Cited by 278Nitric Oxide and Endothelin EffectsNeutrophil, Myeloperoxidase and Oxidative MechanismsRedox biology and oxidative stress

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Coronary Artery Superoxide Production and Nox Isoform Expression in Human Coronary Artery Disease

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Guzik, Tomasz J., Sadowski, Jerzy, Guzik, Bartlomiej, Jopek, Andrew, Kapelak, Boguslaw, Przybyłowski, Piotr, Wierzbicki, Karol, Korbut, Ryszard, Harrison, David G., Channon, Keith M.·2006·Arteriosclerosis, Thrombosis, and Vascular Biology

DOI 10.1161/01.atv.0000196651.64776.51

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Abstract

Background— Oxidative stress plays important role in the pathogenesis of atherosclerosis and coronary artery disease (CAD). We aimed to determine the sources and selected molecular mechanisms of oxidative stress in CAD. Methods and Results— We examined basal and NAD(P)H oxidase-mediated superoxide (O 2 · − ) production using lucigenin chemiluminescence, ferricytochrome c and dihydroethidium fluorescence in human coronary arteries from 19 CAD and 17 non-CAD patients undergoing heart transplantation. NAD(P)H oxidase subunits and xanthine oxidase expression were measured. Superoxide production was greater in coronary arteries from patients with CAD, even in vessels without overt atherosclerotic plaques, and was doubled within branching points of coronary arteries. Studies using pharmacological inhibitors and specific substrates showed that NAD(P)H oxidases (60%) and xanthine oxidase (25%) are primary sources of O 2 · − in CAD. Losartan significantly inhibited superoxide production in coronary arteries. NAD(P)H oxidase activity and protein levels of the NADPH oxidase subunits p22phox, p67 phox , and p47 phox were significantly increased in CAD, as were mRNA levels for p22phox and nox2, and no NAD(P)H oxidase subunit mRNA levels correlated with NAD(P)H oxidase activity in vessels from individual patients. Activity and protein expression of xanthine oxidase were increased in CAD, whereas xanthine dehydrogenase levels were not changed. Conclusions— Increased expression and activity of NAD(P)H oxidase subunits and xanthine oxidase, in part mediated through angiotensin II and PKC-dependent pathways, are important mechanisms underlying increased oxidative stress in human coronary artery disease.

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Show all 22 references

Research works printed but not linked: 12

10.1161/atvb.20.6.1430 · DOI
10.1161/atvb.22.1.21 · DOI
10.1161/circ.104.22.2673 · DOI
10.1161/hyp.38.6.1395 · DOI
10.1161/circ.100.14.1494 · DOI
10.1161/res.86.9.e85 · DOI
10.1161/circ.82.4.2401058 · DOI
10.1161/circ.101.18.2206 · DOI
10.1161/res.88.9.888 · DOI
10.1161/atvb.20.8.1903 · DOI
10.1161/circ.100.3.292 · DOI
10.1161/circ.104.15.1767 · DOI

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Whaley‐Connell, A. T., Govindarajan, G., Habibi, J., Hayden, M. R., Cooper, S. A., Wei, Y., Ma, L., Qazi, M. A., Link, D. C., Karuparthi, P. R., et al. (2007) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00632.2006 · Cited by 92
Health position paper and redox perspectives - Disease burden by transportation noise
Sørensen, M., Pershagen, G., Thacher, J. D., Lanki, T., Wicki, B., Röösli, M., Vienneau, D., Cantuaria, M. L., Schmidt, J. H., Aasvang, G. M., et al. (2023) · Redox Biology · doi:10.1016/j.redox.2023.102995 · Cited by 95
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Xu, H., Goettsch, C., Xia, N., Horke, S., Morawietz, H., Förstermann, U., & Li, H. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.01.023 · Cited by 89
Animal models and animal-free innovations for cardiovascular research: current status and routes to be explored. Consensus document of the ESC Working Group on Myocardial Function and the ESC Working Group on Cellular Biology of the Heart
van der Velden, J., Asselbergs, F. W., Bakkers, J., Bátkai, S., Bertrand, L., Bezzina, C. R., Bot, I., Brundel, B. J. J. M., Carrier, L., Chamuleau, S. A. J., et al. (2022) · Cardiovascular Research · doi:10.1093/cvr/cvab370 · Cited by 96
Self-citation
GLP-1 Inhibits High-Glucose-Induced Oxidative Injury of Vascular Endothelial Cells
Li, Q., Lin, Y., Wang, S., Zhang, L., & Guo, L. (2017) · Scientific Reports · doi:10.1038/s41598-017-06712-z · Cited by 89
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Nediani, C., Raimondi, L., Borchi, E., & Cerbai, E. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3198 · Cited by 83
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Steinkamp-Fenske, K., Bollinger, L., Xu, H., Yao, Y., Horke, S., Förstermann, U., & Li, H. (2007) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.107.123356 · Cited by 81
Effects of novel plant antioxidants on platelet superoxide production and aggregation in atherosclerosis.
Ryszawa, N., Kawczyńska-Drózdz, A., Pryjma, J. R., Czesnikiewicz-Guzik, M., Adamek-Guzik, T., Naruszewicz, M., Korbut, R., & Guzik, T. J. (2006) · PubMed · Cited by 78
Self-citation
Modulation of oxidative stress-induced changes in hypertension and atherosclerosis by antioxidants.
Vasdev, S., Gill, V. D., & Singal, P. K. (2006) · PubMed Central · Cited by 78
Myeloperoxidase: A versatile mediator of endothelial dysfunction and therapeutic target during cardiovascular disease
Maiocchi, S. L., Ku, J., Thai, T., Chan, E., Rees, M. D., & Thomas, S. R. (2020) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2020.107711 · Cited by 78
Nox1 in cardiovascular diseases: regulation and pathophysiology
Gimenez, M., Schickling, B., Lopes, L. R., & Miller, F. J. (2015) · Clinical Science · doi:10.1042/cs20150404 · Cited by 77
Erythrocytes, leukocytes and platelets as a source of oxidative stress in chronic vascular diseases: Detoxifying mechanisms and potential therapeutic options
Madrigal‐Matute, J., Martínez-Pinna, R., Ramos‐Mozo, P., Blanco‐Colio, L. M., Moreno, J. A., Tarín, C., Burillo, E., Fernandez‐Garcia, C. E., Egido, J., Meilhac, O., et al. (2012) · Thrombosis and Haemostasis · doi:10.1160/th12-04-0248 · Cited by 74
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Favor, J. D. L., Dubis, G. S., Yan, H., White, J. D., Nelson, M. A. M., Anderson, E. J., & Hickner, R. C. (2016) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.116.308339 · Cited by 77
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Raaz, U., Toh, R., Mäegdefessel, L., Adam, M., Nakagami, F., Emrich, F. C., Spin, J. M., & Tsao, P. S. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5507 · Cited by 76
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Antonopoulos, A. S., Margaritis, M., Shirodaria, C. C., & Antoniades, C. A. (2012) · Thrombosis and Haemostasis · doi:10.1160/th12-05-0337 · Cited by 74
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
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Ding, H., Hashem, M., & Triggle, C. R. (2007) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2006.12.034 · 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
The Importance of NADPH Oxidases and Redox Signaling in Angiogenesis
Prieto-Bermejo, R., & Hernández‐Hernández, Á. (2017) · Antioxidants · doi:10.3390/antiox6020032 · Cited by 74
Effects of Quercetin on Gene and Protein Expression of NOX and NOS after Myocardial Ischemia and Reperfusion in Rabbit
Wan, L. L., Xia, J., Ye, D., Liu, J., Chen, J., & Wang, G. (2009) · Cardiovascular Therapeutics · doi:10.1111/j.1755-5922.2009.00071.x · Cited by 71
The Role of JAK/STAT Molecular Pathway in Vascular Remodeling Associated with Pulmonary Hypertension
Roger, I., Milara, J., Montero, P., & Cortijo, J. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22094980 · Cited by 75
Garlic and Onion Attenuates Vascular Inflammation and Oxidative Stress in Fructose-Fed Rats
Prieto, M. A. V., Lanzi, C. R., Lembo, C., Galmarini, C. R., & Miatello, R. M. (2011) · Journal of Nutrition and Metabolism · doi:10.1155/2011/475216 · Cited by 73
Mitochondrial haplogroup N9b is protective against myocardial infarction in Japanese males
Nishigaki, Y., Yamada, Y., Fuku, N., Matsuo, H., Segawa, T., Watanabe, S., Kato, K., Yokoi, K., Yamaguchi, S., Nozawa, Y., et al. (2006) · Human Genetics · doi:10.1007/s00439-006-0269-z · Cited by 70
Transcriptional regulation of Nox4 by histone deacetylases in human endothelial cells
Siuda, D., Zechner, U., Hajj, N. E., Prawitt, D., Langer, D. J., Xia, N., Horke, S., Pautz, A., Kleinert, H., Förstermann, U., et al. (2012) · Basic Research in Cardiology · doi:10.1007/s00395-012-0283-3 · Cited by 69
Role of Oxidative Stress in the Pathogenesis of Atherothrombotic Diseases
Petrucci, G., Rizzi, A., Hatem, D., Tosti, G., Rocca, B., & Pitocco, D. (2022) · Antioxidants · doi:10.3390/antiox11071408 · Cited by 68
Nox4 NADPH oxidase contributes to smooth muscle cell phenotypes associated with unstable atherosclerotic plaques
Xu, S., Chamseddine, A. H., Carrell, S., & Miller, F. J. (2014) · Redox Biology · doi:10.1016/j.redox.2014.04.004 · Cited by 66
Mitochondrial Haplogroups
Benn, M., Schwartz, M., Nordestgaard, B. G., & Tybjærg‐Hansen, A. (2008) · Circulation · doi:10.1161/circulationaha.107.756809 · Cited by 65

Authors: Guzik, T. J., Sadowski, J., Guzik, B., Jopek, A., Kapelak, B., Przybyłowski, P., Wierzbicki, K., Korbut, R., Harrison, D. G., & Channon, K. M.
Affiliations: Jagiellonian University (PL)
From the Department of Cardiovascular Medicine (T.J.G., K.M.C.), University of Oxford, John Radcliffe Hospital, United Kingdom; Departments of Medicine, Cardiovascular Surgery, and Transplantology and Pharmacology (T.J.G., J.S., B.G., A.J., B.K., P.P., K.W., R.K.), Jagiellonian University School of Medicine, Krakow, Poland; and the Division of Cardiology (D.G.H., T.J.G.), Emory University, Atlanta, Ga.
ORCID: Guzik, Tomasz J.
Sadowski, Jerzy
Przybyłowski, Piotr
Korbut, Ryszard
Harrison, David G.
Channon, Keith M.
Venue: Arteriosclerosis, Thrombosis, and Vascular Biology
Publisher: Ovid Technologies (Wolters Kluwer Health)
Published: 2006-02
Volume: 26
Issue: 2
Pages: 333-339
ISSN: 1079-5642 (ISSN-L)
1524-4636
DOI: 10.1161/01.atv.0000196651.64776.51
OpenAlex: W2130904954
Cited by: 278
References: 22
Citations by year: 2026: 1 · 2025: 7 · 2024: 6 · 2023: 9 · 2022: 8 · 2021: 12 · 2020: 10 · 2019: 9 · 2018: 6 · 2017: 23 · 2016: 15 · 2015: 14 · 2014: 20 · 2013: 21 · 2012: 18
FWCI: 7.59
Type: journal article
Language: en
Open access: green
ruj.uj.edu.pl
Licence: cc-by-nc-nd
Locations: Arteriosclerosis Thrombosis and Vascular Biology (publishedVersion)
PubMed (publishedVersion)
Jagiellonian University Repository (Jagiellonian University) (submittedVersion, cc-by-nc-nd)
Funders: Wellcome Trust
British Heart Foundation
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: coronary artery disease, superoxide production, NADPH oxidase, xanthine oxidase, oxidative stress, NOX isoforms, p22phox, p67phox, p47phox, NOX2, angiotensin II, protein kinase C, losartan, human coronary arteries, atherosclerosis
MeSH terms: Adult, Angiotensin II, Coronary Artery Disease, Coronary Vessels, Female, Humans, Male, Middle Aged, Phosphoproteins, Protein Kinase C, Superoxides, Vasoconstrictor Agents, Xanthine Oxidase, Oxidative Stress, NADPH Oxidases, Membrane Transport Proteins

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Coronary Artery Superoxide Production and Nox Isoform Expression in Human Coronary Artery Disease

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