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Volumn 20, Issue 1, 1996, Pages 63-73

Nitric oxide donors modulate ferritin and protect endothelium from oxidative injury

Author keywords

Endothelium; Ferritin; Free radicals; Nitric oxide; Oxidative injury

Indexed keywords

ACONITATE HYDRATASE; CHROMIUM 51; DEFEROXAMINE MESYLATE; DIETHYLENETRIAMINE; FERRITIN; FREE RADICAL; HEME OXYGENASE; MESSENGER RNA; N ACETYL S NITROSOPENICILLAMINE; NITRIC OXIDE;

EID: 0030022609     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/0891-5849(95)02024-1     Document Type: Article
Times cited : (37)

References (45)
  • 1
    • 0023187143 scopus 로고
    • Comparative pharmacology of endothelium-derived relaxing factor, nitric oxide and prostacyclin in platelets
    • Radomski, M.; Palmer, R. M. J.; Moncada, S. Comparative pharmacology of endothelium-derived relaxing factor, nitric oxide and prostacyclin in platelets. Br. J. Pharmacol. 92:181-187; 1987.
    • (1987) Br. J. Pharmacol. , vol.92 , pp. 181-187
    • Radomski, M.1    Palmer, R.M.J.2    Moncada, S.3
  • 2
    • 0023187143 scopus 로고
    • Comparative pharmacology of endothelium-derived relaxing factor, nitric oxide and prostacyclin in platelets
    • Radomski, M. W.; Palmer, R. M. J.; Moncada, S. Comparative pharmacology of endothelium-derived relaxing factor, nitric oxide and prostacyclin in platelets. Br. J. Pharmacol. 92:181-187; 1987.
    • (1987) Br. J. Pharmacol. , vol.92 , pp. 181-187
    • Radomski, M.W.1    Palmer, R.M.J.2    Moncada, S.3
  • 3
    • 0025731835 scopus 로고
    • Nitric oxide: An endoge nous modulator of leukocyte adhesion
    • Kubes, P.; Suzuki, M.; Granger, D. N. Nitric oxide: An endoge nous modulator of leukocyte adhesion. Proc. Natl. Acad. Sci. USA 88:4651-4655; 1991.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 4651-4655
    • Kubes, P.1    Suzuki, M.2    Granger, D.N.3
  • 4
    • 0025819677 scopus 로고
    • Exposure to endothelial cells to free heme potentiates damage mediated by granulocytes and toxic oxygen species
    • Balla, G.; Vercellotti, G. M.; Muller-Eberhard, U.; Eaton, J.; Jacob, H. S. Exposure to endothelial cells to free heme potentiates damage mediated by granulocytes and toxic oxygen species. Lab. Invest. 64:648-655; 1991.
    • (1991) Lab. Invest. , vol.64 , pp. 648-655
    • Balla, G.1    Vercellotti, G.M.2    Muller-Eberhard, U.3    Eaton, J.4    Jacob, H.S.5
  • 7
    • 0024121621 scopus 로고
    • Cytoplasmic protein binds in vitro to a highly conserved sequence in the 5′ untranslated region of ferritin heavy-and light-subunit mRNAs
    • Leibold, E. A.; Munro, H. N. Cytoplasmic protein binds in vitro to a highly conserved sequence in the 5′ untranslated region of ferritin heavy-and light-subunit mRNAs. Proc. Natl. Acad. Sci. USA 85:2171-2175; 1988.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 2171-2175
    • Leibold, E.A.1    Munro, H.N.2
  • 8
    • 0023713448 scopus 로고
    • Binding of a cytosolic protein to the iron-responsive element of human ferritin messenger RNA
    • Rouault, T. A.; Hentze, M. W.; Wright-Caughman, S.; Hartford, J. B.; Klausner, R. D. Binding of a cytosolic protein to the iron-responsive element of human ferritin messenger RNA. Science 241:1207-1210; 1988.
    • (1988) Science , vol.241 , pp. 1207-1210
    • Rouault, T.A.1    Hentze, M.W.2    Wright-Caughman, S.3    Hartford, J.B.4    Klausner, R.D.5
  • 9
    • 0027050315 scopus 로고
    • Cellular regulation of the iron-responsive element binding protein: Disassembly of the cubane iron-sulfur cluster results in high-affinity RNA binding
    • Haile, D. J.; Rouault, T. A.; Harford, J. B.; Kennedy, M. C.; Blondin, G. A.; Beinert, H.; Klausner, R. D. Cellular regulation of the iron-responsive element binding protein: Disassembly of the cubane iron-sulfur cluster results in high-affinity RNA binding. Proc. Natl. Acad. Sci. USA 89:11735-11739; 1992.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 11735-11739
    • Haile, D.J.1    Rouault, T.A.2    Harford, J.B.3    Kennedy, M.C.4    Blondin, G.A.5    Beinert, H.6    Klausner, R.D.7
  • 10
    • 0028115810 scopus 로고
    • The iron-responsive element-binding protein: Localization of the RNA-binding site to the aconitase active-site cleft
    • Basilion, J. P.; Rouault, T. A.: Massinople, C. M.; Klausner, R. D.; Burgess, W. H. The iron-responsive element-binding protein: Localization of the RNA-binding site to the aconitase active-site cleft. Proc. Natl. Acad. Sci. USA 91:574-578; 1994.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 574-578
    • Basilion, J.P.1    Rouault, T.A.2    Massinople, C.M.3    Klausner, R.D.4    Burgess, W.H.5
  • 12
    • 0027081042 scopus 로고
    • Purification and characterization of cytosolic aconitase from beef liver and its relationship to the iron-responsive element binding protein
    • Kennedy, M. C.; Mende-Mueller, L.; Blondin, G. A.; Beinert, H. Purification and characterization of cytosolic aconitase from beef liver and its relationship to the iron-responsive element binding protein. Proc. Natl. Acad. Sci. USA 89:11730-11734; 1992.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 11730-11734
    • Kennedy, M.C.1    Mende-Mueller, L.2    Blondin, G.A.3    Beinert, H.4
  • 13
    • 0023198721 scopus 로고
    • Nitric oxide release accounts for the biological activity of endothelium-derived relaxing factor
    • Palmer, R. M. J.; Ferrige, A. G.; Moncada, S. Nitric oxide release 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.J.1    Ferrige, A.G.2    Moncada, S.3
  • 14
    • 0024208276 scopus 로고
    • Macrophage oxidation of L-arginine to nitrite and nitrate: Nitric oxide is an intermediate
    • Marietta, M. A.; Yoon, P. S.; Iyengar, R.; Leaf, C. D.; Wishnook, J. S. Macrophage oxidation of L-arginine to nitrite and nitrate: Nitric oxide is an intermediate. Biochem. 27:8706-8711; 1988.
    • (1988) Biochem. , vol.27 , pp. 8706-8711
    • Marietta, M.A.1    Yoon, P.S.2    Iyengar, R.3    Leaf, C.D.4    Wishnook, J.S.5
  • 15
    • 0343046540 scopus 로고
    • Formation of nitric oxide from L-arginine in the central nervous system: A transduction mechanism for stimulation of the soluble guanylate cyclase
    • Knowles, R. G.; Palacios, M.; Palmer, R. M. J.; Moncada, S. Formation of nitric oxide from L-arginine in the central nervous system: A transduction mechanism for stimulation of the soluble guanylate cyclase. Proc. Natl. Acad. Sci. USA 86:5159-5162; 1989.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 5159-5162
    • Knowles, R.G.1    Palacios, M.2    Palmer, R.M.J.3    Moncada, S.4
  • 16
    • 0027190721 scopus 로고
    • Activation of human peripheral blood mononuclear cells by nitric oxide-generating compounds
    • Lander, H.; Sehajpal, P.; Levine, D. M.; Novogrodsky, A. Activation of human peripheral blood mononuclear cells by nitric oxide-generating compounds. J. Immunol. 150:1509; 1993.
    • (1993) J. Immunol. , vol.150 , pp. 1509
    • Lander, H.1    Sehajpal, P.2    Levine, D.M.3    Novogrodsky, A.4
  • 17
    • 0027301897 scopus 로고
    • Biosynthesis of nitric oxide activates iron regulatory factor in macrophages
    • Drapier, J. C.; Hirling, H.; Wietzeibin, J.; Kaldy, P.; Kuhn, L. C. Biosynthesis of nitric oxide activates iron regulatory factor in macrophages. EMBO J. 12:3643-3649; 1993.
    • (1993) EMBO J. , vol.12 , pp. 3643-3649
    • Drapier, J.C.1    Hirling, H.2    Wietzeibin, J.3    Kaldy, P.4    Kuhn, L.C.5
  • 21
    • 0026586461 scopus 로고
    • The role of nitric oxide in endothelial damage and its inhibition by glucocorticoids
    • Palmer, R. M. J.; Bridge, L.; Foxwell, N. A.; Moncada, S. The role of nitric oxide in endothelial damage and its inhibition by glucocorticoids. Br. J. Pharmacol. 105:11-12; 1992.
    • (1992) Br. J. Pharmacol. , vol.105 , pp. 11-12
    • Palmer, R.M.J.1    Bridge, L.2    Foxwell, N.A.3    Moncada, S.4
  • 22
    • 0022461970 scopus 로고
    • Murine cytotoxic activated macrophages inhibit aconitase in tumor cells
    • Drapier, J. C.; Hibbs, J. B. Murine cytotoxic activated macrophages inhibit aconitase in tumor cells. J. Clin. Invest. 78:790-797; 1986.
    • (1986) J. Clin. Invest. , vol.78 , pp. 790-797
    • Drapier, J.C.1    Hibbs, J.B.2
  • 23
    • 0025938548 scopus 로고
    • Inhibition of tumor cell ribonucleotide reductase by macrophages-derived nitric oxide
    • Kwon, N. S.; Stuehr, D. J.; Nathan, C. F. Inhibition of tumor cell ribonucleotide reductase by macrophages-derived nitric oxide. J. Exp. Med. 174:761-767; 1991.
    • (1991) J. Exp. Med. , vol.174 , pp. 761-767
    • Kwon, N.S.1    Stuehr, D.J.2    Nathan, C.F.3
  • 24
    • 0018394556 scopus 로고
    • Mobilization of iron from reticulocytes
    • Ponka, P.; Borova, J.; Neuwirt, J.; Fuchs, O. Mobilization of iron from reticulocytes. FEBS Lett. 97:317-321; 1979.
    • (1979) FEBS Lett. , vol.97 , pp. 317-321
    • Ponka, P.1    Borova, J.2    Neuwirt, J.3    Fuchs, O.4
  • 25
    • 0020412905 scopus 로고
    • Ferric pyridoxal isonicotinoyl hydrazone can provide iron for heme synthesis in reticulocytes
    • Ponka, P.; Schulman, H. M.; Wilczynska, A. Ferric pyridoxal isonicotinoyl hydrazone can provide iron for heme synthesis in reticulocytes. Biochim. Biophys. Acta 718:151-156; 1982.
    • (1982) Biochim. Biophys. Acta , vol.718 , pp. 151-156
    • Ponka, P.1    Schulman, H.M.2    Wilczynska, A.3
  • 26
    • 0345408097 scopus 로고
    • Translation of ferritin light and heavy subunit mRNAs is regulated by intracellular chelatable iron levels in rat hepatoma cells
    • Rogers, J.; Munro, H. Translation of ferritin light and heavy subunit mRNAs is regulated by intracellular chelatable iron levels in rat hepatoma cells. Proc. Natl. Acad. Sci. USA 84:2277-2281; 1987.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 2277-2281
    • Rogers, J.1    Munro, H.2
  • 28
    • 0014216603 scopus 로고
    • Mechanism of aconitase action
    • Rose, I. A.; O'Connell, E. L. Mechanism of aconitase action. J. Biol. Chem. 242:1870-1879; 1967.
    • (1967) J. Biol. Chem. , vol.242 , pp. 1870-1879
    • Rose, I.A.1    O'Connell, E.L.2
  • 29
    • 0024471801 scopus 로고
    • Regulation of interaction of the iron-responsive element binding protein with iron-responsive elements
    • Haile, D. J.; Hentze, M. W.; Rouault, T. A.; Harford, J. B.; Klausner, R. D. Regulation of interaction of the iron-responsive element binding protein with iron-responsive elements. Mol. Cell Biol. 9:5055-5061; 1989.
    • (1989) Mol. Cell Biol. , vol.9 , pp. 5055-5061
    • Haile, D.J.1    Hentze, M.W.2    Rouault, T.A.3    Harford, J.B.4    Klausner, R.D.5
  • 30
    • 0024411104 scopus 로고
    • Thrombin-treated endothelium primes neutrophil functions: Inhibition by platelet-activating factor receptor antagonists
    • Vercellotti, G. M.; Wickham, N. W. R.; Gustafson, K. S.; Yin, H. Q.; Herbert, M.; Jacob, H. S. Thrombin-treated endothelium primes neutrophil functions: Inhibition by platelet-activating factor receptor antagonists. J. Leuk. Biol. 45:483-490; 1989.
    • (1989) J. Leuk. Biol. , vol.45 , pp. 483-490
    • Vercellotti, G.M.1    Wickham, N.W.R.2    Gustafson, K.S.3    Yin, H.Q.4    Herbert, M.5    Jacob, H.S.6
  • 31
    • 0025969686 scopus 로고
    • Regulation of ferritin and heme oxygenase synthesis in rat fibroblasts by different forms of iron
    • Eisenstein, R. S.; Garcia-Mayol, D.; Pettingell, W.; Munro, H. N. Regulation of ferritin and heme oxygenase synthesis in rat fibroblasts by different forms of iron. Proc. Natl. Acad. Sci. USA 88:688-692; 1991.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 688-692
    • Eisenstein, R.S.1    Garcia-Mayol, D.2    Pettingell, W.3    Munro, H.N.4
  • 33
    • 0026756095 scopus 로고
    • Reciprocal control of RNA-binding and aconitase activity in the regulation of the iron-responsive element binding protein: Role of the iron-sulfur cluster
    • Haile, D. J.; Rouault, T. A.; Tang, C. K.; Chin, J.; Harford, J. B.; Klausner, R. D. Reciprocal control of RNA-binding and aconitase activity in the regulation of the iron-responsive element binding protein: Role of the iron-sulfur cluster. Proc. Natl. Acad. Sci. USA 89:7536-7540; 1992.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 7536-7540
    • Haile, D.J.1    Rouault, T.A.2    Tang, C.K.3    Chin, J.4    Harford, J.B.5    Klausner, R.D.6
  • 34
    • 0028227772 scopus 로고
    • Coinduction of nitric oxide synthesis and intracellular nonheme iron-nitrosyl complexes in murine cytokine-treated fibroblasts
    • Lancaster, J. R., Jr.; Werner-Felmayer, G.; Wachter, H. Coinduction of nitric oxide synthesis and intracellular nonheme iron-nitrosyl complexes in murine cytokine-treated fibroblasts. Free Radic. Biol. Med. 16:869-870; 1994.
    • (1994) Free Radic. Biol. Med. , vol.16 , pp. 869-870
    • Lancaster J.R., Jr.1    Werner-Felmayer, G.2    Wachter, H.3
  • 36
    • 0023274482 scopus 로고
    • Reaction of nitric oxide with heme proteins and model compounds of hemoglobin
    • Sharma, V. S.; Traylor, T. G.; Gardiner, R.; Mizukami, H. Reaction of nitric oxide with heme proteins and model compounds of hemoglobin. Biochem. 26:3837; 1985.
    • (1985) Biochem. , vol.26 , pp. 3837
    • Sharma, V.S.1    Traylor, T.G.2    Gardiner, R.3    Mizukami, H.4
  • 37
    • 0019332526 scopus 로고
    • Oxygenated form and heme-heme oxygenase complex and requirement for second electron to initiate heme degradation from the oxygenated complex
    • Yoshida, T.; Noguchi, M.; Kikuchi, G. Oxygenated form and heme-heme oxygenase complex and requirement for second electron to initiate heme degradation from the oxygenated complex. J. Biol. Chem. 255:4418-4420; 1980.
    • (1980) J. Biol. Chem. , vol.255 , pp. 4418-4420
    • Yoshida, T.1    Noguchi, M.2    Kikuchi, G.3
  • 39
    • 0027440247 scopus 로고
    • Activation by NO of an oxidative-stress response that defends Escherichia call against activated macrophages
    • Nunoshiba, T.; deRojas-Walker, T.; Wishnok, J. S.: Tannenbaum, S. R.; Demple, B. Activation by NO of an oxidative-stress response that defends Escherichia call against activated macrophages. Proc. Natl. Acad. Sci. USA 90:9993-9997; 1993.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 9993-9997
    • Nunoshiba, T.1    DeRojas-Walker, T.2    Wishnok, J.S.3    Tannenbaum, S.R.4    Demple, B.5
  • 40
    • 0027286545 scopus 로고
    • Nitric oxide forms an adduct with serum albumin that has endothelium-derived relaxing factor-like properties
    • Keaney, J. F.; Simon, D. I.; Stamler. J. S.; Jaraki, O.; Scharfstein, J.; Vita, J. A.; Loscalzo, J. Nitric oxide forms an adduct with serum albumin that has endothelium-derived relaxing factor-like properties. J. Clin. Invest. 91:1582-1589; 1993.
    • (1993) J. Clin. Invest. , vol.91 , pp. 1582-1589
    • Keaney, J.F.1    Simon, D.I.2    Stamler, J.S.3    Jaraki, O.4    Scharfstein, J.5    Vita, J.A.6    Loscalzo, J.7
  • 41
    • 0028041593 scopus 로고
    • Induction of iron-derived EPR signals in murine cancers by nitric oxide. Evidence for multiple intracellular targets
    • Bastian, N. R.; Yim, C. Y.; Hibbs, J. B., Jr.; Samlowski, W. E. Induction of iron-derived EPR signals in murine cancers by nitric oxide. Evidence for multiple intracellular targets. J. Biol. Chem. 269:5127-5131; 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 5127-5131
    • Bastian, N.R.1    Yim, C.Y.2    Hibbs J.B., Jr.3    Samlowski, W.E.4
  • 43
    • 0026483360 scopus 로고
    • Iron regulates the activity of the iron-responsive element binding protein without changing its rate of synthesis or degradation
    • Tang, C. K.; Chin, J.; Harford, J. B.; Klausner, R. D.; Rouault, T. A. Iron regulates the activity of the iron-responsive element binding protein without changing its rate of synthesis or degradation. J. Biol. Chem. 267:24466-24470; 1992.
    • (1992) J. Biol. Chem. , vol.267 , pp. 24466-24470
    • Tang, C.K.1    Chin, J.2    Harford, J.B.3    Klausner, R.D.4    Rouault, T.A.5
  • 44
    • 0028090219 scopus 로고
    • Aconitase is readily inactivated by peroxynitrite, but not by its precursor, nitric oxide
    • Castro, L.; Rodriguez, M.; Radi, R. Aconitase is readily inactivated by peroxynitrite, but not by its precursor, nitric oxide. J. biol. Chem. 269:29409-29415; 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 29409-29415
    • Castro, L.1    Rodriguez, M.2    Radi, R.3
  • 45
    • 0027960215 scopus 로고
    • Superoxide and peroxynitrite inactivate aconitases, but nitric oxide does not
    • Hausladen, A.; Fridovich, I. Superoxide and peroxynitrite inactivate aconitases, but nitric oxide does not. J. Biol. Chem. 269:29405-29408; 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 29405-29408
    • Hausladen, A.1    Fridovich, I.2


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