메뉴 건너뛰기




Volumn 2, Issue 9, 2006, Pages 486-493

Ceruloplasmin is a NO oxidase and nitrite synthase that determines endocrine NO homeostasis

Author keywords

[No Author keywords available]

Indexed keywords

BUFFER; CERULOPLASMIN; HEMOGLOBIN; METAL; MULTICOPPER OXIDASE; NITRATE; NITRIC OXIDE; NITRIC OXIDE OXIDASE; NITRITE; NITRITE SYNTHASE; OXIDOREDUCTASE; OXYGEN; SYNTHETASE; UNCLASSIFIED DRUG;

EID: 33747602092     PISSN: 15524450     EISSN: 15524469     Source Type: Journal    
DOI: 10.1038/nchembio813     Document Type: Article
Times cited : (313)

References (52)
  • 1
    • 33644829863 scopus 로고    scopus 로고
    • Nitrite is a signaling molecule and regulator of gene expression in mammalian tissues
    • Bryan, N.S. et al. Nitrite is a signaling molecule and regulator of gene expression in mammalian tissues. Nat. Chem. Biol. 1, 290-297 (2005).
    • (2005) Nat. Chem. Biol. , vol.1 , pp. 290-297
    • Bryan, N.S.1
  • 2
    • 10744220361 scopus 로고    scopus 로고
    • Nitrite reduction to nitric oxide by deoxyhemoglobin vasodilates the human circulation
    • Cosby, K. et al. Nitrite reduction to nitric oxide by deoxyhemoglobin vasodilates the human circulation. Nat. Med. 9, 1498-1505 (2003).
    • (2003) Nat. Med. , vol.9 , pp. 1498-1505
    • Cosby, K.1
  • 3
    • 30444450893 scopus 로고    scopus 로고
    • Hypoxia, red blood cells, and nitrite regulate NO-dependent hypoxic vasodilation
    • Crawford, J.H. et al. Hypoxia, red blood cells, and nitrite regulate NO-dependent hypoxic vasodilation. Blood 107, 566-574 (2006).
    • (2006) Blood , vol.107 , pp. 566-574
    • Crawford, J.H.1
  • 4
    • 33644777197 scopus 로고    scopus 로고
    • The emerging biology of the nitrite anion
    • Gladwin, M.T. et al. The emerging biology of the nitrite anion. Nat. Chem. Biol. 1, 308-314 (2005).
    • (2005) Nat. Chem. Biol. , vol.1 , pp. 308-314
    • Gladwin, M.T.1
  • 5
    • 18244369239 scopus 로고    scopus 로고
    • NO generation from nitrite and its role in vascular control
    • Lundberg, J.O. & Weitzberg, E. NO generation from nitrite and its role in vascular control. Arterioscler. Thromb. Vasc. Biol. 25, 915-922 (2005).
    • (2005) Arterioscler. Thromb. Vasc. Biol. , vol.25 , pp. 915-922
    • Lundberg, J.O.1    Weitzberg, E.2
  • 6
    • 0035816582 scopus 로고    scopus 로고
    • Characterization of the magnitude and kinetics of xanthine oxidase-catalyzed nitrite reduction. Evaluation of its role in nitric oxide generation in anoxic tissues
    • Li, H., Samouilov, A., Liu, X. & Zweier, J.L. Characterization of the magnitude and kinetics of xanthine oxidase-catalyzed nitrite reduction. Evaluation of its role in nitric oxide generation in anoxic tissues. J. Biol. Chem. 276, 24482-24489 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 24482-24489
    • Li, H.1    Samouilov, A.2    Liu, X.3    Zweier, J.L.4
  • 7
    • 0035054644 scopus 로고    scopus 로고
    • Nitrite-derived nitric oxide: A possible mediator of 'acidic-metabolic' vasodilation
    • Modin, A. et al. Nitrite-derived nitric oxide: a possible mediator of 'acidic-metabolic' vasodilation. Acta Physiol. Scand. 171, 9-16 (2001).
    • (2001) Acta Physiol. Scand. , vol.171 , pp. 9-16
    • Modin, A.1
  • 8
    • 0029114339 scopus 로고
    • Enzyme-independent formation of nitric oxide in biological tissues
    • Zweier, J.L., Wang, P., Samouilov, A. & Kuppusamy, P. Enzyme-independent formation of nitric oxide in biological tissues. Nat. Med. 1, 804-809 (1995).
    • (1995) Nat. Med. , vol.1 , pp. 804-809
    • Zweier, J.L.1    Wang, P.2    Samouilov, A.3    Kuppusamy, P.4
  • 9
    • 0344443777 scopus 로고    scopus 로고
    • Active nitric oxide produced in the red cell under hypoxic conditions by deoxyhemoglobin-mediated nitrite reduction
    • Nagababu, E., Ramasamy, S., Abernethy, D.R. & Rifkind, J.M. Active nitric oxide produced in the red cell under hypoxic conditions by deoxyhemoglobin-mediated nitrite reduction. J. Biol. Chem. 278, 46349-46356 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 46349-46356
    • Nagababu, E.1    Ramasamy, S.2    Abernethy, D.R.3    Rifkind, J.M.4
  • 10
    • 20944446791 scopus 로고    scopus 로고
    • Cytoprotective effects of nitrite during in vivo ischemia-reperfusion of the heart and liver
    • Duranski, M.R. et al. Cytoprotective effects of nitrite during in vivo ischemia-reperfusion of the heart and liver. J. Clin. Invest. 115, 1232-1240 (2005).
    • (2005) J. Clin. Invest. , vol.115 , pp. 1232-1240
    • Duranski, M.R.1
  • 11
    • 4544378255 scopus 로고    scopus 로고
    • Reduction of nitrite to nitric oxide during ischemia protects against myocardial ischemia-reperfusion damage
    • Webb, A. et al. Reduction of nitrite to nitric oxide during ischemia protects against myocardial ischemia-reperfusion damage. Proc. Natl. Acad. Sci. USA 101, 13683-13688 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 13683-13688
    • Webb, A.1
  • 12
    • 0032914526 scopus 로고    scopus 로고
    • Nitration of unsaturated fatty acids by nitric oxide-derived reactive nitrogen species peroxynitrite, nitrous acid, nitrogen dioxide, and nitronium ion
    • O'Donnell, V.B. et al. Nitration of unsaturated fatty acids by nitric oxide-derived reactive nitrogen species peroxynitrite, nitrous acid, nitrogen dioxide, and nitronium ion. Chem. Res. Toxicol. 12, 83-92 (1999).
    • (1999) Chem. Res. Toxicol. , vol.12 , pp. 83-92
    • O'Donnell, V.B.1
  • 13
    • 0032739169 scopus 로고    scopus 로고
    • Formation of nitric oxide-derived oxidants by myeloperoxidase in monocytes: Pathways for monocyte-mediated protein nitration and lipid peroxidation in vivo
    • Hazen, S.L. et al. Formation of nitric oxide-derived oxidants by myeloperoxidase in monocytes: pathways for monocyte-mediated protein nitration and lipid peroxidation in vivo. Circ. Res. 85, 950-958 (1999).
    • (1999) Circ. Res. , vol.85 , pp. 950-958
    • Hazen, S.L.1
  • 14
    • 1642447134 scopus 로고    scopus 로고
    • Cellular targets and mechanisms of nitros(yl)ation: An insight into their nature and kinetics in vivo
    • Bryan, N.S. et al. Cellular targets and mechanisms of nitros(yl)ation: an insight into their nature and kinetics in vivo. Proc. Natl. Acad. Sci. USA 101, 4308-4313 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 4308-4313
    • Bryan, N.S.1
  • 15
    • 23644459872 scopus 로고    scopus 로고
    • The reaction between nitrite and deoxyhemoglobin. Reassessment of reaction kinetics and stoichiometry
    • Huang, K.T. et al. The reaction between nitrite and deoxyhemoglobin. Reassessment of reaction kinetics and stoichiometry. J. Biol. Chem. 280, 31126-31131 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 31126-31131
    • Huang, K.T.1
  • 16
    • 23644460670 scopus 로고    scopus 로고
    • Enzymatic function of hemoglobin as a nitrite reductase that produces NO under allosteric control
    • Huang, Z. et al. Enzymatic function of hemoglobin as a nitrite reductase that produces NO under allosteric control. J. Clin. Invest. 115, 2099-2107 (2005).
    • (2005) J. Clin. Invest. , vol.115 , pp. 2099-2107
    • Huang, Z.1
  • 17
    • 22144443537 scopus 로고    scopus 로고
    • Erythrocytes are the major intravascular storage sites of nitrite in human blood
    • Dejam, A. et al. Erythrocytes are the major intravascular storage sites of nitrite in human blood. Blood 106, 734-739 (2005).
    • (2005) Blood , vol.106 , pp. 734-739
    • Dejam, A.1
  • 18
    • 10744229717 scopus 로고    scopus 로고
    • Plasma nitrite reflects constitutive nitric oxide synthase activity in mammals
    • Kleinbongard, P. et al. Plasma nitrite reflects constitutive nitric oxide synthase activity in mammals. Free Radic. Biol. Med. 35, 790-796 (2003).
    • (2003) Free Radic. Biol. Med. , vol.35 , pp. 790-796
    • Kleinbongard, P.1
  • 19
    • 33646671928 scopus 로고    scopus 로고
    • Unraveling the reactions of nitric oxide, nitrite, and hemoglobin in physiology and therapeutics
    • Kim-Shapiro, D.B., Schechter, A.N. & Gladwin, M.T. Unraveling the reactions of nitric oxide, nitrite, and hemoglobin in physiology and therapeutics. Arterioscler. Thromb. Vasc. Biol. 26, 697-705 (2006).
    • (2006) Arterioscler. Thromb. Vasc. Biol. , vol.26 , pp. 697-705
    • Kim-Shapiro, D.B.1    Schechter, A.N.2    Gladwin, M.T.3
  • 20
    • 0027253654 scopus 로고
    • Autoxidation kinetics of aqueous nitric oxide
    • Ford, P.C., Wink, D.A. & Stanbury, D.M. Autoxidation kinetics of aqueous nitric oxide. FEBS Lett. 326, 1-3 (1993).
    • (1993) FEBS Lett. , vol.326 , pp. 1-3
    • Ford, P.C.1    Wink, D.A.2    Stanbury, D.M.3
  • 21
    • 3843070823 scopus 로고    scopus 로고
    • Biological activity of nitric oxide in the plasmatic compartment
    • Wang, X. et al. Biological activity of nitric oxide in the plasmatic compartment. Proc. Natl. Acad. Sci. USA 101, 11477-11482 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 11477-11482
    • Wang, X.1
  • 22
    • 0037345644 scopus 로고    scopus 로고
    • Direct biochemical evidence for eNOS stimulation by bradykinin in the human forearm vasculature
    • Lauer, T. et al. Direct biochemical evidence for eNOS stimulation by bradykinin in the human forearm vasculature. Basic Res. Cardiol. 98, 84-89 (2003).
    • (2003) Basic Res. Cardiol. , vol.98 , pp. 84-89
    • Lauer, T.1
  • 23
    • 0036591864 scopus 로고    scopus 로고
    • Mixing artifacts from the bolus addition of nitric oxide to oxymyoglobin: Implications for S-nitrosothiol formation
    • Zhang, Y. & Hogg, N. Mixing artifacts from the bolus addition of nitric oxide to oxymyoglobin: implications for S-nitrosothiol formation. Free Radic. Biol. Med. 32, 1212-1219 (2002).
    • (2002) Free Radic. Biol. Med. , vol.32 , pp. 1212-1219
    • Zhang, Y.1    Hogg, N.2
  • 24
    • 0037197840 scopus 로고    scopus 로고
    • Catalysis of S-nitrosothiols formation by serum albumin: The mechanism and implication in vascular control
    • Rafikova, O., Rafikov, R. & Nudler, E. Catalysis of S-nitrosothiols formation by serum albumin: the mechanism and implication in vascular control. Proc. Natl. Acad. Sci. USA 99, 5913-5918 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 5913-5918
    • Rafikova, O.1    Rafikov, R.2    Nudler, E.3
  • 25
    • 0036400025 scopus 로고    scopus 로고
    • Ceruloplasmin metabolism and function
    • Hellman, N.E. & Gitlin, J.D. Ceruloplasmin metabolism and function. Annu. Rev. Nutr. 22, 439-458 (2002).
    • (2002) Annu. Rev. Nutr. , vol.22 , pp. 439-458
    • Hellman, N.E.1    Gitlin, J.D.2
  • 26
    • 0033278378 scopus 로고    scopus 로고
    • Structure/function relationships in ceruloplasmin
    • Musci, G., Polticelli, F. & Calabrese, L. Structure/function relationships in ceruloplasmin. Adv. Exp. Med. Biol. 448, 175-182 (1999).
    • (1999) Adv. Exp. Med. Biol. , vol.448 , pp. 175-182
    • Musci, G.1    Polticelli, F.2    Calabrese, L.3
  • 27
    • 0028903259 scopus 로고
    • Aceruloplasminemia: Molecular characterization of this disorder of iron metabolism
    • Harris, Z.L. et al. Aceruloplasminemia: molecular characterization of this disorder of iron metabolism. Proc. Natl. Acad. Sci. USA 92, 2539-2543 (1995).
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 2539-2543
    • Harris, Z.L.1
  • 29
    • 0014027719 scopus 로고
    • The possible significance of the ferrous oxidase activity of ceruloplasmin in normal human serum
    • Osaki, S., Johnson, D.A. & Frieden, E. The possible significance of the ferrous oxidase activity of ceruloplasmin in normal human serum. J. Biol. Chem. 241, 2746-2751 (1966).
    • (1966) J. Biol. Chem. , vol.241 , pp. 2746-2751
    • Osaki, S.1    Johnson, D.A.2    Frieden, E.3
  • 30
    • 0032899131 scopus 로고    scopus 로고
    • The reactions of copper proteins with nitric oxide
    • Torres, J. & Wilson, M.T. The reactions of copper proteins with nitric oxide. Biochim. Biophys. Acta 1411, 310-322 (1999).
    • (1999) Biochim. Biophys. Acta , vol.1411 , pp. 310-322
    • Torres, J.1    Wilson, M.T.2
  • 31
    • 0033578741 scopus 로고    scopus 로고
    • Nitrosothiol formation catalyzed by ceruloplasmin. Implication for cytoprotective mechanism in vivo
    • Inoue, K. et al. Nitrosothiol formation catalyzed by ceruloplasmin. Implication for cytoprotective mechanism in vivo. J. Biol. Chem. 274, 27069-27075 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 27069-27075
    • Inoue, K.1
  • 32
    • 0032902721 scopus 로고    scopus 로고
    • Relationships between nitric oxide, nitroxyl ion, nitrosonium cation and peroxynitrite
    • Hughes, M.N. Relationships between nitric oxide, nitroxyl ion, nitrosonium cation and peroxynitrite. Biochim. Biophys. Acta 1411, 263-272 (1999).
    • (1999) Biochim. Biophys. Acta , vol.1411 , pp. 263-272
    • Hughes, M.N.1
  • 33
    • 0035965212 scopus 로고    scopus 로고
    • Copper transport and metabolism are normal in aceruloplasminemic mice
    • Meyer, L.A., Durley, A.P., Prohaska, J.R. & Harris, Z.L. Copper transport and metabolism are normal in aceruloplasminemic mice. J. Biol. Chem. 276, 36857-36861 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 36857-36861
    • Meyer, L.A.1    Durley, A.P.2    Prohaska, J.R.3    Harris, Z.L.4
  • 34
    • 0346847502 scopus 로고    scopus 로고
    • Aceruloplasminemia, an iron metabolic disorder
    • Miyajima, H. Aceruloplasminemia, an iron metabolic disorder. Neuropathology 23, 345-350 (2003).
    • (2003) Neuropathology , vol.23 , pp. 345-350
    • Miyajima, H.1
  • 35
    • 12244281826 scopus 로고    scopus 로고
    • Aceruloplasminemia
    • Harris, Z.L. Aceruloplasminemia. J. Neurol. Sci. 207, 108-109 (2003).
    • (2003) J. Neurol. Sci. , vol.207 , pp. 108-109
    • Harris, Z.L.1
  • 36
    • 1842504248 scopus 로고    scopus 로고
    • Aceruloplasminemia: An inherited neurodegenerative disease with impairment of iron homeostasis
    • Xu, X., Pin, S., Gathinji, M., Fuchs, R. & Harris, Z.L. Aceruloplasminemia: an inherited neurodegenerative disease with impairment of iron homeostasis. Ann. NY Acad. Sci. 1012, 299-305 (2004).
    • (2004) Ann. NY Acad. Sci. , vol.1012 , pp. 299-305
    • Xu, X.1    Pin, S.2    Gathinji, M.3    Fuchs, R.4    Harris, Z.L.5
  • 37
    • 0034656236 scopus 로고    scopus 로고
    • Increased lipid peroxidation in the brains of aceruloplasminemia patients
    • Yoshida, K. et al. Increased lipid peroxidation in the brains of aceruloplasminemia patients. J. Neurol. Sci. 175, 91-95 (2000).
    • (2000) J. Neurol. Sci. , vol.175 , pp. 91-95
    • Yoshida, K.1
  • 38
    • 0035653522 scopus 로고    scopus 로고
    • Selected contribution: Effects of gender on reduced-size liver ischemia and reperfusion injury
    • Harada, H. et al. Selected contribution: effects of gender on reduced-size liver ischemia and reperfusion injury. J. Appl. Physiol. 91, 2816-2822 (2001).
    • (2001) J. Appl. Physiol. , vol.91 , pp. 2816-2822
    • Harada, H.1
  • 39
    • 0028934992 scopus 로고
    • Structure, oxidant activity, and cardiovascular mechanisms of human ceruloplasmin
    • Fox, P.L., Mukhopadhyay, C. & Ehrenwald, E. Structure, oxidant activity, and cardiovascular mechanisms of human ceruloplasmin. Life Sci. 56, 1749-1758 (1995).
    • (1995) Life Sci. , vol.56 , pp. 1749-1758
    • Fox, P.L.1    Mukhopadhyay, C.2    Ehrenwald, E.3
  • 40
    • 0023897894 scopus 로고
    • Transcriptional regulation of ceruloplasmin gene expression during inflammation
    • Gitlin, J.D. Transcriptional regulation of ceruloplasmin gene expression during inflammation. J. Biol. Chem. 263, 6281-6287 (1988).
    • (1988) J. Biol. Chem. , vol.263 , pp. 6281-6287
    • Gitlin, J.D.1
  • 41
    • 0034705673 scopus 로고    scopus 로고
    • Cytochrome c oxidase rapidly metabolises nitric oxide to nitrite
    • Torres, J., Sharpe, M.A., Rosquist, A., Cooper, C.E. & Wilson, M.T. Cytochrome c oxidase rapidly metabolises nitric oxide to nitrite. FEBS Lett. 475, 263-266 (2000).
    • (2000) FEBS Lett. , vol.475 , pp. 263-266
    • Torres, J.1    Sharpe, M.A.2    Rosquist, A.3    Cooper, C.E.4    Wilson, M.T.5
  • 42
    • 20444412608 scopus 로고    scopus 로고
    • Copper-dependent activation of hypoxia-inducible factor (HIF)-1: Implications for ceruloplasmin regulation
    • Martin, F. et al. Copper-dependent activation of hypoxia-inducible factor (HIF)-1: implications for ceruloplasmin regulation. Blood 105, 4613-4619 (2005).
    • (2005) Blood , vol.105 , pp. 4613-4619
    • Martin, F.1
  • 43
    • 0034647742 scopus 로고    scopus 로고
    • Role of hypoxia-inducible factor-1 in transcriptional activation of ceruloplasmin by iron deficiency
    • Mukhopadhyay, C.K., Mazumder, B. & Fox, P.L. Role of hypoxia-inducible factor-1 in transcriptional activation of ceruloplasmin by iron deficiency. J. Biol. Chem. 275, 21048-21054 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 21048-21054
    • Mukhopadhyay, C.K.1    Mazumder, B.2    Fox, P.L.3
  • 44
    • 0026795206 scopus 로고
    • Serum ceruloplasmin in acute myocardial infarction
    • Singh, T.K. Serum ceruloplasmin in acute myocardial infarction. Acta Cardiol. 47, 321-329 (1992).
    • (1992) Acta Cardiol. , vol.47 , pp. 321-329
    • Singh, T.K.1
  • 45
    • 0028267292 scopus 로고
    • Intact human ceruloplasmin oxidatively modifies low density lipoprotein
    • Ehrenwald, E., Chisolm, G.M. & Fox, P.L. Intact human ceruloplasmin oxidatively modifies low density lipoprotein. J. Clin. Invest. 93, 1493-1501 (1994).
    • (1994) J. Clin. Invest. , vol.93 , pp. 1493-1501
    • Ehrenwald, E.1    Chisolm, G.M.2    Fox, P.L.3
  • 48
    • 0031907553 scopus 로고    scopus 로고
    • Increased very long-chain fatty acids in erythrocyte membranes of patients with aceruloplasminemia
    • Miyajima, H. et al. Increased very long-chain fatty acids in erythrocyte membranes of patients with aceruloplasminemia. Neurology 50, 130-136 (1998).
    • (1998) Neurology , vol.50 , pp. 130-136
    • Miyajima, H.1
  • 49
    • 0034891099 scopus 로고    scopus 로고
    • Increased oxysterols associated with iron accumulation in the brains and visceral organs of acaeruloplasminaemia patients
    • Miyajima, H. et al. Increased oxysterols associated with iron accumulation in the brains and visceral organs of acaeruloplasminaemia patients. QJM 94, 417-422 (2001).
    • (2001) QJM , vol.94 , pp. 417-422
    • Miyajima, H.1
  • 50
    • 0037251861 scopus 로고    scopus 로고
    • Methodologies for the sensitive and specific measurement of S-nitrosothiols, iron-nitrosyls, and nitrite in biological samples
    • Yang, B.K., Vivas, E.X., Reiter, C.D. & Gladwin, M.T. Methodologies for the sensitive and specific measurement of S-nitrosothiols, iron-nitrosyls, and nitrite in biological samples. Free Radic. Res. 37, 1-10 (2003).
    • (2003) Free Radic. Res. , vol.37 , pp. 1-10
    • Yang, B.K.1    Vivas, E.X.2    Reiter, C.D.3    Gladwin, M.T.4
  • 51
    • 27744525932 scopus 로고    scopus 로고
    • The preparation of anaerobic nitric oxide solutions for the study of heme model systems in aqueous and nonaqueous media: Some consequences of NO x impurities
    • Lim, M.D., Lorkovic, I.M. & Ford, P.C. The preparation of anaerobic nitric oxide solutions for the study of heme model systems in aqueous and nonaqueous media: some consequences of NO x impurities. Methods Enzymol. 396, 3-17 (2005).
    • (2005) Methods Enzymol. , vol.396 , pp. 3-17
    • Lim, M.D.1    Lorkovic, I.M.2    Ford, P.C.3
  • 52
    • 0014883924 scopus 로고
    • Measurement of human serum ceruloplasmin by its p-phenylenediamine oxidase activity
    • Sunderman, F.W., Jr & Nomoto, S. Measurement of human serum ceruloplasmin by its p-phenylenediamine oxidase activity. Clin. Chem. 16, 903-910 (1970).
    • (1970) Clin. Chem. , vol.16 , pp. 903-910
    • Sunderman Jr., F.W.1    Nomoto, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.