Nox5 mediates PDGF-induced proliferation in human aortic smooth muscle cells
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The proliferation of vascular smooth muscle cells is important in the pathogenesis of many vascular diseases. Reactive oxygen species (ROS) produced by NADPH oxidases in smooth muscle cells have been shown to participate in signaling cascades regulating proliferation induced by platelet-derived growth factor (PDGF), a powerful smooth muscle mitogen. We sought to determine the role of Nox5 in the regulation of PDGF-stimulated human aortic smooth muscle cell (HASMC) proliferation. Cultured HASMC were found to express four isoforms of Nox5. When HASMC stimulated with PDGF were pretreated with N-acetyl cysteine (NAC), proliferation was significantly reduced. Proliferation induced by PDGF was also heavily dependent on JAK/STAT activation, as the JAK inhibitor, AG490, was able to completely abolish PDGF-stimulated HASMC growth. Specific knockdown of Nox5 with a siRNA strategy reduced PDGF-induced HASMC ROS production and proliferation. Additionally, siRNA to Nox5 inhibited PDGF-stimulated JAK2 and STAT3 phosphorylation. ROS produced by Nox5 play an important role in PDGF-induced JAK/STAT activation and HASMC proliferation.
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The particular architecture of NOX5 indicates a regulation of its activity through Ca2+ levels.
“As indicated above, the particular architecture of NOX5 indicates a regulation of its activity through Ca2+ levels (62, 469).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [469]
In human blood vessels, NOX5 is expressed in ECs and VSMCs.
“In human blood vessels, NOX5 is expressed in ECs and VSMCs (81, 469) (FIGURE 9, Table 5).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [469]
Cites
Sundaresan, M., Yu, Z.-X., Ferrans, V. J., Irani, K., & Finkel, T. (1995) · Science · doi:10.1126/science.270.5234.296 · Cited by 2,520 · see citing works
The JAK/STAT signaling pathway
Rawlings, J. S., Rosler, K. M., & Harrison, D. A. (2004) · Journal of Cell Science · doi:10.1242/jcs.00963 · Cited by 1,858 · see citing works
Ross, R., Glomset, J. A., Kariya, B., & Harker, L. A. (1974) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.71.4.1207 · Cited by 1,848 · see citing works
Inhibition of Neointimal Smooth Muscle Accumulation After Angioplasty by an Antibody to PDGF
Ferns, G. A., Raines, E. W., Sprugel, K. H., Motani, A. S., Reidy, M. A., & Ross, R. (1991) · Science · doi:10.1126/science.1653454 · Cited by 1,064 · see citing works
Lassègue, B., Sorescu, D., Szöcs, K., Yin, Q., Akers, M., Zhang, Y., Grant, S. L., Lambeth, J. D., & Griendling, K. K. (2001) · Circulation Research · doi:10.1161/hh0901.090299 · Cited by 839 · see citing works
Self-citationHomologs of gp91 phox : cloning and tissue expression of Nox3, Nox4, and Nox5
Cheng, G., Cao, Z., Xu, X., Meir, E. G. V., & Lambeth, J. D. (2001) · Gene · doi:10.1016/s0378-1119(01)00449-8 · Cited by 820 · see citing works
Cucoranu, I., Clempus, R., Dikalova, A., Phelan, P. J., Ariyan, S., Dikalov, S., & Sorescu, D. (2005) · Circulation Research · doi:10.1161/01.res.0000187457.24338.3d · Cited by 786 · see citing works
Self-citationA Ca2+-activated NADPH Oxidase in Testis, Spleen, and Lymph Nodes
Bánfi, B., Molnár, G., Maturana, A., Steger, K., Hegedûs, B., Demaurex, N., & Krause, K.-H. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m103034200 · Cited by 622 · see citing works
Activation of the JAK-STAT pathway by reactive oxygen species
Simon, A. R., Rai, U., Fanburg, B. L., & Cochran, B. (1998) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.1998.275.6.c1640 · Cited by 600 · see citing works
Distinct Subcellular Localizations of Nox1 and Nox4 in Vascular Smooth Muscle Cells
Hilenski, L. L., Clempus, R. E., Quinn, M. T., Lambeth, J. D., & Griendling, K. K. (2004) · Arteriosclerosis, Thrombosis, and Vascular Biology · doi:10.1161/01.atv.0000112024.13727.2c · Cited by 573 · see citing works
Self-citationMeasurement of Reactive Oxygen Species in Cardiovascular Studies
Dikalov, S., Griendling, K. K., & Harrison, D. G. (2007) · Hypertension · doi:10.1161/01.hyp.0000258594.87211.6b · Cited by 532 · see citing works
Self-citationPDGF and cardiovascular disease
Raines, E. W. (2004) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2004.03.004 · Cited by 484 · see citing works
Mechanism of Ca2+ Activation of the NADPH Oxidase 5 (NOX5)
Bánfi, B., Tirone, F., Durussel, I., Knisz, J., Moskwa, P., Molnár, G. Z., Krause, K.-H., & Cox, J. A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m310268200 · Cited by 389 · see citing works
Reactive oxygen species signaling in vascular smooth muscle cells
Clempus, R. E., & Griendling, K. K. (2006) · Cardiovascular Research · doi:10.1016/j.cardiores.2006.02.033 · Cited by 358 · see citing works
Self-citationNox4 Is Required for Maintenance of the Differentiated Vascular Smooth Muscle Cell Phenotype
Clempus, R. E., Sorescu, D., Dikalova, A., Pounkova, L., Jo, P. C., Sorescu, G. P., Lassegue, B. P., & Griendling, K. K. (2006) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.0000251500.94478.18 · Cited by 334 · see citing works
Self-citationNox/Duox family of nicotinamide adenine dinucleotide (phosphate) oxidases
Lambeth, J. D. (2002) · Current Opinion in Hematology · doi:10.1097/00062752-200201000-00003 · Cited by 282 · see citing works
Barraclough, B. M. (1976) · The Lancet · doi:10.1016/s0140-6736(76)92691-x · Cited by 279 · see citing works
NOX5 NAD(P)H oxidase regulates growth and apoptosis in DU 145 prostate cancer cells
Brar, S. S., Corbin, Z. A., Kennedy, T. P., Hemendinger, R. A., Thornton, L., Bommarius, B., Arnold, R. S., Whorton, A. R., Sturrock, A., Huecksteadt, T. P., et al. (2003) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00525.2002 · Cited by 259 · see citing works
NOX5 variants are functionally active in endothelial cells
BelAiba, R. S., Djordjevic, T., Petry, A., Diemer, K., Bonello, S., Banfi, B., Hess, J., Pogrebniak, A., Bickel, C., & Görlach, A. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2006.10.054 · Cited by 255 · see citing works
Novel Mechanism of Activation of NADPH Oxidase 5
Jagnandan, D., Church, J. E., Banfi, B., Stuehr, D. J., Marrero, M. B., & Fulton, D. J. R. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m608966200 · Cited by 210 · see citing works
Local Expression of Inflammatory Cytokines in Human Atherosclerotic Plaques
Wilcox, J. N., Nelken, N. A., Coughlin, S. R., Gordon, D., & Schall, T. J. (1994) · Journal of Atherosclerosis and Thrombosis · doi:10.5551/jat1994.1.supplemment1_s10 · Cited by 177 · see citing works
Sirois, M. G., Simons, M., & Edelman, E. R. (1997) · Circulation · doi:10.1161/01.cir.95.3.669 · Cited by 153 · see citing works
Fu, X., Beer, D. G., Behar, J., Wands, J. R., Lambeth, D. J., & Cao, W. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m603353200 · Cited by 130 · see citing works
Expression and Activity of NOX5 in the Circulating Malignant B Cells of Hairy Cell Leukemia
Kamiguti, A. S., Serrander, L., Lin, K., Harris, R. J., Cawley, J. C., Allsup, D. J., Slupsky, J. R., Krause, K., & Zuzel, M. (2005) · The Journal of Immunology · doi:10.4049/jimmunol.175.12.8424 · Cited by 117 · see citing works
Role of the JAK-STAT pathway in PDGF-stimulated proliferation of human airway smooth muscle cells
Simon, A. R., Takahashi, S., Severgnini, M., Fanburg, B. L., & Cochran, B. (2002) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00315.2001 · Cited by 110 · see citing works
NADPH oxidase 5 (NOX5) interacts with and is regulated by calmodulin
Tirone, F., & Cox, J. A. (2007) · FEBS Letters · doi:10.1016/j.febslet.2007.02.047 · Cited by 94 · see citing works
Kappert, K., Sparwel, J., Sandin, Å., Seiler, A., Siebolts, U., Leppänen, O., Rosenkranz, S., & Östman, A. (2006) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.0000246777.30819.85 · Cited by 75 · see citing works
Masamune, A. (2005) · World Journal of Gastroenterology · doi:10.3748/wjg.v11.i22.3385 · Cited by 56 · see citing works
Human monocyte-endothelial cell interaction induces platelet-derived growth factor expression
Funayama, H., Ikeda, U., Takahashi, M., Sakata, Y., Kitagawa, S., Takahashi, Y., Masuyama, J., Furukawa, Y., Miura, Y., Kano, S., et al. (1998) · Cardiovascular Research · doi:10.1016/s0008-6363(97)00224-1 · Cited by 48 · see citing works
Rutherford, C. L., Martin, W., CARRIER, M. J., Änggård, E., & Ferns, G. A. (1997) · International Journal of Experimental Pathology · doi:10.1046/j.1365-2613.1997.d01-237.x · Cited by 39 · see citing works
Noiseux, N., Boucher, C. H., Cartier, R., & Sirois, M. G. (2000) · Circulation · doi:10.1161/01.cir.102.11.1330 · Cited by 33 · see citing works
Nie, L., Mogami, H., Kanzaki, M., Shibata, H., & Kojima, I. (1996) · Molecular Pharmacology · doi:10.1016/s0026-895x(25)09376-9 · Cited by 31 · see citing works
Lee, J. S., Kypreos, K. E., & Sonenshein, G. E. (1998) · Experimental Cell Research · doi:10.1006/excr.1997.3919 · Cited by 21 · see citing works
Lamb, D. J., Avades, T. Y., & Ferns, G. A. (2001) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.21.6.997 · Cited by 21 · see citing works
Early PDGF-induced alterations in cytosolic free calcium are required for mitogenesis.
Diliberto, P. A., Hubbert, T., & Herman, B. A. (1991) · PubMed · Cited by 17 · see citing works
Seewald, S., Sachinidis, A., Seul, C., Kettenhofen, R. F., Ko, Y. D., & Vetter, H. (1997) · Journal of Hypertension · doi:10.1097/00004872-199715120-00071 · Cited by 14 · see citing works
Böhm, M., Blasius, S., & Roessner, A. (1994) · PubMed · Cited by 7 · see citing works
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Mittal, M., Siddiqui, M. R., Tran, K., Reddy, S. P., & Malik, A. B. (2014) · Antioxidants & Redox Signaling · doi:10.1089/ars.2012.5149 · Cited by 4,897 · see citing works
Combating oxidative stress in vascular disease: NADPH oxidases as therapeutic targets
Drummond, G. R., Selemidis, S., Griendling, K. K., & Sobey, C. G. (2011) · Nature Reviews Drug Discovery · doi:10.1038/nrd3403 · Cited by 899 · see citing works
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Brown, D., & Griendling, K. K. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.07.023 · Cited by 822 · see citing works
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Lassegue, B. P., Martín, A. S., & Griendling, K. K. (2012) · Circulation Research · doi:10.1161/circresaha.111.243972 · Cited by 768 · see citing works
Self-citationMitochondrial dynamics, mitophagy and cardiovascular disease
Vásquez-Trincado, C., García‐Carvajal, I., Pennanen, C., Parra, V., Hill, J. A., Rothermel, B. A., & Lavandero, S. (2015) · The Journal of Physiology · doi:10.1113/jp271301 · Cited by 625 · see citing works
NADPH Oxidases: Functions and Pathologies in the Vasculature
Lassègue, B., & Griendling, K. K. (2010) · Arteriosclerosis, Thrombosis, and Vascular Biology · doi:10.1161/atvbaha.108.181610 · Cited by 592 · see citing works
Self-citationSources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation
Tejero, J., Shiva, S., & Gladwin, M. T. (2019) · Physiological Reviews · doi:10.1152/physrev.00036.2017 · Cited by 541 · see citing works
NADPH oxidases and oxidase crosstalk in cardiovascular diseases: novel therapeutic targets
Zhang, Y., Murugesan, P., Huang, K., & Cai, H. “. (2019) · Nature Reviews Cardiology · doi:10.1038/s41569-019-0260-8 · Cited by 546 · see citing works
Reactive oxygen species and vascular biology: implications in human hypertension
Touyz, R. M., & Briones, A. M. (2010) · Hypertension Research · doi:10.1038/hr.2010.201 · Cited by 469 · see citing works
Solleiro-Villavicencio, H., & Rivas-Arancibia, S. (2018) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2018.00114 · Cited by 463 · see citing works
NADPH Oxidases in Vascular Pathology
Konior, A., Schramm‐Luc, A., Cześnikiewicz‐Guzik, M., & Guzik, T. J. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5607 · Cited by 451 · see citing works
Petsophonsakul, P., Furmanik, M., Forsythe, R. O., Dweck, M. R., Schurink, G. W. H., Natour, E., Reutelingsperger, C. P. M., Jacobs, M. J. H. M., Mees, B., & Schurgers, L. J. (2019) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.119.312787 · Cited by 344 · see citing works
Endothelial Dysfunction: Is There a Hyperglycemia-Induced Imbalance of NOX and NOS?
Meza, C. A., La Favor, J. D., Kim, D.-H., & Hickner, R. C. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20153775 · Cited by 323 · see citing works
Biochemical basis and metabolic interplay of redox regulation
Zhang, L., Wang, X., Cueto, R., Effi, C., Zhang, Y., Tan, H., Qin, X., Ji, Y., Yang, X., & Wang, H. (2019) · Redox Biology · doi:10.1016/j.redox.2019.101284 · Cited by 308 · see citing works
Montezano, A. C. I., & Touyz, R. M. (2011) · Basic & Clinical Pharmacology & Toxicology · doi:10.1111/j.1742-7843.2011.00785.x · Cited by 309 · see citing works
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Ghouleh, I. A., Khoo, N. K. H., Knaus, U. G., Griendling, K. K., Touyz, R. M., Thannickal, V. J., Barchowsky, A., Nauseef, W. M., Kelley, E. E., Bauer, P. M., et al. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.06.011 · Cited by 249 · see citing works
Self-citationRoy, K., Wu, Y., Meitzler, J. L., Juhasz, A. N., Liu, H., Jiang, G., Lu, J., Antony, S., & Doroshow, J. H. (2015) · Clinical Science · doi:10.1042/cs20140542 · Cited by 231 · see citing works
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Jha, J. C., Ho, F., Dan, C., & Jandeleit-Dahm, K. A. M. (2018) · Clinical Science · doi:10.1042/cs20171459 · Cited by 207 · see citing works
Furmanik, M., Chatrou, M. L. L., van Gorp, R. H., Akbulut, A. C., Willems, B. A. G., Schmidt, H. H. H. W., van Eys, G. J. J. M., Bochaton‐Piallat, M., Proudfoot, D., Biessen, E. A. L., et al. (2020) · Circulation Research · doi:10.1161/circresaha.119.316159 · Cited by 200 · see citing works
Oxidative stress, Noxs, and hypertension: Experimental evidence and clinical controversies
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Montezano, A. C., Burger, D., Paravicini, T. M., Chignalia, A. Z., Yusuf, H., Almasri, M., He, Y., Callera, G. E., He, G., Krause, K.-H., et al. (2010) · Circulation Research · doi:10.1161/circresaha.109.216036 · Cited by 188 · see citing works
From form to function: the role of Nox4 in the cardiovascular system
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NADPH oxidases as a source of oxidative stress and molecular target in ischemia/reperfusion injury
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Musset, B., Clark, R. A., DeCoursey, T. E., Petheö, G. L., Geiszt, M., Chen, Y., Cornell, J. E., Eddy, C. A., Brzyski, R. G., & Jamali, A. E. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.314955 · Cited by 168 · see citing works
NADPH oxidase-derived reactive oxygen species: involvement in vascular physiology and pathology
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Nox, Reactive Oxygen Species and Regulation of Vascular Cell Fate
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NOX and inflammation in the vascular adventitia
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Trebak, M., Ginnan, R. G., Singer, H. A., & Jourd’heuil, D. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2842 · Cited by 131 · see citing works
Nephropathy and Elevated BP in Mice with Podocyte-Specific NADPH Oxidase 5 Expression
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NOX5: Molecular biology and pathophysiology
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Reactive Oxygen Species (ROS), Intimal Thickening, and Subclinical Atherosclerotic Disease
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Nox as a target for diabetic complications
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NOX5: from basic biology to signaling and disease
Bedard, K., Jaquet, V., & Krause, K. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.11.023 · Cited by 120 · see citing works
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Song, P., & Zou, M. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.01.025 · Cited by 119 · see citing works
Parascandolo, A., & Laukkanen, M. O. (2018) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7268 · Cited by 117 · see citing works
Physiological roles of NOX/NADPH oxidase, the superoxide-generating enzyme
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Nox1, 2, 4, 5: Counting out oxidative stress
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Niu, X.-L., Madamanchi, N. R., Vendrov, A. E., Tchivilev, I., Rojas, M., Madamanchi, C., Brandes, R. P., Krause, K. H., Humphries, J., Smith, A., et al. (2010) · Circulation · doi:10.1161/circulationaha.109.908319 · Cited by 115 · see citing works
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Knock, G. A. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2019.09.029 · Cited by 108 · see citing works
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Katsuyama, M. (2010) · Journal of Pharmacological Sciences · doi:10.1254/jphs.10r01cr · Cited by 104 · see citing works
Comità, S., Femminò, S., Thairi, C., Alloatti, G., Boengler, K., Pagliaro, P., & Penna, C. R. R. (2021) · Basic Research in Cardiology · doi:10.1007/s00395-021-00898-0 · Cited by 97 · see citing works
Nitric oxide reduces NADPH oxidase 5 (Nox5) activity by reversible S-nitrosylation
Qian, J., Chen, F., Kovalenkov, Y. O., Pandey, D., Moseley, M. A., Foster, M. W., Black, S. M., Venema, R. C., Stepp, D. W., & Fulton, D. J. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.02.029 · Cited by 96 · see citing works
Pandey, D., Gratton, J.-P., Rafikov, R., Black, S. M., & Fulton, D. J. R. (2011) · Molecular Pharmacology · doi:10.1124/mol.110.070193 · Cited by 95 · see citing works
NOX signaling in molecular cardiovascular mechanisms involved in the blood pressure homeostasis
Santillo, M., Colantuoni, A., Mondola, P., Guida, B., & Damiano, S. (2015) · Frontiers in Physiology · doi:10.3389/fphys.2015.00194 · Cited by 95 · see citing works
NADPH Oxidases and Their Role in Atherosclerosis
Poznyak, A. V., Grechko, A. V., Orekhova, V. A., Khotina, V. A., Ivanova, E. A., & Orekhov, A. N. (2020) · Biomedicines · doi:10.3390/biomedicines8070206 · Cited by 95 · see citing works
Redox-mediated signal transduction by cardiovascular Nox NADPH oxidases
Brandes, R. P., Weißmann, N., & Schröder, K. (2014) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2014.02.006 · Cited by 92 · see citing works
The Hypoxia-Inducible Factor-2α Is Stabilized by Oxidative Stress Involving NOX4
Diebold, I., Flügel, D., Becht, S., BelAiba, R. S., Bonello, S., Hess, J., Kietzmann, T., & Görlach, A. (2010) · Antioxidants & Redox Signaling · doi:10.1089/ars.2009.3014 · Cited by 92 · see citing works
Oxidative Stress in Kidney Injury and Hypertension
Arendshorst, W. J., Vendrov, A. E., Kumar, N., Ganesh, S. K., & Madamanchi, N. R. (2024) · Antioxidants · doi:10.3390/antiox13121454 · Cited by 103 · see citing works
Differential regulation of Nox1, Nox2 and Nox4 in vascular smooth muscle cells from WKY and SHR
Briones, A. M., Tabet, F., Callera, G. E., Montezano, A. C. I., Yogi, Á., He, Y., Quinn, M. T., Salaíces, M., & Touyz, R. M. (2011) · Journal of the American Society of Hypertension · doi:10.1016/j.jash.2011.02.001 · Cited by 89 · see citing works
NADPH oxidase 4 mediates TGF-β-induced smooth muscle α-actin via p38MAPK and serum response factor
Martín-Garrido, A., Brown, D., Lyle, A. N., Dikalova, A., Seidel-Rogol, B. L., Lassegue, B. P., Martín, A. S., & Griendling, K. K. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.11.007 · Cited by 90 · see citing works
Self-citationReactive Oxygen Species in Vascular Formation and Development
Zhou, Y., Yan, H. M., Guo, M., Zhu, J., Xiao, Q., & Zhang, L. (2013) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2013/374963 · Cited by 85 · see citing works
Nediani, C., Raimondi, L., Borchi, E., & Cerbai, E. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3198 · Cited by 83 · see citing works
NADPH Oxidases NOXs and DUOXs as Putative Targets for Cancer Therapy
Weyemi, U., Redon, C. E., Parekh, P. R., Dupuy, C., & Bonner, W. M. (2013) · Anti-Cancer Agents in Medicinal Chemistry · doi:10.2174/1871520611313030013 · Cited by 85 · see citing works
The pathobiology of diabetic vascular complications—cardiovascular and kidney disease
Gray, S. P., & Jandeleit-Dahm, K. A. M. (2014) · Journal of Molecular Medicine · doi:10.1007/s00109-014-1146-1 · Cited by 83 · see citing works
Pandey, D., Patel, A., Patel, V., Chen, F., Qian, J., Wang, Y., Barman, S. A., Venema, R. C., Stepp, D. W., Daniel Rudic, R., et al. (2012) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00910.2011 · Cited by 81 · see citing works
Shao, B., & Bayraktutan, U. (2014) · Redox Biology · doi:10.1016/j.redox.2014.05.005 · Cited by 78 · see citing works
Opportunity Nox: The Future of NADPH Oxidases as Therapeutic Targets in Cardiovascular Disease
Streeter, J., Thiel, W. H., Brieger, K., & Miller, F. J. (2012) · Cardiovascular Therapeutics · doi:10.1111/j.1755-5922.2011.00310.x · Cited by 73 · see citing works
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 · see citing works
Montezano, A. C. I., Camargo, L. L., Persson, P., Rios, F. J. O., Harvey, A., Anagnostopoulou, A., Palacios, R., Gandara, A. C. P., Alves-Lopes, R., Neves, K. B., et al. (2018) · Journal of the American Heart Association · doi:10.1161/jaha.118.009388 · Cited by 72 · see citing works
Manea, A., Manea, S.-A., Gan, A. M., Constantin, A., Fenyo, I. M., Raicu, M., Muresian, H., & Simionescu, M. (2015) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2015.04.021 · Cited by 69 · see citing works
Koju, N., Taleb, A., Zhou, J., Ge, L., Yang, J., Cao, X., Lei, H., & Ding, Q. (2019) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2018.11.128 · Cited by 71 · see citing works
NADPH Oxidase as a Therapeutic Target for Oxalate Induced Injury in Kidneys
Joshi, S. K., Peck, A. B., & Khan, S. R. (2013) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2013/462361 · Cited by 69 · see citing works
Redox control of vascular smooth muscle cell function and plasticity
Durgin, B. G., & Straub, A. C. (2018) · Laboratory Investigation · doi:10.1038/s41374-018-0032-9 · Cited by 69 · see citing works
Hahn, N. E., Meischl, C., Kawahara, T., Musters, R. J. P., Verhoef, V. M. J., van der Velden, J., Vonk, A. B. A., Paulus, W. J., van Rossum, A. C., Niessen, H. W. M., et al. (2012) · The American Journal of Pathology · doi:10.1016/j.ajpath.2012.02.018 · Cited by 67 · see citing works
NOX 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 65 · see citing works
Kawahara, T., & Lambeth, J. D. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-12-1223 · Cited by 64 · see citing works
Tirone, F., Radu, L., Craescu, C. T., & Cox, J. A. (2010) · Biochemistry · doi:10.1021/bi901846y · Cited by 63 · see citing works
Current status of NADPH oxidase research in cardiovascular pharmacology
Álvarez, E., Rodiño-Janeiro, Paradela-Dobarro, Castiñeiras-Landeira, Raposeiras‐Roubín, S., & González‐Juanatey, J. R. (2013) · Vascular Health and Risk Management · doi:10.2147/vhrm.s33053 · Cited by 64 · see citing works
NOX5 and p22phox are 2 novel regulators of human monocytic differentiation into dendritic cells
Marzaioli, V., Hurtado-Nédelec, M., Pintard, C., Tlili, A., Marie, J., Monteiro, R. C., Gougerot‐Pocidalo, M., Dang, P. M., & Benna, J. E. (2017) · Blood · doi:10.1182/blood-2016-10-746347 · Cited by 62 · see citing works
NADPH Oxidase Inhibition: Preclinical and Clinical Studies in Diabetic Complications
Urner, S., Ho, F., Jha, J. C., Ziegler, D., & Jandeleit-Dahm, K. A. M. (2020) · Antioxidants and Redox Signaling · doi:10.1089/ars.2020.8047 · Cited by 64 · see citing works
The emerging role of NADPH oxidase NOX5 in vascular disease
Jha, J. C., Watson, A. M. D., Mathew, G., de Vos, L. C., & Jandeleit-Dahm, K. A. M. (2017) · Clinical Science · doi:10.1042/cs20160846 · Cited by 58 · see citing works
Antony, S., Wu, Y., Hewitt, S. M., Anver, M. R., Butcher, D. O., Jiang, G., Meitzler, J. L., Liu, H., Juhasz, A. N., Lu, J., et al. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.07.005 · Cited by 58 · see citing works
Molecular regulation of NADPH oxidase 5 via the MAPK pathway
Pandey, D., & Fulton, D. J. R. (2011) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.01163.2010 · Cited by 55 · see citing works
Nox5 Forms a Functional Oligomer Mediated by Self-Association of Its Dehydrogenase Domain
Kawahara, T., Jackson, H. M., Smith, S. M. E., Simpson, P. D., & Lambeth, J. D. (2011) · Biochemistry · doi:10.1021/bi1020088 · Cited by 55 · see citing works
Roles of Reactive Oxygen Species in Physiology and Pathology
Song, P., & Zou, M. (2015) · Atherosclerosis · doi:10.1002/9781118828533.ch30 · Cited by 55 · see citing works
Oxidative metabolism in cancer
Bourgeais, J., Gouilleux‐Gruart, V., & Gouilleux, F. (2013) · JAK-STAT · doi:10.4161/jkst.25764 · Cited by 54 · see citing works
NADPH Oxidases in Diastolic Dysfunction and Heart Failure with Preserved Ejection Fraction
Teuber, J. P., Essandoh, K., Hummel, S. L., Madamanchi, N. R., & Brody, M. J. (2022) · Antioxidants · doi:10.3390/antiox11091822 · Cited by 52 · see citing works
Unique role of NADPH oxidase 5 in oxidative stress in human renal proximal tubule cells
Yu, P., Han, W., Villar, V. A. M., Yang, Y., Lu, Q., Lee, H., Li, F., Quinn, M. T., Gildea, J. J., Felder, R. A., et al. (2014) · Redox Biology · doi:10.1016/j.redox.2014.01.020 · Cited by 53 · see citing works
Manea, A., Manea, S. A., Florea, I. C., Luca, C. M., & Raicu, M. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.02.018 · Cited by 52 · see citing works
Differential roles of NADPH oxidases in vascular physiology and pathophysiology
Griendling, K. K. (2012) · Frontiers in Bioscience-Scholar · doi:10.2741/s317 · Cited by 51 · see citing works
Self-citationNox and Inflammation in the Vascular Adventitia
Meijles, D. N., & Pagano, P. J. (2015) · Hypertension · doi:10.1161/hypertensionaha.115.03622 · Cited by 52 · see citing works
Linher‐Melville, K., & Singh, G. (2017) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2017.02.014 · Cited by 50 · see citing works
Stanić, B., Pandey, D., Fulton, D. J., & Miller, F. J. (2012) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.112.256107 · Cited by 49 · see citing works
Çevik, M. Ö., Katsuyama, M., Kanda, S., Kaneko, T., Iwata, K., Ibi, M., Matsuno, K., Kakehi, T., Cui, W., Sasaki, M., et al. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.07.027 · Cited by 43 · see citing works
Bonetti, J., Corti, A., Lerouge, L., Alfonso Pompella, C., & Gaucher, C. (2021) · Antioxidants · doi:10.3390/antiox10040516 · Cited by 43 · see citing works
The microbicidal and cytoregulatory roles of NADPH oxidases
Yang, H., Cheng, M., Ho, H., & Chiu, D. T.-Y. (2010) · Microbes and Infection · doi:10.1016/j.micinf.2010.10.008 · Cited by 43 · see citing works
NADPH oxidase 5 promotes proliferation and fibrosis in human hepatic stellate cells
Andueza, A., Garde, N., García-Garzón, A., Ansorena, E., López-Zabalza, M. J., Iraburu, M. J., Zalba, G., & Martínez-Irujo, J. J. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.07.013 · Cited by 42 · see citing works
- Authors
- Jay, D. B., Papaharalambus, C. A., Seidel-Rogol, B., Dikalova, A. E., Lassègue, B., & Griendling, K. K.
- Affiliations
- Emory University (US)
- Corresponding author
- Griendling, Kathy K.
- Venue
- Free Radical Biology and Medicine
- Publisher
- Elsevier BV
- Published
- 2008-08
- Volume
- 45
- Issue
- 3
- Pages
- 329-335
- ISSN
- 0891-5849 (ISSN-L)
- PMC
- PMC2459308
- OpenAlex
- W2049535510
- Cited by
- 166
- References
- 38
- Citations by year
- 2026: 1 · 2024: 4 · 2023: 4 · 2022: 9 · 2021: 3 · 2020: 6 · 2019: 9 · 2018: 12 · 2017: 8 · 2016: 2 · 2015: 12 · 2014: 15 · 2013: 18 · 2012: 18
- FWCI
- 10.16
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Free Radical Biology and Medicine (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health
- National Heart, Lung, and Blood Institute (HL058863, F32HL074604, HL074604, R01HL058863)
- Topics
- Health Sciences › Medicine › Physiology › Nitric Oxide and Endothelin Effects
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
- Keywords
- NADPH oxidase 5, platelet-derived growth factor, smooth muscle cell proliferation, human aortic smooth muscle cells, reactive oxygen species, NADPH oxidase, JAK/STAT signaling, JAK2 phosphorylation, STAT3 phosphorylation, N-acetylcysteine, siRNA knockdown, vascular smooth muscle
- MeSH terms
- NADPH Oxidase 5, Aorta, Cells, Cultured, Enzyme Inhibitors, Humans, Membrane Proteins, Muscle, Smooth, Vascular, Phosphorylation, Platelet-Derived Growth Factor, Transfection, Blotting, Western, Reactive Oxygen Species, NADPH Oxidases, Protein Isoforms, Myocytes, Smooth Muscle, Cell Proliferation, STAT3 Transcription Factor, Janus Kinase 2
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