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Volumn 1233, Issue C, 2002, Pages 405-414

Nitration of prostacyclin synthase: Mechanism and physiological implications

Author keywords

Nitration; Peroxynitrite; Prostacyclin synthase; Scavenger; Vascular system

Indexed keywords


EID: 80052218732     PISSN: 05315131     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0531-5131(02)00375-8     Document Type: Article
Times cited : (3)

References (43)
  • 1
    • 0032964853 scopus 로고    scopus 로고
    • Selective nitration of prostacyclin synthase and defective vasorelaxation in atherosclerotic bovine coronary arteries
    • Zou, M.H., Leist, M., Ullrich, V., Selective nitration of prostacyclin synthase and defective vasorelaxation in atherosclerotic bovine coronary arteries. Am. J. Pathol. 154:5 (1999), 1359–1365.
    • (1999) Am. J. Pathol. , vol.154 , Issue.5 , pp. 1359-1365
    • Zou, M.H.1    Leist, M.2    Ullrich, V.3
  • 2
    • 0030877284 scopus 로고    scopus 로고
    • Tyrosine nitration as a mechanism of selective inactivation of prostacyclin synthase by peroxynitrite
    • Zou, M., Martin, C., Ullrich, V., Tyrosine nitration as a mechanism of selective inactivation of prostacyclin synthase by peroxynitrite. Biol. Chem. 378:7 (1997), 707–713.
    • (1997) Biol. Chem. , vol.378 , Issue.7 , pp. 707-713
    • Zou, M.1    Martin, C.2    Ullrich, V.3
  • 3
    • 0029879266 scopus 로고    scopus 로고
    • Peroxynitrite formed by simultaneous generation of nitric oxide and superoxide selectively inhibits bovine aortic prostacyclin synthase
    • Zou, M.H., Ullrich, V., Peroxynitrite formed by simultaneous generation of nitric oxide and superoxide selectively inhibits bovine aortic prostacyclin synthase. FEBS Lett. 382:1–2 (1996), 101–104.
    • (1996) FEBS Lett. , vol.382 , Issue.1-2 , pp. 101-104
    • Zou, M.H.1    Ullrich, V.2
  • 4
    • 0029039754 scopus 로고
    • Peroxynitrite-mediated oxidative protein modifications
    • Ischiropoulos, H., al-Mehdi, A.B., Peroxynitrite-mediated oxidative protein modifications. FEBS Lett. 364:3 (1995), 279–282.
    • (1995) FEBS Lett. , vol.364 , Issue.3 , pp. 279-282
    • Ischiropoulos, H.1    al-Mehdi, A.B.2
  • 5
    • 0031045423 scopus 로고    scopus 로고
    • Peroxynitrite-induced tyrosine nitration and phosphorylation in human platelets
    • Mondoro, T.H., Shafer, B.C., Vostal, J.G., Peroxynitrite-induced tyrosine nitration and phosphorylation in human platelets. Free Radical Biol. Med. 22:6 (1997), 1055–1063.
    • (1997) Free Radical Biol. Med. , vol.22 , Issue.6 , pp. 1055-1063
    • Mondoro, T.H.1    Shafer, B.C.2    Vostal, J.G.3
  • 6
    • 0032538450 scopus 로고    scopus 로고
    • Lack of tyrosine nitration by peroxynitrite generated at physiological pH
    • Pfeiffer, S., Mayer, B., Lack of tyrosine nitration by peroxynitrite generated at physiological pH. J. Biol. Chem. 273:42 (1998), 27280–27285.
    • (1998) J. Biol. Chem. , vol.273 , Issue.42 , pp. 27280-27285
    • Pfeiffer, S.1    Mayer, B.2
  • 7
    • 0032499878 scopus 로고    scopus 로고
    • Nitration of the low molecular weight neurofilament is equivalent in sporadic amyotrophic lateral sclerosis and control cervical spinal cord
    • Strong, M.J., Sopper, M.M., Crow, J.P., Strong, W.L., Beckman, J.S., Nitration of the low molecular weight neurofilament is equivalent in sporadic amyotrophic lateral sclerosis and control cervical spinal cord. Biochem. Biophys. Res. Commun. 248:1 (1998), 157–164.
    • (1998) Biochem. Biophys. Res. Commun. , vol.248 , Issue.1 , pp. 157-164
    • Strong, M.J.1    Sopper, M.M.2    Crow, J.P.3    Strong, W.L.4    Beckman, J.S.5
  • 8
    • 0029895815 scopus 로고    scopus 로고
    • Inducible nitric oxide synthase is present within human atherosclerotic lesions and promotes the formation and activity of peroxynitrite
    • Buttery, L.D., Springall, D.R., Chester, A.H., Evans, T.J., Standfield, E.N., Parums, D.V., Yacoub, M.H., Polak, J.M., Inducible nitric oxide synthase is present within human atherosclerotic lesions and promotes the formation and activity of peroxynitrite. Lab. Invest. 75:1 (1996), 77–85.
    • (1996) Lab. Invest. , vol.75 , Issue.1 , pp. 77-85
    • Buttery, L.D.1    Springall, D.R.2    Chester, A.H.3    Evans, T.J.4    Standfield, E.N.5    Parums, D.V.6    Yacoub, M.H.7    Polak, J.M.8
  • 10
    • 0033150608 scopus 로고    scopus 로고
    • Tyrosine modifications and inactivation of active site manganese superoxide dismutase mutant (Y34F) by peroxynitrite
    • MacMillan-Crow, L.A., Thompson, J.A., Tyrosine modifications and inactivation of active site manganese superoxide dismutase mutant (Y34F) by peroxynitrite. Arch. Biochem. Biophys. 366:1 (1999), 82–88.
    • (1999) Arch. Biochem. Biophys. , vol.366 , Issue.1 , pp. 82-88
    • MacMillan-Crow, L.A.1    Thompson, J.A.2
  • 11
    • 0031750066 scopus 로고    scopus 로고
    • Manganese porphyrins as redox-coupled peroxynitrite reductase
    • Lee, J., Hunt, J.A., Groves, J.T., Manganese porphyrins as redox-coupled peroxynitrite reductase. J. Am. Chem. Soc. 120 (1998), 6053–6061.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 6053-6061
    • Lee, J.1    Hunt, J.A.2    Groves, J.T.3
  • 13
    • 0032486758 scopus 로고    scopus 로고
    • Mechanism of iron porphyrin reactions with peroxynitrite
    • Lee, J., Hunt, J.A., Groves, J.T., Mechanism of iron porphyrin reactions with peroxynitrite. J. Am. Chem. Soc. 120 (1998), 7493–7501.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 7493-7501
    • Lee, J.1    Hunt, J.A.2    Groves, J.T.3
  • 15
    • 0027303364 scopus 로고
    • Interaction of myeloperoxidase with peroxynitrite. A comparison with lactoperoxidase, horseradish peroxidase and catalase
    • Floris, R., Piersma, S.R., Yang, G., Jones, P., Wever, R., Interaction of myeloperoxidase with peroxynitrite. A comparison with lactoperoxidase, horseradish peroxidase and catalase. Eur. J. Biochem. 215:3 (1993), 767–775.
    • (1993) Eur. J. Biochem. , vol.215 , Issue.3 , pp. 767-775
    • Floris, R.1    Piersma, S.R.2    Yang, G.3    Jones, P.4    Wever, R.5
  • 16
    • 0033599558 scopus 로고    scopus 로고
    • Hydroxyl radical formation during peroxynitrous acid decomposition
    • Coddington, J.W., Hurst, J.K., Lymar, S.V., Hydroxyl radical formation during peroxynitrous acid decomposition. J. Am. Chem. Soc. 121 (1999), 2438–2443.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 2438-2443
    • Coddington, J.W.1    Hurst, J.K.2    Lymar, S.V.3
  • 17
    • 0033678831 scopus 로고    scopus 로고
    • Nitration and inactivation of cytochrome P450BM-3 by peroxynitrite: stopped-flow measurements prove ferryl intermediates
    • Daiber, A., Herold, S., Schoneich, C., Namgaladze, D., Peterson, J.A., Ullrich, V., Nitration and inactivation of cytochrome P450BM-3 by peroxynitrite: stopped-flow measurements prove ferryl intermediates. Eur. J. Biochem. 267:23 (2000), 6729–6739.
    • (2000) Eur. J. Biochem. , vol.267 , Issue.23 , pp. 6729-6739
    • Daiber, A.1    Herold, S.2    Schoneich, C.3    Namgaladze, D.4    Peterson, J.A.5    Ullrich, V.6
  • 18
    • 0028855905 scopus 로고
    • Prostacyclin and thromboxane synthases
    • Tanabe, T., Ullrich, V., Prostacyclin and thromboxane synthases. J. Lipid Mediators Cell Signal. 12:2–3 (1995), 243–255.
    • (1995) J. Lipid Mediators Cell Signal. , vol.12 , Issue.2-3 , pp. 243-255
    • Tanabe, T.1    Ullrich, V.2
  • 19
    • 0032436901 scopus 로고    scopus 로고
    • New aspects in the reaction mechanism of phenol with peroxynitrite: the role of phenoxy radicals
    • Daiber, A., Mehl, M., Ullrich, V., New aspects in the reaction mechanism of phenol with peroxynitrite: the role of phenoxy radicals. Nitric Oxide 2:4 (1998), 259–268.
    • (1998) Nitric Oxide , vol.2 , Issue.4 , pp. 259-268
    • Daiber, A.1    Mehl, M.2    Ullrich, V.3
  • 20
    • 0030052854 scopus 로고    scopus 로고
    • Nitration and hydroxylation of phenolic compounds by peroxynitrite
    • Ramezanian, M.S., Padmaja, S., Koppenol, W.H., Nitration and hydroxylation of phenolic compounds by peroxynitrite. Chem. Res. Toxicol. 9 (1996), 232–240.
    • (1996) Chem. Res. Toxicol. , vol.9 , pp. 232-240
    • Ramezanian, M.S.1    Padmaja, S.2    Koppenol, W.H.3
  • 21
    • 0029437225 scopus 로고
    • Reactions between nitric oxide, superoxide and peroxynitrite: footprints of peroxynitrite in vivo
    • Crow, J.P., Beckman, J.S., Reactions between nitric oxide, superoxide and peroxynitrite: footprints of peroxynitrite in vivo. Adv. Pharmacol. 34 (1995), 17–43.
    • (1995) Adv. Pharmacol. , vol.34 , pp. 17-43
    • Crow, J.P.1    Beckman, J.S.2
  • 22
    • 0032387681 scopus 로고    scopus 로고
    • Interleukin 1β decreases prostacyclin synthase activity in rat mesangial cells via endogenous peroxynitrite formation
    • Zou, M.H., Klein, T., Pasquet, J.P., Ullrich, V., Interleukin 1β decreases prostacyclin synthase activity in rat mesangial cells via endogenous peroxynitrite formation. Biochem. J. 336:Pt. 2 (1998), 507–512.
    • (1998) Biochem. J. , vol.336 , pp. 507-512
    • Zou, M.H.1    Klein, T.2    Pasquet, J.P.3    Ullrich, V.4
  • 23
    • 0033990512 scopus 로고    scopus 로고
    • Ebselen as a peroxynitrite scavenger in vitro and ex vivo
    • Daiber, A., Zou, M.H., Bachschmid, M., Ullrich, V., Ebselen as a peroxynitrite scavenger in vitro and ex vivo. Biochem. Pharmacol. 59 (2000), 153–160.
    • (2000) Biochem. Pharmacol. , vol.59 , pp. 153-160
    • Daiber, A.1    Zou, M.H.2    Bachschmid, M.3    Ullrich, V.4
  • 24
    • 0030566871 scopus 로고    scopus 로고
    • Kinetic study of the reaction of ebselen with peroxynitrite
    • Masumoto, H., Kissner, R., Koppenol, W.H., Sies, H., Kinetic study of the reaction of ebselen with peroxynitrite. FEBS Lett. 398 (1996), 179–182.
    • (1996) FEBS Lett. , vol.398 , pp. 179-182
    • Masumoto, H.1    Kissner, R.2    Koppenol, W.H.3    Sies, H.4
  • 25
    • 0030250041 scopus 로고    scopus 로고
    • Carbon dioxide enhancement of peroxynitrite-mediated protein tyrosine nitration
    • Gow, A., Duran, D., Thom, S.R., Ischiropoulos, H., Carbon dioxide enhancement of peroxynitrite-mediated protein tyrosine nitration. Arch. Biochem. Biophys. 333:1 (1996), 42–48.
    • (1996) Arch. Biochem. Biophys. , vol.333 , Issue.1 , pp. 42-48
    • Gow, A.1    Duran, D.2    Thom, S.R.3    Ischiropoulos, H.4
  • 27
    • 0034176278 scopus 로고    scopus 로고
    • Rapid reactions of peroxynitrite with heme-thiolate proteins as the basis for protection of prostacyclin synthase from inactivation by nitration
    • Zou, M.H., Daiber, A., Peterson, J.A., Shoun, H., Ullrich, V., Rapid reactions of peroxynitrite with heme-thiolate proteins as the basis for protection of prostacyclin synthase from inactivation by nitration. Arch. Biochem. Biophys. 376:1 (2000), 149–155.
    • (2000) Arch. Biochem. Biophys. , vol.376 , Issue.1 , pp. 149-155
    • Zou, M.H.1    Daiber, A.2    Peterson, J.A.3    Shoun, H.4    Ullrich, V.5
  • 28
    • 0035872246 scopus 로고    scopus 로고
    • Colocalization prostacyclin (PGI2) synthase-caveolin-1 in endothelial cells and new roles for PGI2 in angiogenesis
    • Spisni, E., Griffoni, C., Santi, S., Riccio, M., Marulli, R., Bartolini, G., Toni, M., Ullrich, V., Tomasi, V., Colocalization prostacyclin (PGI2) synthase-caveolin-1 in endothelial cells and new roles for PGI2 in angiogenesis. Exp. Cell Res. 266:1 (2001), 31–43.
    • (2001) Exp. Cell Res. , vol.266 , Issue.1 , pp. 31-43
    • Spisni, E.1    Griffoni, C.2    Santi, S.3    Riccio, M.4    Marulli, R.5    Bartolini, G.6    Toni, M.7    Ullrich, V.8    Tomasi, V.9
  • 29
    • 0032575596 scopus 로고    scopus 로고
    • Effect of xanthine oxidase inhibition on endothelium-dependent and nitrergic relaxations
    • Ellis, A., Li, C.G., Rand, M.J., Effect of xanthine oxidase inhibition on endothelium-dependent and nitrergic relaxations. Eur. J. Pharmacol. 356:1 (1998), 41–47.
    • (1998) Eur. J. Pharmacol. , vol.356 , Issue.1 , pp. 41-47
    • Ellis, A.1    Li, C.G.2    Rand, M.J.3
  • 30
    • 0032051656 scopus 로고    scopus 로고
    • Expression of functional neutrophil-type NADPH oxidase in cultured rat coronary microvascular endothelial cells
    • Bayraktutan, U., Draper, N., Lang, D., Shah, A.M., Expression of functional neutrophil-type NADPH oxidase in cultured rat coronary microvascular endothelial cells. Cardiovasc. Res. 38:1 (1998), 256–262.
    • (1998) Cardiovasc. Res. , vol.38 , Issue.1 , pp. 256-262
    • Bayraktutan, U.1    Draper, N.2    Lang, D.3    Shah, A.M.4
  • 31
    • 0343990001 scopus 로고    scopus 로고
    • Involvement of the reductase domain of neuronal nitric oxide synthase in superoxide anion production
    • Miller, R.T., Martasek, P., Roman, L.J., Nishimura, J.S., Masters, B.S., Involvement of the reductase domain of neuronal nitric oxide synthase in superoxide anion production. Biochemistry 36:49 (1997), 15277–15284.
    • (1997) Biochemistry , vol.36 , Issue.49 , pp. 15277-15284
    • Miller, R.T.1    Martasek, P.2    Roman, L.J.3    Nishimura, J.S.4    Masters, B.S.5
  • 32
    • 0032921588 scopus 로고    scopus 로고
    • Role of increased production of superoxide anions by NAD(P)H oxidase and xanthine oxidase in prolonged endotoxemia
    • Brandes, R.P., Koddenberg, G., Gwinner, W., Kim, D., Kruse, H.J., Busse, R., Mugge, A., Role of increased production of superoxide anions by NAD(P)H oxidase and xanthine oxidase in prolonged endotoxemia. Hypertension 33:5 (1999), 1243–1249.
    • (1999) Hypertension , vol.33 , Issue.5 , pp. 1243-1249
    • Brandes, R.P.1    Koddenberg, G.2    Gwinner, W.3    Kim, D.4    Kruse, H.J.5    Busse, R.6    Mugge, A.7
  • 33
    • 0032924640 scopus 로고    scopus 로고
    • Oxidative stress in brain ischemia
    • Love, S., Oxidative stress in brain ischemia. Brain Pathol. 9:1 (1999), 119–131.
    • (1999) Brain Pathol. , vol.9 , Issue.1 , pp. 119-131
    • Love, S.1
  • 34
    • 0033609715 scopus 로고    scopus 로고
    • Prostacyclin synthase is localized in rat, bovine and human neuronal brain cells
    • Mehl, M., Bidmon, H.J., Hilbig, H., Zilles, K., Dringen, R., Ullrich, V., Prostacyclin synthase is localized in rat, bovine and human neuronal brain cells. Neurosci. Lett. 271 (1999), 187–190.
    • (1999) Neurosci. Lett. , vol.271 , pp. 187-190
    • Mehl, M.1    Bidmon, H.J.2    Hilbig, H.3    Zilles, K.4    Dringen, R.5    Ullrich, V.6
  • 35
    • 0032529412 scopus 로고    scopus 로고
    • Myeloperoxidase and horseradish peroxidase catalyze tyrosine nitration in proteins from nitrite and hydrogen peroxide
    • Sampson, J.B., Ye, Y., Rosen, H., Beckman, J.S., Myeloperoxidase and horseradish peroxidase catalyze tyrosine nitration in proteins from nitrite and hydrogen peroxide. Arch. Biochem. Biophys. 356:2 (1998), 207–213.
    • (1998) Arch. Biochem. Biophys. , vol.356 , Issue.2 , pp. 207-213
    • Sampson, J.B.1    Ye, Y.2    Rosen, H.3    Beckman, J.S.4
  • 36
    • 0029760021 scopus 로고    scopus 로고
    • Formation of nitrating and chlorinating species by reaction of nitrite with hypochlorous acid. A novel mechanism for nitric oxide-mediated protein modification
    • Eiserich, J.P., Cross, C.E., Jones, A.D., Halliwell, B., van der Vliet, A., Formation of nitrating and chlorinating species by reaction of nitrite with hypochlorous acid. A novel mechanism for nitric oxide-mediated protein modification. J. Biol. Chem. 271:32 (1996), 19199–19208.
    • (1996) J. Biol. Chem. , vol.271 , Issue.32 , pp. 19199-19208
    • Eiserich, J.P.1    Cross, C.E.2    Jones, A.D.3    Halliwell, B.4    van der Vliet, A.5
  • 37
    • 0033066640 scopus 로고    scopus 로고
    • Prostaglandin endoperoxide-dependent vasospasm in bovine coronary arteries after nitration of prostacyclin synthase
    • Zou, M.H., Jendral, M., Ullrich, V., Prostaglandin endoperoxide-dependent vasospasm in bovine coronary arteries after nitration of prostacyclin synthase. Br. J. Pharmacol. 126:6 (1999), 1283–1292.
    • (1999) Br. J. Pharmacol. , vol.126 , Issue.6 , pp. 1283-1292
    • Zou, M.H.1    Jendral, M.2    Ullrich, V.3
  • 38
    • 0023607527 scopus 로고
    • Cyclic cGMP synthesis and function
    • Waldmann, S.A., Murad, F., Cyclic cGMP synthesis and function. Pharmacol. Rev. 39 (1987), 163–196.
    • (1987) Pharmacol. Rev. , vol.39 , pp. 163-196
    • Waldmann, S.A.1    Murad, F.2
  • 39
    • 0031895339 scopus 로고    scopus 로고
    • The endothelium in acute coronary syndromes
    • Noll, G., Luscher, T.F., The endothelium in acute coronary syndromes. Eur. Heart J. 19:Suppl. C (1998), C30–C38.
    • (1998) Eur. Heart J. , vol.19 , pp. C30-C38
    • Noll, G.1    Luscher, T.F.2
  • 40
    • 0027339829 scopus 로고
    • Identification of functional PGH2/TxA2 receptors on human endothelial cells
    • Kent, K.C., Collins, L.J., Schwerin, F.T., Raychowdhury, M.K., Ware, J.A., Identification of functional PGH2/TxA2 receptors on human endothelial cells. Circ. Res. 72:5 (1993), 958–965.
    • (1993) Circ. Res. , vol.72 , Issue.5 , pp. 958-965
    • Kent, K.C.1    Collins, L.J.2    Schwerin, F.T.3    Raychowdhury, M.K.4    Ware, J.A.5
  • 41
    • 0026773264 scopus 로고
    • Role of superoxide anion and endothelium in vasoconstrictor action of prostaglandin endoperoxide
    • Tesfamariam, B., Cohen, R.A., Role of superoxide anion and endothelium in vasoconstrictor action of prostaglandin endoperoxide. Am. J. Physiol. 262:6 Pt 2 (1992), H1915–H1919.
    • (1992) Am. J. Physiol. , vol.262 , Issue.6 , pp. H1915-H1919
    • Tesfamariam, B.1    Cohen, R.A.2
  • 42
    • 0033031694 scopus 로고    scopus 로고
    • Denitration of peroxynitrite-treated proteins by “protein nitratases” from dog prostate
    • Kuo, W.N., Kanadia, R.N., Shanbhag, V.P., Denitration of peroxynitrite-treated proteins by “protein nitratases” from dog prostate. Biochem. Mol. Biol. Int. 47:6 (1999), 1061–1067.
    • (1999) Biochem. Mol. Biol. Int. , vol.47 , Issue.6 , pp. 1061-1067
    • Kuo, W.N.1    Kanadia, R.N.2    Shanbhag, V.P.3


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