메뉴 건너뛰기




Volumn 47, Issue 2, 2009, Pages 145-151

A role for NADPH oxidase 4 in the activation of vascular endothelial cells by oxidized phospholipids

Author keywords

Atherosclerosis; Endothelium; Free radicals; NOX4; Ox PAPC; Reactive oxygen species; VEGFR2

Indexed keywords

INTERLEUKIN 8; LOW DENSITY LIPOPROTEIN RECEPTOR; MONOCYTE CHEMOTACTIC PROTEIN 1; OXIDIZED 1 PALMITOYL 2 ARACHIDONYL SN GLYCEROL 3 PHOSPHORYLCHOLINE; PHOSPHOLIPID; PHOSPHORYLCHOLINE; PROTEIN P22; RAC1 PROTEIN; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE 4; UNCLASSIFIED DRUG; VASCULOTROPIN RECEPTOR 2;

EID: 67349208391     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2009.04.013     Document Type: Article
Times cited : (58)

References (43)
  • 5
    • 44649113051 scopus 로고    scopus 로고
    • Endothelial cell regulation by phospholipid oxidation products. Free Radic
    • Berliner J.A., and Gharavi N.M. Endothelial cell regulation by phospholipid oxidation products. Free Radic. Biol. Med. 45 (2008) 119-123
    • (2008) Biol. Med. , vol.45 , pp. 119-123
    • Berliner, J.A.1    Gharavi, N.M.2
  • 7
    • 27544456760 scopus 로고    scopus 로고
    • Oxidized-1-palmitoyl-2-arachidonoyl-sn-glycero-3-phosphorylcholine induces vascular endothelial superoxide production: implication of NADPH oxidase
    • Rouhanizadeh M., Hwang J., Clempus R.E., Marcu L., Lassegue B., Sevanian A., and Hsiai T.K. Oxidized-1-palmitoyl-2-arachidonoyl-sn-glycero-3-phosphorylcholine induces vascular endothelial superoxide production: implication of NADPH oxidase. Free Radic. Biol. Med. 39 (2005) 1512-1522
    • (2005) Free Radic. Biol. Med. , vol.39 , pp. 1512-1522
    • Rouhanizadeh, M.1    Hwang, J.2    Clempus, R.E.3    Marcu, L.4    Lassegue, B.5    Sevanian, A.6    Hsiai, T.K.7
  • 8
    • 33846794822 scopus 로고    scopus 로고
    • The NOX family of ROS-generating NADPH oxidases: physiology and pathophysiology
    • Bedard K., and Krause K.H. The NOX family of ROS-generating NADPH oxidases: physiology and pathophysiology. Physiol. Rev. 87 (2007) 245-313
    • (2007) Physiol. Rev. , vol.87 , pp. 245-313
    • Bedard, K.1    Krause, K.H.2
  • 9
    • 0038160993 scopus 로고    scopus 로고
    • Beyond LDL oxidation: ROS in vascular signal transduction
    • Chen K., Thomas S.R., and Keaney Jr. J.F. Beyond LDL oxidation: ROS in vascular signal transduction. Free Radic. Biol. Med. 35 (2003) 117-132
    • (2003) Free Radic. Biol. Med. , vol.35 , pp. 117-132
    • Chen, K.1    Thomas, S.R.2    Keaney Jr., J.F.3
  • 12
    • 8644255770 scopus 로고    scopus 로고
    • Assembly of the phagocyte NADPH oxidase
    • Nauseef W.M. Assembly of the phagocyte NADPH oxidase. Histochem. Cell Biol. 122 (2004) 277-291
    • (2004) Histochem. Cell Biol. , vol.122 , pp. 277-291
    • Nauseef, W.M.1
  • 15
    • 33745821178 scopus 로고    scopus 로고
    • Identification of the maturation factor for dual oxidase: evolution of an eukaryotic operon equivalent
    • Grasberger H., and Refetoff S. Identification of the maturation factor for dual oxidase: evolution of an eukaryotic operon equivalent. J. Biol. Chem. 281 (2006) 18269-18272
    • (2006) J. Biol. Chem. , vol.281 , pp. 18269-18272
    • Grasberger, H.1    Refetoff, S.2
  • 16
    • 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
  • 19
    • 0036510551 scopus 로고    scopus 로고
    • Epoxyisoprostane and epoxycyclopentenone phospholipids regulate monocyte chemotactic protein-1 and interleukin-8 synthesis: formation of these oxidized phospholipids in response to interleukin-1beta
    • Subbanagounder G., Wong J.W., Lee H., Faull K.F., Miller E., Witztum J.L., and Berliner J.A. Epoxyisoprostane and epoxycyclopentenone phospholipids regulate monocyte chemotactic protein-1 and interleukin-8 synthesis: formation of these oxidized phospholipids in response to interleukin-1beta. J. Biol. Chem. 277 (2002) 7271-7281
    • (2002) J. Biol. Chem. , vol.277 , pp. 7271-7281
    • Subbanagounder, G.1    Wong, J.W.2    Lee, H.3    Faull, K.F.4    Miller, E.5    Witztum, J.L.6    Berliner, J.A.7
  • 20
    • 0034665060 scopus 로고    scopus 로고
    • Role for peroxisome proliferator-activated receptor alpha in oxidized phospholipid-induced synthesis of monocyte chemotactic protein-1 and interleukin-8 by endothelial cells
    • Lee H., Shi W., Tontonoz P., Wang S., Subbanagounder G., Hedrick C.C., Hama S., Borromeo C., Evans R.M., Berliner J.A., and Nagy L. Role for peroxisome proliferator-activated receptor alpha in oxidized phospholipid-induced synthesis of monocyte chemotactic protein-1 and interleukin-8 by endothelial cells. Circ. Res. 87 (2000) 516-521
    • (2000) Circ. Res. , vol.87 , pp. 516-521
    • Lee, H.1    Shi, W.2    Tontonoz, P.3    Wang, S.4    Subbanagounder, G.5    Hedrick, C.C.6    Hama, S.7    Borromeo, C.8    Evans, R.M.9    Berliner, J.A.10    Nagy, L.11
  • 21
    • 0024242941 scopus 로고
    • Monocyte migration into the subendothelial space of a coculture of adult human aortic endothelial and smooth muscle cells
    • Navab M., Hough G.P., Stevenson L.W., Drinkwater D.C., Laks H., and Fogelman A.M. Monocyte migration into the subendothelial space of a coculture of adult human aortic endothelial and smooth muscle cells. J. Clin. Invest. 82 (1988) 1853-1863
    • (1988) J. Clin. Invest. , vol.82 , pp. 1853-1863
    • Navab, M.1    Hough, G.P.2    Stevenson, L.W.3    Drinkwater, D.C.4    Laks, H.5    Fogelman, A.M.6
  • 22
    • 33947164292 scopus 로고    scopus 로고
    • OKL38 is an oxidative stress response gene stimulated by oxidized phospholipids
    • Li R., Chen W., Yanes R., Lee S., and Berliner J.A. OKL38 is an oxidative stress response gene stimulated by oxidized phospholipids. J. Lipid Res. 48 (2007) 709-715
    • (2007) J. Lipid Res. , vol.48 , pp. 709-715
    • Li, R.1    Chen, W.2    Yanes, R.3    Lee, S.4    Berliner, J.A.5
  • 23
    • 38349132722 scopus 로고    scopus 로고
    • Amplification of CD95 activation by caspase 8-induced endosomal acidification in rat hepatocytes
    • Reinehr R., Sommerfeld A., Keitel V., Grether-Beck S., and Haussinger D. Amplification of CD95 activation by caspase 8-induced endosomal acidification in rat hepatocytes. J. Biol. Chem. 283 (2008) 2211-2222
    • (2008) J. Biol. Chem. , vol.283 , pp. 2211-2222
    • Reinehr, R.1    Sommerfeld, A.2    Keitel, V.3    Grether-Beck, S.4    Haussinger, D.5
  • 25
    • 47849120473 scopus 로고    scopus 로고
    • Superoxide dismutase 1 regulates caspase-1 and endotoxic shock
    • Meissner F., Molawi K., and Zychlinsky A. Superoxide dismutase 1 regulates caspase-1 and endotoxic shock. Nat. Immunol. 9 (2008) 866-872
    • (2008) Nat. Immunol. , vol.9 , pp. 866-872
    • Meissner, F.1    Molawi, K.2    Zychlinsky, A.3
  • 27
    • 0346750816 scopus 로고    scopus 로고
    • Pulsatile versus oscillatory shear stress regulates NADPH oxidase subunit expression: implication for native LDL oxidation
    • Hwang J., Ing M.H., Salazar A., Lassegue B., Griendling K., Navab M., Sevanian A., and Hsiai T.K. Pulsatile versus oscillatory shear stress regulates NADPH oxidase subunit expression: implication for native LDL oxidation. Circ. Res. 93 (2003) 1225-1232
    • (2003) Circ. Res. , vol.93 , pp. 1225-1232
    • Hwang, J.1    Ing, M.H.2    Salazar, A.3    Lassegue, B.4    Griendling, K.5    Navab, M.6    Sevanian, A.7    Hsiai, T.K.8
  • 29
    • 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., Wunsch S., Kreutz R., Rothermund L., Paul M., and 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. 31 (2001) 1456-1464
    • (2001) Free Radic. Biol. Med. , vol.31 , pp. 1456-1464
    • Wingler, K.1    Wunsch, S.2    Kreutz, R.3    Rothermund, L.4    Paul, M.5    Schmidt, H.H.6
  • 30
    • 0042379916 scopus 로고    scopus 로고
    • The vascular NAD(P)H oxidases as therapeutic targets in cardiovascular diseases
    • Cai H., Griendling K.K., and Harrison D.G. 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
  • 31
    • 0029151369 scopus 로고
    • Measurement of Rac translocation from cytosol to membranes in activated neutrophils
    • Quinn M.T., and Bokoch G.M. Measurement of Rac translocation from cytosol to membranes in activated neutrophils. Methods Enzymol. 256 (1995) 256-267
    • (1995) Methods Enzymol. , vol.256 , pp. 256-267
    • Quinn, M.T.1    Bokoch, G.M.2
  • 32
    • 0034677947 scopus 로고    scopus 로고
    • NAD(P)H oxidase: role in cardiovascular biology and disease
    • Griendling K.K., Sorescu D., and Ushio-Fukai M. 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
  • 33
    • 34249071326 scopus 로고    scopus 로고
    • VEGF signaling through NADPH oxidase-derived ROS
    • Ushio-Fukai M. VEGF signaling through NADPH oxidase-derived ROS. Antioxid. Redox Signal. 9 (2007) 731-739
    • (2007) Antioxid. Redox Signal. , vol.9 , pp. 731-739
    • Ushio-Fukai, M.1
  • 35
    • 34548443831 scopus 로고    scopus 로고
    • Vascular endothelial growth factor receptor-2: structure, function, intracellular signalling and therapeutic inhibition
    • Holmes K., Roberts O.L., Thomas A.M., and Cross M.J. Vascular endothelial growth factor receptor-2: structure, function, intracellular signalling and therapeutic inhibition. Cell. Signal. 19 (2007) 2003-2012
    • (2007) Cell. Signal. , vol.19 , pp. 2003-2012
    • Holmes, K.1    Roberts, O.L.2    Thomas, A.M.3    Cross, M.J.4
  • 38
    • 14544290505 scopus 로고    scopus 로고
    • Apocynin inhibits NADPH oxidase in phagocytes but stimulates ROS production in non-phagocytic cells
    • Vejrazka M., Micek R., and Stipek S. Apocynin inhibits NADPH oxidase in phagocytes but stimulates ROS production in non-phagocytic cells. Biochim. Biophys. Acta 1722 (2005) 143-147
    • (2005) Biochim. Biophys. Acta , vol.1722 , pp. 143-147
    • Vejrazka, M.1    Micek, R.2    Stipek, S.3
  • 39
    • 33646130154 scopus 로고    scopus 로고
    • The NADPH oxidase inhibitor apocynin (acetovanillone) induces oxidative stress
    • Riganti C., Costamagna C., Bosia A., and Ghigo D. The NADPH oxidase inhibitor apocynin (acetovanillone) induces oxidative stress. Toxicol. Appl. Pharmacol. 212 (2006) 179-187
    • (2006) Toxicol. Appl. Pharmacol. , vol.212 , pp. 179-187
    • Riganti, C.1    Costamagna, C.2    Bosia, A.3    Ghigo, D.4
  • 40
    • 33646348711 scopus 로고    scopus 로고
    • To be or not to be an oxidase: challenging the oxygen reactivity of flavoenzymes
    • Mattevi A. To be or not to be an oxidase: challenging the oxygen reactivity of flavoenzymes. Trends Biochem. Sci. 31 (2006) 276-283
    • (2006) Trends Biochem. Sci. , vol.31 , pp. 276-283
    • Mattevi, A.1
  • 41
    • 0036829501 scopus 로고    scopus 로고
    • Reaction of reduced flavins and flavoproteins with diphenyliodonium chloride
    • Chakraborty S., and Massey V. Reaction of reduced flavins and flavoproteins with diphenyliodonium chloride. J. Biol. Chem. 277 (2002) 41507-41516
    • (2002) J. Biol. Chem. , vol.277 , pp. 41507-41516
    • Chakraborty, S.1    Massey, V.2
  • 42
    • 33748751198 scopus 로고    scopus 로고
    • role for neutral sphingomyelinase activation in the inhibition of LPS action by phospholipid oxidation products
    • Walton K.A., Gugiu B.G., Thomas M., Basseri R.J., Eliav D.R., Salomon R.G., and Berliner J.A.A. role for neutral sphingomyelinase activation in the inhibition of LPS action by phospholipid oxidation products. J. Lipid Res. 47 (2006) 1967-1974
    • (2006) J. Lipid Res. , vol.47 , pp. 1967-1974
    • Walton, K.A.1    Gugiu, B.G.2    Thomas, M.3    Basseri, R.J.4    Eliav, D.R.5    Salomon, R.G.6    Berliner, J.A.A.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.