The DOI matches its Crossref record; 48 of the 48 references it cites were found in a registry or an index.
Localization of a constitutively active, phagocyte-like NADPH oxidase in rabbit aortic adventitia: Enhancement by angiotensin II
Open accessAbstract
Superoxide anion (O 2 − ) plays a key role in the endogenous suppression of endothelium-derived nitric oxide (NO) bioactivity and has been implicated in the development of hypertension. In previous studies, we found that O 2 − is produced predominantly in the adventitia of isolated rabbit aorta and acts as a barrier to NO. In the present studies, we characterize the enzyme responsible for O 2 − production in the adventitia and show that this enzyme is a constitutively active NADPH oxidase with similar composition as the phagocyte NADPH oxidase. Constitutive O 2 − -generating activity was localized to aortic adventitial fibroblasts and was enhanced by the potent vasoconstrictor angiotensin II. Immunohistochemistry of aortic sections demonstrated the presence of p22 phox , gp91 phox , p47 phox , and p67 phox localized exclusively in rabbit aortic adventitia, coincident with the site of staining for O 2 − production. Furthermore, immunodepletion of p67 phox from adventitial fibroblast particulates resulted in the loss of NADPH oxidase activity, which could be restored by the addition of recombinant p67 phox . Further study into the regulation of this adventitial source of O 2 − is important in elucidating the mechanisms regulating the bioactivity of NO and may contribute to our understanding of the pathogenesis of hypertension.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“but CO can also be, in low concentrations, a signaling molecule (713, 739, 805, 807).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [713]
In the citing paper
“High levels of HO-1 are present in the spleen, consistent with an important role in the processing of heme from red blood cell turnover (713, 805).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [713]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Angiotensin II stimulates NADH and NADPH oxidase activity in cultured vascular smooth muscle cells.
Griendling, K. K., Minieri, C. A., Ollerenshaw, J. D., & Alexander, R. W. (1994) · Circulation Research · doi:10.1161/01.res.74.6.1141 · Cited by 2,735
Rajagopalan, S., Kurz, S. D., Münzel, T. F., Tarpey, M. M., Freeman, B. Α., Griendling, K. K., & Harrison, D. G. (1996) · Journal of Clinical Investigation · doi:10.1172/jci118623 · Cited by 2,467
Mitogenic Signaling Mediated by Oxidants in Ras-Transformed Fibroblasts
Irani, K., Xia, Y., Zweier, J. L., Sollott, S. J., Der, C. J., Fearon, E. R., Sundaresan, M., Finkel, T., & Goldschmidt-Clermont, P. J. (1997) · Science · doi:10.1126/science.275.5306.1649 · Cited by 1,588
Role of Superoxide in Angiotensin II–Induced but Not Catecholamine-Induced Hypertension
Laursen, J. B., Rajagopalan, S., Galis, Z. S., Tarpey, M. M., Freeman, B. Α., & Harrison, D. G. (1997) · Circulation · doi:10.1161/01.cir.95.3.588 · Cited by 820
Ushio‐Fukai, M., Zafari, A. M., Fukui, T., Ishizaka, N., & Griendling, K. K. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.38.23317 · Cited by 766
Regulation of Phagocyte Oxygen Radical Production by the GTP-Binding Protein Rac 2
Knaus, U. G., Heyworth, P. G., Evans, T., Curnutte, J. T., & Bokoch, G. (1991) · Science · doi:10.1126/science.1660188 · Cited by 673
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
Coxon, A., Rieu, P., Barkalow, F. J., Askari, S., Sharpe, A. H., von Andrian, U. H., Arnaout, M. A., & Mayadas, T. N. (1996) · Immunity · doi:10.1016/s1074-7613(00)80278-2 · Cited by 627
Modulation of fibroblast proliferation by oxygen free radicals
Murrell, G. A. C., Francis, M. J. O., & Bromley, L. (1990) · Biochemical Journal · doi:10.1042/bj2650659 · Cited by 625
NADH oxidoreductase is a major source of superoxide anion in bovine coronary artery endothelium
Mohazzab, K. M., Kaminski, P. M., & Wolin, M. S. (1994) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.1994.266.6.h2568 · Cited by 536
Research works printed but not linked: 7
- R A Miller, B E Brittigan J Invest Med 43, 39–49 (1995).
- K M Mohazzab, M S Wolin Am J Physiol 267, L815–L822 (1994).
- K M Mohazzab, P M Kaminski, M S Wolin Am J Physiol 266, H2568–H2572 (1994).
- S A Jones, V B O’Donnell, J D Wood, J D Broughton, E J Hughes, O T G Jones Am J Physiol 271, H1626–H1634 (1996).
- P J Pagano, Y Ito, K Tornheim, P M Gallop, A I Tauber, R A Cohen Am J Physiol 268, H2274–H2280 (1995).
- H Wang, P J Pagano, Y Du, A J Cayatte, P Brecher, R A Cohen FASEB J 11, A477 (1997).
- G W Hacker, I Zehbe, W H Muss, C Hauser-Kronberger, A-H Graf, O Dietze CellVision 2, 247–253 (1995).
Cited by
Sorted by citations
Items 201–300 of 453
Regression of Atherosclerosis in Monkeys Reduces Vascular Superoxide Levels
Hathaway, C. A., Heistad, D. D., Piegors, D. J., & Miller, F. J. (2002) · Circulation Research · doi:10.1161/hh0302.104724 · Cited by 76
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
Nogueira‐Machado, J. A., & Chaves, M. M. (2008) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.12.7.871 · Cited by 74
Activation of AP-1 through reactive oxygen species by angiotensin II in rat cardiomyocytes
WU, S., Gao, J., Ohlemeyer, C., Roos, D., Niessen, H. W. M., Köttgen, E., & Gessner, R. V. (2005) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2005.08.006 · Cited by 75
Zhao, M., Wimmer, A., Trieu, K., DiScipio, R. G., & Schraufstätter, I. U. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m405118200 · Cited by 72
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 74
Effects and Mechanisms of Tea Regulating Blood Pressure: Evidences and Promises
Li, D., Wang, R., Huang, J., Cai, Q., Yang, C. S., Wan, X., & Xie, Z. (2019) · Nutrients · doi:10.3390/nu11051115 · Cited by 78
Cigarette smoke condensate induces MMP-12 gene expression in airway-like epithelia
Lavigne, M. C., & Eppihimer, M. J. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.02.144 · Cited by 75
de Souza, H. P., Laurindo, F. R. M., Ziegelstein, R. C., Berlowitz, C. O., & Zweier, J. L. (2001) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.2001.280.2.h658 · Cited by 73
Akasaki, T., Ohya, Y., Kuroda, J., Eto, K., Abe, I., Sumimoto, H., & Iida, M. (2006) · Hypertension Research · doi:10.1291/hypres.29.813 · Cited by 70
Oxidative Stress and Lipid Retention in Vascular Grafts
Shi, Y., Patel, S. R., Davenpeck, K. L., Niculescu, R., Rodriguez, E., Magno, M. G., Ormont, M. L., Mannion, J. D., & Zalewski, A. A. (2001) · Circulation · doi:10.1161/01.cir.103.19.2408 · Cited by 69
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
Molecular and biochemical changes of the cardiovascular system due to smoking exposure
Armani, C., Landini Jr., L., & Leone, A. (2009) · Current Pharmaceutical Design · doi:10.2174/138161209787846973 · Cited by 68
Role 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
Oxidative Stress and Diabetic Complications: The Role of Antioxidant Vitamins and Flavonoids
Omolola, R., Nicole, L., & Oluwafemi, O. S. (2014) · InTech eBooks · doi:10.5772/57282 · Cited by 73
TNFα Activates c-Jun Amino Terminal Kinase through p47phox
Gu, Y., Xu, Y. C., Wu, R. F., Souza, R. F., Nwariaku, F. E., & Terada, L. S. (2002) · Experimental Cell Research · doi:10.1006/excr.2001.5404 · Cited by 67
Altitude as a risk factor for congenital anomalies
Castilla, E. E., López‐Camelo, J. S., & Campa�a, H. (1999) · American Journal of Medical Genetics · doi:10.1002/(sici)1096-8628(19990903)86:1 · Cited by 147
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
Estrogen Inhibits Vascular Smooth Muscle Cell–Dependent Adventitial Fibroblast Migration In Vitro
Li, G., Chen, Y.-F., Greene, G. L., Oparil, S., & Thompson, J. A. (1999) · Circulation · doi:10.1161/01.cir.100.15.1639 · Cited by 64
Yu, J., Weïwer, M., Linhardt, R. J., & Dordick, J. S. (2008) · Current Vascular Pharmacology · doi:10.2174/157016108784911984 · Cited by 62
Chronic Hypoxia Accelerates the Progression of Atherosclerosis in Apolipoprotein E-Knockout Mice
Nakano, D., Hayashi, T., Tazawa, N., Yamashita, C., Inamoto, S., Okuda, N., Mori, T., Sohmiya, K., Kitaura, Y., Okada, Y., et al. (2005) · Hypertension Research · doi:10.1291/hypres.28.837 · Cited by 62
The Role of Nox4 in Oxidative Stress–Induced MUC5AC Overexpression in Human Airway Epithelial Cells
Kim, H. J., Park, Y.-D., Moon, U. Y., Jun-Hee, K., Jeon, J. H., Lee, J., Bae, Y. S., & Yoon, J. (2008) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2007-0262oc · Cited by 61
The Local Regulation of Vascular Function: From an Inside-Outside to an Outside-Inside Model
Nava, E., & Llorens, S. (2019) · Frontiers in Physiology · doi:10.3389/fphys.2019.00729 · Cited by 62
Nitric oxide and renal and cardiac dysfunction in cirrhosis
García‐Estañ, J., Ortíz, M. C., & Lee, S. S. (2002) · Clinical Science · doi:10.1042/cs1020213 · Cited by 61
Interaction between nitric oxide and oxygen radicals in regulation of tubuloglomerular feedback
Wilcox, & Welch (2000) · Acta Physiologica Scandinavica · doi:10.1046/j.1365-201x.2000.00668.x · Cited by 61
Mani, A. R., Ippolito, S., Ollosson, R., & Moore, K. P. (2006) · Hepatology · doi:10.1002/hep.21115 · Cited by 59
Perez-Cruz, I., Cárcamo, J. M., & Golde, D. W. (2006) · APOPTOSIS · doi:10.1007/s10495-006-0475-0 · Cited by 60
Catarzi, S., Biagioni, C., Giannoni, E., Favilli, F., Marcucci, T., Iantomasi, T., & VINCENZINI, M. T. (2005) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2005.03.004 · Cited by 62
Kundi, R., Hollenbeck, S. T., Yamanouchi, D., Herman, B. C., Edlin, R. S., Ryer, E. J., Wang, C., Tsai, S. X., Liu, B., & Kent, K. C. (2009) · Cardiovascular Research · doi:10.1093/cvr/cvp220 · Cited by 58
Regulation of Endogenous Reactive Oxygen Species in Platelets Can Reverse Aggregation
Clutton, P., Miermont, A. M., & Freedman, J. E. (2003) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.0000105889.29687.cc · Cited by 58
Effect of green tea supplementation on blood pressure
Xu, R., Yang, K., Ding, J., & Chen, G. (2020) · Medicine · doi:10.1097/md.0000000000019047 · Cited by 59
Nichols, J. H., Samy, B., Nasir, K., Fox, C. S., Schulze, P. C., Bamberg, F., & Hoffmann, U. (2008) · Journal of cardiovascular computed tomography · doi:10.1016/j.jcct.2008.08.008 · Cited by 56
Abdala‐Valencia, H., Earwood, J. D., Bansal, S., Jansen, M., Babcock, G. F., Garvy, B. A., Wills-Karp, M. A., & Cook‐Mills, J. M. (2007) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00208.2006 · Cited by 56
Radical scavenging effect of gliclazide in diabetic rats fed with a high cholesterol diet
Onozato, M. L., Tojo, A., Goto, A., & Fujita, T. (2004) · Kidney International · doi:10.1111/j.1523-1755.2004.00470.x · 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
Park, 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
Oxidative Stress and the Vascular Wall
Keaney, J. F. (2005) · Circulation · doi:10.1161/circulationaha.105.578146 · Cited by 55
Anning, P. B., Coles, B., Bermúdez-Fajardo, A., Martin, P. E., Levison, B. S., Hazen, S. L., Funk, C. D., Kühn, H., & O’Donnell, V. B. (2005) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)62287-0 · Cited by 53
Eligini, S., Barbieri, S. S., Cavalca, V., Camera, M., Brambilla, M., Defranceschi, M., Tremoli, E., & Colli, S. (2004) · Cardiovascular Research · doi:10.1016/j.cardiores.2004.10.024 · Cited by 54
Hu, R., Wang, Y., Edderkaoui, M., Lugea, A., Apte, M. V., & Pandol, S. J. (2007) · Pancreatology · doi:10.1159/000105499 · 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
Self-citationFrazziano, G., Al Ghouleh, I., Baust, J., Shiva, S., Champion, H. C., & Pagano, P. J. (2014) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00977.2012 · Cited by 51
Self-citationSuperoxide production from paraquat evoked by exogenous NADPH in pulmonary endothelial cells
Tampo, Y., Tsukamoto, M., & Yonaha, M. (1999) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(99)00110-0 · Cited by 51
Cerebral 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
Weaver, M., Liu, J. J., Pimentel, D. R., Reddy, D. J., Harding, P., Peterson, E. L., & Pagano, P. J. (2006) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00690.2005 · Cited by 49
Self-citationCommunication Is Key: Mechanisms of Intercellular Signaling in Vasodilation
Freed, J. K., & Gutterman, D. D. (2017) · Journal of Cardiovascular Pharmacology · doi:10.1097/fjc.0000000000000463 · Cited by 50
Wang, H. D., Rätsep, M. T., Chapman, A., & Boyd, R. (2010) · Canadian Journal of Physiology and Pharmacology · doi:10.1139/y10-015 · Cited by 52
Li, L., & Frei, B. (2006) · Arteriosclerosis, Thrombosis, and Vascular Biology · doi:10.1161/01.atv.0000245820.34238.da · Cited by 49
González‐Candia, A., Veliz, M., Carrasco‐Pozo, C., Castillo, R. L., Cárdenas, C., Ebensperger, G., Reyes, R. V., Llanos, A. J., & Herrera, E. A. (2019) · Redox Biology · doi:10.1016/j.redox.2019.101128 · Cited by 49
Wambi-Kiéssé, C. O., & Katušić, Z. S. (1999) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.1999.276.3.h1043 · Cited by 49
Oxidative stress and endothelial activation
Terada, L. S. (2002) · Critical Care Medicine · doi:10.1097/00003246-200205001-00003 · Cited by 51
Superoxide Regulation of Endothelin-converting Enzyme
López‐Ongil, S., Senchak, V., Saura, M., Zaragoza, C., Ames, M. R., Ballermann, B. J., Rodrı́guez-Puyol, M., Rodrı́guez-Puyol, D., & Lowenstein, C. J. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m000767200 · Cited by 48
Li, L., Crockett, E. T., Wang, D. H., Galligan, J. J., Fink, G. D., & Chen, A. F. (2002) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/hq0202.104124 · Cited by 48
The Redox Regulation of LMW‐PTP During Cell Proliferation or Growth Inhibition
Chiarugi, P. (2001) · IUBMB Life · doi:10.1080/15216540252774775 · Cited by 45
Hayek, T., Kaplan, M., Raz, A., Keidar, S., Coleman, R., & Aviram, M. (2002) · Atherosclerosis · doi:10.1016/s0021-9150(01)00621-9 · Cited by 45
Kennedy, J. A., Beck-Oldach, K., McFadden-Lewis, K., Murphy, G. A., Wong, Y. W., Zhang, Y., & Horowitz, J. D. (2006) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2005.11.058 · Cited by 44
Inhibition of the renin angiotensin system: Implications for the endothelium
Savoia, C., & Schiffrin, E. L. (2006) · Current Diabetes Reports · doi:10.1007/s11892-006-0060-5 · Cited by 43
Li, L., & Frei, B. B. (2009) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.108.183210 · Cited by 42
González-Perilli, L., Álvarez, M. N., Prolo, C., Radí, R., Rubbo, H., & Trostchansky, A. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.12.020 · Cited by 41
Effects of Angiotensin II on NO Bioavailability Evaluated Using a Catheter-Type NO Sensor
Imanishi, T., Kobayashi, K., Kuroi, A., Mochizuki, S., Goto, M., Yoshida, K., & Akasaka, T. (2006) · Hypertension · doi:10.1161/01.hyp.0000248920.16956.d8 · Cited by 41
Antioxidant therapy for atherosclerotic vascular disease: the promise and the pitfalls
Shihabi, A., Li, W.-G., Miller, F. J., & Weintraub, N. L. (2002) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.2002.282.3.h797 · Cited by 41
Catarzi, S., Romagnoli, C., Marcucci, G., Favilli, F., Iantomasi, T., & VINCENZINI, M. T. (2011) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2011.01.005 · Cited by 40
Red wine: A drink to your heart
Saleem, T. S. M., & Basha, S. D. (2010) · Journal of Cardiovascular Disease Research · doi:10.4103/0975-3583.74259 · Cited by 40
Beltrán, A. E., Briones, A. M., García‐Redondo, A. B., Rodrı́guez, C., Miguel, M., Álvarez, Y., Alonso, M. J., Martínez‐González, J., & Salaíces, M. (2008) · Journal of Hypertension · doi:10.1097/hjh.0b013e328317a730 · Cited by 40
Varela, M., Herrera, M., & Garvin, J. L. (2004) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00427.2003 · Cited by 40
Endothelin, hypercholesterolemia and atherosclerosis
Barton, M., Traupe, T., & Haudenschild, C. C. (2003) · Coronary Artery Disease · doi:10.1097/00019501-200311000-00002 · Cited by 39
NADPH oxidase: recent evidence for its role in erectile dysfunction
Jin, L., & Burnett, A. L. “. (2008) · Asian Journal of Andrology · doi:10.1111/j.1745-7262.2008.00371.x · Cited by 37
Mechanisms of Dexamethasone-Induced Hypertension
Ong, S. L. H., Zhang, Y., & Whitworth, J. A. (2009) · Current Hypertension Reviews · doi:10.2174/157340209787314315 · Cited by 39
Expression dynamics of NADPH oxidases during early zebrafish development
Weaver, C. J., Leung, Y. F., & Suter, D. M. (2015) · The Journal of Comparative Neurology · doi:10.1002/cne.23938 · Cited by 41
NADPH Oxidases: Molecular Understanding Finally Reaching the Clinical Level?
Guzik, T. J., & Griendling, K. K. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2615 · Cited by 38
Schnittker, D. L. K., Kwofie, K., Ashkar, A. A., Trigatti, B. L., & Richards, C. D. (2013) · Mediators of Inflammation · doi:10.1155/2013/317503 · Cited by 37
NADPH Oxidase in Human Lung Fibroblasts
Dhaunsi, G. S., Paintlia, M. K., Kaur, J., & Turner, R. B. (2004) · Journal of Biomedical Science · doi:10.1007/bf02256127 · Cited by 38
Chen, O., Sharma, A., Ahmad, I., Bourji, N., Nestoiter, K. G., Hua, P., Hua, B., Ivanov, A. V., Yossef, J., Klem, I., et al. (2014) · European Heart Journal - Cardiovascular Imaging · doi:10.1093/ehjci/jeu145 · Cited by 38
The paracrine control of vascular motion. A historical perspective
Nava, E., & Llorens, S. (2016) · Pharmacological Research · doi:10.1016/j.phrs.2016.08.003 · Cited by 36
Tea in cardiovascular health and disease: a critical appraisal of the evidence
Lange, K. W. (2022) · Food Science and Human Wellness · doi:10.1016/j.fshw.2021.12.034 · Cited by 37
Villamor, E., Kessels, C. G. A., Fischer, M. A. J. G., Bast, A., Mey, J. G. R. D., & Blanco, C. E. (2003) · Pediatric Research · doi:10.1203/01.pdr.0000077481.15081.c8 · Cited by 36
Gowrisankar, Y. V., & Clark, M. A. (2016) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2016.08.013 · Cited by 36
Collin, B., Busseuil, D., Zeller, M., Perrin‐Sarrado, C., Barthez, O., Duvillard, L., Vergely, C., Bardou, M., Dumas, M., Cottin, Y., et al. (2006) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-006-9263-y · Cited by 35
Acute production of vascular superoxide by angiotensin II but not by catecholamines
Kawazoe, T., Kosaka, H., Yoneyama, H., & Hata, Y. (2000) · Journal of Hypertension · doi:10.1097/00004872-200018020-00008 · Cited by 35
Macías-Reyes, A., Rodríguez‐Esparragón, F., Caballero-Hidalgo, A., Hernández-Trujillo, Y., Medina, A., & Rodríguez-Pérez, J. C. (2008) · Free Radical Research · doi:10.1080/10715760701796918 · Cited by 34
Ponatinib treatment promotes arterial thrombosis and hyperactive platelets
Merkulova, A. A., Mitchell, S. C., Stavrou, E. X., Forbes, G. L., & Schmaier, A. H. (2019) · Blood Advances · doi:10.1182/bloodadvances.2019000034 · Cited by 34
Ponatinib and other CML Tyrosine Kinase Inhibitors in Thrombosis
Zeng, P., & Schmaier, A. H. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21186556 · Cited by 35
Vitamin C and quinapril abrogate LVH and endothelial dysfunction in aortic-banded guinea pigs
Bell, J., Mosfer, S. I., Lang, D., Donaldson, F., & LEWIS, M. J. (2001) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.2001.281.4.h1704 · Cited by 34
Microsomal cytochromes P450 catalyze the oxidation of low density lipoprotein
Aviram, M., Kent, U. M., & Hollenberg, P. F. (1999) · Atherosclerosis · doi:10.1016/s0021-9150(98)00296-2 · Cited by 34
Superoxide does not mediate the acute vasoconstrictor effects of angiotensin II
Schuijt, M. P., Tom, B., VRIES, R. D., Saxena, P. R., Sluiter, W. J., van Kats, J. P., & Danser, A. J. (2003) · Journal of Hypertension · doi:10.1097/00004872-200312000-00023 · Cited by 34
Li, D., Huang, L., Zhang, C.-P., Li, Q., & Wang, J. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.890509 · Cited by 38
Zhang, G., Wu, L., Dai, T., Chen, S., Wang, A., Kang, L., Lin, D., Yang, J., Cheng, B., Zhang, L., et al. (2014) · Experimental Dermatology · doi:10.1111/exd.12479 · Cited by 32
Vasopressin Induces Vascular Superoxide Via Endothelin-1 in Mineralocorticoid Hypertension
Li, L., Galligan, J. J., Fink, G. D., & Chen, A. F. (2003) · Hypertension · doi:10.1161/01.hyp.0000047875.43777.79 · Cited by 32
REACTIVE OXYGEN SPECIES AND GLUCOCORTICOID‐INDUCED HYPERTENSION
Ong, S. L., Zhang, Y., & Whitworth, J. A. (2008) · Clinical and Experimental Pharmacology and Physiology · doi:10.1111/j.1440-1681.2008.04900.x · Cited by 32
Inhibition of NADPH Oxidase Attenuates Vasospasm After Experimental Subarachnoid Hemorrhage in Rats
Zheng, J.-S., Zhan, R., Zheng, S., Zhou, Y.-Q., Tong, Y., & Wan, S. (2005) · Stroke · doi:10.1161/01.str.0000163102.49888.b7 · Cited by 32
RetractedResistance of endothelium-dependent relaxation to elevation of O 2 − levels in rabbit carotid artery
Pagano, P. J., Griswold, M. C., Najibi, S., Marklund, S. L., & Cohen, R. A. (1999) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.1999.277.5.h2109 · Cited by 32
Self-citationThe Vascular Adventitia: Its Role in the Arterial Injury Response
Havelka, G. E., & Kibbe, M. R. (2011) · Vascular and Endovascular Surgery · doi:10.1177/1538574411407698 · Cited by 31
Gatti, C., Osto, E., Kouroedov, A., Eto, M., Shaw, S., Volpe, M., Lüscher, T. F., & Cosentino, F. (2008) · Clinical and Experimental Hypertension · doi:10.1080/10641960802443183 · Cited by 31
Ding, L., Chapman, A., Boyd, R., & Wang, H. D. (2007) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00388.2006 · Cited by 31
Cao, X., Demel, S. L., Quinn, M. T., Galligan, J. J., & Kreulen, D. L. (2009) · Autonomic Neuroscience · doi:10.1016/j.autneu.2009.07.010 · Cited by 30
Self-citationAngiotensin II and oxidized LDL: an unholy alliance creating oxidative stress
Galle, J., & Heermeier, K. (1999) · Nephrology Dialysis Transplantation · doi:10.1093/ndt/14.11.2585 · Cited by 29
Gu, M., & Brecher, P. I. (2000) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.20.1.27 · Cited by 29
Desbalanço redox: NADPH oxidase como um alvo terapêutico no manejo cardiovascular
Rabelo, L. A., de Souza, V. N., da Fonseca, L. J. S., & Sampaio, W. O. (2010) · Arquivos Brasileiros de Cardiologia · doi:10.1590/s0066-782x2010000500018 · Cited by 28
Volume-sensitive NADPH oxidase activity and taurine efflux in NIH3T3 mouse fibroblasts
Friis, M., Vorum, K. G., & Lambert, I. H. (2008) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00571.2007 · Cited by 28
Metadata
- Authors
- Pagano, P. J., Clark, J. K., Cifuentes-Pagano, M. E., Clark, S. M., Callis, G. M., & Quinn, M. T.
- Affiliations
- Boston Medical Center (US)
- Vascular Biology Unit, Boston Medical Center, Boston, MA 02118; and Department of Veterinary Molecular Biology, Montana State University, Bozeman, MT 59717
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 1997-12-23
- Volume
- 94
- Issue
- 26
- Pages
- 14483-14488
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC25029
- OpenAlex
- W2170708014
- Cited by
- 455
- References
- 48
- Citations by year
- 2026: 1 · 2025: 3 · 2024: 3 · 2023: 1 · 2022: 4 · 2021: 2 · 2020: 8 · 2019: 8 · 2018: 3 · 2017: 8 · 2016: 12 · 2015: 4 · 2014: 14 · 2013: 9 · 2012: 14
- FWCI
- 12.21
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (7r29hl055425-03)
- National Heart, Lung, and Blood Institute (R29 HL55425-02, R01HL055425)
- National Institute of Arthritis and Musculoskeletal and Skin Diseases (R01AR042426)
- 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
- NADPH oxidase, superoxide, aortic adventitia, adventitial fibroblasts, angiotensin II, p67phox, p22phox, gp91phox, p47phox, nitric oxide, hypertension, vasoconstriction, rabbits
- MeSH terms
- Angiotensin II, Animals, Aorta, Cells, Cultured, Immunohistochemistry, NADPH Dehydrogenase, Phagocytes, Phosphoproteins, Rabbits, Vasoconstrictor Agents, NADPH Oxidases, Membrane Transport Proteins
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review