메뉴 건너뛰기




Volumn 37, Issue 10, 2004, Pages 1542-1549

Functional association of Nox1 with p22phox in vascular smooth muscle cells

Author keywords

Free radicals; NAD(P)H oxidase; Nox; p22phox; Reactive oxygen species; Superoxide; Vascular smooth muscle

Indexed keywords

1 HYDROXY 3 CARBOXYPYRROLIDINE; GLYCOPROTEIN GP 91; PROTEIN P22; PROTEIN P22PHOX; PYRROLIDINE DERIVATIVE; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE 1; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE 2; SUPEROXIDE; UNCLASSIFIED DRUG;

EID: 5344232726     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2004.08.011     Document Type: Article
Times cited : (73)

References (35)
  • 1
    • 0344043305 scopus 로고    scopus 로고
    • Superoxide production in vascular smooth muscle contributes to oxidative stress and impaired relaxation in atherosclerosis
    • F.J.J. Miller, 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 Circulation Res. 82 1998 1298 1305
    • (1998) Circulation Res. , vol.82 , pp. 1298-1305
    • Miller, F.J.J.1    Gutterman, D.D.2    Rios, C.D.3    Heistad, D.D.4    Davidson, B.L.5
  • 2
    • 0028233138 scopus 로고
    • NADH oxidoreductase is the major source of superoxide anion in bovine coronary artery endothelium
    • K.M. Mohazzab-H, P.M. Kaminski, and M.S. Wolin NADH oxidoreductase is the major source of superoxide anion in bovine coronary artery endothelium Am. J. Physiol. 266 1994 H2568 H2572
    • (1994) Am. J. Physiol. , vol.266
    • Mohazzab-H, K.M.1    Kaminski, P.M.2    Wolin, M.S.3
  • 4
    • 0030005713 scopus 로고    scopus 로고
    • Angiotensin II mediated hypertension in the rat increases vascular superoxide production via membrane NADH/NADPH oxidase activation: Contribution to alterations of vasomotor tone
    • S. Rajagopalan, S. Kurz, T. Münzel, M. Tarpey, B.A. Freeman, K.K. Griendling, and D.G. Harrison Angiotensin II mediated hypertension in the rat increases vascular superoxide production via membrane NADH/NADPH oxidase activation: contribution to alterations of vasomotor tone J. Clin. Invest. 97 1996 1916 1923
    • (1996) J. Clin. Invest. , vol.97 , pp. 1916-1923
    • Rajagopalan, S.1    Kurz, S.2    Münzel, T.3    Tarpey, M.4    Freeman, B.A.5    Griendling, K.K.6    Harrison, D.G.7
  • 5
    • 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
  • 7
    • 0023483148 scopus 로고
    • Purified cytochrome b from human granulocyte plasma membrane is comprised of two polypeptides with relative molecular weights of 91,000 and 22,000
    • C.A. Parkos, R.A. Allen, C.G. Cochrane, and A.J. Jesaitis Purified cytochrome b from human granulocyte plasma membrane is comprised of two polypeptides with relative molecular weights of 91,000 and 22,000 J. Clin. Invest. 80 1987 732 742
    • (1987) J. Clin. Invest. , vol.80 , pp. 732-742
    • Parkos, C.A.1    Allen, R.A.2    Cochrane, C.G.3    Jesaitis, A.J.4
  • 8
    • 0029841511 scopus 로고    scopus 로고
    • Stoichiometry of the subunits of flavocytochrome b558 of the NADPH oxidase of phagocytes
    • T.M. Wallach, and A.W. Segal Stoichiometry of the subunits of flavocytochrome b558 of the NADPH oxidase of phagocytes Biochem. J. 320 1996 33 38
    • (1996) Biochem. J. , vol.320 , pp. 33-38
    • Wallach, T.M.1    Segal, A.W.2
  • 10
  • 12
    • 0035844030 scopus 로고    scopus 로고
    • Novel gp91phox homologues in vascular smooth muscle cells: Nox1 mediates angiotensin II-induced superoxide formation and redox-sensitive signaling pathways
    • B. Lassegue, D. Sorescu, K. Szocs, M. Akers, Y. Zhang, S.L. Grant, J.D. Lambeth, and K.K. Griendling Novel gp91phox homologues in vascular smooth muscle cells: Nox1 mediates angiotensin II-induced superoxide formation and redox-sensitive signaling pathways Circ. Res. 88 2001 888 894
    • (2001) Circ. Res. , vol.88 , pp. 888-894
    • Lassegue, B.1    Sorescu, D.2    Szocs, K.3    Akers, M.4    Zhang, Y.5    Grant, S.L.6    Lambeth, J.D.7    Griendling, K.K.8
  • 13
    • 0038036799 scopus 로고    scopus 로고
    • Proteins homologous to p47phox and p67phox support superoxide production by NAD(P)H oxidase 1 in colon epithelial cells
    • M. Geiszt, K. Lekstrom, J. Witta, and T.L. Leto 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
  • 14
    • 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
  • 15
    • 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
  • 16
    • 0029661428 scopus 로고    scopus 로고
    • P22phox is a critical component of the superoxide-generating NADH/NADPH oxidase system and regulates angiotensin II-induced hypertrophy in vascular smooth muscle cells
    • M. Ushio-Fukai, A.M. Zafari, T. Fukui, N. Ishizaka, and K.K. Griendling p22phox is a critical component of the superoxide-generating NADH/NADPH oxidase system and regulates angiotensin II-induced hypertrophy in vascular smooth muscle cells J. Biol. Chem. 271 1996 23317 23321
    • (1996) J. Biol. Chem. , vol.271 , pp. 23317-23321
    • Ushio-Fukai, M.1    Zafari, A.M.2    Fukui, T.3    Ishizaka, N.4    Griendling, K.K.5
  • 17
    • 0025881171 scopus 로고
    • Characterization of phosphatidylinositol-specific phospholipase C from cultured vascular smooth muscle cells
    • K.K. Griendling, M.B. Taubman, M. Akers, M. Mendlowitz, and R.W. Alexander Characterization of phosphatidylinositol-specific phospholipase C from cultured vascular smooth muscle cells J. Biol. Chem. 266 1991 15498 15504
    • (1991) J. Biol. Chem. , vol.266 , pp. 15498-15504
    • Griendling, K.K.1    Taubman, M.B.2    Akers, M.3    Mendlowitz, M.4    Alexander, R.W.5
  • 20
    • 0029016908 scopus 로고
    • Topological mapping of neutrophil cytochrome b epitopes with phage-display libraries
    • J.B. Burritt, M.T. Quinn, M.A. Jutila, C.W. Bond, and A.J. Jesaitis Topological mapping of neutrophil cytochrome b epitopes with phage-display libraries J. Biol. Chem. 270 1995 16974 16980
    • (1995) J. Biol. Chem. , vol.270 , pp. 16974-16980
    • Burritt, J.B.1    Quinn, M.T.2    Jutila, M.A.3    Bond, C.W.4    Jesaitis, A.J.5
  • 21
    • 0026754805 scopus 로고
    • Human neutrophil cytochrome b contains multiple hemes: Evidence for heme associated with both subunits
    • M.T. Quinn, M.L. Mullen, and A.J. Jesaitis Human neutrophil cytochrome b contains multiple hemes: evidence for heme associated with both subunits J. Biol. Chem. 267 1992 7303 7309
    • (1992) J. Biol. Chem. , vol.267 , pp. 7303-7309
    • Quinn, M.T.1    Mullen, M.L.2    Jesaitis, A.J.3
  • 23
    • 0037098504 scopus 로고    scopus 로고
    • New non-invasive diagnostic tool for inflammation-induced oxidative stress using electron spin resonance spectroscopy and cyclic hydroxylamine
    • S.I. Dikalov, A.E. Dikalova, and R.P. Mason New non-invasive diagnostic tool for inflammation-induced oxidative stress using electron spin resonance spectroscopy and cyclic hydroxylamine Arch. Biochem. Biophys. 402 2001 218 226
    • (2001) Arch. Biochem. Biophys. , vol.402 , pp. 218-226
    • Dikalov, S.I.1    Dikalova, A.E.2    Mason, R.P.3
  • 24
    • 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
    • R.M. Touyz, X. Chen, F. Tabet, G. Yao, G. He, M.T. Quinn, P.J. Pagano, and E.L. Schiffrin Expression of a functionally active gp91phox-containing neutrophil-type NAD(P)H oxidase in smooth muscle cells from human resistance arteries Circ. Res. 90 2002 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
  • 26
    • 0034607821 scopus 로고    scopus 로고
    • Processing and maturation of flavocytochrome b558 include incorporation of heme as pre-requisite for heterodimer assembly
    • F.R. DeLeo, J.B. Burritt, L. Yu, A.J. Jesaitis, M.C. Dinauer, and W.M. Nauseef Processing and maturation of flavocytochrome b558 include incorporation of heme as pre-requisite for heterodimer assembly J. Biol. Chem. 275 2000 13986 13993
    • (2000) J. Biol. Chem. , vol.275 , pp. 13986-13993
    • Deleo, F.R.1    Burritt, J.B.2    Yu, L.3    Jesaitis, A.J.4    Dinauer, M.C.5    Nauseef, W.M.6
  • 27
    • 0033579491 scopus 로고    scopus 로고
    • A phosphatidic acid-activated protein kinase and conventional protein kinase C isoforms phosphorylate p22phox, an NADPH oxidase component
    • D.S. Regier, K.A. Waite, R. Wallin, and L.C. McPhail A phosphatidic acid-activated protein kinase and conventional protein kinase C isoforms phosphorylate p22phox, an NADPH oxidase component J. Biol. Chem. 274 1999 36601 36608
    • (1999) J. Biol. Chem. , vol.274 , pp. 36601-36608
    • Regier, D.S.1    Waite, K.A.2    Wallin, R.3    McPhail, L.C.4
  • 28
    • 0034664253 scopus 로고    scopus 로고
    • Phosphorylation of p22phox is mediated by phospholipase D-dependent and -independent mechanisms
    • D.S. Regier, D.G. Greene, S. Sergeant, A.J. Jesaitis, and L.C. McPhail Phosphorylation of p22phox is mediated by phospholipase D-dependent and -independent mechanisms J. Biol. Chem. 275 2000 28406 28412
    • (2000) J. Biol. Chem. , vol.275 , pp. 28406-28412
    • Regier, D.S.1    Greene, D.G.2    Sergeant, S.3    Jesaitis, A.J.4    McPhail, L.C.5
  • 29
    • 0030827909 scopus 로고    scopus 로고
    • Biosynthesis of the phagocyte NADPH oxidase cytochrome b558: Role of heme incorporation and heterodimer formation in maturation and stability of gp91phox and p22phox subunits
    • L. Yu, L. Zhen, and M.C. Dinauer Biosynthesis of the phagocyte NADPH oxidase cytochrome b558: role of heme incorporation and heterodimer formation in maturation and stability of gp91phox and p22phox subunits J. Biol. Chem. 272 1997 27288 27294
    • (1997) J. Biol. Chem. , vol.272 , pp. 27288-27294
    • Yu, L.1    Zhen, L.2    Dinauer, M.C.3
  • 30
    • 0025989760 scopus 로고
    • Chronic treatment with polyethylene-glycolated superoxide dismutase partially restores endothelium-dependent vascular relaxations in cholesterol-fed rabbits
    • A. Mugge, J.H. Elwell, T.E. Peterson, T.G. Hofmeyer, D.D. Heistad, and D.G. Harrison Chronic treatment with polyethylene-glycolated superoxide dismutase partially restores endothelium-dependent vascular relaxations in cholesterol-fed rabbits Circ. Res. 69 1991 1293 1300
    • (1991) Circ. Res. , vol.69 , pp. 1293-1300
    • Mugge, A.1    Elwell, J.H.2    Peterson, T.E.3    Hofmeyer, T.G.4    Heistad, D.D.5    Harrison, D.G.6
  • 31
    • 0029783343 scopus 로고    scopus 로고
    • Activation of NADPH oxidase required for macrophage-mediated oxidation of low-density lipoprotein
    • M. Aviram, M. Rosenbalt, A. Etzioni, and R. Levy Activation of NADPH oxidase required for macrophage-mediated oxidation of low-density lipoprotein Metabolism 45 1996 1069 1079
    • (1996) Metabolism , vol.45 , pp. 1069-1079
    • Aviram, M.1    Rosenbalt, M.2    Etzioni, A.3    Levy, R.4
  • 32
    • 10544246489 scopus 로고    scopus 로고
    • Reactive oxygen species produced by macrophage-derived foam cells regulate the activity of vascular matrix metalloproteinases in vitro
    • S. Rajagopalan, X.P. Meng, S. Ramasamy, D.G. Harrison, and Z.S. Galis Reactive oxygen species produced by macrophage-derived foam cells regulate the activity of vascular matrix metalloproteinases in vitro J. Clin. Invest. 98 1996 2572 2579
    • (1996) J. Clin. Invest. , vol.98 , pp. 2572-2579
    • Rajagopalan, S.1    Meng, X.P.2    Ramasamy, S.3    Harrison, D.G.4    Galis, Z.S.5
  • 35
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.