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A gp91phox Containing NADPH Oxidase Selectively Expressed in Endothelial Cells Is a Major Source of Oxygen Radical Generation in the Arterial Wall
Abstract
Abstract —Reactive oxygen species (ROS) play an important role in regulating vascular tone and intracellular signaling; the enzymes producing ROS in the vascular wall are, however, poorly characterized. We investigated whether a functionally active NADPH oxidase similar to the leukocyte enzyme, ie, containing the subunits p22phox and gp91phox, is expressed in endothelial cells (ECs) and smooth muscle cells (SMCs). Phorbol 12-myristate 13-acetate (PMA), a stimulus for leukocyte NADPH oxidase, increased ROS generation in cultured ECs and endothelium-intact rat aortic segments, but not in SMCs or endothelium-denuded arteries. NADPH enhanced chemiluminescence in all preparations. p22phox mRNA and protein was detected in ECs and SMCs, whereas the expression of gp91phox was confined to ECs. Endothelial gp91phox was identical to the leukocyte form as determined by sequence analysis. In contrast, mitogenic oxidase-1 (mox1) was expressed in SMCs, but not in ECs. To determine the functional relevance of gp91phox expression, experiments were performed in aortic segments from wild-type, gp91phox − /− , and endothelial NO synthase (eNOS) − /− mice. PMA-induced ROS generation was comparable in aortae from wild-type and eNOS − /− mice, but was attenuated in segments from gp91phox − /− mice. Endothelium-dependent relaxation was greater in aortae from gp91phox − /− than from wild-type mice. The ROS scavenger tiron increased endothelium-dependent relaxation in segments from wild-type, but not from gp91phox − /− mice. These data demonstrate that ECs, in contrast to SMCs, express a gp91phox-containing leukocyte-type NADPH oxidase. This enzyme is a major source for arterial ROS generation and affects the bioavailability of endothelium-derived NO. ( Circ Res. 2000;87:26-32.)
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“NOX2 expression has been also reported in other cell types including endothelial cells and adventitial fibroblasts (376, 382, 657, 714, 715, 736, 876) (FIGURE 9, Table 5).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [376]
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Cites
BABIOR, B. M. (1999) · Blood · doi:10.1182/blood.v93.5.1464 · Cited by 2,147
Cell transformation by the superoxide-generating oxidase Mox1
Suh, Y.-A., Arnold, R. S., Lassegue, B., Shi, J., Xu, X., Sorescu, D., Chung, A. B., Griendling, K. K., & Lambeth, J. D. (1999) · Nature · doi:10.1038/43459 · Cited by 1,480
An essential role for free radicals and derived species in signal transduction
Lander, H. M. (1997) · The FASEB Journal · doi:10.1096/fasebj.11.2.9039953 · Cited by 908
Royer-Pokora, B., Kunkel, L. M., Monaco, A. P., Goff, S. C., Newburger, P. E., Baehner, R. L., Cole, F. S., Curnutte, J. T., & Orkin, S. H. (1986) · Nature · doi:10.1038/322032a0 · Cited by 833
Xia, Y., Dawson, V. L., Dawson, T. M., Snyder, S. H., & Zweier, J. L. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.13.6770 · Cited by 717
Active oxygen species stimulate vascular smooth muscle cell growth and proto-oncogene expression.
Rao, G. N., & Berk, B. C. (1992) · Circulation Research · doi:10.1161/01.res.70.3.593 · Cited by 649
Role of NADH/NADPH Oxidase–Derived H 2 O 2 in Angiotensin II–Induced Vascular Hypertrophy
Zafari, A. M., Ushio‐Fukai, M., Akers, M., Yin, Q., Shah, A. A., Harrison, D. G., Taylor, W. R., & Griendling, K. K. (1998) · Hypertension · doi:10.1161/01.hyp.32.3.488 · Cited by 610
Expression of phagocyte NADPH oxidase components in human endothelial cells
Jones, S. A., O’Donnell, V. B., Wood, J. D., Broughton, J. P., Hughes, E. J., & Jones, O. T. (1996) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.1996.271.4.h1626 · Cited by 427
Dinauer, M. C., Pierce, E. A., Bruns, G. A. P., Curnutte, J. T., & Orkin, S. H. (1990) · Journal of Clinical Investigation · doi:10.1172/jci114898 · Cited by 334
Bouloumié, A., Bauersachs, J. K., Linz, W., Schölkens, B. A., Wiemer, G., Fleming, I., & Busse, R. (1997) · Hypertension · doi:10.1161/01.hyp.30.4.934 · Cited by 303
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Items 201–300 of 598
Ellis, A., & Triggle, C. R. (2003) · Canadian Journal of Physiology and Pharmacology · doi:10.1139/y03-106 · Cited by 96
Oxidative Stress and Endothelial Nitric Oxide Bioactivity
Thomas, S. R., Chen, K., & Keaney, J. F. (2003) · Antioxidants and Redox Signaling · doi:10.1089/152308603764816541 · Cited by 93
“2 that impaired NO bioactivity (35).”
Involvement of NADPH Oxidases in Cardiac Remodelling and Heart Failure
Sirker, A. A., Zhang, M., Murdoch, C. E., & Shah, A. M. (2007) · American Journal of Nephrology · doi:10.1159/000109148 · Cited by 93
Chen, J.-X., Zeng, H., Tuo, Q., Yu, H., Meyrick, B. O., & Aschner, J. L. (2007) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.01138.2006 · Cited by 93
“Many components of the phagocytic NADPH oxidase complex, including p22, p47, p67, gp91 and Rac1, have been identified in endothelial cells, cardiomyocytes and vascular smooth muscle cells (14-16; 33; 39).”
BackgroundNAD(P)H Oxidases and Their Relevance to Atherosclerosis
Sorescu, D. (2001) · Trends in Cardiovascular Medicine · doi:10.1016/s1050-1738(01)00097-4 · Cited by 91
Kane, N. M., Xiao, Q., Baker, A. H., Luo, Z., Xu, Q., & Emanueli, C. (2010) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2010.10.004 · Cited by 89
Zhao, W., Li, Y., Yang, S., Chen, Y., Zheng, J., Liu, C., Qing, Z., Li, J., & Yang, R. (2016) · Analytical Chemistry · doi:10.1021/acs.analchem.6b00521 · Cited by 90
Statins reduce vascular inflammation in atherogenesis: A review of underlying molecular mechanisms
Liberale, L., Carbone, F., Montecucco, F., & Sahebkar, A. (2020) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2020.105735 · Cited by 91
Paravicini, T. M., Gulluyan, L. M., Dusting, G. J., & Drummond, G. R. (2002) · Circulation Research · doi:10.1161/01.res.0000024106.81401.95 · Cited by 90
Noxa1 is a central component of the smooth muscle NADPH oxidase in mice
Ambasta, R. K., Schreiber, J. G., Janiszewski, M., Busse, R., & Brandes, R. P. (2006) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2005.12.035 · Cited by 89
Self-citationInvolvement of TRAF4 in Oxidative Activation of c-Jun N-terminal Kinase
Xu, Y. C., Wu, R. F., Gu, Y., Yang, Y. S., Yang, M.-C., Nwariaku, F. E., & Terada, L. S. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202665200 · Cited by 89
Mukherjee, T. K., Mukhopadhyay, S., & Hoidal, J. R. (2005) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2005.03.007 · Cited by 86
“Gp91phox is the catalytic subunit of the classical NADPH oxidase of phagocytes [45].”
Background[5] Detection of intracellular reactive oxygen species in cultured cells using fluorescent probes
Nègre‐Salvayre, A., Augè, N., Duval, C., Robbesyn, F., Thiers, J., Nazzal, D., Benoist, H., & Salvayre, R. (2002) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(02)52007-3 · Cited by 85
Nediani, C., Raimondi, L., Borchi, E., & Cerbai, E. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3198 · Cited by 83
“Nox2 (or gp91, the original neutrophil isoform) is expressed in endothelial cells (144, 223), cardiomyocytes (34, 162, 402), fibroblasts (292), and some ventricular smooth muscle cells (375).”
Differential vascular functions of Nox family NADPH oxidases
Brandes, R. P., & Schröder, K. (2008) · Current Opinion in Lipidology · doi:10.1097/mol.0b013e32830c91e3 · Cited by 86
Self-citationROS signalling, NADPH oxidases and cancer
Landry, W. D., & Cotter, T. G. (2014) · Biochemical Society Transactions · doi:10.1042/bst20140060 · Cited by 83
NADPH oxidase(s): new source(s) of reactive oxygen species in the vascular system?
van Heerebeek, L., Meischl, C., Stooker, W., Meijer, C. J. L. M., Niessen, H. W. M., & Roos, D. (2002) · Journal of Clinical Pathology · doi:10.1136/jcp.55.8.561 · Cited by 83
Sankaralingam, S., Xu, Y., Sawamura, T., & Davidge, S. T. (2008) · Hypertension · doi:10.1161/hypertensionaha.108.122630 · Cited by 82
Pircher, A., Treps, L., Bodrug, N., & Carmeliet, P. (2016) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2016.08.011 · Cited by 84
Increased oxidative stress during hyperglycemic cerebral ischemia
Bémeur, C., Ste-Marie, L.-G., & Montgomery, J. A. (2007) · Neurochemistry International · doi:10.1016/j.neuint.2007.03.002 · Cited by 82
A novel marine compound xyloketal B protects against oxidized LDL-induced cell injury in vitro
Chen, W.-L., Qian, Y., Meng, W.-F., Pang, J., Lin, Y., Guan, Y., Chen, S.-P., Liu, J., Pei, Z., & Wang, G. (2009) · Biochemical Pharmacology · doi:10.1016/j.bcp.2009.05.029 · Cited by 82
“A rapid post-translational activation and/or an increased expression of oxidase subunits can be involved in the upregulation of NADPH oxidase activity [32].”
BackgroundAngiopoietin-1-induced angiogenesis is modulated by endothelial NADPH oxidase
Chen, J., Zeng, H., Lawrence, M. L., Blackwell, T. S., & Meyrick, B. O. (2006) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.01081.2005 · Cited by 80
“Furthermore, endothelial cells release a small amount of ROS as signaling messengers to modulate vascular homeostasis (2, 13, 17, 38).”
BackgroundRedox sensitive signaling pathways in cardiac remodeling, hypertrophy and failure
Anilkumar, N. P. (2009) · Frontiers in bioscience · doi:10.2741/3443 · Cited by 81
“In addition to neutrophils, the Nox2 oxidase complex is now known to be also expressed in endothelial cells (29-31), cardiomyocytes (32,33), fibroblasts (34) and some vascular smooth muscle cells (VSMC) (35).”
BackgroundAntioxidant efficacy of vitamin D
Mokhtari, Z., Hekmatdoost, A., & Nourian, M. (2016) · Journal of Parathyroid Disease · Cited by 79
AN, S., BOYD, R., Zhu, M., CHAPMAN, A., Pimentel, D. R., & Wang, H. (2007) · Cardiovascular Research · doi:10.1016/j.cardiores.2007.02.015 · Cited by 77
“The adenovirus-trans- duced cells were stimulated with Ang II (100 nmol/L) and then collected for preproET-1, ET-1 peptide, superoxide and type I procollagen-α-I measurements.”
MethodLipid Raft Redox Signaling Platforms in Endothelial Dysfunction
Li, P., Zhang, Y., & Yi, F. (2007) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.1667 · Cited by 77
“:3) mice (32).”
Walch, L., Massaad-Massade, L., David‐Dufilho, M., Brunet, A., & Rendu, F. (2005) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2005.09.016 · Cited by 77
Ying, C., Xu, J., Ikeda, K., Takahashi, K., Nara, Y., & Yamori, Y. (2003) · Hypertension Research · doi:10.1291/hypres.26.823 · Cited by 76
“principal source of superoxide anion (16).”
Diebold, I., Djordjevic, T., Petry, A., Hatzelmann, A., Tenor, H., Hess, J., & Görlach, A. (2009) · Circulation Research · doi:10.1161/circresaha.109.196592 · Cited by 75
gp91phox Contributes to NADPH oxidase activity in aortic fibroblasts but not smooth muscle cells
Chamseddine, A. H., & Miller, F. J. (2003) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00459.2003 · Cited by 75
“(5) have shown that gp91phox is expressed and contributes to O2 production and intracellular signaling in endothelial cells.”
BackgroundResultInsulin resistance, lipotoxicity and endothelial dysfunction
Imrie, H., Abbas, A., & Kearney, M. T. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2009.09.025 · Cited by 74
Goettsch, C., Göettsch, W., Brux, M., Haschke, C., Brunßen, C., Müller, G. M., Bornstein, S. R., Duerrschmidt, N., Wagner, A. H., & Morawietz, H. (2011) · Basic Research in Cardiology · doi:10.1007/s00395-011-0170-3 · Cited by 75
“NADPH oxidase complexes have been described as major sources of reactive oxygen species in all vascular cells, which are important signaling molecules under physiological conditions [17].”
BackgroundKoay, M. A., Christman, J. W., Segal, B. H., Venkatakrishnan, A., Blackwell, T. R., Holland, S. M., & Blackwell, T. S. (2001) · Infection and Immunity · doi:10.1128/iai.69.10.5991-5996.2001 · Cited by 77
“While originally described in neutrophils and macrophages (1), NADPH oxidase has subsequently been defined in a variety of nonphagocytes, including smooth muscle cells, synoviocytes and chondrocytes (1), endothelial cells (16), and epithelial cells (15, 31).”
BackgroundColonic blood flow responses in experimental colitis: time course and underlying mechanisms
Mori, M., Stokes, K. Y., Vowinkel, T., Watanabe, N., Elrod, J. W., Harris, N. R., Lefer, D. J., Hibi∥, T., & Granger, D. N. (2005) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00247.2005 · Cited by 74
“Although both cell types possess NAD(P)H oxidase with a functional gp91 subunit (8, 10), neutrophilic NAD(P)H oxidase would be less likely to G1028 BLOOD FLOW AND COLITIS”
BackgroundDikalov, S., Li, W., Doughan, A. K., Blanco, R. R., & Zafari, A. M. (2012) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00842.2010 · Cited by 73
“Nox2, previously known as gp91, is present in endothelial and phagocytic cells and contributes to blood pressure regulation, inflammation, and cell growth (14, 19, 37, 40).”
Role of Nadph Oxidase in Atherosclerosis
Violi, F., Basili, S., Nigro, C., & Pignatelli, P. (2008) · Future Cardiology · doi:10.2217/14796678.5.1.83 · Cited by 73
Perner, A., Andresen, L. O., Pedersen, G., & Rask-Madsen, J. (2003) · Gut · doi:10.1136/gut.52.2.231 · Cited by 72
Herkert, O., Djordjevic, T., BelAiba, R. S., & Görlach, A. (2004) · Antioxidants and Redox Signaling · doi:10.1089/1523086041361695 · Cited by 72
Jones, C. I., Zhu, H., Martín, S. F., Han, Z., Li, Y., & Alevriadou, B. R. (2007) · Annals of Biomedical Engineering · doi:10.1007/s10439-007-9279-9 · Cited by 72
Organizers and activators: Cytosolic Nox proteins impacting on vascular function
Schröder, K., Weißmann, N., & Brandes, R. P. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.03.017 · Cited by 74
“By that mechanism, overproduction of •O2ˉ is rather detrimental to endothelial function [4,12], provides a pro-inflammatory stimulus and mediates uncoupling of endothelial nitric oxidase synthase (eNOS) [13].”
Self-citationNox4 overexpression activates reactive oxygen species and p38 MAPK in human endothelial cells
Goettsch, C., Göettsch, W., Müller, G. M., Seebach, J., Schnittler, H., & Morawietz, H. (2009) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2009.01.107 · Cited by 71
The HIF1 target geneNOX2promotes angiogenesis through urotensin-II
Diebold, I., Petry, A., Sabrane, K., Djordjevic, T., Hess, J., & Görlach, A. (2012) · Journal of Cell Science · doi:10.1242/jcs.094060 · Cited by 72
Angiotensin (1-7) and Alamandine: Similarities and differences
Qaradakhi, T., Apostolopoulos, V., & Zulli, A. (2016) · Pharmacological Research · doi:10.1016/j.phrs.2016.07.025 · Cited by 69
“…believed to occur mainly due to a reduction in the bio-availability of nitric oxide, possible due to an altered activity of endothelial nitric oxide synthase (eNOS) [8] or an over-activation of the protein kinase C (PKC) signalling pathway [9] coupled with an overproduction of superoxide [10, 11].”
Morawietz, H., Weber, M., Rueckschloss, U., Lauer, N., Hacker, A., & Kojda, G. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.5312 · Cited by 69
Extracellular Superoxide Dismutase Deficiency and Atherosclerosis in Mice
Sentman, M.-L., Brännström, T., Westerlund, S., Laukkanen, M. O., Ylä‐Herttuala, S., Basu, S., & Marklund, S. L. (2001) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/hq0901.094248 · Cited by 67
“SS/ee F 8† 8.666.4 (8) 10.463.0 ( 8 ) 0.660.3 (8) 1.560.2 (2) 2.960.4 (7) 27.564.4 (8)”
InfluentialRole of NADPH Oxidases in the Control of Vascular Gene Expression
Brandes, R. P. (2003) · Antioxidants and Redox Signaling · doi:10.1089/152308603770380115 · Cited by 67
“In addition to the nox homologues, p22phox has been detected by Western blot analysis and reverse transcription– polymerase chain reaction (RT-PCR) (29, 85, 89, 90) and shown to be involved in agonist-induced O 2 2 formation of VSMCs (9, 90, 93). p67phox, although essential for the activity of the…”
InfluentialSelf-citationShiner, M., Fuhrman, B., & Aviram, M. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.09.003 · Cited by 68
Molecular aspects of atherogenesis: new insights and unsolved questions
Puddu, G. M., Cravero, E., Arnone, G., Muscari, A., & Puddu, P. (2005) · Journal of Biomedical Science · doi:10.1007/s11373-005-9024-z · Cited by 69
Yoshida, L. S., & Tsunawaki, S. (2008) · International Immunopharmacology · doi:10.1016/j.intimp.2008.05.004 · Cited by 68
Thrombin Impairs Alveolar Fluid Clearance by Promoting Endocytosis of Na+,K+-ATPase
Vadász, I., Morty, R. E., Olschewski, A., Königshoff, M., Kohstall, M. G., Ghofrani, H. A., Grimminger, F., & Seeger, W. (2005) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2004-0407oc · Cited by 67
“Because thrombin signaling both induces ROS production in endothelial cells (55) and induces PKC- in endothelial cells (56), we reasoned that ROS and PKC- might be involved in the signal transduction pathway elicited by thrombin.”
BackgroundComposition and Functions of Vascular Nicotinamide Adenine Dinucleotide Phosphate Oxidases
Brandes, R. P., & Schröder, K. (2008) · Trends in Cardiovascular Medicine · doi:10.1016/j.tcm.2007.11.001 · Cited by 67
Self-citationSuperoxide and derived reactive oxygen species in the regulation of hypoxia-inducible factors
Görlach, A., & Kietzmann, T. (2007) · Methods in Enzymology · doi:10.1016/s0076-6879(07)35022-2 · Cited by 73
Calabriso, N., Massaro, M., Scoditti, E., D’Amore, S., Gnoni, A., Pellegrino, M., Storelli, C., Caterina, R. D., Palasciano, G., & Carluccio, M. A. (2015) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2015.09.026 · Cited by 68
“Each of these NADPH oxidase components has been identified in endothelial cells [9], which express also Nox4, a homologue of Nox2 [10].”
BackgroundRole of NOX2 in the regulation of afferent arteriole responsiveness
Carlström, M., Lai, E. Y., Ma, Z., Patzak, A., Brown, R. D., & Persson, A. E. G. (2009) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.90718.2008 · Cited by 65
“The latter is surprising as NOX2 is the most widely expressed NOX-isoform and significantly expressed in endothelial cells (10, 14, 21) and smooth muscle cells including renal vasculature (5, 7).”
BackgroundNOX Inhibitors: From Bench to Naxibs to Bedside
Elbatreek, M. H., Mucke, H. A., & Schmidt, H. H. H. W. (2020) · Handbook of experimental pharmacology · doi:10.1007/164_2020_387 · Cited by 68
Lysophosphatidylcholine Enhances Superoxide Anions Production via Endothelial NADH/NADPH Oxidase
Takeshita, S., Inoue, N., Gao, D., Rikitake, Y., Kawashima, S., Tawa, R., Sakurai, H., & Yokoyama, M. (2000) · Journal of Atherosclerosis and Thrombosis · doi:10.5551/jat1994.7.238 · Cited by 65
Kanie, N., Matsumoto, T., Kobayashi, T., & Kamata, K. (2003) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0705414 · Cited by 65
“…complex – including p22phox, p47phox, p67phox and gp91phox (or a related homologue) – have been identified in endothelial cells or vascular smooth muscle cells (Jones et al., 1996; Ushio-Fukai et al., 1996; Bayraktutan et al., 1998; Patterson et al., 1999; Gorlach et al., 2000).”
BackgroundKobayashi, S., Nojima, Y., Shibuya, M., & Maru, Y. (2004) · Experimental Cell Research · doi:10.1016/j.yexcr.2004.07.023 · Cited by 65
NADPH Oxidase 1 and Its Derived Reactive Oxygen Species Mediated Tissue Injury and Repair
Fu, X., Peng, Y.-B., Hu, Y.-P., Shi, Y.-Z., Yao, M., & Zhang, X. (2014) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2014/282854 · Cited by 66
Santos, D., Rafacho, B. P. M., Gonçalves, A. D. F., Jaldin, R. G., Bruder-Nascimento, T. B., Silva, M. A. B., Cáu, S. B. D. A., Roscani, M. G., Azevedo, P. S., Minicucci, M. F., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0098895 · Cited by 64
“NADPH oxidase complex is one of the most important of these sources and may be the largest producer of O2 2 in the vascular wall [66].”
BackgroundDistinct Regulatory Effects of Myeloid Cell and Endothelial Cell NAPDH Oxidase 2 on Blood Pressure
Sag, C. M., Schnelle, M., Zhang, J., Murdoch, C. E., Kossmann, S., Protti, A., Santos, C. X. C., Sawyer, G. J., Zhang, X., Mongue‐Din, H., et al. (2017) · Circulation · doi:10.1161/circulationaha.116.023877 · Cited by 62
The oxygen sensing signal cascade under the influence of reactive oxygen species
Acker, H. (2005) · Philosophical Transactions of the Royal Society B: Biological Sciences · doi:10.1098/rstb.2005.1760 · Cited by 63
NO Modulates Monocyte Chemotactic Protein-1 Expression in Endothelial Cells Under Cyclic Strain
Wung, B., Cheng, J., Shyue, S., & Wang, D. L. (2001) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/hq1201.099428 · Cited by 63
Benkhoff, S., Loot, A. E., Pierson, I., Sturza, A., Kohlstedt, K., Fleming, I., Shimokawa, H., Grisk, O., Brandes, R. P., & Schröder, K. (2012) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.112.251140 · Cited by 62
Self-citationYu, J., Weïwer, M., Linhardt, R. J., & Dordick, J. S. (2008) · Current Vascular Pharmacology · doi:10.2174/157016108784911984 · Cited by 62
“A number of studies support the presence of a functional NADPH oxidase in EC, which is capable of producing ROS and similar to that of phagocytes [96, 101-107].”
BackgroundResultInfluentialAssessment of Renal Functional Phenotype in Mice Lacking gp91 PHOX Subunit of NAD(P)H Oxidase
Haque, M. Z., & Majid, D. S. A. (2004) · Hypertension · doi:10.1161/01.hyp.0000111137.15873.4a · Cited by 63
Mechanisms for suppressing NADPH oxidase in the vascular wall
Dusting, G. J., Selemidis, S., & Jiang, F. (2005) · Memórias do Instituto Oswaldo Cruz · doi:10.1590/s0074-02762005000900016 · Cited by 62
“Third, whilst the Nox homologue and the membrane-bound p22phox subunit are essential to maintain a stable unit capable of supporting electron transfer for superoxide generation (Ambasta et al. 2004), it remains unclear what role the cytosolic components play in the vascular NADPH oxidase: this latter point has implica…”
BackgroundRole of NADPH Oxidase in Retinal Microvascular Permeability Increase by RAGE Activation
Warboys, C. M., Toh, H.-B., & Fraser, P. A. (2009) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.08-2730 · Cited by 61
“Endothelial cells express a gp91phox-containing NADPH oxidase (NOX2) responsible for significant ROS production in response to agonist stimulation.(27) Some evidence suggests that increased ROS generation by NADPH oxidase may play a significant role in the progression of diabetic microvascular complications.”
BackgroundLiu, W., Chen, Q., Liu, J., & Liu, K. (2011) · Medical Gas Research · doi:10.1186/2045-9912-1-22 · Cited by 61
“Deletion of Nox2 (or gp91) results in reduced BBB damage in mouse models of ischemic stroke [22-27].”
BackgroundHayashi, T., Yamashita, C., Matsumoto, C., Kwak, C.-J., Fujii, K., Hirata, T., Miyamura, M., Mori, T., Ukimura, A., Okada, Y., et al. (2008) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.91496.2007 · Cited by 61
“NADPH oxidase has been identified as a major source of reactive oxygen species, which might aggravate hypertrophy of cardiomyocytes and interstitial fibrosis, and has been expressed in several kinds of cells, including endothelial cells (10), fibroblasts (34), and cardiomyocytes (19, 25).”
BackgroundIntegrins and Coagulation: A Role for ROS/Redox Signaling?
Gregg, D., de Carvalho, D. D., & Kovacic, H. (2004) · Antioxidants and Redox Signaling · doi:10.1089/1523086041361604 · Cited by 61
Saad, M. I., Abdelkhalek, T. M., Saleh, M. M., Kamel, M. A. E.-N., Youssef, M., Tawfik, S. H., & Domínguez, H. (2015) · Endocrine · doi:10.1007/s12020-015-0709-4 · Cited by 61
“Both Nox2 and Nox4 are expressed in ECs [51–53].”
BackgroundChanges in the mucosa of the Roux‐limb after gastric bypass surgery
Spak, E., Björklund, P., Helander, H. F., Vieth, M. W., Olbers, T., Casselbrant, A., Lönroth, H., & Fändriks, L. (2010) · Histopathology · doi:10.1111/j.1365-2559.2010.03677.x · Cited by 59
Polytarchou, C., & Papadimitriou, Ε. (2005) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2005.01.004 · Cited by 58
Use of Rapid-Scan EPR to Improve Detection Sensitivity for Spin-Trapped Radicals
Mitchell, D. G., Rosen, G. M., Tseitlin, M., Symmes, B. A., Eaton, S. S., & Eaton, G. R. (2013) · Biophysical Journal · doi:10.1016/j.bpj.2013.06.005 · Cited by 59
Leung, J. W. C., Chung, S. S. M., & Chung, S. K. (2009) · Brain Research · doi:10.1016/j.brainres.2009.01.070 · Cited by 59
Kanie, N., & Kamata, K. (2002) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0704659 · Cited by 59
“…NADPHoxidase complex ± including p22phox, p47phox, p67phox and gp91phox (or a related homologue) ± have been identi®ed in endothelial cells or vascular smooth muscle cells (Jones et al., 1996; Bayraktutan et al., 1998; Gorlach et al., 2000; Patterson et al., 1999; Ushio-Fukai et al., 1996).”
BackgroundZhang, R., Thor, D., Han, X., Anderson, L. C., & Rahimian, R. (2012) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00327.2012 · Cited by 57
Richardson, R. T., Ballinger, M. N., Qian, F., Christman, J. W., & Johnson, R. M. (2018) · Apidologie · doi:10.1007/s13592-018-0566-2 · Cited by 56
“On a 60-s time stagger, cells were stimulated through addition of 20 μL of insect medium containing 2 μL of 1000 μM H2DCFDA dye and 2 μL of 2 mg/mL PMA (Alfa Aesar, Fisher Scientific, Hampton, NH, USA) in dimethyl sulfoxide (DMSO) (ACS Reagent Grade, Fisher Scientific, Hampton, NH, USA).”
MethodInfluentialNg, D. S., Maguire, G. F., Wylie, J. G., Ravandi, A., Xuan, W., Ahmed, Z., Eskandarian, M. R., Kuksis, A., & Connelly, P. W. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m112320200 · Cited by 57
Suppression of Oxidative Stress in the Endothelium and Vascular Wall
Jiang, F., Drummond, G. R., & Dusting, G. J. (2004) · Endothelium · doi:10.1080/10623320490482600 · Cited by 57
“A gp91phox-containing NADPH oxidase also appears to be involved in ROS production in endothelial cells and adventitial fibroblasts because cultures of these cells derived from gp91phox-deficient (gp91phox−/−) mice fail to generate superoxide in response to known stimuli of leucocyte NADPH oxidase (Gorlach et al. 2000;…”
InfluentialTreatment with 17-β-estradiol reduces superoxide production in aorta of ovariectomized rats
Florian, M., Freiman, A., & Magder, S. A. (2004) · Steroids · doi:10.1016/j.steroids.2004.09.008 · Cited by 56
Park, M., Hennig, B., & Toborek, M. J. (2011) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2011.01320.x · Cited by 55
“Similar to the leukocyte form, NOX expressed in endothelial cells contains both gp91 and p22 [19], that is, the subunits that binding to p47 was increased in hCMEC/D3 cells in response to METH treatment in this study (Fig.”
BackgroundPark, L., Anrather, J., Zhou, P., Frys, K. A., Wang, G., & Iadecola, C. (2004) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.0000142446.75898.44 · Cited by 55
Li, J., Mullen, A. M., & Shah, A. M. (2001) · Journal of Molecular and Cellular Cardiology · doi:10.1006/jmcc.2001.1372 · Cited by 54
Role of NADPH oxidase-derived superoxide in reduced size liver ischemia and reperfusion injury
Harada, H., Hines, I. N., Flores, S. C., Gao, B., McCord, J. M., Scheerens, H., & Grisham, M. B. (2003) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2003.08.035 · Cited by 54
Lin, F., Chen, Y., Chen, Y., Wu, T.-C., Li, C., Chen, J., & Lin, S. (2007) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf062945r · Cited by 54
Redox Signaling through NADPH Oxidases: Involvement in Vascular Proliferation and Coagulation
Görlach, A., Kietzmann, T., & Hess, J. (2002) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2002.tb04691.x · Cited by 53
Nox and Inflammation in the Vascular Adventitia
Meijles, D. N., & Pagano, P. J. (2015) · Hypertension · doi:10.1161/hypertensionaha.115.03622 · Cited by 54
“Nox2 [27,54-56] ND [40] or low [67] [65] [9,59]”
BackgroundMethodInfluentialEffect of NADPH oxidase inhibition on cardiopulmonary bypass-induced lung injury
Dodd‐o, J. M., Welsh, L. E., Salazar, J. D., Walinsky, P. L., Peck, E. A., Shake, J. G., Caparrelli, D. J., Ziegelstein, R. C., Zweier, J. L., Baumgartner, W. A., et al. (2004) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.01138.2003 · Cited by 52
“The endothelial form of the enzyme appears to differ by having an intracellular location, constitutive activity, and lower ROS production (23, 35, 54).”
Regulation of postischemic liver injury following different durations of ischemia
Hines, I. N., Hoffman, J. M., Scheerens, H., Day, B. J., Harada, H., Pavlick, K. P., Bharwani, S., Wolf, R., Gao, B., Flores, S. C., et al. (2003) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00400.2002 · Cited by 53
ROS-Induced Endothelial Dysfunction in the Pathogenesis of Atherosclerosis
Yan, R., Zhang, X., Xu, W., Li, J., Sun, Y., Cui, S., Xu, R., Li, W., Jiao, L., & Wang, T. (2024) · Aging and Disease · doi:10.14336/ad.2024.0309 · Cited by 54
Nam, S. M., Lee, E. Y., Koh, J. H., Park, J. H., Shin, J. Y., Shin, Y. G., Koh, S. B., Lee, E. Y., & Chung, C. H. (2008) · Diabetes Research and Clinical Practice · doi:10.1016/j.diabres.2008.10.007 · Cited by 51
Heo, K., Berk, B. C., & Abe, J. (2015) · Antioxidants and Redox Signaling · doi:10.1089/ars.2015.6556 · Cited by 51
“Among various ROS-producing enzymes, NADPH oxidase 4 has been identified as the major ROS-producing enzyme generated in blood vessels in response to d-flow (42).”
BackgroundCerebral vascular effects of reactive oxygen species: Recent evidence for a role of NADPH‐oxidase
Paravicini, T. M., & Sobey, C. G. (2003) · Clinical and Experimental Pharmacology and Physiology · doi:10.1046/j.1440-1681.2003.03920.x · Cited by 50
Jung, O., Marklund, S. L., Xia, N., Busse, R., & Brandes, R. P. (2006) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.0000254823.15843.1f · Cited by 51
Self-citationJuan, S., Chen, J.-J., Chen, C., Lin, H., Cheng, C., Liu, J., HSIEH, M., Chen, Y., Chao, H., Chen, T.-H., et al. (2004) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00723.2003 · Cited by 51
“There appears to be mounting evidence that NADPH oxidase, a major source of ROS, within endothelial cells (10, 27), plays a critical role in the development of atherosclerosis (28).”
BackgroundCyclic Strain Activates Redox-sensitive Proline-rich Tyrosine Kinase 2 (PYK2) in Endothelial Cells
Cheng, J., Chao, Y., & Wang, D. L. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m110937200 · Cited by 51
Porwol, T., Ehleben, W., Brand, V. B., & Acker, H. (2001) · Respiration Physiology · doi:10.1016/s0034-5687(01)00310-3 · Cited by 51
Resveratrol and curcumin reduce the respiratory burst of Chlamydia-primed THP-1 cells
Deby-Dupont, G. P., Mouithys-Mickalad, A. A., Serteyn, D., Lamy, M., & Deby, C. M. T. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.05.073 · Cited by 50
“NOX is considered as the major source of ROS in the arterial walls [8].”
Background
Metadata
- Authors
- Görlach, A., Brandes, R. P., Nguyen, K., Amidi, M., Dehghani, F., & Busse, R.
- Affiliations
- From the Institut für Kardiovaskuläre Physiologie (A.G., R.P.B., K.N., M.A., R.B.), and Institut für Anatomie II (F.D.), Klinikum der J.W. Goethe-Universität, Frankfurt/Main, Germany.
- Goethe University Frankfurt (DE)
- Corresponding author
- Brandes, R. P.
- Venue
- Circulation Research
- Published
- 2000-07-07
- Volume
- 87
- Issue
- 1
- Pages
- 26-32
- ISSN
- 0009-7330 (ISSN-L)
- 1524-4571
- OpenAlex
- W2169235788
- Cited by
- 598
- References
- 28
- Citations by year
- 2026: 3 · 2024: 4 · 2023: 5 · 2022: 14 · 2021: 12 · 2020: 8 · 2019: 11 · 2018: 10 · 2017: 17 · 2016: 23 · 2015: 13 · 2014: 25 · 2013: 18 · 2012: 28
- FWCI
- 26.10
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Circulation Research (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Deutscher Akademischer Austauschdienst
- Deutsche Forschungsgemeinschaft (SFB 553, TP B1)
- Genentech
- Topics
- Health Sciences › Medicine › Physiology (medical) › Nitric Oxide and Endothelin Effects
- Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Keywords
- gp91phox, NADPH oxidase, endothelial cells, reactive oxygen species, oxygen free radicals, arterial wall, smooth muscle cells, p22phox, endothelium-dependent relaxation, nitric oxide bioavailability, endothelial nitric oxide synthase, chemiluminescence, Tiron, aorta
- MeSH terms
- NADPH Oxidase 2, Acetylcholine, Animals, Aorta, Endothelium, Vascular, Free Radicals, Membrane Glycoproteins, Muscle, Smooth, Vascular, Nitric Oxide, Tetradecanoylphorbol Acetate, Reactive Oxygen Species, NADPH Oxidases, Reverse Transcriptase Polymerase Chain Reaction, Mice, Rats
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