nuclear diacylglycerol and apparently induces translocation of protein kinase C to the nucleus
    • Divecha, N.; Banfić, H.; Irvine, R.F. The polyphosphoinositide cycle exists in the nuclei of Swiss 3T3 cells under the control of a receptor (for IGF-I) in the plasma membrane, and stimulation of the cycle increases nuclear diacylglycerol and apparently induces translocation of protein kinase C to the nucleus. EMBO J. 1991, 10, 3207-3214.
    • (1991) EMBO J , vol.10 , pp. 3207-3214
    • Divecha, N.1    Banfić, H.2    Irvine, R.F.3
  • 153
    • 0032491522 scopus 로고    scopus 로고
    • Nuclear diacylglycerol produced by phosphoinositide-specific phospholipase C is responsible for nuclear translocation of protein kinase C-alpha
    • Neri, L.M.; Borgatti, P.; Capitani, S.; Martelli, A.M. Nuclear diacylglycerol produced by phosphoinositide-specific phospholipase C is responsible for nuclear translocation of protein kinase C-alpha. J. Biol. Chem. 1998, 273, 29738-29744.
    • (1998) J. Biol. Chem , vol.273 , pp. 29738-29744
    • Neri, L.M.1    Borgatti, P.2    Capitani, S.3    Martelli, A.M.4
  • 154
    • 0030722721 scopus 로고    scopus 로고
    • A role for nuclear phosphatidylinositol-specific phospholipase C in the G2/M phase transition
    • Sun, B.; Murray, N.R.; Fields, A.P. A role for nuclear phosphatidylinositol-specific phospholipase C in the G2/M phase transition. J. Biol. Chem. 1997, 272, 26313-26317.
    • (1997) J. Biol. Chem , vol.272 , pp. 26313-26317
    • Sun, B.1    Murray, N.R.2    Fields, A.P.3
  • 155
    • 0036500525 scopus 로고    scopus 로고
    • Generation of diacylglycerol molecular species through the cell cycle: A role for 1-stearoyl, 2-arachidonyl glycerol in the activation of nuclear protein kinase C-betaII at G2/M
    • Deacon, E.M.; Pettitt, T.R.; Webb, P.; Cross, T.; Chahal, H.; Wakelam, M.J.; Lord, J.M. Generation of diacylglycerol molecular species through the cell cycle: A role for 1-stearoyl, 2-arachidonyl glycerol in the activation of nuclear protein kinase C-betaII at G2/M. J. Cell. Sci. 2002, 115, 983-989.
    • (2002) J. Cell. Sci , vol.115 , pp. 983-989
    • Deacon, E.M.1    Pettitt, T.R.2    Webb, P.3    Cross, T.4    Chahal, H.5    Wakelam, M.J.6    Lord, J.M.7
  • 156
    • 0037057801 scopus 로고    scopus 로고
    • The nuclear phosphoinositide 3-kinase/AKT pathway: A new second messenger system
    • Neri, L.M.; Borgatti, P.; Capitani, S.; Martelli, A.M. The nuclear phosphoinositide 3-kinase/AKT pathway: A new second messenger system. Biochim. Biophys. Acta 2002, 1584, 73-80.
    • (2002) Biochim. Biophys. Acta , vol.1584 , pp. 73-80
    • Neri, L.M.1    Borgatti, P.2    Capitani, S.3    Martelli, A.M.4
  • 157
    • 0032797276 scopus 로고    scopus 로고
    • Increase in nuclear phosphatidylinositol 3-kinase activity and phosphatidylinositol (3,4,5) trisphosphate synthesis precede PKC-zeta translocation to the nucleus of NGF-treated PC12 cells
    • Neri, L.M.; Martelli, A.M.; Borgatti, P.; Colamussi, M.L.; Marchisio, M.; Capitani, S. Increase in nuclear phosphatidylinositol 3-kinase activity and phosphatidylinositol (3,4,5) trisphosphate synthesis precede PKC-zeta translocation to the nucleus of NGF-treated PC12 cells. FASEB J. 1999, 13, 2299-2310.
    • (1999) FASEB J , vol.13 , pp. 2299-2310
    • Neri, L.M.1    Martelli, A.M.2    Borgatti, P.3    Colamussi, M.L.4    Marchisio, M.5    Capitani, S.6
  • 158
    • 0030758084 scopus 로고    scopus 로고
    • Transport of protein kinase C isoforms to the nucleus of PC12 cells by nerve growth factor: Association of atypical zeta-PKC with the nuclear matrix
    • Wooten, M.W.; Zhou, G.; Wooten, M.C.; Seibenhener, M.L. Transport of protein kinase C isoforms to the nucleus of PC12 cells by nerve growth factor: Association of atypical zeta-PKC with the nuclear matrix. J. Neurosci. Res. 1997, 49, 393-403.
    • (1997) J. Neurosci. Res , vol.49 , pp. 393-403
    • Wooten, M.W.1    Zhou, G.2    Wooten, M.C.3    Seibenhener, M.L.4
  • 159
    • 0037070603 scopus 로고    scopus 로고
    • Involvement of phosphatidylinositol 3-kinase in nuclear translocation of protein kinase C zeta induced by C2-ceramide in rat hepatocytes
    • Calcerrada, M.C.; Miguel, B.G.; Martín, L.; Catalán, R.E.; Martínez, A.M. Involvement of phosphatidylinositol 3-kinase in nuclear translocation of protein kinase C zeta induced by C2-ceramide in rat hepatocytes. FEBS Lett. 2002, 514, 361-365.
    • (2002) FEBS Lett , vol.514 , pp. 361-365
    • Calcerrada, M.C.1    Miguel, B.G.2    Martín, L.3    Catalán, R.E.4    Martínez, A.M.5
  • 161
    • 0033989653 scopus 로고    scopus 로고
    • The role of protein kinase C in the regulation of cell growth and in signalling to the cell nucleus
    • Buchner, K. The role of protein kinase C in the regulation of cell growth and in signalling to the cell nucleus. J. Cancer Res. Clin. Oncol. 2000, 126, 1-11.
    • (2000) J. Cancer Res. Clin. Oncol , vol.126 , pp. 1-11
    • Buchner, K.1
  • 162
    • 33749047437 scopus 로고    scopus 로고
    • Localizing NADPH oxidase-derived ROS
    • Ushio-Fukai, M. Localizing NADPH oxidase-derived ROS. Sci. STKE 2006, 2006, re8.
    • (2006) Sci. STKE 2006
    • Ushio-Fukai, M.1
  • 163
    • 8544270180 scopus 로고    scopus 로고
    • Direct interaction of the novel Nox proteins with p22phox is required for the formation of a functionally active NADPH oxidase
    • Ambasta, R.K.; Kumar, P.; Griendling, K.K.; Schmidt, H.H.; Busse, R.; Brandes, R.P. Direct interaction of the novel Nox proteins with p22phox is required for the formation of a functionally active NADPH oxidase. J. Biol. Chem. 2004, 279, 45935-45941.
    • (2004) J. Biol. Chem , vol.279 , pp. 45935-45941
    • Ambasta, R.K.1    Kumar, P.2    Griendling, K.K.3    Schmidt, H.H.4    Busse, R.5    Brandes, R.P.6
  • 171
    • 13244259440 scopus 로고    scopus 로고
    • Selective inhibition of juxtanuclear translocation of protein kinase C betaII by a negative feedback mechanism involving ceramide formed from the salvage pathway
    • Becker, K.P.; Kitatani, K.; Idkowiak-Baldys, J.; Bielawski, J.; Hannun, Y.A. Selective inhibition of juxtanuclear translocation of protein kinase C betaII by a negative feedback mechanism involving ceramide formed from the salvage pathway. J. Biol. Chem. 2005, 280, 2606-2612.
    • (2005) J. Biol. Chem , vol.280 , pp. 2606-2612
    • Becker, K.P.1    Kitatani, K.2    Idkowiak-Baldys, J.3    Bielawski, J.4    Hannun, Y.A.5
  • 175
    • 0034731404 scopus 로고    scopus 로고
    • Phorbol ester-induced generation of reactive oxygen species is protein kinase cbeta -dependent and required for SAPK activation
    • Datta, R.; Yoshinaga, K.; Kaneki, M.; Pandey, P.; Kufe, D. Phorbol ester-induced generation of reactive oxygen species is protein kinase cbeta -dependent and required for SAPK activation. J. Biol. Chem. 2000, 275, 41000-41003.
    • (2000) J. Biol. Chem , vol.275 , pp. 41000-41003
    • Datta, R.1    Yoshinaga, K.2    Kaneki, M.3    Pandey, P.4    Kufe, D.5
  • 176
    • 78650873412 scopus 로고    scopus 로고
    • Role of protein kinase C and mitochondrial permeability transition pore in the neuroprotective effect of ceramide in ischemia-induced cell death
    • Agudo-López, A.; Miguel, B.G.; Fernández, I.; Martínez, A.M. Role of protein kinase C and mitochondrial permeability transition pore in the neuroprotective effect of ceramide in ischemia-induced cell death. FEBS Lett. 2011, 585, 99-103.
    • (2011) FEBS Lett , vol.585 , pp. 99-103
    • Agudo-López, A.1    Miguel, B.G.2    Fernández, I.3    Martínez, A.M.4
  • 177
    • 60749137151 scopus 로고    scopus 로고
    • NADPH oxidase-dependent signaling in endothelial cells: Role in physiology and pathophysiology
    • Frey, R.S.; Ushio-Fukai, M.; Malik, A.B. NADPH oxidase-dependent signaling in endothelial cells: Role in physiology and pathophysiology. Antioxid. Redox Signal. 2009, 11, 791-810.
    • (2009) Antioxid. Redox Signal , vol.11 , pp. 791-810
    • Frey, R.S.1    Ushio-Fukai, M.2    Malik, A.B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.