메뉴 건너뛰기




Volumn 38, Issue 5, 2005, Pages 616-630

The expression of the NADPH oxidase subunit p22phox is regulated by a redox-sensitive pathway in endothelial cells

Author keywords

Endothelial cells; Endothelial dysfunction; Free radicals; NADPH oxidase; p22phox; Reactive oxygen species; Thrombin

Indexed keywords

ANTIOXIDANT; ASCORBIC ACID; DIPHENYLIODONIUM SALT; HYDROGEN PEROXIDE; MESSENGER RNA; MITOGEN ACTIVATED PROTEIN KINASE P38; P22PHOX PROTEIN; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN KINASE B; PROTEIN P22; PROTEIN SUBUNIT; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; THROMBIN; UNCLASSIFIED DRUG;

EID: 15744368783     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2004.09.036     Document Type: Article
Times cited : (124)

References (44)
  • 1
    • 0033781454 scopus 로고    scopus 로고
    • Modulation of protein kinase activity and gene expression by reactive oxygen species and their role in vascular physiology and pathophysiology
    • K.K. Griendling, D. Sorescu, B. Lassegue, and M. Ushio-Fukai Modulation of protein kinase activity and gene expression by reactive oxygen species and their role in vascular physiology and pathophysiology Arterioscler. Thromb. Vasc. Biol. 20 2000 2175 2183
    • (2000) Arterioscler. Thromb. Vasc. Biol. , vol.20 , pp. 2175-2183
    • Griendling, K.K.1    Sorescu, D.2    Lassegue, B.3    Ushio-Fukai, M.4
  • 2
    • 0034894990 scopus 로고    scopus 로고
    • Multiple role of reactive oxygen species in the arterial wall
    • C. Napoli, F. de Nigris, and W. Palinski Multiple role of reactive oxygen species in the arterial wall J. Cell Biochem. 82 2001 674 682
    • (2001) J. Cell Biochem. , vol.82 , pp. 674-682
    • Napoli, C.1    De Nigris, F.2    Palinski, W.3
  • 3
    • 0036963969 scopus 로고    scopus 로고
    • Redox signaling through NADPH oxidases: Involvement in vascular proliferation and coagulation
    • A. Gorlach, T. Kietzmann, and J. Hess Redox signaling through NADPH oxidases: involvement in vascular proliferation and coagulation Ann. NY Acad. Sci. 973 2002 505 507
    • (2002) Ann. NY Acad. Sci. , vol.973 , pp. 505-507
    • Gorlach, A.1    Kietzmann, T.2    Hess, J.3
  • 4
    • 0348109425 scopus 로고    scopus 로고
    • Reactive oxygen species in the vasculature: Molecular and cellular mechanisms
    • Y. Taniyama, and K.K. Griendling Reactive oxygen species in the vasculature: molecular and cellular mechanisms Hypertension 42 2003 1075 1081
    • (2003) Hypertension , vol.42 , pp. 1075-1081
    • Taniyama, Y.1    Griendling, K.K.2
  • 6
    • 0036908442 scopus 로고    scopus 로고
    • Mechanisms of superoxide production in human blood vessels: Relationship to endothelial dysfunction, clinical and genetic risk factors
    • K.M. Channon, and T.J. Guzik Mechanisms of superoxide production in human blood vessels: relationship to endothelial dysfunction, clinical and genetic risk factors J. Physiol. Pharmacol. 53 2002 515 524
    • (2002) J. Physiol. Pharmacol. , vol.53 , pp. 515-524
    • Channon, K.M.1    Guzik, T.J.2
  • 7
    • 0344043305 scopus 로고    scopus 로고
    • Superoxide production in vascular smooth muscle contributes to oxidative stress and impaired relaxation in atherosclerosis
    • F.J. Miller Jr., D.D. Gutterman, C.D. Rios, D.D. Heistad, and B.L. Davidson Superoxide production in vascular smooth muscle contributes to oxidative stress and impaired relaxation in atherosclerosis Circ. Res. 82 1998 1298 1305
    • (1998) Circ. Res. , vol.82 , pp. 1298-1305
    • Miller Jr., F.J.1    Gutterman, D.D.2    Rios, C.D.3    Heistad, D.D.4    Davidson, B.L.5
  • 9
    • 0034677947 scopus 로고    scopus 로고
    • NAD(P)H oxidase: Role in cardiovascular biology and disease
    • K.K. Griendling, D. Sorescu, and M. Ushio-Fukai NAD(P)H oxidase: role in cardiovascular biology and disease Circ. Res. 86 2000 494 501
    • (2000) Circ. Res. , vol.86 , pp. 494-501
    • Griendling, K.K.1    Sorescu, D.2    Ushio-Fukai, M.3
  • 11
    • 0347711117 scopus 로고    scopus 로고
    • NADPH oxidases: Not just for leukocytes anymore!
    • G.M. Bokoch, and U.G. Knaus NADPH oxidases: not just for leukocytes anymore! Trends Biochem. Sci. 28 2003 502 508
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 502-508
    • Bokoch, G.M.1    Knaus, U.G.2
  • 13
    • 0034617071 scopus 로고    scopus 로고
    • A gp91phox containing NADPH oxidase selectively expressed in endothelial cells is a major source of oxygen radical generation in the arterial wall
    • A. Gorlach, R.P. Brandes, K. Nguyen, M. Amidi, F. Dehghani, and R. Busse A gp91phox containing NADPH oxidase selectively expressed in endothelial cells is a major source of oxygen radical generation in the arterial wall Circ. Res. 87 2000 26 32
    • (2000) Circ. Res. , vol.87 , pp. 26-32
    • Gorlach, A.1    Brandes, R.P.2    Nguyen, K.3    Amidi, M.4    Dehghani, F.5    Busse, R.6
  • 14
    • 0032051656 scopus 로고    scopus 로고
    • Expression of functional neutrophil-type NADPH oxidase in cultured rat coronary microvascular endothelial cells
    • U. Bayraktutan, N. Draper, D. Lang, and A.M. Shah Expression of functional neutrophil-type NADPH oxidase in cultured rat coronary microvascular endothelial cells Cardiovasc. Res. 38 1998 256 262
    • (1998) Cardiovasc. Res. , vol.38 , pp. 256-262
    • Bayraktutan, U.1    Draper, N.2    Lang, D.3    Shah, A.M.4
  • 15
    • 0042991381 scopus 로고    scopus 로고
    • Novel human homologues of p47phox and p67phox participate in activation of superoxide-producing NADPH oxidases
    • R. Takeya, N. Ueno, K. Kami, M. Taura, M. Kohjima, T. Izaki, H. Nunoi, and H. Sumimoto Novel human homologues of p47phox and p67phox participate in activation of superoxide-producing NADPH oxidases J. Biol. Chem. 278 2003 25234 25246
    • (2003) J. Biol. Chem. , vol.278 , pp. 25234-25246
    • Takeya, R.1    Ueno, N.2    Kami, K.3    Taura, M.4    Kohjima, M.5    Izaki, T.6    Nunoi, H.7    Sumimoto, H.8
  • 16
    • 0035897653 scopus 로고    scopus 로고
    • Homologs of gp91phox: Cloning and tissue expression of Nox3, Nox4, and Nox5
    • G. Cheng, Z. Cao, X. Xu, E.G. van Meir, and J.D. Lambeth Homologs of gp91phox: cloning and tissue expression of Nox3, Nox4, and Nox5 Gene 269 2001 131 140
    • (2001) Gene , vol.269 , pp. 131-140
    • Cheng, G.1    Cao, Z.2    Xu, X.3    Van Meir, E.G.4    Lambeth, J.D.5
  • 17
    • 0038789165 scopus 로고    scopus 로고
    • Two novel proteins activate superoxide generation by the NADPH oxidase NOX1
    • B. Banfi, R.A. Clark, K. Steger, and K.H. Krause Two novel proteins activate superoxide generation by the NADPH oxidase NOX1 J. Biol. Chem. 278 2003 3510 3513
    • (2003) J. Biol. Chem. , vol.278 , pp. 3510-3513
    • Banfi, B.1    Clark, R.A.2    Steger, K.3    Krause, K.H.4
  • 19
    • 0038363762 scopus 로고    scopus 로고
    • Preliminary characterisation of the promoter of the human p22(phox) gene: Identification of a new polymorphism associated with hypertension
    • M.U. Moreno, G. San Jose, J. Orbe, J.A. Paramo, O. Beloqui, J. Diez, and G. Zalba Preliminary characterisation of the promoter of the human p22(phox) gene: identification of a new polymorphism associated with hypertension FEBS Lett. 542 2003 27 31
    • (2003) FEBS Lett. , vol.542 , pp. 27-31
    • Moreno, M.U.1    San Jose, G.2    Orbe, J.3    Paramo, J.A.4    Beloqui, O.5    Diez, J.6    Zalba, G.7
  • 21
    • 0042379916 scopus 로고    scopus 로고
    • The vascular NAD(P)H oxidases as therapeutic targets in cardiovascular diseases
    • H. Cai, K.K. Griendling, and D.G. Harrison The vascular NAD(P)H oxidases as therapeutic targets in cardiovascular diseases Trends Pharmacol. Sci. 24 2003 471 478
    • (2003) Trends Pharmacol. Sci. , vol.24 , pp. 471-478
    • Cai, H.1    Griendling, K.K.2    Harrison, D.G.3
  • 22
    • 0035816732 scopus 로고    scopus 로고
    • Thrombin activates the hypoxia-inducible factor-1 signaling pathway in vascular smooth muscle cells: Role of the p22(phox)-containing NADPH oxidase
    • A. Gorlach, I. Diebold, V.B. Schini-Kerth, U. Berchner-Pfannschmidt, U. Roth, R.P. Brandes, T. Kietzmann, and R. Busse Thrombin activates the hypoxia-inducible factor-1 signaling pathway in vascular smooth muscle cells: role of the p22(phox)-containing NADPH oxidase Circ. Res. 89 2001 47 54
    • (2001) Circ. Res. , vol.89 , pp. 47-54
    • Gorlach, A.1    Diebold, I.2    Schini-Kerth, V.B.3    Berchner-Pfannschmidt, U.4    Roth, U.5    Brandes, R.P.6    Kietzmann, T.7    Busse, R.8
  • 23
    • 0034975449 scopus 로고    scopus 로고
    • Thrombin-induced MCP-1 expression involves activation of the p22phox-containing NADPH oxidase in human vascular smooth muscle cells
    • R.P. Brandes, C. Viedt, K. Nguyen, S. Beer, J. Kreuzer, R. Busse, and A. Gorlach Thrombin-induced MCP-1 expression involves activation of the p22phox-containing NADPH oxidase in human vascular smooth muscle cells Thromb. Haemost. 85 2001 1104 1110
    • (2001) Thromb. Haemost. , vol.85 , pp. 1104-1110
    • Brandes, R.P.1    Viedt, C.2    Nguyen, K.3    Beer, S.4    Kreuzer, J.5    Busse, R.6    Gorlach, A.7
  • 24
    • 0037197795 scopus 로고    scopus 로고
    • NADPH oxidase mediates tissue factor-dependent surface procoagulant activity by thrombin in human vascular smooth muscle cells
    • O. Herkert, I. Diebold, R.P. Brandes, J. Hess, R. Busse, and A. Gorlach NADPH oxidase mediates tissue factor-dependent surface procoagulant activity by thrombin in human vascular smooth muscle cells Circulation 105 2002 2030 2036
    • (2002) Circulation , vol.105 , pp. 2030-2036
    • Herkert, O.1    Diebold, I.2    Brandes, R.P.3    Hess, J.4    Busse, R.5    Gorlach, A.6
  • 26
    • 0001637870 scopus 로고
    • Permanent cell line expressing human factor VIII-related antigen established by hybridization
    • C.J. Edgell, C.C. McDonald, and J.B. Graham Permanent cell line expressing human factor VIII-related antigen established by hybridization Proc. Natl. Acad. Sci. USA 80 1983 3734 3737
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 3734-3737
    • Edgell, C.J.1    McDonald, C.C.2    Graham, J.B.3
  • 27
    • 2542506333 scopus 로고    scopus 로고
    • Redox-sensitive regulation of the HIF pathway under non-hypoxic conditions in pulmonary artery smooth muscle cells
    • R.S. BelAiba, T. Djordjevic, S. Bonello, D. Flugel, J. Hess, T. Kietzmann, and A. Gorlach Redox-sensitive regulation of the HIF pathway under non-hypoxic conditions in pulmonary artery smooth muscle cells Biol. Chem. 385 2004 249 257
    • (2004) Biol. Chem. , vol.385 , pp. 249-257
    • Belaiba, R.S.1    Djordjevic, T.2    Bonello, S.3    Flugel, D.4    Hess, J.5    Kietzmann, T.6    Gorlach, A.7
  • 30
    • 0037205457 scopus 로고    scopus 로고
    • Intracellular localization and preassembly of the NADPH oxidase complex in cultured endothelial cells
    • J.M. Li, and A.M. Shah Intracellular localization and preassembly of the NADPH oxidase complex in cultured endothelial cells J. Biol. Chem. 277 2002 19952 19960
    • (2002) J. Biol. Chem. , vol.277 , pp. 19952-19960
    • Li, J.M.1    Shah, A.M.2
  • 31
    • 0037809230 scopus 로고    scopus 로고
    • Mechanism of endothelial cell NADPH oxidase activation by angiotensin II: Role of the p47phox subunit
    • J.M. Li, and A.M. Shah Mechanism of endothelial cell NADPH oxidase activation by angiotensin II: role of the p47phox subunit J. Biol. Chem. 278 2003 12094 12100
    • (2003) J. Biol. Chem. , vol.278 , pp. 12094-12100
    • Li, J.M.1    Shah, A.M.2
  • 34
    • 0033538516 scopus 로고    scopus 로고
    • Stimulation of a vascular smooth muscle cell NAD(P)H oxidase by thrombin: Evidence that p47(phox) may participate in forming this oxidase in vitro and in vivo
    • C. Patterson, J. Ruef, N.R. Madamanchi, P. Barry-Lane, Z. Hu, C. Horaist, C.A. Ballinger, A.R. Brasier, C. Bode, and M.S. Runge Stimulation of a vascular smooth muscle cell NAD(P)H oxidase by thrombin: evidence that p47(phox) may participate in forming this oxidase in vitro and in vivo J. Biol. Chem. 274 1999 19814 19822
    • (1999) J. Biol. Chem. , vol.274 , pp. 19814-19822
    • Patterson, C.1    Ruef, J.2    Madamanchi, N.R.3    Barry-Lane, P.4    Hu, Z.5    Horaist, C.6    Ballinger, C.A.7    Brasier, A.R.8    Bode, C.9    Runge, M.S.10
  • 35
    • 0035793313 scopus 로고    scopus 로고
    • Polymorphisms and promoter overactivity of the p22(phox) gene in vascular smooth muscle cells from spontaneously hypertensive rats
    • G. Zalba, G. San Jose, F.J. Beaumont, M.A. Fortuno, A. Fortuno, and J. Diez Polymorphisms and promoter overactivity of the p22(phox) gene in vascular smooth muscle cells from spontaneously hypertensive rats Circ. Res. 88 2001 217 222
    • (2001) Circ. Res. , vol.88 , pp. 217-222
    • Zalba, G.1    San Jose, G.2    Beaumont, F.J.3    Fortuno, M.A.4    Fortuno, A.5    Diez, J.6
  • 36
    • 0031938880 scopus 로고    scopus 로고
    • NAD(P)H oxidase activity in cultured human podocytes: Effects of adenosine triphosphate
    • S. Greiber, T. Munzel, S. Kastner, B. Muller, P. Schollmeyer, and H. Pavenstadt NAD(P)H oxidase activity in cultured human podocytes: effects of adenosine triphosphate Kidney Int. 53 1998 654 663
    • (1998) Kidney Int. , vol.53 , pp. 654-663
    • Greiber, S.1    Munzel, T.2    Kastner, S.3    Muller, B.4    Schollmeyer, P.5    Pavenstadt, H.6
  • 37
    • 0029417335 scopus 로고
    • 2-generating NADH oxidase in human lung fibroblasts by transforming growth factor beta 1
    • 2-generating NADH oxidase in human lung fibroblasts by transforming growth factor beta 1 J. Biol. Chem. 270 1995 30334 30338
    • (1995) J. Biol. Chem. , vol.270 , pp. 30334-30338
    • Thannickal, V.J.1    Fanburg, B.L.2
  • 38
    • 0242300561 scopus 로고    scopus 로고
    • Intermittent high glucose enhances apoptosis related to oxidative stress in human umbilical vein endothelial cells: The role of protein kinase C and NAD(P)H-oxidase activation
    • L. Quagliaro, L. Piconi, R. Assaloni, L. Martinelli, E. Motz, and A. Ceriello Intermittent high glucose enhances apoptosis related to oxidative stress in human umbilical vein endothelial cells: the role of protein kinase C and NAD(P)H-oxidase activation Diabetes 52 2003 2795 2804
    • (2003) Diabetes , vol.52 , pp. 2795-2804
    • Quagliaro, L.1    Piconi, L.2    Assaloni, R.3    Martinelli, L.4    Motz, E.5    Ceriello, A.6
  • 39
    • 0346096545 scopus 로고    scopus 로고
    • Angiotensin II induces endothelin-1 gene expression via extracellular signal-regulated kinase pathway in rat aortic smooth muscle cells
    • H.J. Hong, P. Chan, J.C. Liu, S.H. Juan, M.T. Huang, J.G. Lin, and T.H. Cheng Angiotensin II induces endothelin-1 gene expression via extracellular signal-regulated kinase pathway in rat aortic smooth muscle cells Cardiovasc. Res. 61 2004 159 168
    • (2004) Cardiovasc. Res. , vol.61 , pp. 159-168
    • Hong, H.J.1    Chan, P.2    Liu, J.C.3    Juan, S.H.4    Huang, M.T.5    Lin, J.G.6    Cheng, T.H.7
  • 40
    • 0642375804 scopus 로고    scopus 로고
    • Chromosomal DNA fragmentation in apoptosis and necrosis induced by oxidative stress
    • Y. Higuchi Chromosomal DNA fragmentation in apoptosis and necrosis induced by oxidative stress Biochem. Pharmacol. 66 2003 1527 1535
    • (2003) Biochem. Pharmacol. , vol.66 , pp. 1527-1535
    • Higuchi, Y.1
  • 41
    • 0032545526 scopus 로고    scopus 로고
    • Stimulation of in vitro angiogenesis by hydrogen peroxide and the relation with ETS-1 in endothelial cells
    • M. Yasuda, Y. Ohzeki, S. Shimizu, S. Naito, A. Ohtsuru, T. Yamamoto, and Y. Kuroiwa Stimulation of in vitro angiogenesis by hydrogen peroxide and the relation with ETS-1 in endothelial cells Life Sci. 64 1999 249 258
    • (1999) Life Sci. , vol.64 , pp. 249-258
    • Yasuda, M.1    Ohzeki, Y.2    Shimizu, S.3    Naito, S.4    Ohtsuru, A.5    Yamamoto, T.6    Kuroiwa, Y.7
  • 44
    • 1342281664 scopus 로고    scopus 로고
    • P22phox-derived superoxide mediates enhanced proliferative capacity of diabetic vascular smooth muscle cells
    • H.Y. Jeong, and C.D. Kim p22phox-derived superoxide mediates enhanced proliferative capacity of diabetic vascular smooth muscle cells Diabetes Res. Clin. Pract. 64 2004 1 10
    • (2004) Diabetes Res. Clin. Pract. , vol.64 , pp. 1-10
    • Jeong, H.Y.1    Kim, C.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.