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Volumn 4, Issue , 2004, Pages

Peroxynitrite-mediated inactivation of heme oxygenases

Author keywords

[No Author keywords available]

Indexed keywords

3,3 BIS(2 AMINOETHYL) 1 HYDROXY 2 OXOTRIAZENE; CARBON MONOXIDE; HEME OXYGENASE; HEME OXYGENASE 1; NITRIC OXIDE; NITRIC OXIDE SYNTHASE; NITROMETHANE; PEROXYNITRITE; REACTIVE OXYGEN METABOLITE; S NITROSOGLUTATHIONE; THIOL DERIVATIVE; TYROSINE; HEME OXYGENASE 2; HEME OXYGENASE-2; NITRITE; PEROXYNITROUS ACID;

EID: 12944289490     PISSN: 14712210     EISSN: None     Source Type: Journal    
DOI: 10.1186/1471-2210-4-26     Document Type: Article
Times cited : (38)

References (46)
  • 1
    • 0031732387 scopus 로고    scopus 로고
    • Endogenous carbon monoxide in control of respiration
    • Prabhakar NR: Endogenous carbon monoxide in control of respiration. Respir Physiol 1998, 114:57-64.
    • (1998) Respir. Physiol. , vol.114 , pp. 57-64
    • Prabhakar, N.R.1
  • 2
    • 0030923630 scopus 로고    scopus 로고
    • The heme oxygenase system: A regulator of second messenger gases
    • Maines MD: The heme oxygenase system: a regulator of second messenger gases. Annu Rev Pharmacol Toxicol 1997, 37: 17-554.
    • (1997) Annu. Rev. Pharmacol. Toxicol. , vol.37 , pp. 517-554
    • Maines, M.D.1
  • 3
    • 0031757984 scopus 로고    scopus 로고
    • Antibody-induced transplant arteriosclerosis is prevented by graft expression of anti-oxidant and anti-apoptotic genes
    • Hancock WW, Buelow R, Sayegh MH, Turka LA: Antibody-induced transplant arteriosclerosis is prevented by graft expression of anti-oxidant and anti-apoptotic genes. Nat Med 1998, 4:1392-1396.
    • (1998) Nat. Med. , vol.4 , pp. 1392-1396
    • Hancock, W.W.1    Buelow, R.2    Sayegh, M.H.3    Turka, L.A.4
  • 6
    • 0027176344 scopus 로고
    • Biliverdin reductase is heat resistant and coexpressed with constitutive and heat shock forms of heme oxygenase in brain
    • Ewing JF, Weber CM, Maines MD: Biliverdin reductase is heat resistant and coexpressed with constitutive and heat shock forms of heme oxygenase in brain. J Neurochem 1993, 61:1015-1023.
    • (1993) J. Neurochem. , vol.61 , pp. 1015-1023
    • Ewing, J.F.1    Weber, C.M.2    Maines, M.D.3
  • 7
    • 0023831291 scopus 로고
    • Resolution of the rat brain heme oxygenase activity: Absence of a detectable amount of the inducible form (HO-1)
    • Trakshel GM, Kutty RK, Maines MD: Resolution of the rat brain heme oxygenase activity: absence of a detectable amount of the inducible form (HO-1). Arch Biochem Biophys 1988, 260: 32-739.
    • (1988) Arch. Biochem. Biophys. , vol.260 , pp. 732-739
    • Trakshel, G.M.1    Kutty, R.K.2    Maines, M.D.3
  • 8
    • 8544246393 scopus 로고    scopus 로고
    • Isolation and characterization of a cDNA from the rat brain that encodes hemoprotein heme oxygenase-3
    • McCoubrey WK Jr, Huang TJ, Maines MD: Isolation and characterization of a cDNA from the rat brain that encodes hemoprotein heme oxygenase-3. Eur J Biochem 1997, 247:725-732.
    • (1997) Eur. J. Biochem. , vol.247 , pp. 725-732
    • McCoubrey Jr., W.K.1    Huang, T.J.2    Maines, M.D.3
  • 9
    • 0027452195 scopus 로고
    • A beneficial role of bile pigments as an endogenous tissue protector: Anti-complement effects of biliverdin and conjugated bilirubin
    • Nakagami T, Toyomura K, Kinoshita T, Morisawa S: A beneficial role of bile pigments as an endogenous tissue protector: anti-complement effects of biliverdin and conjugated bilirubin. Biochim Biophys Acta 1993, 1158:189-193.
    • (1993) Biochim. Biophys. Acta , vol.1158 , pp. 189-193
    • Nakagami, T.1    Toyomura, K.2    Kinoshita, T.3    Morisawa, S.4
  • 10
    • 0030045835 scopus 로고    scopus 로고
    • Heme oxygenase: A novel target for the modulation of the inflammatory response
    • Willis D, Moore AR, Frederick R, Willoughby DA: Heme oxygenase: a novel target for the modulation of the inflammatory response Nat Med 1996, 2:87-90.
    • (1996) Nat. Med. , vol.2 , pp. 87-90
    • Willis, D.1    Moore, A.R.2    Frederick, R.3    Willoughby, D.A.4
  • 12
    • 0028929741 scopus 로고
    • Nitric oxide signaling to iron-regulatory protein: Direct control of ferritin mRNA translation and transferrin receptor mRNA stability in transfected fibroblasts
    • Pantopoulos K, Hentze MW: Nitric oxide signaling to iron-regulatory protein: direct control of ferritin mRNA translation and transferrin receptor mRNA stability in transfected fibroblasts. Proc Natl Acad Sci U S A 1995, 92:1267-1271.
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 1267-1271
    • Pantopoulos, K.1    Hentze, M.W.2
  • 13
    • 0035014540 scopus 로고    scopus 로고
    • Molecular mechanisms by which iron induces nitric oxide synthesis in cultured proximal tubule cells
    • Chen L, Wang Y, Kairaitis LK, Wang Y, Zhang BH, Harris DC: Molecular mechanisms by which iron induces nitric oxide synthesis in cultured proximal tubule cells. Exp Nephrol 2001, 9: 98-204.
    • (2001) Exp. Nephrol. , vol.9 , pp. 198-204
    • Chen, L.1    Wang, Y.2    Kairaitis, L.K.3    Wang, Y.4    Zhang, B.H.5    Harris, D.C.6
  • 14
    • 0026034934 scopus 로고
    • Endothelium-dependent and - Independent vasodilation involving cyclic GMP: Relaxation induced by nitric oxide, carbon monoxide and light
    • Furchgott RF, Jothianandan D: Endothelium-dependent and - independent vasodilation involving cyclic GMP: relaxation induced by nitric oxide, carbon monoxide and light. Blood Vessels 1991, 28:52-61.
    • (1991) Blood Vessels , vol.28 , pp. 52-61
    • Furchgott, R.F.1    Jothianandan, D.2
  • 15
    • 0005770648 scopus 로고    scopus 로고
    • The direct effect of carbon monoxide on KCa channels in vascular smooth muscle cells
    • Wang R, Wu L, Wang Z: The direct effect of carbon monoxide on KCa channels in vascular smooth muscle cells. Pflugers Arch 1997, 434:285-291.
    • (1997) Pflugers Arch. , vol.434 , pp. 285-291
    • Wang, R.1    Wu, L.2    Wang, Z.3
  • 16
    • 0000647710 scopus 로고    scopus 로고
    • Carbon monoxide and vascular cell function
    • (Review)
    • Durante W, Schafer AI: Carbon monoxide and vascular cell function (Review). Int J Mol Med 1998, 2:255-262.
    • (1998) Int. J. Mol. Med. , vol.2 , pp. 255-262
    • Durante, W.1    Schafer, A.I.2
  • 21
    • 0029037495 scopus 로고
    • The chemistry of peroxynitrite: A product from the reaction of nitric oxide with superoxide
    • Pryor WA, Squadrito GL: The chemistry of peroxynitrite: a product from the reaction of nitric oxide with superoxide. Am J Physiol 1995, 268:2699-2722.
    • (1995) Am. J. Physiol. , vol.268 , pp. 2699-2722
    • Pryor, W.A.1    Squadrito, G.L.2
  • 22
    • 0033136330 scopus 로고    scopus 로고
    • Peroxynitrite induces haem oxygenase-1 in vascular endothelial cells: A link to apoptosis
    • Foresti R, Sarathchandra P, Clark JE, Green CJ, Motterlini R: Peroxynitrite induces haem oxygenase-1 in vascular endothelial cells: a link to apoptosis. Biochem J 1999, 339:729-736.
    • (1999) Biochem. J. , vol.339 , pp. 729-736
    • Foresti, R.1    Sarathchandra, P.2    Clark, J.E.3    Green, C.J.4    Motterlini, R.5
  • 23
    • 0030875968 scopus 로고    scopus 로고
    • Thiol compounds interact with nitric oxide in regulating heme oxygenase-1 induction in endothelial cells. Involvement of superoxide and peroxynitrite anions
    • Foresti R, Clark JE, Green CJ, Motterlini R: Thiol compounds interact with nitric oxide in regulating heme oxygenase-1 induction in endothelial cells. Involvement of superoxide and peroxynitrite anions. J Biol Chem 1997, 272:18411-18417.
    • (1997) J. Biol. Chem. , vol.272 , pp. 18411-18417
    • Foresti, R.1    Clark, J.E.2    Green, C.J.3    Motterlini, R.4
  • 24
    • 0034607632 scopus 로고    scopus 로고
    • Endothelial heme oxygenase-1 induction by hypoxia. Modulation by inducible nitric-oxide synthase and S-nitrosothiols
    • Motterlini R, Foresti R, Bassi R, Calabrese V, Clark JE, Green CJ: Endothelial heme oxygenase-1 induction by hypoxia. Modulation by inducible nitric-oxide synthase and S-nitrosothiols. J Biol Chem 2000, 275:13613-20.
    • (2000) J. Biol. Chem. , vol.275 , pp. 13613-13620
    • Motterlini, R.1    Foresti, R.2    Bassi, R.3    Calabrese, V.4    Clark, J.E.5    Green, C.J.6
  • 27
    • 1842587604 scopus 로고    scopus 로고
    • Nitric oxide and its role in ischaemic brain injury
    • Keynes RG, Garthwaite J: Nitric oxide and its role in ischaemic brain injury. Curr Mol Med 2004, 4:179-191.
    • (2004) Curr. Mol. Med. , vol.4 , pp. 179-191
    • Keynes, R.G.1    Garthwaite, J.2
  • 28
    • 1442324343 scopus 로고    scopus 로고
    • Peroxynitrite induces apoptosis in rat aortic smooth muscle cells: Possible relation to vascular diseases
    • Li J, Li W, Su J, Liu W, Altura BT, Altura BM: Peroxynitrite induces apoptosis in rat aortic smooth muscle cells: possible relation to vascular diseases. Exp Biol Med (Maywood) 2004, 229:264-269.
    • (2004) Exp. Biol. Med. (Maywood) , vol.229 , pp. 264-269
    • Li, J.1    Li, W.2    Su, J.3    Liu, W.4    Altura, B.T.5    Altura, B.M.6
  • 30
    • 0029959717 scopus 로고    scopus 로고
    • DNA strand breakage and activation of poly-ADP ribosyltransferase: A cytotoxic pathway triggered by peroxynitrite
    • Szabo C: DNA strand breakage and activation of poly-ADP ribosyltransferase: a cytotoxic pathway triggered by peroxynitrite. Free Radic Biol Med 1996, 21:855-869.
    • (1996) Free Radic. Biol. Med. , vol.21 , pp. 855-869
    • Szabo, C.1
  • 31
    • 1942489300 scopus 로고    scopus 로고
    • Kaposi sarcoma-associated herpesvirus (KSHV) induces heme oxygenase-1 expression and activity in KSHV-infected endothelial cells
    • McAllister SC, Hansen SG, Ruhl RA, Raggo CM, DeFilippis VR, Greenspan D, Fruh K, Moses AV: Kaposi sarcoma-associated herpesvirus (KSHV) induces heme oxygenase-1 expression and activity in KSHV-infected endothelial cells. Blood 2004, 103:3465-73.
    • (2004) Blood , vol.103 , pp. 3465-3473
    • McAllister, S.C.1    Hansen, S.G.2    Ruhl, R.A.3    Raggo, C.M.4    DeFilippis, V.R.5    Greenspan, D.6    Fruh, K.7    Moses, A.V.8
  • 32
    • 0035213116 scopus 로고    scopus 로고
    • Effect of selenolipoic acid on peroxynitrite-dependent inactivation of NADPHcytochrome P450 reductase
    • Sergeeva SV, Slepneva IA, Khramtsov VV: Effect of selenolipoic acid on peroxynitrite-dependent inactivation of NADPHcytochrome P450 reductase. Free Radic Res 2001, 35: 91-497.
    • (2001) Free Radic. Res. , vol.35 , pp. 491-497
    • Sergeeva, S.V.1    Slepneva, I.A.2    Khramtsov, V.V.3
  • 33
    • 0037222168 scopus 로고    scopus 로고
    • Activation of microsomal glutathione s-transferase by peroxynitrite
    • Ji Y, Bennett BM: Activation of microsomal glutathione s-transferase by peroxynitrite. Mol Pharmacol 2003, 63: 36-146.
    • (2003) Mol. Pharmacol. , vol.63 , pp. 136-146
    • Ji, Y.1    Bennett, B.M.2
  • 35
    • 0024556871 scopus 로고
    • Structural organization of the human heme oxygenase gene and the function of its promoter
    • Shibahara S, Sato M, Muller RM, Yoshida T: Structural organization of the human heme oxygenase gene and the function of its promoter. Eur J Biochem 1989, 179:557-563.
    • (1989) Eur. J. Biochem. , vol.179 , pp. 557-563
    • Shibahara, S.1    Sato, M.2    Muller, R.M.3    Yoshida, T.4
  • 36
    • 0023854047 scopus 로고
    • Evidence suggesting that the two forms of heme oxygenase are products of different genes
    • Cruse I, Maines MD: Evidence suggesting that the two forms of heme oxygenase are products of different genes. J Biol Chem 1988, 263:3348-3353.
    • (1988) J. Biol. Chem. , vol.263 , pp. 3348-3353
    • Cruse, I.1    Maines, M.D.2
  • 37
    • 0026653813 scopus 로고
    • Human heme oxygenase-2: Characterization and expression of a full-length cDNA and evidence suggesting that the two HO-2 transcripts may differ by choice of polyadenylation signal
    • McCoubrey WK Jr, Ewing JF, Maines MD: Human heme oxygenase-2: characterization and expression of a full-length cDNA and evidence suggesting that the two HO-2 transcripts may differ by choice of polyadenylation signal. Arch Biochem Biophys 1992, 295: 3-20.
    • (1992) Arch. Biochem. Biophys. , vol.295 , pp. 13-20
    • McCoubrey Jr., W.K.1    Ewing, J.F.2    Maines, M.D.3
  • 38
    • 0033568133 scopus 로고    scopus 로고
    • Interaction of heme oxygenase-2 with nitric oxide donors. Is the oxygenase an intracellular 'sink' for NO?
    • Ding Y, McCoubrey WK Jr, Maines MD: Interaction of heme oxygenase-2 with nitric oxide donors. Is the oxygenase an intracellular 'sink' for NO? Eur J Biochem 1999, 264:854-861.
    • (1999) Eur. J. Biochem. , vol.264 , pp. 854-861
    • Ding, Y.1    McCoubrey Jr., W.K.2    Maines, M.D.3
  • 39
    • 0034871085 scopus 로고    scopus 로고
    • Heme oxygenase-2 interaction with metalloporphyrins: Function of heme regulatory motifs
    • Huang TJ, McCoubrey WK Jr, Maines MD: Heme oxygenase-2 interaction with metalloporphyrins: function of heme regulatory motifs Antioxid Redox Signal 2001, 3:685-696.
    • (2001) Antioxid. Redox Signal , vol.3 , pp. 685-696
    • Huang, T.J.1    McCoubrey Jr., W.K.2    Maines, M.D.3
  • 40
    • 0032483454 scopus 로고    scopus 로고
    • Heme and the endothelium. Effects of nitric oxide on catalytic iron and heme degradation by heme oxygenase
    • Juckett M, Zheng Y, Yuan H, Pastor T, Antholine W, Weber M, Vercellotti G: Heme and the endothelium. Effects of nitric oxide on catalytic iron and heme degradation by heme oxygenase. J Biol Chem 1998, 273:23388-23397.
    • (1998) J. Biol. Chem. , vol.273 , pp. 23388-23397
    • Juckett, M.1    Zheng, Y.2    Yuan, H.3    Pastor, T.4    Antholine, W.5    Weber, M.6    Vercellotti, G.7
  • 41
    • 0346100520 scopus 로고    scopus 로고
    • Peroxynitrite reactivity with amino acids and proteins
    • Alvarez B, Radi R: Peroxynitrite reactivity with amino acids and proteins. Amino Acids 2003, 25:295-311.
    • (2003) Amino Acids , vol.25 , pp. 295-311
    • Alvarez, B.1    Radi, R.2
  • 43
    • 0030065519 scopus 로고    scopus 로고
    • Microsomal formation of S-nitrosoglutathione from organic nitrites: Possible role of membrane-bound glutathione transferase
    • Ji Y, Akerboom TP, Sies H: Microsomal formation of S-nitrosoglutathione from organic nitrites: possible role of membrane-bound glutathione transferase. Biochem J 1996, 313: 77-380.
    • (1996) Biochem. J. , vol.313 , pp. 377-380
    • Ji, Y.1    Akerboom, T.P.2    Sies, H.3
  • 46
    • 0023837193 scopus 로고
    • Heme oxygenase activity as measured by carbon monoxide production
    • Vreman HJ, Stevenson DK: Heme oxygenase activity as measured by carbon monoxide production. Anal Biochem 1988, 168:31-38.
    • (1988) Anal. Biochem. , vol.168 , pp. 31-38
    • Vreman, H.J.1    Stevenson, D.K.2


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