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Volumn 26, Issue 5, 2006, Pages 1948-1954

Sodium nitroprusside promotes IRP2 degradation via an increase in intracellular iron and in the absence of S nitrosylation at C178

Author keywords

[No Author keywords available]

Indexed keywords

2 OXOGLUTARIC ACID; BETA ACTIN; CALCEIN; CYCLOHEXIMIDE; DACTINOMYCIN; DIMETHYLOXALYLGLYCINE; FERRIC AMMONIUM CITRATE; GLYCINE DERIVATIVE; IRON; IRON REGULATORY PROTEIN 1; IRON REGULATORY PROTEIN 2; NITRITE; NITROPRUSSIDE SODIUM; OXYGENASE; PROTEASOME; S NITROSOGLUTATHIONE; SUCCINYLACETONE; TETRACYCLINE; UNCLASSIFIED DRUG;

EID: 33644526911     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.26.5.1948-1954.2006     Document Type: Article
Times cited : (31)

References (41)
  • 2
    • 0025787957 scopus 로고
    • Nitric oxide generation from nitroprusside by vascular tissue. Evidence that reduction of the nitroprusside anion and cyanide loss are required
    • Bates, J. N., M. T. Baker, R. Guerra, Jr., and D. G. Harrison. 1991. Nitric oxide generation from nitroprusside by vascular tissue. Evidence that reduction of the nitroprusside anion and cyanide loss are required. Biochem. Pharmacol. 42(Suppl.):S157-S165.
    • (1991) Biochem. Pharmacol. , vol.42 , Issue.SUPPL.
    • Bates, J.N.1    Baker, M.T.2    Guerra Jr., R.3    Harrison, D.G.4
  • 3
    • 0348111398 scopus 로고    scopus 로고
    • The role of endogenous heme synthesis and degradation domain cysteines in cellular iron-dependent degradation of IRP2
    • Bourdon, E., D. K. Kang, M. C. Ghosh, S. K. Drake, J. Wey, R. L. Levine, and T. A. Rouault. 2003. The role of endogenous heme synthesis and degradation domain cysteines in cellular iron-dependent degradation of IRP2. Blood Cells Mol. Dis. 31:247-255.
    • (2003) Blood Cells Mol. Dis. , vol.31 , pp. 247-255
    • Bourdon, E.1    Kang, D.K.2    Ghosh, M.C.3    Drake, S.K.4    Wey, J.5    Levine, R.L.6    Rouault, T.A.7
  • 4
    • 2542534741 scopus 로고    scopus 로고
    • S-nitrosylation of parkin regulates ubiquitination and compromises parkin's protective function
    • Chung, K. K., B. Thomas, X. Li, O. Pletnikova, J. C. Troncoso, L. Marsh, V. L. Dawson, and T. M. Dawson. 2004. S-nitrosylation of parkin regulates ubiquitination and compromises parkin's protective function. Science 304: 1328-1331.
    • (2004) Science , vol.304 , pp. 1328-1331
    • Chung, K.K.1    Thomas, B.2    Li, X.3    Pletnikova, O.4    Troncoso, J.C.5    Marsh, L.6    Dawson, V.L.7    Dawson, T.M.8
  • 5
    • 23044503950 scopus 로고    scopus 로고
    • Microcytic anemia, erythropoietic protoporphyria, and neurodegeneration in mice with targeted deletion of iron regulatory protein 2
    • Cooperman, S. S., E. G. Meyron-Holtz, H. Olivierre-Wilson, M. C. Ghosh, J. P. McConnell, and T. A. Rouault. 2005. Microcytic anemia, erythropoietic protoporphyria, and neurodegeneration in mice with targeted deletion of iron regulatory protein 2. Blood 106:1084-1091.
    • (2005) Blood , vol.106 , pp. 1084-1091
    • Cooperman, S.S.1    Meyron-Holtz, E.G.2    Olivierre-Wilson, H.3    Ghosh, M.C.4    McConnell, J.P.5    Rouault, T.A.6
  • 6
    • 0031866842 scopus 로고    scopus 로고
    • The use of nitric oxide donors in pharmacological studies
    • Feelisch, M. 1998. The use of nitric oxide donors in pharmacological studies. Naunyn Schmiedebergs Arch. Pharmacol. 358:113-122.
    • (1998) Naunyn Schmiedebergs Arch. Pharmacol. , vol.358 , pp. 113-122
    • Feelisch, M.1
  • 8
  • 9
    • 0029070270 scopus 로고
    • Sodium nitroprusside: Twenty years and counting
    • Friederich, J. A., and J. F. t. Butterworth. 1995. Sodium nitroprusside: twenty years and counting. Anesth. Analg. 81:152-162.
    • (1995) Anesth. Analg. , vol.81 , pp. 152-162
    • Friederich, J.A.1    Butterworth, J.F.T.2
  • 10
    • 27144467097 scopus 로고    scopus 로고
    • Altered body iron distribution and microcytosis in mice deficient for iron regulatory protein 2 (IRP2)
    • Galy, B., D. Ferring, B. Minana, O. Bell, H. G. Janser, M. Muckenthaler, K. Schumann, and M. W. Hentze. 2005. Altered body iron distribution and microcytosis in mice deficient for iron regulatory protein 2 (IRP2). Blood 106:2580-2589.
    • (2005) Blood , vol.106 , pp. 2580-2589
    • Galy, B.1    Ferring, D.2    Minana, B.3    Bell, O.4    Janser, H.G.5    Muckenthaler, M.6    Schumann, K.7    Hentze, M.W.8
  • 11
    • 0032524657 scopus 로고    scopus 로고
    • Involvement of heme in the degradation of iron-regulatory protein 2
    • Goessling, L. S., D. P. Mascotti, and R. E. Thach. 1998. Involvement of heme in the degradation of iron-regulatory protein 2. J. Biol. Chem. 273:12555-12557.
    • (1998) J. Biol. Chem. , vol.273 , pp. 12555-12557
    • Goessling, L.S.1    Mascotti, D.P.2    Thach, R.E.3
  • 12
    • 0141890273 scopus 로고    scopus 로고
    • Oxygen and iron regulation of iron regulatory protein 2
    • Hanson, E. S., M. L. Rawlins, and E. A. Leibold. 2003. Oxygen and iron regulation of iron regulatory protein 2. J. Biol. Chem. 278:40337-40342.
    • (2003) J. Biol. Chem. , vol.278 , pp. 40337-40342
    • Hanson, E.S.1    Rawlins, M.L.2    Leibold, E.A.3
  • 13
    • 2042546096 scopus 로고    scopus 로고
    • Balancing acts; molecular control of mammalian iron metabolism
    • Hentze, M. W., M. U. Muckenthaler, and N. C. Andrews. 2004. Balancing acts; molecular control of mammalian iron metabolism. Cell 117:285-297.
    • (2004) Cell , vol.117 , pp. 285-297
    • Hentze, M.W.1    Muckenthaler, M.U.2    Andrews, N.C.3
  • 15
    • 22544452148 scopus 로고    scopus 로고
    • Involvement of heme regulatory motif in heme-mediated ubiquitination and degradation of IRP2
    • Ishikawa, H., M. Kato, H. Hori, K. Ishimori, T. Kirisako, F. Tokunaga, and K. Iwai. 2005. Involvement of heme regulatory motif in heme-mediated ubiquitination and degradation of IRP2. Mol. Cell 19:171-181.
    • (2005) Mol. Cell , vol.19 , pp. 171-181
    • Ishikawa, H.1    Kato, M.2    Hori, H.3    Ishimori, K.4    Kirisako, T.5    Tokunaga, F.6    Iwai, K.7
  • 17
    • 0028788316 scopus 로고
    • Requirements for iron-regulated degradation of the RNA binding protein, iron regulatory protein 2
    • Iwai, K., R. D. Klausner, and T. A. Rouault. 1995. Requirements for iron-regulated degradation of the RNA binding protein, iron regulatory protein 2. EMBO J. 14:5350-5357.
    • (1995) EMBO J. , vol.14 , pp. 5350-5357
    • Iwai, K.1    Klausner, R.D.2    Rouault, T.A.3
  • 19
    • 8544244946 scopus 로고    scopus 로고
    • Identification of a heme-sensing domain in iron regulatory protein 2
    • Jeong, J., T. A. Rouault, and R. L. Levine. 2004. Identification of a heme-sensing domain in iron regulatory protein 2. J. Biol. Chem. 279:45450-45454.
    • (2004) J. Biol. Chem. , vol.279 , pp. 45450-45454
    • Jeong, J.1    Rouault, T.A.2    Levine, R.L.3
  • 20
    • 0037108199 scopus 로고    scopus 로고
    • The labile iron pool: Characterization, measurement, and participation in cellular processes
    • Kakhlon, O., and Z. I. Cabantchik. 2002. The labile iron pool: characterization, measurement, and participation in cellular processes. Free Radic. Biol. Med. 33:1037-1046.
    • (2002) Free Radic. Biol. Med. , vol.33 , pp. 1037-1046
    • Kakhlon, O.1    Cabantchik, Z.I.2
  • 21
    • 0038013736 scopus 로고    scopus 로고
    • Iron-regulatory protein 2 as iron sensor: Iron-dependent oxidative modification of cysteine
    • Kang, D. K., J. Jeong, S. K. Drake, N. Wehr, T. A. Rouault, and R. L. Levine. 2003. Iron-regulatory protein 2 as iron sensor: iron-dependent oxidative modification of cysteine. J. Biol. Chem. 278:14857-14864.
    • (2003) J. Biol. Chem. , vol.278 , pp. 14857-14864
    • Kang, D.K.1    Jeong, J.2    Drake, S.K.3    Wehr, N.4    Rouault, T.A.5    Levine, R.L.6
  • 22
    • 0032746973 scopus 로고    scopus 로고
    • Control of transferrin receptor expression via nitric oxide-mediated modulation of iron-regulatory protein 2
    • Kim, S., and P. Ponka. 1999. Control of transferrin receptor expression via nitric oxide-mediated modulation of iron-regulatory protein 2. J. Biol. Chem. 274:33035-33042.
    • (1999) J. Biol. Chem. , vol.274 , pp. 33035-33042
    • Kim, S.1    Ponka, P.2
  • 23
    • 0034089867 scopus 로고    scopus 로고
    • Effects of interferon-gamma and lipopolysaccharide on macrophage iron metabolism are mediated by nitric oxide-induced degradation of iron regulatory protein 2
    • Kim, S., and P. Ponka. 2000. Effects of interferon-gamma and lipopolysaccharide on macrophage iron metabolism are mediated by nitric oxide-induced degradation of iron regulatory protein 2. J. Biol. Chem. 275:6220-6226.
    • (2000) J. Biol. Chem. , vol.275 , pp. 6220-6226
    • Kim, S.1    Ponka, P.2
  • 24
    • 0242590646 scopus 로고    scopus 로고
    • Nitric oxide-mediated modulation of iron regulatory proteins: Implication for cellular iron homeostasis
    • Kim, S., and P. Ponka. 2002. Nitric oxide-mediated modulation of iron regulatory proteins: implication for cellular iron homeostasis. Blood Cells Mol. Dis. 29:400-410.
    • (2002) Blood Cells Mol. Dis. , vol.29 , pp. 400-410
    • Kim, S.1    Ponka, P.2
  • 25
    • 0037125975 scopus 로고    scopus 로고
    • Nitrogen monoxide-mediated control of ferritin synthesis: Implications for macrophage iron homeostasis
    • Kim, S., and P. Ponka. 2002. Nitrogen monoxide-mediated control of ferritin synthesis: implications for macrophage iron homeostasis. Proc. Natl. Acad. Sci. USA 99:12214-12219.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 12214-12219
    • Kim, S.1    Ponka, P.2
  • 26
    • 0347624596 scopus 로고    scopus 로고
    • S nitrosylation of IRP2 regulates its stability via the ubiquitin-proteasome pathway
    • Kim, S., S. S. Wing, and P. Ponka. 2004. S nitrosylation of IRP2 regulates its stability via the ubiquitin-proteasome pathway. Mol. Cell. Biol. 24:330-337.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 330-337
    • Kim, S.1    Wing, S.S.2    Ponka, P.3
  • 30
    • 10844282789 scopus 로고    scopus 로고
    • Mammalian tissue oxygen levels modulate iron-regulatory protein activities in vivo
    • Meyron-Holtz, E. G., M. C. Ghosh, and T. A. Rouault. 2004. Mammalian tissue oxygen levels modulate iron-regulatory protein activities in vivo. Science 306:2087-2090.
    • (2004) Science , vol.306 , pp. 2087-2090
    • Meyron-Holtz, E.G.1    Ghosh, M.C.2    Rouault, T.A.3
  • 31
    • 0036358643 scopus 로고    scopus 로고
    • Activation of iron regulatory protein-1 (IRP1) by oxidative stress
    • Mueller, S., and K. Pantopoulos. 2002. Activation of iron regulatory protein-1 (IRP1) by oxidative stress. Methods Enzymol. 348:324-337.
    • (2002) Methods Enzymol. , vol.348 , pp. 324-337
    • Mueller, S.1    Pantopoulos, K.2
  • 32
    • 1842608845 scopus 로고    scopus 로고
    • Iron metabolism and the IRE/IRP regulatory system: An update
    • Pantopoulos, K. 2004. Iron metabolism and the IRE/IRP regulatory system: an update. Ann. N. Y. Acad. Sci. 1012:1-13.
    • (2004) Ann. N. Y. Acad. Sci. , vol.1012 , pp. 1-13
    • Pantopoulos, K.1
  • 34
    • 0025761057 scopus 로고
    • Reductive metabolism of nitroprusside in rat hepatocytes and human erythrocytes
    • Rao, D. N., S. Elguindi, and P. J. O'Brien. 1991. Reductive metabolism of nitroprusside in rat hepatocytes and human erythrocytes. Arch. Biochem. Biophys. 286:30-37.
    • (1991) Arch. Biochem. Biophys. , vol.286 , pp. 30-37
    • Rao, D.N.1    Elguindi, S.2    O'Brien, P.J.3
  • 35
    • 0036268267 scopus 로고    scopus 로고
    • Contradictory effects of sodium nitroprusside and S-nitroso-N- acetylpenicillamine on oxidative stress in brain dopamine neurons in vivo
    • Rauhala, P., T. Andoh, K. Yeh, and C. C. Chiueh. 2002. Contradictory effects of sodium nitroprusside and S-nitroso-N-acetylpenicillamine on oxidative stress in brain dopamine neurons in vivo. Ann. N. Y. Acad. Sci. 962:60-72.
    • (2002) Ann. N. Y. Acad. Sci. , vol.962 , pp. 60-72
    • Rauhala, P.1    Andoh, T.2    Yeh, K.3    Chiueh, C.C.4
  • 36
    • 0032077132 scopus 로고    scopus 로고
    • Apparent role of hydroxyl radicals in oxidative brain injury induced by sodium nitroprusside
    • Rauhala, P., A. Khaldi, K. P. Mohanakumar, and C. C. Chiueh. 1998. Apparent role of hydroxyl radicals in oxidative brain injury induced by sodium nitroprusside. Free Radic. Biol. Med. 24:1065-1073.
    • (1998) Free Radic. Biol. Med. , vol.24 , pp. 1065-1073
    • Rauhala, P.1    Khaldi, A.2    Mohanakumar, K.P.3    Chiueh, C.C.4
  • 37
    • 17544375708 scopus 로고    scopus 로고
    • Release of NO from reduced nitroprusside ion: Iron-dinitrosyl formation and NO-disproportionation reactions
    • Roncaroli, F., R. van Eldik, and J. A. Olabe. 2005. Release of NO from reduced nitroprusside ion: iron-dinitrosyl formation and NO-disproportionation reactions. Inorg. Chem. 44:2781-2790.
    • (2005) Inorg. Chem. , vol.44 , pp. 2781-2790
    • Roncaroli, F.1    Van Eldik, R.2    Olabe, J.A.3
  • 39
    • 1642458415 scopus 로고    scopus 로고
    • Iron-mediated degradation of IRP2: An unexpected pathway involving a 2-oxoglutarate-dependent oxygenase activity
    • Wang, J., G. Chen, M. Muckenthaler, B. Galy, M. W. Hentze, and K. Pantopoulos. 2004. Iron-mediated degradation of IRP2: an unexpected pathway involving a 2-oxoglutarate-dependent oxygenase activity. Mol. Cell. Biol. 24:954-965.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 954-965
    • Wang, J.1    Chen, G.2    Muckenthaler, M.3    Galy, B.4    Hentze, M.W.5    Pantopoulos, K.6
  • 40
    • 13444252613 scopus 로고    scopus 로고
    • Nitric oxide inhibits the degradation of IRP2
    • Wang, J., G. Chen, and K. Pantopoulos. 2005. Nitric oxide inhibits the degradation of IRP2. Mol. Cell. Biol. 25:1347-1353.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 1347-1353
    • Wang, J.1    Chen, G.2    Pantopoulos, K.3


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