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Volumn 276, Issue 3 45-3, 1999, Pages

Inhibition of copper/zinc superoxide dismutase impairs NO·-mediated endothelium-dependent relaxations

Author keywords

A 23187; Bradykinin; Cerebral vessels; Inflammation; Tiron

Indexed keywords

BRADYKININ; CALCIMYCIN; COPPER ZINC SUPEROXIDE DISMUTASE; NITRIC OXIDE;

EID: 17144458417     PISSN: 03636135     EISSN: None     Source Type: Journal    
DOI: 10.1152/ajpheart.1999.276.3.h1043     Document Type: Article
Times cited : (45)

References (37)
  • 1
    • 0023924814 scopus 로고
    • Superoxide dismutase and catalase conjugated to polyethylene glycol increases endothelial enzyme activity and oxidant resistance
    • Beckman, J. S., R. L. Minor, C. W. White, J. E. Repine, G. M. Rosen, and B. A. Freeman. Superoxide dismutase and catalase conjugated to polyethylene glycol increases endothelial enzyme activity and oxidant resistance. J. Biol. Chem. 263: 6884-6892, 1988.
    • (1988) J. Biol. Chem. , vol.263 , pp. 6884-6892
    • Beckman, J.S.1    Minor, R.L.2    White, C.W.3    Repine, J.E.4    Rosen, G.M.5    Freeman, B.A.6
  • 3
    • 0018263443 scopus 로고
    • Biology of oxygen radicals
    • Fridovich, I. Biology of oxygen radicals. Science 201: 875-879, 1978.
    • (1978) Science , vol.201 , pp. 875-879
    • Fridovich, I.1
  • 4
    • 0030464496 scopus 로고    scopus 로고
    • Tetrahydrobiopterin-free neuronal nitric oxide synthase: Evidence for two identical highly anticooperative pteridine binding sites
    • Gorren, A. C., B. M. List, A. Schrammel, E. Pitters, B. Hemmens, E. R. Werner, K. Schmidt, and B. Mayer. Tetrahydrobiopterin-free neuronal nitric oxide synthase: evidence for two identical highly anticooperative pteridine binding sites. Biochemistry 35: 16735-16745, 1996.
    • (1996) Biochemistry , vol.35 , pp. 16735-16745
    • Gorren, A.C.1    List, B.M.2    Schrammel, A.3    Pitters, E.4    Hemmens, B.5    Werner, E.R.6    Schmidt, K.7    Mayer, B.8
  • 5
    • 0016806352 scopus 로고
    • The oxidation of Tiron by superoxide anion. Kinetics of the reaction in aqueous solution in chloroplasts
    • Greenstock, C. L., and R. W. Miller. The oxidation of Tiron by superoxide anion. Kinetics of the reaction in aqueous solution in chloroplasts. Biochim. Biophys. Acta 396: 11-16, 1975.
    • (1975) Biochim. Biophys. Acta , vol.396 , pp. 11-16
    • Greenstock, C.L.1    Miller, R.W.2
  • 6
    • 0022640297 scopus 로고
    • Superoxide anion is involved in the breakdown of endothelium-derived vascular relaxing factor
    • Gryglewski, R. J., R. M. Palmer, and S. Moncada. Superoxide anion is involved in the breakdown of endothelium-derived vascular relaxing factor. Nature 320: 454-456, 1986.
    • (1986) Nature , vol.320 , pp. 454-456
    • Gryglewski, R.J.1    Palmer, R.M.2    Moncada, S.3
  • 8
    • 0023518452 scopus 로고
    • Endothelium-derived relaxing factor from pulmonary artery and vein possesses pharmacologic and chemical properties identical to those of nitric oxide radical
    • Ignarro, L. J., R. E. Byrns, G. M. Buga, and K. S. Wood. Endothelium-derived relaxing factor from pulmonary artery and vein possesses pharmacologic and chemical properties identical to those of nitric oxide radical. Circ. Res. 61: 866-879, 1987.
    • (1987) Circ. Res. , vol.61 , pp. 866-879
    • Ignarro, L.J.1    Byrns, R.E.2    Buga, G.M.3    Wood, K.S.4
  • 9
    • 0029942652 scopus 로고    scopus 로고
    • Superoxide anion and endothelial regulation of arterial tone
    • Katusic, Z. S. Superoxide anion and endothelial regulation of arterial tone. Free Radic. Biol. Med. 20: 443-448, 1996.
    • (1996) Free Radic. Biol. Med. , vol.20 , pp. 443-448
    • Katusic, Z.S.1
  • 10
    • 0024460847 scopus 로고
    • Similar responsiveness of smooth muscle of the canine basilar artery to EDRF and nitric oxide
    • Heart Circ. Physiol. 26
    • Katusic, Z. S., J. J. Marshall, H. A. Kontos, and P. M. Vanhoutte. Similar responsiveness of smooth muscle of the canine basilar artery to EDRF and nitric oxide. Am. J. Physiol. 257 (Heart Circ. Physiol. 26): H1235-H1239, 1989.
    • (1989) Am. J. Physiol. , vol.257
    • Katusic, Z.S.1    Marshall, J.J.2    Kontos, H.A.3    Vanhoutte, P.M.4
  • 11
    • 0023182673 scopus 로고
    • Endothelium-dependent contraction to stretch in canine basilar arteries
    • Heart Circ. Physiol. 21
    • Katusic, Z. S., J. T. Shepherd, and P. M. Vanhoutte. Endothelium-dependent contraction to stretch in canine basilar arteries. Am. J. Physiol. 252 (Heart Circ. Physiol. 21): H671-H673, 1987.
    • (1987) Am. J. Physiol. , vol.252
    • Katusic, Z.S.1    Shepherd, J.T.2    Vanhoutte, P.M.3
  • 12
    • 33751290467 scopus 로고    scopus 로고
    • Inhibition of tetrahydrobiopterin biosynthesis impairs endothelium-dependent relaxations in canine basilar artery
    • Heart Circ. Physiol. 42
    • Kinoshita, H., S. Milstien, C. Wambi, and Z. S. Katusic. Inhibition of tetrahydrobiopterin biosynthesis impairs endothelium-dependent relaxations in canine basilar artery. Am. J. Physiol. 273 (Heart Circ. Physiol. 42): H718-H724, 1997.
    • (1997) Am. J. Physiol. , vol.273
    • Kinoshita, H.1    Milstien, S.2    Wambi, C.3    Katusic, Z.S.4
  • 13
    • 0021158707 scopus 로고
    • Oxygen radicals mediate cerebral arteriolar dilation from arachidonate and bradykinin in cats
    • Kontos, H. A., E. P. Wei, J. T. Povlishock, and C. W. Christman. Oxygen radicals mediate cerebral arteriolar dilation from arachidonate and bradykinin in cats. Circ. Res. 55: 295-303, 1984.
    • (1984) Circ. Res. , vol.55 , pp. 295-303
    • Kontos, H.A.1    Wei, E.P.2    Povlishock, J.T.3    Christman, C.W.4
  • 14
    • 0026490413 scopus 로고
    • Cytochemical detection of superoxide in cerebral inflammation and ischemia in vivo
    • Heart Circ. Physiol. 32
    • Kontos, C. D., E. P. Wei, J. I. Williams, H. A. Kontos, and J. T. Povlishock. Cytochemical detection of superoxide in cerebral inflammation and ischemia in vivo. Am. J. Physiol. 263 (Heart Circ. Physiol. 32): H1234-H1242, 1992.
    • (1992) Am. J. Physiol. , vol.263
    • Kontos, C.D.1    Wei, E.P.2    Williams, J.I.3    Kontos, H.A.4    Povlishock, J.T.5
  • 15
    • 0028285606 scopus 로고
    • Agonist-induced peroxynitrite production from endothelial cells
    • Kooy, N. W., and J. A. Royall. Agonist-induced peroxynitrite production from endothelial cells. Arch. Biochem. Biophys. 310: 352-359, 1994.
    • (1994) Arch. Biochem. Biophys. , vol.310 , pp. 352-359
    • Kooy, N.W.1    Royall, J.A.2
  • 16
    • 0031953601 scopus 로고    scopus 로고
    • Calcium in ischemic cell death
    • Kristián, T., and B. K. Siesjö. Calcium in ischemic cell death. Stroke 29: 705-718, 1998.
    • (1998) Stroke , vol.29 , pp. 705-718
    • Kristián, T.1    Siesjö, B.K.2
  • 17
    • 0028327284 scopus 로고
    • Cerebral vasospasm and free radicals
    • Macdonald, R. L., and B. K. Weir. Cerebral vasospasm and free radicals. Free Radic. Biol. Med. 16: 633-643, 1994.
    • (1994) Free Radic. Biol. Med. , vol.16 , pp. 633-643
    • Macdonald, R.L.1    Weir, B.K.2
  • 18
    • 0006157248 scopus 로고
    • Human copper-containing superoxide dismutase of high molecular weight
    • Marklund, S. L. Human copper-containing superoxide dismutase of high molecular weight. Proc. Natl. Acad. Sci. USA 79: 7634-7638, 1982.
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 7634-7638
    • Marklund, S.L.1
  • 19
    • 0023023315 scopus 로고
    • Increased superoxide anion release from human endothelial cells in response to cytokines
    • Matsubara, T., and M. Ziff. Increased superoxide anion release from human endothelial cells in response to cytokines. J. Immunol. 137: 3295-3298, 1986.
    • (1986) J. Immunol. , vol.137 , pp. 3295-3298
    • Matsubara, T.1    Ziff, M.2
  • 20
    • 0014691242 scopus 로고
    • Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein)
    • McCord, J. M., and I. Fridovich. Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein). J. Biol. Chem. 244: 6049-6055, 1969.
    • (1969) J. Biol. Chem. , vol.244 , pp. 6049-6055
    • McCord, J.M.1    Fridovich, I.2
  • 21
    • 0015816319 scopus 로고
    • The oxidation of catechols by reduced flavins and dehydrogenases
    • Miller, R. W., and U. Rapp. The oxidation of catechols by reduced flavins and dehydrogenases. J. Biol. Chem. 248: 6084-6090, 1973.
    • (1973) J. Biol. Chem. , vol.248 , pp. 6084-6090
    • Miller, R.W.1    Rapp, U.2
  • 22
    • 0028233138 scopus 로고
    • NADH oxidoreductase is a major source of superoxide anion in bovine coronary artery endothelium
    • Heart Circ. Physiol. 35
    • Mohazzab-H, K. M., P. M. Kaminski, and M. S. Wolin. NADH oxidoreductase is a major source of superoxide anion in bovine coronary artery endothelium. Am. J. Physiol. 266 (Heart Circ. Physiol. 35): H2568-H2572, 1994.
    • (1994) Am. J. Physiol. , vol.266
    • Mohazzab-H, K.M.1    Kaminski, P.M.2    Wolin, M.S.3
  • 23
    • 0026034681 scopus 로고
    • Release of intact endothelium-derived relaxing factor depends on endothelial superoxide dismutase activity
    • Cell Physiol. 29
    • Mügge, A., J. H. Elwell, T. E. Peterson, and D. G. Harrison. Release of intact endothelium-derived relaxing factor depends on endothelial superoxide dismutase activity. Am. J. Physiol. 260 (Cell Physiol. 29): C219-C225, 1991.
    • (1991) Am. J. Physiol. , vol.260
    • Mügge, A.1    Elwell, J.H.2    Peterson, T.E.3    Harrison, D.G.4
  • 24
    • 0032579513 scopus 로고    scopus 로고
    • 1 receptor gene in inflammation
    • 1 receptor gene in inflammation. J. Biol. Chem. 273: 2784-2791, 1998.
    • (1998) J. Biol. Chem. , vol.273 , pp. 2784-2791
    • Ni, A.1    Chao, L.2    Chao, J.3
  • 25
    • 0026014272 scopus 로고
    • Inhibition of coronary artery superoxide dismutase attenuates endothelium-dependent and -independent nitrovasodilator relaxation
    • Omar, H. A., P. D. Cherry, M. P. Mortelliti, T. Burke-Wolin, and M. S. Wolin. Inhibition of coronary artery superoxide dismutase attenuates endothelium-dependent and -independent nitrovasodilator relaxation. Circ. Res. 69: 601-608, 1991.
    • (1991) Circ. Res. , vol.69 , pp. 601-608
    • Omar, H.A.1    Cherry, P.D.2    Mortelliti, M.P.3    Burke-Wolin, T.4    Wolin, M.S.5
  • 26
    • 0029848789 scopus 로고    scopus 로고
    • Extracellular superoxide dismutase: A regulator of nitric oxide bioavailability
    • Oury, T. D., B. J. Day, and J. D. Crapo. Extracellular superoxide dismutase: a regulator of nitric oxide bioavailability. Lab. Invest. 75: 617-636, 1996.
    • (1996) Lab. Invest. , vol.75 , pp. 617-636
    • Oury, T.D.1    Day, B.J.2    Crapo, J.D.3
  • 27
    • 0030007683 scopus 로고    scopus 로고
    • Extracellular superoxide dismutase in vessels and airway of humans and baboons
    • Oury, T. D., B. J. Day, and J. D. Crapo. Extracellular superoxide dismutase in vessels and airway of humans and baboons. Free Radic. Biol. Med. 20: 957-965, 1996.
    • (1996) Free Radic. Biol. Med. , vol.20 , pp. 957-965
    • Oury, T.D.1    Day, B.J.2    Crapo, J.D.3
  • 28
    • 0031443873 scopus 로고    scopus 로고
    • Localization of a constitutively active phagocyte-like NADPH oxidase in rabbit aortic adventitia: Enhancement by angiotensin II
    • Pagano, P. J., J. K. Clark, M. E. Cifuentes-Pagano, S. M. Clark, G. M. Callis, and M. T. Quinn. Localization of a constitutively active phagocyte-like NADPH oxidase in rabbit aortic adventitia: enhancement by angiotensin II. Proc. Natl. Acad. Sci. USA 94: 14483-14488, 1997.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 14483-14488
    • Pagano, P.J.1    Clark, J.K.2    Cifuentes-Pagano, M.E.3    Clark, S.M.4    Callis, G.M.5    Quinn, M.T.6
  • 29
    • 0028997671 scopus 로고
    • An NADPH oxidase superoxide-generating system in rabbit aorta
    • Heart Circ. Physiol. 37
    • Pagano, P. J., Y. Ito, K. Torteim, P. M. Gallop, A. I. Tauber, and R. A. Cohen. An NADPH oxidase superoxide-generating system in rabbit aorta. Am. J. Physiol. 268 (Heart Circ. Physiol. 37): H2274-H2280, 1995.
    • (1995) Am. J. Physiol. , vol.268
    • Pagano, P.J.1    Ito, Y.2    Torteim, K.3    Gallop, P.M.4    Tauber, A.I.5    Cohen, R.A.6
  • 30
    • 0027302632 scopus 로고
    • Superoxide anion production by rabbit thoracic aorta: Effect of endothelium-derived nitric oxide
    • Heart Circ. Physiol. 34
    • Pagano, P. J., K. Tornheim, and R. Cohen. Superoxide anion production by rabbit thoracic aorta: effect of endothelium-derived nitric oxide. Am. J. Physiol. 265 (Heart Circ. Physiol. 34): H707-H712, 1993.
    • (1993) Am. J. Physiol. , vol.265
    • Pagano, P.J.1    Tornheim, K.2    Cohen, R.3
  • 31
    • 0023198721 scopus 로고
    • Nitric oxide accounts for the biological activity of endothelium-derived relaxing factor
    • Palmer, R. M., A. G. Ferrige, and S. Moncada. Nitric oxide accounts for the biological activity of endothelium-derived relaxing factor. Nature 327: 524-526, 1987.
    • (1987) Nature , vol.327 , pp. 524-526
    • Palmer, R.M.1    Ferrige, A.G.2    Moncada, S.3
  • 32
    • 0030005713 scopus 로고    scopus 로고
    • Angiotensin II-mediated hypertension in the rat increases vascular superoxide production via membrane NADH/NADPH oxidase activation
    • Rajagopalan, S., S. Kurz, T. Münzel, M. Tarpey, B. A. Freeman, K. K. Griendling, and D. G. Harrison. Angiotensin II-mediated hypertension in the rat increases vascular superoxide production via membrane NADH/NADPH oxidase activation. J. Clin. Invest. 97: 1916-1923, 1996.
    • (1996) J. Clin. Invest. , vol.97 , pp. 1916-1923
    • Rajagopalan, S.1    Kurz, S.2    Münzel, T.3    Tarpey, M.4    Freeman, B.A.5    Griendling, K.K.6    Harrison, D.G.7
  • 33
    • 0022456638 scopus 로고
    • Superoxide anions and hyperoxia inactivate endothelium-derived relaxing factor
    • Heart Circ. Physiol. 19
    • Rubanyi, G. M., and P. M. Vanhoutte. Superoxide anions and hyperoxia inactivate endothelium-derived relaxing factor. Am. J. Physiol. 250 (Heart Circ. Physiol. 19): H822-H827, 1986.
    • (1986) Am. J. Physiol. , vol.250
    • Rubanyi, G.M.1    Vanhoutte, P.M.2
  • 35
    • 0027138959 scopus 로고
    • Manganese-superoxide dismutase in endothelial cells: Localization and mechanism of induction
    • Heart Circ. Physiol. 34
    • Suzuki, K., H. Tatsumi, S. Satoh, T. Senda, T. Nakata, J. Fujii, and N. Taniguchi. Manganese-superoxide dismutase in endothelial cells: localization and mechanism of induction. Am. J. Physiol. 265 (Heart Circ. Physiol. 34): H1173-H1178, 1993.
    • (1993) Am. J. Physiol. , vol.265
    • Suzuki, K.1    Tatsumi, H.2    Satoh, S.3    Senda, T.4    Nakata, T.5    Fujii, J.6    Taniguchi, N.7
  • 36
    • 0031577442 scopus 로고    scopus 로고
    • Tetrahydrobiopterin regulates superoxide and nitric oxide generation by recombinant endothelial nitric oxide synthase
    • Wever, R. M., T. van Dam, H. J. van Rijn, F. de Groot, and T. J. Rabelink. Tetrahydrobiopterin regulates superoxide and nitric oxide generation by recombinant endothelial nitric oxide synthase. Biochem. Biophys. Res. Commun. 237: 340-344, 1997.
    • (1997) Biochem. Biophys. Res. Commun. 237 , pp. 340-344
    • Wever, R.M.1    Van Dam, T.2    Van Rijn, H.J.3    De Groot, F.4    Rabelink, T.J.5
  • 37
    • 0025858127 scopus 로고
    • Mechanisms of impaired endothelium-dependent cerebral vasodilatation in response to bradykinin in hypertensive rats
    • Yang, S. T., W. G. Mayhan, F. M. Faraci, and D. D. Heistad. Mechanisms of impaired endothelium-dependent cerebral vasodilatation in response to bradykinin in hypertensive rats. Stroke 22: 1177-1182, 1991.
    • (1991) Stroke , vol.22 , pp. 1177-1182
    • Yang, S.T.1    Mayhan, W.G.2    Faraci, F.M.3    Heistad, D.D.4


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