Interactions of oxidants with vascular signaling systems
Abstract
Abstract—Individual reactive oxygen species (ROS) and oxidation products of NO interact with vascular signaling mechanisms in ways that appear to have fundamental roles in the control of vascular physiological and pathophysiological function. The activities of ROS-producing systems (including various NADPH and NADH oxidases, xanthine oxidase, and NO synthase) in endothelium and/or vascular smooth muscle are controlled by receptor activation, oxygen tension, metabolic processes, and physiological forces associated with blood pressure and flow. This review focuses on how the chemical properties and metabolic sensing interactions of individual ROS (including superoxide anion, hydrogen peroxide, and peroxynitrite) interact with cellular regulatory systems to produce vascular responses. These species appear to often function through producing selective alterations in individual heme or thiol redox–regulated systems (including guanylate cyclase, cyclooxygenase, mitochondrial electron transport, and tyrosine phosphatases) to initiate physiological responses through signaling pathways that control phospholipases, protein kinases, ion channels, contractile proteins, and gene expression.
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Superoxide radicals, hydrogen peroxide, singlet oxygen and hypochlorous acid HOCl are generated in the cell membrane through the action of the enzymes NADPH oxidase, myeloperoxidase and xanthine oxidase.
“Superoxide radicals, hydrogen peroxide, singlet oxygen and hypochlorous acid HOCl are generated in the cell membrane through the action of the enzymes NADPH oxidase, myeloperoxidase and xanthine oxidase [35,36].”
From Superoxide Anion Chemistry—Its Role at the Core of the Innate Immunity (2023) · cites this paper as [35]
Other enzymes, such as lipooxygenase and cyclooxygenase also generate ROS during the synthesis of leukotrienes, thromboxanes and prostaglandins.
“Other enzymes, such as lipooxygenase and cyclooxygenase also generate ROS during the synthesis of leukotrienes, thromboxanes and prostaglandins [35].”
From Superoxide Anion Chemistry—Its Role at the Core of the Innate Immunity (2023) · cites this paper as [35]
Cites
Hydroperoxide metabolism in mammalian organs.
Chance, B., Sies, H., & Boveris, A. (1979) · Physiological Reviews · doi:10.1152/physrev.1979.59.3.527 · Cited by 5,827 · see citing works
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 · see citing works
Peroxynitrite oxidation of sulfhydryls.
Radí, R., Beckman, J. S., Bush, K., & Freeman, B. Α. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)64313-7 · Cited by 2,499 · see citing works
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 2,441 · see citing works
BABIOR, B. M. (1999) · Blood · doi:10.1182/blood.v93.5.1464 · Cited by 2,147 · see citing works
Hypercholesterolemia increases endothelial superoxide anion production.
Ohara, Y., Peterson, T. E., & Harrison, D. G. (1993) · Journal of Clinical Investigation · doi:10.1172/jci116491 · Cited by 1,765 · see citing works
Nitric oxide directly activates calcium-dependent potassium channels in vascular smooth muscle
Bolotina, V. M., Najibi, S., Palacino, J. J., Pagano, P. J., & Cohen, R. A. (1994) · Nature · doi:10.1038/368850a0 · Cited by 1,676 · see citing works
Wink, D. A., & Mitchell, J. B. (1998) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(98)00092-6 · Cited by 1,606 · see citing works
Formation of nitric oxide-derived inflammatory oxidants by myeloperoxidase in neutrophils
Eiserich, J. P., Hristova, M., Cross, C. E., Jones, A. D., Freeman, B. A., Halliwell, B., & van der Vliet, A. (1998) · Nature · doi:10.1038/34923 · Cited by 1,496 · see citing works
Peroxynitrite-mediated tyrosine nitration catalyzed by superoxide dismutase
Ischiropoulos, H., Zhu, L., Chen, J., Tsai, M., Martin, J. C., Smith, C. D. L., & Beckman, J. S. (1992) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(92)90431-u · Cited by 1,495 · see citing works
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 · see citing works
Lipoxygenases: Occurrence, Functions, Catalysis, and Acquisition of Substrate
Brash, A. R. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.34.23679 · Cited by 1,335 · see citing works
Hyperglycemic Pseudohypoxia and Diabetic Complications
Williamson, J. R., Chang, K. C., Frangos, M., Hasan, K. S., Ido, Y., Kawamura, T., Nyengaard, J. R., den Enden, M. V., Kilo, C., & Tilton, R. G. (1993) · Diabetes · doi:10.2337/diab.42.6.801 · Cited by 1,092 · see citing works
Role of xanthine oxidase and granulocytes in ischemia-reperfusion injury
Granger, D. N. (1988) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.1988.255.6.h1269 · Cited by 825 · see citing works
Reactivity of biologically important thiol compounds with superoxide and hydrogen peroxide
Winterbourn, C. C., & Metodiewa, D. (1999) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(99)00051-9 · Cited by 799 · see citing works
Oxidative chemistry of nitric oxide: the roles of superoxide, peroxynitrite, and carbon dioxide
Squadrito, G. L., & Pryor, W. A. (1998) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(98)00095-1 · Cited by 795 · see citing works
Oxidative Stress as a Regulator of Gene Expression in the Vasculature
KUNSCH, C. A., & Medford, R. M. (1999) · Circulation Research · doi:10.1161/01.res.85.8.753 · Cited by 795 · see citing works
Kojda, G. (1999) · Cardiovascular Research · doi:10.1016/s0008-6363(99)00169-8 · Cited by 769 · see citing works
Inhibition of Mitochondrial Electron Transport by Peroxynitrite
Radi, R., Rodriguez, M., Castro, L., & Telleri, R. (1994) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1994.1013 · Cited by 693 · see citing works
Oscillatory and Steady Laminar Shear Stress Differentially Affect Human Endothelial Redox State
Keulenaer, G. W. D., Chappell, D. C., Ishizaka, N., Nerem, R. M., Alexander, R. W., & Griendling, K. K. (1998) · Circulation Research · doi:10.1161/01.res.82.10.1094 · Cited by 605 · see citing works
Activation of protein kinase C by tyrosine phosphorylation in response to H 2 O 2
Konishi, H., Tanaka, M., Takemura, Y., Matsuzaki, H., Ono, Y., Kikkawa, U., & Nishizuka, Y. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.21.11233 · Cited by 604 · see citing works
Liu, X., Miller, M. J. S., Joshi, M. S., Thomas, D. D., & Lancaster, J. R. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.5.2175 · Cited by 602 · see citing works
Ushio‐Fukai, M., Alexander, R. W., Akers, M., Yin, Q., Fujio, Y., Walsh, K., & Griendling, K. K. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.32.22699 · Cited by 558 · see citing works
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 · see citing works
Self-citationClaiborne, A., Yeh, J. I., Mallett, T. C., Luba, J. P., Crane, E. J., Charrier, V., & Parsonage, D. (1999) · Biochemistry · doi:10.1021/bi992025k · Cited by 500 · see citing works
A Molecular Redox Switch on p21
Lander, H. M., Hajjar, D. P., Hempstead, B. L., Mirza, U. A., Chait, B. T., Campbell, S. L., & Quilliam, L. A. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.7.4323 · Cited by 488 · see citing works
PGH synthase and lipoxygenase generate superoxide in the presence of NADH or NADPH.
Kukreja, R. C., Kontos, H. A., Hess, M. L., & Ellis, E. F. (1986) · Circulation Research · doi:10.1161/01.res.59.6.612 · Cited by 487 · see citing works
Pritchard, K. A., Groszek, L., Smalley, D. M., Sessa, W. C., Wu, M., Villalon, P., Wolin, M. S., & Stemerman, M. B. (1995) · Circulation Research · doi:10.1161/01.res.77.3.510 · Cited by 471 · see citing works
Self-citationThe mechanism of acute hypoxic pulmonary vasoconstriction: the tale of two channels
Weir, E. K., & Archer, S. L. (1995) · The FASEB Journal · doi:10.1096/fasebj.9.2.7781921 · Cited by 466 · see citing works
Drummond, G. R., Cai, H., Davis, M. E., Ramasamy, S., & Harrison, D. G. (2000) · Circulation Research · doi:10.1161/01.res.86.3.347 · Cited by 430 · see citing works
Landino, L. M., Crews, B. C., Timmons, M. D., Morrow, J. D., & Marnett, L. J. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.26.15069 · Cited by 423 · see citing works
Gardner, P. R., Nguyen, D., & White, C. W. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.25.12248 · Cited by 414 · see citing works
Protein Sulfhydryls and Their Role in the Antioxidant Function of Protein S-Thiolation
Thomas, J. A., Poland, B. W., & Honzatko, R. B. (1995) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1995.1261 · Cited by 399 · see citing works
Isoprostanes: Formation, Analysis and Use As Indices of Lipid Peroxidation in Vivo
Lawson, J. A., FitzGerald, G. A., & Rokach, J. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.35.24441 · Cited by 381 · see citing works
Endothelial Function in Hypertension
McIntyre, M., Bohr, D. F., & Dominiczak, A. F. (1999) · Hypertension · doi:10.1161/01.hyp.34.4.539 · Cited by 355 · see citing works
Prostaglandin biosynthesis can be triggered by lipid peroxides
Hemler, M. E., Cook, H. W., & Lands, W. E. M. (1979) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(79)90038-9 · Cited by 352 · see citing works
Stimulation of a Vascular Smooth Muscle Cell NAD(P)H Oxidase by Thrombin
Patterson, C., Ruef, J., Madamanchi, N. R., Barry-Lane, P., Hu, Z., Horaist, C., Ballinger, C. A., Brasier, A. R., Bode, C., & Runge, M. S. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.28.19814 · Cited by 330 · see citing works
Cyclic strain upregulates nitric oxide synthase in cultured bovine aortic endothelial cells.
Awolesi, M. A., Sessa, W. C., & Sumpio, B. E. (1995) · Journal of Clinical Investigation · doi:10.1172/jci118181 · Cited by 328 · see citing works
A molecular basis for nitric oxide sensing by soluble guanylate cyclase
Zhao, Y., Brandish, P. E., Ballou, D. P., & Marletta, M. A. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.26.14753 · Cited by 323 · see citing works
Mügge, A., Elwell, J. H., Peterson, T. E., & Harrison, D. G. (1991) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.1991.260.2.c219 · Cited by 314 · see citing works
Inactivation of Glutathione Peroxidase by Nitric Oxide
Asahi, M., Fujii, J., Suzuki, K., Seo, H. G., Kuzuya, T., Hori, M., Tada, M., Fujii, S., & Taniguchi, N. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.36.21035 · Cited by 309 · see citing works
Tumour necrosis factor α activates a p22phox-based NADH oxidase in vascular smooth muscle
KEULENAER, W. G. D., Alexander, R. W., Ushio‐Fukai, M., Ishizaka, N., & Griendling, K. K. (1998) · Biochemical Journal · doi:10.1042/bj3290653 · Cited by 308 · see citing works
Mechanisms of cerebral vasodilation by superoxide, hydrogen peroxide, and peroxynitrite
Wei, E. P., Kontos, H. A., & Beckman, J. S. (1996) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.1996.271.3.h1262 · Cited by 303 · see citing works
Tetrahydrobiopterin and Dysfunction of Endothelial Nitric Oxide Synthase in Coronary Arteries
Cosentino, F., & Katušić, Z. S. (1995) · Circulation · doi:10.1161/01.cir.91.1.139 · Cited by 294 · see citing works
Selective inhibition of protein tyrosine phosphatase activities by H2O2 and vanadate In vitro
Hecht, D., & Zick, Y. (1992) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(92)91123-8 · Cited by 273 · see citing works
Rubbo, H., Parthasarathy, S., Barnes, S., KIRK, M. C., Kalyanaraman, B., & Freeman, B. Α. (1995) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1995.9935 · Cited by 263 · see citing works
Reactive Oxygen Species as Mediators of Signal Transduction in Cardiovascular Disease
Abe, J.-I., & Berk, B. C. (1998) · Trends in Cardiovascular Medicine · doi:10.1016/s1050-1738(97)00133-3 · Cited by 260 · see citing works
Pulmonary Artery NADPH-Oxidase is Activated in Hypoxic Pulmonary Vasoconstriction
Marshall, C., Mamary, A. J., Verhoeven, A. J., & Marshall, B. E. (1996) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/ajrcmb.15.5.8918370 · Cited by 257 · see citing works
Hydrogen peroxide elicits pulmonary arterial relaxation and guanylate cyclase activation
Burke, T. M., & Wolin, M. S. (1987) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.1987.252.4.h721 · Cited by 256 · see citing works
Self-citationPolymorphism of the NADH/NADPH Oxidase p22 phox Gene in Patients With Coronary Artery Disease
Inoue, N., Kawashima, S., Kanazawa, K., Yamada, S., Akita, H., & Yokoyama, M. (1998) · Circulation · doi:10.1161/01.cir.97.2.135 · Cited by 238 · see citing works
Granger, D. N. (1999) · Microcirculation · doi:10.1111/j.1549-8719.1999.tb00099.x · Cited by 218 · see citing works
Laurindo, F. R. M., Pedro, M. D. A., Barbeiro, H. V., Pileggi, F., de Carvalho, M. H. C., Augusto, O., & da Luz, P. L. (1994) · Circulation Research · doi:10.1161/01.res.74.4.700 · Cited by 215 · see citing works
Omar, H. Α., Cherry, P. D., Mortelliti, M. P., Burke-Wolin, T., & Wolin, M. S. (1991) · Circulation Research · doi:10.1161/01.res.69.3.601 · Cited by 212 · see citing works
Self-citationMohr, S., Stamler, J. S., & Brüne, B. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)00596-6 · Cited by 208 · see citing works
Takakura, K., Beckman, J. S., MacMillan-Crow, L. A., & Crow, J. P. (1999) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1999.1374 · Cited by 202 · see citing works
Bhunia, A. K., Han, H., Snowden, A., & Chatterjee, S. B. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.25.15642 · Cited by 200 · see citing works
Nitric oxide inhibits creatine kinase and regulates rat heart contractile reserve.
Gross, W. L., Bak, M. I., Ingwall, J. S., Arstall, M. A., Smith, T. W., Balligand, J., & Kelly, R. A. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.11.5604 · Cited by 199 · see citing works
The formation of nitric oxide donors from peroxynitrite
Moro, M. Á., Darley-Usmar, V. M., Lizasoaín, I., Su, Y., Knowles, R. G., Moncada, S., & Radomski, M. W. (1995) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.1995.tb16404.x · Cited by 197 · see citing works
Nitric oxide regulates oxygen uptake and hydrogen peroxide release by the isolated beating rat heart
Poderoso, J. J., Peralta, J. G., Lisdero, C. L., Carreras, M. C., Radisic, M., Schopfer, F. J., Cadenas, E., & Boveris, A. (1998) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.1998.274.1.c112 · Cited by 194 · see citing works
Mechanisms of Bradykinin-Induced Cerebral Vasodilatation in Rats
Sobey, C. G., Heistad, D. D., & Faraci, F. M. (1997) · Stroke · doi:10.1161/01.str.28.11.2290 · Cited by 183 · see citing works
Min, D. S., Kim, E., & Exton, J. H. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.45.29986 · Cited by 174 · see citing works
S-Nitrosylation and S-Glutathiolation of Protein Sulfhydryls byS-Nitroso Glutathione
Ji, Y., Akerboom, T. P. M., Sies, H., & Thomas, J. A. (1999) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1998.1013 · Cited by 173 · see citing works
Hinterleitner, T. A., Saada, J. I., Berschneider, H. M., Powell, D. W., & Valentich, J. D. (1996) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.1996.271.4.c1262 · Cited by 164 · see citing works
Redox regulation of signal transduction in mammalian cells
Herrlich, P. A., & Böhmer, F. (2000) · Biochemical Pharmacology · doi:10.1016/s0006-2952(99)00298-1 · Cited by 158 · see citing works
Dessy, C., Kim, I., Sougnez, C. L., et al. (1998) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.1998.275.4.c1081 · Cited by 158 · see citing works
Go, Y., Patel, R. P., Maland, M. C., Park, H., Beckman, J. S., Darley-Usmar, V. M., & Jo, H. (1999) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.1999.277.4.h1647 · Cited by 153 · see citing works
Ruef, J., Rao, G. N., Li, F., Bode, C., Patterson, C., Bhatnagar, A., & Runge, M. S. (1998) · Circulation · doi:10.1161/01.cir.97.11.1071 · Cited by 151 · see citing works
Mixed Disulfides: Biological Functions and Increase in Oxidative Stress
Brigelius, R. (1985) · Elsevier eBooks · doi:10.1016/b978-0-12-642760-8.50015-6 · Cited by 149 · see citing works
Balazy, M., Kaminski, P. M., Mao, K., Tan, J., & Wolin, M. S. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.48.32009 · Cited by 143 · see citing works
Self-citationLee, S.-L., Wang, W., Finlay, G. A., & Fanburg, B. L. (1999) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.1999.277.2.l282 · Cited by 141 · see citing works
Komalavilas, P., Shah, P. K., Jo, H., et al. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.48.34301 · Cited by 138 · see citing works
Reactive Oxygen Species and Vascular Signal Transduction Mechanisms
Wolin, M. S. (1996) · Microcirculation · doi:10.3109/10739689609146778 · Cited by 135 · see citing works
Self-citationHuang, A., Sun, D., Kaley, G., et al. (1998) · Circulation Research · doi:10.1161/01.res.83.9.960 · Cited by 135 · see citing works
Redox status in the control of pulmonary vascular tone.
Archer, S., Will, J. A., & Weir, E. K. (1986) · PubMed · Cited by 128 · see citing works
Endothelium-derived relaxing factors
Vanhoutte, P. M. (1995) · European Journal of Medicinal Chemistry · doi:10.1016/s0223-5234(23)00136-8 · Cited by 123 · see citing works
Mohazzab, K. M., & Wolin, M. S. (1994) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.1994.267.6.l823 · Cited by 122 · see citing works
Self-citationWung, B., Cheng, J., Chao, Y., Hsieh, H. J., & Wang, D. L. (1999) · Circulation Research · doi:10.1161/01.res.84.7.804 · Cited by 121 · see citing works
Superoxide anion inhibits cGMP-associated bovine pulmonary arterial relaxation
Cherry, P. D., Omar, H. Α., Farrell, K. A., Stuart, J. S., & Wolin, M. S. (1990) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.1990.259.4.h1056 · Cited by 112 · see citing works
Self-citationAbrahamsson, T., Brandt, U., Marklund, S. L., & Sjöqvist, P.-O. (1992) · Circulation Research · doi:10.1161/01.res.70.2.264 · Cited by 107 · see citing works
Effect of the thiol-oxidizing agent diamide on NH2Cl-induced rat colonic electrolyte secretion
Tamai, H., Kachur, J. F., Grisham, M. B., Musch, M. W., Chang, E. B., & Gaginella, T. S. (1993) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.1993.265.1.c166 · Cited by 107 · see citing works
Hydrogen peroxide activation of cytosolic phospholipase A2 in vascular smooth muscle cells
Rao, G. N., Runge, M. S., & Alexander, R. W. (1995) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/0167-4889(95)91997-z · Cited by 106 · see citing works
Cardiovascular Significance of Endothelium-Derived Vasoactive Factors
Rubanyi, G. M. (1992) · Critical Care Medicine · doi:10.1097/00003246-199201000-00036 · Cited by 96 · see citing works
Zou, M., Jendral, M. J., & Ullrich, V. (1999) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0702434 · Cited by 93 · see citing works
Formation and Release of Dinitrosyl Iron Complexes by Endothelial Cells
Mülsch, A., Mordvintcev, P. I., Vanin, A. F., & Busse, R. (1993) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1993.2394 · Cited by 82 · see citing works
Nitric oxide and cellular respiration
Brunori, M., Giuffr�, A., Sarti, P., Stubauer, G., & Wilson, M. T. (1999) · Cellular and Molecular Life Sciences · doi:10.1007/s000180050452 · Cited by 81 · see citing works
Zou, M.-H., & Bachschmid, M. M. (1999) · The Journal of Experimental Medicine · doi:10.1084/jem.190.1.135 · Cited by 80 · see citing works
Superoxide dismutases: regularities and irregularities.
Fridovich, I. (1986) · PubMed · Cited by 69 · see citing works
Hydrogen peroxide-induced endothelium-dependent
Yang, Z., Zhang, A., Altura, B. T., & Altura, B. M. (1999) · General Pharmacology The Vascular System · doi:10.1016/s0306-3623(99)00019-1 · Cited by 65 · see citing works
Roles for NAD(P)H oxidases and reactive oxygen species in vascular oxygen sensing mechanisms
Wolin, M. S., Burke-Wolin, T., & Mohazzab-H., K. M. (1999) · Respiration Physiology · doi:10.1016/s0034-5687(99)00023-7 · Cited by 64 · see citing works
Self-citationNatarajan, V., Scribner, W. M., Al‐Hassani, M., & Vepa, S. (1998) · Environmental Health Perspectives · doi:10.1289/ehp.98106s51205 · Cited by 61 · see citing works
Grover, A. K., Samson, S. E., Fomin, V. P., et al. (1995) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.1995.269.3.c546 · Cited by 59 · see citing works
Oxidant--nitric oxide signalling mechanisms in vascular tissue.
Ms, W., Ca, D., Kaminski, P. M., et al. (1998) · PubMed · Cited by 58 · see citing works
Comparison of branched-chain and tightly coupled reaction mechanisms for prostaglandin H synthase
Wei, C., Kulmacz, R. J., & Tsai, A. (1995) · Biochemistry · doi:10.1021/bi00026a034 · Cited by 57 · see citing works
Madden, J. A., & Christman, N. J. T. (1999) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.1999.277.6.h2264 · Cited by 55 · see citing works
Wolin, M. S., & Belloni, F. L. (1985) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.1985.249.6.h1127 · Cited by 53 · see citing works
Self-citationNO elicits prolonged relaxation of bovine pulmonary arteries via endogenous peroxynitrite generation
Davidson, C. A., Kaminski, P. M., & Wolin, M. S. (1997) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.1997.273.2.l437 · Cited by 50 · see citing works
Self-citationWolin, M. S., Rodenburg, J. M., Messina, E. J., et al. (1990) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1016/s0022-3565(25)12998-4 · Cited by 48 · see citing works
Self-citationWolin, M. S., Hintze, T. H., Shen, W., Mohazzab-H., K. M., & Xie, Y.-W. (1997) · Biochemical Society Transactions · doi:10.1042/bst0250934 · Cited by 41 · see citing works
Self-citationNADPH and heme redox modulate pulmonary artery relaxation and guanylate cyclase activation by NO
Gupte, S. A., Rupawalla, T., Phillibert, D., & Wolin, M. S. (1999) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.1999.277.6.l1124 · Cited by 39 · see citing works
Self-citationRedox Control of Ion Channel Activity in Vascular Endothelial Cells by Glutathione
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- Authors
- Wolin, M. S.
- Affiliations
- New York Medical College (US)
- Corresponding author
- Wolin, Michael S.
- ORCID
- Wolin, Michael S.
- Venue
- Arteriosclerosis, Thrombosis, and Vascular Biology
- Published
- 2000-06
- Volume
- 20
- Issue
- 6
- Pages
- 1430-1442
- ISSN
- 1079-5642 (ISSN-L)
- 1524-4636
- OpenAlex
- W2133872346
- Cited by
- 463
- References
- 110
- Citations by year
- 2025: 1 · 2024: 2 · 2023: 4 · 2022: 6 · 2021: 7 · 2020: 9 · 2019: 8 · 2018: 7 · 2017: 9 · 2016: 8 · 2015: 6 · 2014: 15 · 2013: 19 · 2012: 16
- FWCI
- 4.75
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Arteriosclerosis Thrombosis and Vascular Biology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Heart, Lung, and Blood Institute (P01HL043023, HL 43023, HL-31069)
- 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
- reactive oxygen species, vascular signaling, superoxide, hydrogen peroxide, peroxynitrite, NADPH oxidase, NADH oxidase, xanthine oxidase, nitric oxide synthase, endothelium, vascular smooth muscle, thiol redox regulation, guanylate cyclase, cyclooxygenase, mitochondrial electron transport chain, protein tyrosine phosphatase, protein kinases, ion channels, vascular contractility, gene expression
- MeSH terms
- Animals, Blood Vessels, Endothelium, Vascular, Humans, Muscle, Smooth, Vascular, Signal Transduction, Oxidants, Reactive Oxygen Species
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