메뉴 건너뛰기




Volumn 42, Issue 2, 2007, Pages 175-179

The 'A's and 'O's of NADPH oxidase regulation: A commentary on "Subcellular localization and function of alternatively spliced Noxo1 isoforms"

Author keywords

[No Author keywords available]

Indexed keywords

NITRIC OXIDE; PROTEIN NOX1; PROTEIN NOX3; PROTEIN NOX4; PROTEIN NOX5; PROTEIN NOXA; PROTEIN NOXO1; REACTIVE NITROGEN SPECIES; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE 2;

EID: 33845620993     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2006.11.003     Document Type: Note
Times cited : (54)

References (47)
  • 1
    • 4744349398 scopus 로고    scopus 로고
    • Structure and regulation of the neutrophil respiratory burst oxidase: comparison with nonphagocyte oxidases
    • Quinn M.T., and Gauss K.A. Structure and regulation of the neutrophil respiratory burst oxidase: comparison with nonphagocyte oxidases. J. Leukoc. Biol. 76 (2004) 760-781
    • (2004) J. Leukoc. Biol. , vol.76 , pp. 760-781
    • Quinn, M.T.1    Gauss, K.A.2
  • 2
    • 0028365310 scopus 로고
    • Angiotensin II stimulates NADH and NADPH oxidase activity in cultured vascular smooth muscle cells
    • Griendling K.K., Minieri C.A., Ollerenshaw J.D., and Alexander R.W. Angiotensin II stimulates NADH and NADPH oxidase activity in cultured vascular smooth muscle cells. Circ. Res. 74 (1994) 1141-1148
    • (1994) Circ. Res. , vol.74 , pp. 1141-1148
    • Griendling, K.K.1    Minieri, C.A.2    Ollerenshaw, J.D.3    Alexander, R.W.4
  • 3
    • 0028233138 scopus 로고
    • NADH oxidoreductase is a major source of superoxide anion in bovine coronary artery endothelium
    • Mohazzab K.M., Kaminski P.M., and Wolin M.S. NADH oxidoreductase is a major source of superoxide anion in bovine coronary artery endothelium. Am. J. Physiol. 266 (1994) H2568-H2572
    • (1994) Am. J. Physiol. , vol.266
    • Mohazzab, K.M.1    Kaminski, P.M.2    Wolin, M.S.3
  • 4
    • 0035897653 scopus 로고    scopus 로고
    • Homologs of gp91phox: cloning and tissue expression of Nox3, Nox4, and Nox5
    • Cheng G., Cao Z., Xu X., van Meir E.G., and Lambeth J.D. 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
  • 6
    • 33845635605 scopus 로고    scopus 로고
    • Subcellular localization and function of alternatively spliced Noxo1 isoforms
    • (this issue)
    • Ueyama, et al. Subcellular localization and function of alternatively spliced Noxo1 isoforms. Free Radical Biol. Med 42 (2006) 180-190 (this issue)
    • (2006) Free Radical Biol. Med , vol.42 , pp. 180-190
    • Ueyama1
  • 7
    • 0036710445 scopus 로고    scopus 로고
    • The superoxide-generating NADPH oxidase: structural aspects and activation mechanism
    • Vignais P.V. The superoxide-generating NADPH oxidase: structural aspects and activation mechanism. Cell. Mol. Life Sci. 59 (2002) 1428-1459
    • (2002) Cell. Mol. Life Sci. , vol.59 , pp. 1428-1459
    • Vignais, P.V.1
  • 8
    • 0038789165 scopus 로고    scopus 로고
    • Two novel proteins activate superoxide generation by the NADPH oxidase NOX1
    • Banfi B., Clark R.A., Steger K., and Krause K.H. 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
  • 9
    • 0038036799 scopus 로고    scopus 로고
    • Proteins homologous to p47phox and p67phox support superoxide production by NAD(P)H oxidase 1 in colon epithelial cells
    • Geiszt M., Lekstrom K., Witta J., and Leto T.L. Proteins homologous to p47phox and p67phox support superoxide production by NAD(P)H oxidase 1 in colon epithelial cells. J. Biol. Chem. 278 (2003) 20006-20012
    • (2003) J. Biol. Chem. , vol.278 , pp. 20006-20012
    • Geiszt, M.1    Lekstrom, K.2    Witta, J.3    Leto, T.L.4
  • 10
    • 0042991381 scopus 로고    scopus 로고
    • Novel human homologues of p47phox and p67phox participate in activation of superoxide-producing NADPH oxidases
    • Takeya R., Ueno N., Kami K., Taura M., Kohjima M., Izaki T., Nunoi H., and Sumimoto H. 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
  • 11
    • 0035421216 scopus 로고    scopus 로고
    • Novel modular domain PB1 recognizes PC motif to mediate functional protein-protein interactions
    • Ito T., Matsui Y., Ago T., Ota K., and Sumimoto H. Novel modular domain PB1 recognizes PC motif to mediate functional protein-protein interactions. EMBO J. 20 (2001) 3938-3946
    • (2001) EMBO J. , vol.20 , pp. 3938-3946
    • Ito, T.1    Matsui, Y.2    Ago, T.3    Ota, K.4    Sumimoto, H.5
  • 12
    • 0029850711 scopus 로고    scopus 로고
    • Novel domains in NADPH oxidase subunits, sorting nexins, and PtdIns 3-kinases: binding partners of SH3 domains?
    • Ponting C.P. Novel domains in NADPH oxidase subunits, sorting nexins, and PtdIns 3-kinases: binding partners of SH3 domains?. Protein Sci. 5 (1996) 2353-2357
    • (1996) Protein Sci. , vol.5 , pp. 2353-2357
    • Ponting, C.P.1
  • 13
    • 0035976622 scopus 로고    scopus 로고
    • Location, location, location: membrane targeting directed by PX domains
    • Sato T.K., Overduin M., and Emr S.D. Location, location, location: membrane targeting directed by PX domains. Science 294 (2001) 1881-1885
    • (2001) Science , vol.294 , pp. 1881-1885
    • Sato, T.K.1    Overduin, M.2    Emr, S.D.3
  • 14
    • 0034995037 scopus 로고    scopus 로고
    • Solution structure of the PX domain, a target of the SH3 domain
    • Hiroaki H., Ago T., Ito T., Sumimoto H., and Kohda D. Solution structure of the PX domain, a target of the SH3 domain. Nat. Struct. Biol. 8 (2001) 526-530
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 526-530
    • Hiroaki, H.1    Ago, T.2    Ito, T.3    Sumimoto, H.4    Kohda, D.5
  • 16
    • 0037446850 scopus 로고    scopus 로고
    • Phosphorylation of p47phox directs phox homology domain from SH3 domain toward phosphoinositides, leading to phagocyte NADPH oxidase activation
    • Ago T., Kuribayashi F., Hiroaki H., Takeya R., Ito T., Kohda D., and Sumimoto H. Phosphorylation of p47phox directs phox homology domain from SH3 domain toward phosphoinositides, leading to phagocyte NADPH oxidase activation. Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 4474-4479
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 4474-4479
    • Ago, T.1    Kuribayashi, F.2    Hiroaki, H.3    Takeya, R.4    Ito, T.5    Kohda, D.6    Sumimoto, H.7
  • 17
    • 0036094545 scopus 로고    scopus 로고
    • Chronic granulomatous disease mutations and the PX domain
    • Heyworth P.G., and Cross A.R. Chronic granulomatous disease mutations and the PX domain. Nat. Cell Biol. 4 (2002) E110
    • (2002) Nat. Cell Biol. , vol.4
    • Heyworth, P.G.1    Cross, A.R.2
  • 18
    • 23844493190 scopus 로고    scopus 로고
    • Alternative mRNA splice forms of NOXO1: differential tissue expression and regulation of Nox1 and Nox3
    • Cheng G., and Lambeth J.D. Alternative mRNA splice forms of NOXO1: differential tissue expression and regulation of Nox1 and Nox3. Gene 356 (2005) 118-126
    • (2005) Gene , vol.356 , pp. 118-126
    • Cheng, G.1    Lambeth, J.D.2
  • 19
    • 33746779417 scopus 로고    scopus 로고
    • Expression and function of Noxo1gamma, an alternative splicing form of the NADPH oxidase organizer 1
    • Takeya R., Taura M., Yamasaki T., Naito S., and Sumimoto H. Expression and function of Noxo1gamma, an alternative splicing form of the NADPH oxidase organizer 1. FEBS J. 273 (2006) 3663-3677
    • (2006) FEBS J. , vol.273 , pp. 3663-3677
    • Takeya, R.1    Taura, M.2    Yamasaki, T.3    Naito, S.4    Sumimoto, H.5
  • 20
    • 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., and 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. 279 (2004) 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
  • 21
    • 0037205457 scopus 로고    scopus 로고
    • Intracellular localization and preassembly of the NADPH oxidase complex in cultured endothelial cells
    • Li J.M., and Shah A.M. 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
  • 22
    • 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., and Knaus U.G. Functional analysis of Nox4 reveals unique characteristics compared to other NADPH oxidases. Cell Signal. 18 (2006) 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
  • 24
    • 33845656600 scopus 로고    scopus 로고
    • Apocynin: mother nature's gift to combat oxidative stress
    • Wind S., and Kumar A. Apocynin: mother nature's gift to combat oxidative stress. Phcog. Mag. 1 (2005) 136-139
    • (2005) Phcog. Mag. , vol.1 , pp. 136-139
    • Wind, S.1    Kumar, A.2
  • 25
    • 33746885455 scopus 로고    scopus 로고
    • Neutrophils from p40phox-/-mice exhibit severe defects in NADPH oxidase regulation and oxidant-dependent bacterial killing
    • Ellson C.D., Davidson K., Ferguson G.J., Connor O.'R., Stephens L.R., and Hawkins P.T. Neutrophils from p40phox-/-mice exhibit severe defects in NADPH oxidase regulation and oxidant-dependent bacterial killing. J. Exp. Med. 203 (2006) 1927-1937
    • (2006) J. Exp. Med. , vol.203 , pp. 1927-1937
    • Ellson, C.D.1    Davidson, K.2    Ferguson, G.J.3    Connor, O.'R.4    Stephens, L.R.5    Hawkins, P.T.6
  • 26
    • 33746896166 scopus 로고    scopus 로고
    • The phosphoinositide-binding protein p40phox activates the NADPH oxidase during FcgammaIIA receptor-induced phagocytosis
    • Suh C.I., Stull N.D., Li X.J., Tian W., Price M.O., Grinstein S., Yaffe M.B., Atkinson S., and Dinauer M.C. The phosphoinositide-binding protein p40phox activates the NADPH oxidase during FcgammaIIA receptor-induced phagocytosis. J. Exp. Med. 203 (2006) 1915-1925
    • (2006) J. Exp. Med. , vol.203 , pp. 1915-1925
    • Suh, C.I.1    Stull, N.D.2    Li, X.J.3    Tian, W.4    Price, M.O.5    Grinstein, S.6    Yaffe, M.B.7    Atkinson, S.8    Dinauer, M.C.9
  • 27
    • 18744403007 scopus 로고    scopus 로고
    • The adaptor protein p40(phox) as a positive regulator of the superoxide-producing phagocyte oxidase
    • Kuribayashi F., Nunoi H., Wakamatsu K., Tsunawaki S., Sato K., Ito T., and Sumimoto H. The adaptor protein p40(phox) as a positive regulator of the superoxide-producing phagocyte oxidase. EMBO J. 21 (2002) 6312-6320
    • (2002) EMBO J. , vol.21 , pp. 6312-6320
    • Kuribayashi, F.1    Nunoi, H.2    Wakamatsu, K.3    Tsunawaki, S.4    Sato, K.5    Ito, T.6    Sumimoto, H.7
  • 28
    • 0028151013 scopus 로고
    • Rac translocates independently of the neutrophil NADPH oxidase components p47phox and p67phox. Evidence for its interaction with flavocytochrome b558
    • Heyworth P.G., Bohl B.P., Bokoch G.M., and Curnutte J.T. Rac translocates independently of the neutrophil NADPH oxidase components p47phox and p67phox. Evidence for its interaction with flavocytochrome b558. J. Biol. Chem. 269 (1994) 30749-30752
    • (1994) J. Biol. Chem. , vol.269 , pp. 30749-30752
    • Heyworth, P.G.1    Bohl, B.P.2    Bokoch, G.M.3    Curnutte, J.T.4
  • 29
    • 0033105874 scopus 로고    scopus 로고
    • NADPH oxidase: an update
    • Babior B.M. NADPH oxidase: an update. Blood 93 (1999) 1464-1476
    • (1999) Blood , vol.93 , pp. 1464-1476
    • Babior, B.M.1
  • 30
    • 9144257277 scopus 로고    scopus 로고
    • Tissue distribution and putative physiological function of NOX family NADPH oxidases
    • Krause K.H. Tissue distribution and putative physiological function of NOX family NADPH oxidases. Jpn. J. Infect. Dis. 57 (2004) S28-S29
    • (2004) Jpn. J. Infect. Dis. , vol.57
    • Krause, K.H.1
  • 31
    • 33745815084 scopus 로고    scopus 로고
    • Nox1-dependent reactive oxygen generation is regulated by Rac1
    • Cheng G., Diebold B.A., Hughes Y., and Lambeth J.D. Nox1-dependent reactive oxygen generation is regulated by Rac1. J. Biol. Chem. 281 (2006) 17718-17726
    • (2006) J. Biol. Chem. , vol.281 , pp. 17718-17726
    • Cheng, G.1    Diebold, B.A.2    Hughes, Y.3    Lambeth, J.D.4
  • 32
    • 33746848094 scopus 로고    scopus 로고
    • Direct involvement of the small GTPase Rac in activation of the superoxide-producing NADPH oxidase Nox1
    • Miyano K., Ueno N., Takeya R., and Sumimoto H. Direct involvement of the small GTPase Rac in activation of the superoxide-producing NADPH oxidase Nox1. J. Biol. Chem. 281 (2006) 21857-21868
    • (2006) J. Biol. Chem. , vol.281 , pp. 21857-21868
    • Miyano, K.1    Ueno, N.2    Takeya, R.3    Sumimoto, H.4
  • 33
    • 33644750712 scopus 로고    scopus 로고
    • Involvement of Rac1 in activation of multicomponent Nox1-and Nox3-based NADPH oxidases
    • Ueyama T., Geiszt M., and Leto T.L. Involvement of Rac1 in activation of multicomponent Nox1-and Nox3-based NADPH oxidases. Mol. Cell. Biol. 26 (2006) 2160-2174
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 2160-2174
    • Ueyama, T.1    Geiszt, M.2    Leto, T.L.3
  • 35
    • 4544274760 scopus 로고    scopus 로고
    • Nox3 regulation by NOXO1, p47phox, and p67phox
    • Cheng G., Ritsick D., and Lambeth J.D. Nox3 regulation by NOXO1, p47phox, and p67phox. J. Biol. Chem. 279 (2004) 34250-34255
    • (2004) J. Biol. Chem. , vol.279 , pp. 34250-34255
    • Cheng, G.1    Ritsick, D.2    Lambeth, J.D.3
  • 38
    • 20744440943 scopus 로고    scopus 로고
    • The NADPH oxidase Nox3 constitutively produces superoxide in a p22phox-dependent manner: its regulation by oxidase organizers and activators
    • Ueno N., Takeya R., Miyano K., Kikuchi H., and Sumimoto H. The NADPH oxidase Nox3 constitutively produces superoxide in a p22phox-dependent manner: its regulation by oxidase organizers and activators. J. Biol. Chem. 280 (2005) 23328-23339
    • (2005) J. Biol. Chem. , vol.280 , pp. 23328-23339
    • Ueno, N.1    Takeya, R.2    Miyano, K.3    Kikuchi, H.4    Sumimoto, H.5
  • 43
    • 24744468043 scopus 로고    scopus 로고
    • Point mutations in the proline-rich region of p22phox are dominant inhibitors of Nox1-and Nox2-dependent reactive oxygen generation
    • Kawahara T., Ritsick D., Cheng G., and Lambeth J.D. Point mutations in the proline-rich region of p22phox are dominant inhibitors of Nox1-and Nox2-dependent reactive oxygen generation. J. Biol. Chem. 280 (2005) 31859-31869
    • (2005) J. Biol. Chem. , vol.280 , pp. 31859-31869
    • Kawahara, T.1    Ritsick, D.2    Cheng, G.3    Lambeth, J.D.4
  • 44
    • 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. 4 (2004) 181-189
    • (2004) Nat. Rev. Immunol. , vol.4 , pp. 181-189
    • Lambeth, J.D.1
  • 46
    • 0037168483 scopus 로고    scopus 로고
    • There's NO binding like NOS binding: protein-protein interactions in NO/cGMP signaling
    • Nedvetsky P.I., Sessa W.C., and Schmidt H.H. There's NO binding like NOS binding: protein-protein interactions in NO/cGMP signaling. Proc. Natl. Acad. Sci. U. S. A. 99 (2002) 16510-16512
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 16510-16512
    • Nedvetsky, P.I.1    Sessa, W.C.2    Schmidt, H.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.