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Volumn 28, Issue 1, 2013, Pages 95-104

NADPH oxidase-dependent and -independent mechanisms of reported inhibitors of reactive oxygen generation

Author keywords

NADPH oxidase isoform 2; Perhexiline; Reactive oxygen species; Suramin; VAS2870

Indexed keywords

LATAMOXEF; NUCLEOTIDYLTRANSFERASE INHIBITOR; PERHEXILINE; PROTEIN KINASE C BETA; PROTEIN P47; PROTEIN P67; RAC2 PROTEIN; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; SUPEROXIDE; SURAMIN; UNCLASSIFIED DRUG; VAS2870;

EID: 84874168194     PISSN: 14756366     EISSN: 14756374     Source Type: Journal    
DOI: 10.3109/14756366.2011.636360     Document Type: Article
Times cited : (67)

References (50)
  • 2
    • 1042278903 scopus 로고    scopus 로고
    • NADPH oxidase
    • DOI 10.1016/j.coi.2003.12.001
    • Babior BM. NADPH oxidase. Curr Opin Immunol 2004;16:42-47 (Pubitemid 38198116)
    • (2004) Current Opinion in Immunology , vol.16 , Issue.1 , pp. 42-47
    • Babior, B.M.1
  • 3
    • 33846794822 scopus 로고    scopus 로고
    • The NOX family of ROS-generating NADPH oxidases: Physiology and pathophysiology
    • DOI 10.1152/physrev.00044.2005
    • Bedard K, Krause KH. The NOX family of ROS-generating NADPH oxidases: Physiology and pathophysiology. Physiol Rev 2007;87:245-313 (Pubitemid 46209993)
    • (2007) Physiological Reviews , vol.87 , Issue.1 , pp. 245-313
    • Bedard, K.1    Krause, K.-H.2
  • 5
    • 0037421492 scopus 로고    scopus 로고
    • Role of oxidative stress in atherosclerosis
    • DOI 10.1016/S0002-9149(02)03144-2, PII S0002914902031442
    • Harrison D, Griendling KK, Landmesser U, Hornig B, Drexler H. Role of oxidative stress in atherosclerosis. Am J Cardiol 2003;91:7A-11A. 6. Sirker A, Zhang M, Murdoch C, Shah AM. Involvement of NADPH oxidases in cardiac remodelling and heart failure. Am J Nephrol 2007;27:649-660 (Pubitemid 36351457)
    • (2003) American Journal of Cardiology , vol.91 , Issue.3 SUPPL.
    • Harrison, D.1    Griendling, K.K.2    Landmesser, U.3    Hornig, B.4    Drexler, H.5
  • 6
    • 6044257599 scopus 로고    scopus 로고
    • Reactive oxygen species in the cerebral circulation: Physiological roles and therapeutic implications for hypertension and stroke
    • DOI 10.2165/00003495-200464190-00001
    • Paravicini TM, Drummond GR, Sobey CG. Reactive oxygen species in the cerebral circulation: Physiological roles and therapeutic implications for hypertension and stroke. Drugs 2004;64:2143-2157 (Pubitemid 39382206)
    • (2004) Drugs , vol.64 , Issue.19 , pp. 2143-2157
    • Paravicini, T.M.1    Drummond, G.R.2    Sobey, C.G.3
  • 7
    • 34347257042 scopus 로고    scopus 로고
    • Nox enzymes, ROS, and chronic disease: An example of antagonistic pleiotropy
    • DOI 10.1016/j.freeradbiomed.2007.03.027, PII S0891584907002225
    • Lambeth JD. Nox enzymes, ROS, and chronic disease: An example of antagonistic pleiotropy. Free Radic Biol Med 2007;43:332-347 (Pubitemid 46992767)
    • (2007) Free Radical Biology and Medicine , vol.43 , Issue.3 , pp. 332-347
    • Lambeth, J.D.1
  • 8
    • 0037154308 scopus 로고    scopus 로고
    • phox-containing NADPH oxidase in angiotensin II-induced cardiac hypertrophy in mice
    • DOI 10.1161/hc0302.103712
    • Bendall JK, Cave AC, Heymes C, Gall N, Shah AM. Pivotal role of a gp91phox-containing NADPH oxidase in angiotensin II-induced cardiac hypertrophy in mice. Circulation 2002;105:293-296 (Pubitemid 34106175)
    • (2002) Circulation , vol.105 , Issue.3 , pp. 293-296
    • Bendall, J.K.1    Cave, A.C.2    Heymes, C.3    Gall, N.4    Shah, A.M.5
  • 9
    • 0036792751 scopus 로고    scopus 로고
    • Role of p47phox in vascular oxidative stress and hypertension caused by angiotensin I.I
    • Landmesser U, Cai H, Dikalov S, McCann L, Hwang J, Jo H et al. Role of p47phox in vascular oxidative stress and hypertension caused by angiotensin II. Hypertension 2002;40:511-515
    • (2002) Hypertension , vol.40 , pp. 511-515
    • Landmesser, U.1    Cai, H.2    Dikalov, S.3    McCann, L.4    Hwang, J.5    Jo, H.6
  • 10
    • 33747119962 scopus 로고    scopus 로고
    • phox attenuates angiotensin II-induced abdominal aortic aneurysm formation in apolipoprotein E-deficient mice
    • DOI 10.1161/CIRCULATIONAHA.105.607168, PII 0000301720060801000011
    • Thomas M, Gavrila D, McCormick ML, Miller FJ Jr, Daugherty A, Cassis LA et al. Deletion of p47phox attenuates angiotensin II-induced abdominal aortic aneurysm formation in apolipoprotein E-deficient mice. Circulation 2006;114:404-413 (Pubitemid 44264822)
    • (2006) Circulation , vol.114 , Issue.5 , pp. 404-413
    • Thomas, M.1    Gavrila, D.2    McCormick, M.L.3    Miller Jr., F.J.4    Daugherty, A.5    Cassis, L.A.6    Dellsperger, K.C.7    Weintraub, N.L.8
  • 13
    • 3042527868 scopus 로고    scopus 로고
    • The NADPH oxidase of professional phagocytes - Prototype of the NOX electron transport chain systems
    • DOI 10.1016/j.bbabio.2004.03.008, PII S0005272804000556
    • Cross AR, Segal AW. The NADPH oxidase of professional phagocytes-prototype of the NOX electron transport chain systems. Biochim Biophys Acta 2004;1657:1-22 (Pubitemid 38823040)
    • (2004) Biochimica et Biophysica Acta - Bioenergetics , vol.1657 , Issue.1 , pp. 1-22
    • Cross, A.R.1    Segal, A.W.2
  • 15
    • 79957890939 scopus 로고    scopus 로고
    • Combating oxidative stress in vascular disease: NADPH oxidases as therapeutic targets
    • Drummond GR, Selemidis S, Griendling KK, Sobey CG. Combating oxidative stress in vascular disease: NADPH oxidases as therapeutic targets. Nat Rev Drug Discov 2011;10:453-471
    • (2011) Nat Rev Drug Discov , Issue.10 , pp. 453-471
    • Drummond, G.R.1    Selemidis, S.2    Griendling, K.K.3    Sobey, C.G.4
  • 16
    • 0027479814 scopus 로고
    • Studies on the inhibitory mechanism of iodonium compounds with special reference to neutrophil NADPH oxidase
    • O'Donnell BV, Tew DG, Jones OT, England PJ. Studies on the inhibitory mechanism of iodonium compounds with special reference to neutrophil NADPH oxidase. Biochem J 1993;290 (Pt 1):41-49 (Pubitemid 23081198)
    • (1993) Biochemical Journal , vol.290 , Issue.1 , pp. 41-49
    • O'Donnell, V.B.1    Tew, D.G.2    Jones, O.T.G.3    England, P.J.4
  • 17
    • 0028473441 scopus 로고
    • Characteristics of the inhibition of NADPH oxidase activation in neutrophils by apocynin, a methoxy-substituted catechol
    • Stolk J, Hiltermann TJ, Dijkman JH, Verhoeven AJ. Characteristics of the inhibition of NADPH oxidase activation in neutrophils by apocynin, a methoxy-substituted catechol. Am J Respir Cell Mol Biol 1994;11:95-102
    • (1994) Am J Respir Cell Mol Biol , vol.11 , pp. 95-102
    • Stolk, J.1    Hiltermann, T.J.2    Dijkman, J.H.3    Verhoeven, A.J.4
  • 20
    • 33846025045 scopus 로고    scopus 로고
    • The oxidation of apocynin catalyzed by myeloperoxidase: Proposal for NADPH oxidase inhibition
    • DOI 10.1016/j.abb.2006.11.010, PII S0003986106004498
    • Ximenes VF, Kanegae MP, Rissato SR, Galhiane MS. The oxidation of apocynin catalyzed by myeloperoxidase: Proposal for NADPH oxidase inhibition. Arch Biochem Biophys 2007;457: 134-141 (Pubitemid 46048700)
    • (2007) Archives of Biochemistry and Biophysics , vol.457 , Issue.2 , pp. 134-141
    • Ximenes, V.F.1    Kanegae, M.P.P.2    Rissato, S.R.3    Galhiane, M.S.4
  • 21
    • 56149093044 scopus 로고    scopus 로고
    • NADPH oxidases in the vasculature: Molecular features, roles in disease and pharmacological inhibition
    • Selemidis S, Sobey CG, Wingler K, Schmidt HH, Drummond GR. NADPH oxidases in the vasculature: Molecular features, roles in disease and pharmacological inhibition. Pharmacol Ther 2008;120:254-291
    • (2008) Pharmacol Ther , vol.120 , pp. 254-291
    • Selemidis, S.1    Sobey, C.G.2    Wingler, K.3    Schmidt, H.H.4    Drummond, G.R.5
  • 22
    • 0035725015 scopus 로고    scopus 로고
    • NADH/NADPH oxidase and enhanced superoxide production in the mineralocorticoid hypertensive rat
    • Beswick RA, Dorrance AM, Leite R, Webb RC. NADH/NADPH oxidase and enhanced superoxide production in the mineralocorticoid hypertensive rat. Hypertension 2001;38:1107-1111 (Pubitemid 34252814)
    • (2001) Hypertension , vol.38 , Issue.5 , pp. 1107-1111
    • Beswick, R.A.1    Dorrance, A.M.2    Leite, R.3    Webb, R.C.4
  • 23
    • 0035980160 scopus 로고    scopus 로고
    • - and systolic blood pressure in mice
    • Rey FE, Cifuentes ME, Kiarash A, Quinn MT, Pagano PJ. Novel competitive inhibitor of NAD(P)H oxidase assembly attenuates vascular O(2)(-) and systolic blood pressure in mice. Circ Res 2001;89:408-414 (Pubitemid 34132656)
    • (2001) Circulation Research , vol.89 , Issue.5 , pp. 408-414
    • Rey, F.E.1    Cifuentes, M.E.2    Kiarash, A.3    Quinn, M.T.4    Pagano, P.J.5
  • 24
    • 4644363091 scopus 로고    scopus 로고
    • Gene transfer of NAD(P)H oxidase inhibitor to the vascular adventitia attenuates medial smooth muscle hypertrophy
    • DOI 10.1161/01.RES.0000142317.88591.e6
    • Liu J, Ormsby A, Oja-Tebbe N, Pagano PJ. Gene transfer of NAD(P) H oxidase inhibitor to the vascular adventitia attenuates medial smooth muscle hypertrophy. Circ Res 2004;95:587-594 (Pubitemid 39274373)
    • (2004) Circulation Research , vol.95 , Issue.6 , pp. 587-594
    • Liu, J.1    Ormsby, A.2    Oja-Tebbe, N.3    Pagano, P.J.4
  • 25
    • 0347063994 scopus 로고    scopus 로고
    • NAD(P)H oxidase inhibitor prevents blood pressure elevation and cardiovascular hypertrophy in aldosterone-infused rats
    • DOI 10.1016/j.bbrc.2003.11.173
    • Park YM, Park MY, Suh YL, Park JB. NAD(P)H oxidase inhibitor prevents blood pressure elevation and cardiovascular hypertrophy in aldosterone-infused rats. Biochem Biophys Res Commun 2004;313:812-817 (Pubitemid 38021903)
    • (2004) Biochemical and Biophysical Research Communications , vol.313 , Issue.3 , pp. 812-817
    • Park, Y.M.1    Park, M.Y.2    Suh, Y.-L.3    Park, J.B.4
  • 28
    • 0007619884 scopus 로고    scopus 로고
    • Systematic review of the efficacy and safety of perhexiline in the treatment of ischemic heart disease
    • Killalea SM, Krum H. Systematic review of the efficacy and safety of perhexiline in the treatment of ischemic heart disease. Am J Cardiovasc Drugs 2001;1:193-204
    • (2001) Am J Cardiovasc Drugs , vol.1 , pp. 193-204
    • Killalea, S.M.1    Krum, H.2
  • 30
    • 0023197795 scopus 로고
    • Inhibition by suramin of the NADPH oxidase from horse polymorphonuclear leukocytes
    • Heyneman RA. Inhibition by suramin of the NADPH oxidase from horse polymorphonuclear leukocytes. Vet Res Commun 1987;11:149-157 (Pubitemid 17136873)
    • (1987) Veterinary Research Communications , vol.11 , Issue.2 , pp. 149-157
    • Heyneman, R.A.1
  • 31
    • 85172045484 scopus 로고    scopus 로고
    • Suramin inhibits NADPH oxidase activity in cerebral arteries after subarachnoid hemorrhage
    • Sobey C, Chrissobolis S, Hickey H, Drummond G. Suramin inhibits NADPH oxidase activity in cerebral arteries after subarachnoid hemorrhage. FASEB J 2006;20:A725
    • (2006) FASEB J , vol.20
    • Sobey, C.1    Chrissobolis, S.2    Hickey, H.3    Drummond, G.4
  • 33
    • 33745189788 scopus 로고    scopus 로고
    • Novel Nox inhibitor VAS2870 attenuates PDGFdependent smooth muscle cell chemotaxis, but not proliferation
    • ten Freyhaus H, Huntgeburth M, Wingler K, Schnitker J, Bäumer AT, Vantler M et al. Novel Nox inhibitor VAS2870 attenuates PDGFdependent smooth muscle cell chemotaxis, but not proliferation. Cardiovasc Res 2006;71:331-341
    • (2006) Cardiovasc Res , vol.71 , pp. 331-341
    • Ten Freyhaus, H.1    Huntgeburth, M.2    Wingler, K.3    Schnitker, J.4    Bäumer, A.T.5    Vantler, M.6
  • 34
    • 0027262939 scopus 로고
    • 558 allows reconstitution of the phagocyte NADPH oxidase solely from recombinant proteins
    • Rotrosen D, Yeung CL, Katkin JP. Production of recombinant cytochrome b558 allows reconstitution of the phagocyte NADPH oxidase solely from recombinant proteins. J Biol Chem 1993;268:14256-14260. (Pubitemid 23195550)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.19 , pp. 14256-14260
    • Rotrosen, D.1    Yeung, C.L.2    Katkin, J.P.3
  • 35
    • 36048941952 scopus 로고    scopus 로고
    • Gene expression in mammalian cells using BacMam, a modified baculovirus system
    • DOI 10.1385/1-59745-457-5:95, Baculovirus and Insect Cell Expression Protocols, Second Edition
    • Fornwald JA, Lu Q, Wang D, Ames RS. Gene expression in mammalian cells using BacMam, a modified baculovirus system. Methods Mol Biol 2007;388:95-114 (Pubitemid 350189948)
    • (2007) Methods in Molecular Biology , vol.388 , pp. 95-114
    • Fornwald, J.A.1    Lu, Q.2    Wang, D.3    Ames, R.S.4
  • 36
    • 0029123886 scopus 로고
    • Reconstitution of cell-free NADPH oxidase activity by purified components
    • Abo A, Segal AW. Reconstitution of cell-free NADPH oxidase activity by purified components. Meth Enzymol 1995;256:268-278
    • (1995) Meth Enzymol , vol.256 , pp. 268-278
    • Abo, A.1    Segal, A.W.2
  • 37
    • 0035897653 scopus 로고    scopus 로고
    • Homologs of gp91phox: Cloning and tissue expression of Nox3, Nox4, and Nox5
    • DOI 10.1016/S0378-1119(01)00449-8, PII S0378111901004498
    • Cheng G, Cao Z, Xu X, van Meir EG, Lambeth JD. Homologs of gp91phox: Cloning and tissue expression of Nox3, Nox4, and Nox5. Gene 2001;269:131-140 (Pubitemid 32488913)
    • (2001) Gene , vol.269 , Issue.1-2 , pp. 131-140
    • Cheng, G.1    Cao, Z.2    Xu, X.3    Meir, E.G.V.4    Lambeth, J.D.5
  • 38
    • 0028893203 scopus 로고
    • Mouse model of X-linked chronic granulomatous disease, an inherited defect in phagocyte superoxide production
    • Pollock JD, Williams DA, Gifford MA, Li LL, Du X, Fisherman J et al. Mouse model of X-linked chronic granulomatous disease, an inherited defect in phagocyte superoxide production. Nat Genet 1995;9:202-209
    • (1995) Nat Genet , vol.9 , pp. 202-209
    • Pollock, J.D.1    Williams, D.A.2    Gifford, M.A.3    Li, L.L.4    Du, X.5    Fisherman, J.6
  • 42
    • 0035937784 scopus 로고    scopus 로고
    • Roles for β II-protein kinase C and RACK1 in positive and negative signaling for superoxide anion generation in differentiated HL60 cells
    • Korchak HM, Kilpatrick LE. Roles for β II-protein kinase C and RACK1 in positive and negative signaling for superoxide anion generation in differentiated HL60 cells. J Biol Chem 2001;276:8910-8917
    • (2001) J Biol Chem , vol.276 , pp. 8910-8917
    • Korchak, H.M.1    Kilpatrick, L.E.2
  • 43
    • 0023931716 scopus 로고
    • Sangivamycin, a nucleoside analogue, is a potent inhibitor of protein kinase C
    • Loomis CR, Bell RM. Sangivamycin, a nucleoside analogue, is a potent inhibitor of protein kinase C. J Biol Chem 1988;263: 1682-1692 (Pubitemid 18052115)
    • (1988) Journal of Biological Chemistry , vol.263 , Issue.4 , pp. 1682-1692
    • Loomis, C.R.1    Bell, R.M.2
  • 44
    • 30144442688 scopus 로고    scopus 로고
    • phox and can be rescued by exogenous arachidonic acid
    • DOI 10.1189/jlb.0705371
    • Kim C, Dinauer MC. Impaired NADPH oxidase activity in Rac2-deficient murine neutrophils does not result from defective translocation of p47phox and p67phox and can be rescued by exogenous arachidonic acid. J Leukoc Biol 2006;79:223-234 (Pubitemid 43054268)
    • (2006) Journal of Leukocyte Biology , vol.79 , Issue.1 , pp. 223-234
    • Kim, C.1    Dinauer, M.C.2
  • 46
    • 0027298410 scopus 로고
    • Suramin: A novel antineoplastic agent with multiple potential mechanisms of action
    • Stein CA. Suramin: A novel antineoplastic agent with multiple potential mechanisms of action. Cancer Res 1993;53:2239-2248 (Pubitemid 23156807)
    • (1993) Cancer Research , vol.53 , Issue.10 , pp. 2239-2248
    • Stein, C.A.1
  • 47
    • 0030602865 scopus 로고    scopus 로고
    • Inhibition of carnitine palmitoyltransferase-1 in rat heart and liver by perhexiline and amiodarone
    • DOI 10.1016/0006-2952(96)00204-3
    • Kennedy JA, Unger SA, Horowitz JD. Inhibition of carnitine palmitoyltransferase-1 in rat heart and liver by perhexiline and amiodarone. Biochem Pharmacol 1996;52:273-280 (Pubitemid 26233756)
    • (1996) Biochemical Pharmacology , vol.52 , Issue.2 , pp. 273-280
    • Kennedy, J.A.1    Unger, S.A.2    Horowitz, J.D.3
  • 48
    • 0024358286 scopus 로고
    • Response of isolated working hearts to fatty acids and carnitine palmitoyltransferase I inhibition during reduction of coronary flow in acutely and chronically diabetic rats
    • Lopaschuk GD, Spafford M. Response of isolated working hearts to fatty acids and carnitine palmitoyltransferase I inhibition during reduction of coronary flow in acutely and chronically diabetic rats. Circ Res 1989;65:378-387 (Pubitemid 19194624)
    • (1989) Circulation Research , vol.65 , Issue.2 , pp. 378-387
    • Lopaschuk, G.D.1    Spafford, M.2


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