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Volumn 51, Issue 7, 2011, Pages 1445-1453

Vascular peroxidase-1 is rapidly secreted, circulates in plasma, and supports dityrosine cross-linking reactions

Author keywords

Biosynthesis; Dityrosine formation; Free radicals; Glycosylated protein; Peroxidase cyclooxygenase; Plasma concentration; VPO1

Indexed keywords

MESSENGER RNA; MONOMER; MYELOPEROXIDASE; OLIGOSACCHARIDE; PLASMA PROTEIN; PLASMA PROTEIN VPO1; PROSTAGLANDIN SYNTHASE; RECOMBINANT PROTEIN; TUMOR NECROSIS FACTOR ALPHA; TYROSINE; UNCLASSIFIED DRUG;

EID: 80052272683     PISSN: 08915849     EISSN: 18734596     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2011.07.002     Document Type: Article
Times cited : (33)

References (36)
  • 2
    • 46449130668 scopus 로고    scopus 로고
    • The peroxidase-cyclooxygenase superfamily: Reconstructed evolution of critical enzymes of the innate immune system
    • DOI 10.1002/prot.21950
    • M. Zamocky, C. Jakopitsch, P.G. Furtmuller, C. Dunand, and C. Obinger The peroxidase-cyclooxygenase superfamily: reconstructed evolution of critical enzymes of the innate immune system Proteins 72 2008 589 605 (Pubitemid 351928514)
    • (2008) Proteins: Structure, Function and Genetics , vol.72 , Issue.2 , pp. 589-605
    • Zamocky, M.1    Jakopitsch, C.2    Furtmuller, P.G.3    Dunand, C.4    Obinger, C.5
  • 3
    • 18244390487 scopus 로고    scopus 로고
    • Myeloperoxidase: Friend and foe
    • DOI 10.1189/jlb.1204697
    • S.J. Klebanoff Myeloperoxidase: friend and foe J. Leukoc. Biol. 77 2005 598 625 (Pubitemid 40628741)
    • (2005) Journal of Leukocyte Biology , vol.77 , Issue.5 , pp. 598-625
    • Klebanoff, S.J.1
  • 4
    • 43049173503 scopus 로고    scopus 로고
    • Mammalian heme peroxidases: From molecular mechanisms to health implications
    • DOI 10.1089/ars.2007.1927
    • M.J. Davies, C.L. Hawkins, D.I. Pattison, and M.D. Rees Mammalian heme peroxidases: from molecular mechanisms to health implications Antioxid. Redox Signal. 10 2008 1199 1234 (Pubitemid 351634397)
    • (2008) Antioxidants and Redox Signaling , vol.10 , Issue.7 , pp. 1199-1234
    • Davies, M.J.1    Hawkins, C.L.2    Pattison, D.I.3    Rees, M.D.4
  • 5
    • 56349167084 scopus 로고    scopus 로고
    • Identification and characterization of VPO1, a new animal heme-containing peroxidase
    • G. Cheng, J.C. Salerno, Z. Cao, P.J. Pagano, and J.D. Lambeth Identification and characterization of VPO1, a new animal heme-containing peroxidase Free Radic. Biol. Med. 45 2008 1682 1694
    • (2008) Free Radic. Biol. Med. , vol.45 , pp. 1682-1694
    • Cheng, G.1    Salerno, J.C.2    Cao, Z.3    Pagano, P.J.4    Lambeth, J.D.5
  • 6
    • 0042626223 scopus 로고    scopus 로고
    • Emerging role of myeloperoxidase and oxidant stress markers in cardiovascular risk assessment
    • DOI 10.1097/00041433-200308000-00003
    • M.L. Brennan, and S.L. Hazen Emerging role of myeloperoxidase and oxidant stress markers in cardiovascular risk assessment Curr. Opin. Lipidol. 14 2003 353 359 (Pubitemid 36951900)
    • (2003) Current Opinion in Lipidology , vol.14 , Issue.4 , pp. 353-359
    • Brennan, M.-L.1    Hazen, S.L.2
  • 8
    • 66349123572 scopus 로고    scopus 로고
    • Myeloperoxidase, modified lipoproteins, and atherogenesis
    • Suppl
    • S.J. Nicholls, and S.L. Hazen Myeloperoxidase, modified lipoproteins, and atherogenesis J. Lipid Res. 50 2009 S346 S351 Suppl.
    • (2009) J. Lipid Res. , vol.50
    • Nicholls, S.J.1    Hazen, S.L.2
  • 10
    • 33748157807 scopus 로고    scopus 로고
    • Myeloperoxidase: An inflammatory enzyme for generating dysfunctional high density lipoprotein
    • DOI 10.1097/01.hco.0000231402.87232.aa, PII 0000157320060700000011
    • B. Shao, M.N. Oda, J.F. Oram, and J.W. Heinecke Myeloperoxidase: an inflammatory enzyme for generating dysfunctional high density lipoprotein Curr. Opin. Cardiol. 21 2006 322 328 (Pubitemid 44315065)
    • (2006) Current Opinion in Cardiology , vol.21 , Issue.4 , pp. 322-328
    • Shao, B.1    Oda, M.N.2    Oram, J.F.3    Heinecke, J.W.4
  • 11
    • 33646941974 scopus 로고    scopus 로고
    • Myeloperoxidase impairs ABCA1-dependent cholesterol efflux through methionine oxidation and site-specific tyrosine chlorination of apolipoprotein A-I
    • DOI 10.1074/jbc.C600011200
    • B. Shao, M.N. Oda, C. Bergt, X. Fu, P.S. Green, N. Brot, J.F. Oram, and J.W. Heinecke Myeloperoxidase impairs ABCA1-dependent cholesterol efflux through methionine oxidation and site-specific tyrosine chlorination of apolipoprotein A-I J. Biol. Chem. 281 2006 9001 9004 (Pubitemid 43864611)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.14 , pp. 9001-9004
    • Shao, B.1    Oda, M.N.2    Bergt, C.3    Fu, X.4    Green, P.S.5    Brot, N.6    Oram, J.F.7    Heinecke, J.W.8
  • 12
    • 33746292135 scopus 로고    scopus 로고
    • Antineutrophil cytoplasmic antibodies
    • DOI 10.1016/S0140-6736(06)69114-9, PII S0140673606691149
    • X. Bosch, A. Guilabert, and J. Font Antineutrophil cytoplasmic antibodies Lancet 368 2006 404 418 (Pubitemid 44108124)
    • (2006) Lancet , vol.368 , Issue.9533 , pp. 404-418
    • Bosch, X.1    Guilabert, A.2    Font, J.3
  • 13
    • 33646714645 scopus 로고    scopus 로고
    • Mapping of myeloperoxidase epitopes recognized by MPO-ANCA using human-mouse MPO chimers
    • DOI 10.1038/sj.ki.5000354, PII 5000354
    • U. Erdbrugger, T. Hellmark, D.O. Bunch, D.A. Alcorta, J.C. Jennette, R.J. Falk, and P.H. Nachman Mapping of myeloperoxidase epitopes recognized by MPO-ANCA using human-mouse MPO chimeras Kidney Int. 69 2006 1799 1805 (Pubitemid 43739208)
    • (2006) Kidney International , vol.69 , Issue.10 , pp. 1799-1805
    • Erdbrugger, U.1    Hellmark, T.2    Bunch, D.O.3    Alcorta, D.A.4    Jennette, J.C.5    Falk, R.J.6    Nachman, P.H.7
  • 14
    • 0023878734 scopus 로고
    • Anti-neutrophil cytoplasmic autoantibodies with specificity for myeloperoxidase in patients with systemic vasculitis and idiopathic necrotizing and crescentic glomerulonephritis
    • R.J. Falk, and J.C. Jennette Anti-neutrophil cytoplasmic autoantibodies with specificity for myeloperoxidase in patients with systemic vasculitis and idiopathic necrotizing and crescentic glomerulonephritis N. Engl. J. Med. 318 1988 1651 1657
    • (1988) N. Engl. J. Med. , vol.318 , pp. 1651-1657
    • Falk, R.J.1    Jennette, J.C.2
  • 15
    • 0020533077 scopus 로고
    • Biochemical and immunologic analysis of hereditary myeloperoxidase deficiency
    • W.M. Nauseef, R.K. Root, and H.L. Malech Biochemical and immunologic analysis of hereditary myeloperoxidase deficiency J. Clin. Invest. 71 1983 1297 1307 (Pubitemid 13098917)
    • (1983) Journal of Clinical Investigation , vol.71 , Issue.5 , pp. 1297-1307
    • Nauseef, W.M.1    Root, R.K.2    Malech, H.L.3
  • 17
    • 33745815084 scopus 로고    scopus 로고
    • Nox1-dependent reactive oxygen generation is regulated by Rac1
    • DOI 10.1074/jbc.M512751200
    • G. Cheng, B.A. Diebold, Y. Hughes, and J.D. Lambeth Nox1-dependent reactive oxygen generation is regulated by Rac1 J. Biol. Chem. 281 2006 17718 17726 (Pubitemid 44035570)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.26 , pp. 17718-17726
    • Cheng, G.1    Diebold, B.A.2    Hughes, Y.3    Lambeth, J.D.4
  • 18
    • 0025157291 scopus 로고
    • Isolation and characterization of extracellular myeloperoxidase precursor in HL-60 cell cultures
    • DOI 10.1016/0006-291X(90)90888-T
    • M. Yamada, S.J. Hur, and H. Toda Isolation and characterization of extracellular myeloperoxidase precursor in HL-60 cell cultures Biochem. Biophys. Res. Commun. 166 1990 852 859 (Pubitemid 20049923)
    • (1990) Biochemical and Biophysical Research Communications , vol.166 , Issue.2 , pp. 852-859
    • Yamada, M.1    Hur, S.-J.2    Toda, H.3
  • 19
    • 0022640063 scopus 로고
    • Myeloperoxidase biosynthesis by a human promyelocytic leukemia cell line: Insight into myeloperoxidase deficiency
    • W.M. Nauseef Myeloperoxidase biosynthesis by a human promyelocytic leukemia cell line: insight into myeloperoxidase deficiency Blood 67 1986 865 872 (Pubitemid 16116388)
    • (1986) Blood , vol.67 , Issue.4 , pp. 865-872
    • Nauseef, W.M.1
  • 20
    • 0021675964 scopus 로고
    • Biosynthesis, transport and processing of myeloperoxidase in the human leukaemic promyelocytic cell line HL-60 and normal marrow cells
    • I. Olsson, A.M. Persson, and K. Stromberg Biosynthesis, transport and processing of myeloperoxidase in the human leukaemic promyelocytic cell line HL-60 and normal marrow cells Biochem. J. 223 1984 911 920 (Pubitemid 15209080)
    • (1984) Biochemical Journal , vol.223 , Issue.3 , pp. 911-920
    • Olsson, I.1    Persson, A.-M.2    Stromberg, K.3
  • 21
    • 0023227571 scopus 로고
    • Myeloperoxidase precursors incorporate heme
    • K. Arnljots, and I. Olsson Myeloperoxidase precursors incorporate heme J. Biol. Chem. 262 1987 10430 10433 (Pubitemid 17127035)
    • (1987) Journal of Biological Chemistry , vol.262 , Issue.22 , pp. 10430-10433
    • Arnljots, K.1    Olsson, I.2
  • 22
    • 0032548935 scopus 로고    scopus 로고
    • The role of the propeptide for processing and sorting of human myeloperoxidase
    • DOI 10.1074/jbc.273.8.4747
    • E. Andersson, L. Hellman, U. Gullberg, and I. Olsson The role of the propeptide for processing and sorting of human myeloperoxidase J. Biol. Chem. 273 1998 4747 4753 (Pubitemid 28103224)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.8 , pp. 4747-4753
    • Andersson, E.1    Hellman, L.2    Gullberg, U.3    Olsson, I.4
  • 23
    • 0034697020 scopus 로고    scopus 로고
    • X-ray crystal structure and characterization of halide-binding sites of human myeloperoxidase at 1.8 A resolution
    • DOI 10.1074/jbc.275.16.11964
    • T.J. Fiedler, C.A. Davey, and R.E. Fenna X-ray crystal structure and characterization of halide-binding sites of human myeloperoxidase at 1.8 A resolution J. Biol. Chem. 275 2000 11964 11971 (Pubitemid 30237768)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.16 , pp. 11964-11971
    • Fiedler, T.J.1    Davey, C.A.2    Fenna, R.E.3
  • 25
    • 0025012904 scopus 로고
    • Assay of the human leukocyte enzymes myeloperoxidase and eosinophil peroxidase
    • DOI 10.1016/0022-1759(90)90020-V
    • P.M. Bozeman, D.B. Learn, and E.L. Thomas Assay of the human leukocyte enzymes myeloperoxidase and eosinophil peroxidase J. Immunol. Methods 126 1990 125 133 (Pubitemid 20041436)
    • (1990) Journal of Immunological Methods , vol.126 , Issue.1 , pp. 125-133
    • Bozeman, P.M.1    Learn, D.B.2    Thomas, E.L.3
  • 26
    • 0025891959 scopus 로고
    • Structural and biological properties of human recombinant myeloperoxidase produced by Chinese hamster ovary cell lines
    • N. Moguilevsky, L. Garcia-Quintana, A. Jacquet, C. Tournay, L. Fabry, L. Pierard, and A. Bollen Structural and biological properties of human recombinant myeloperoxidase produced by Chinese hamster ovary cell lines Eur. J. Biochem. 197 1991 605 614
    • (1991) Eur. J. Biochem. , vol.197 , pp. 605-614
    • Moguilevsky, N.1    Garcia-Quintana, L.2    Jacquet, A.3    Tournay, C.4    Fabry, L.5    Pierard, L.6    Bollen, A.7
  • 27
    • 4444276213 scopus 로고
    • Further studies on preparation and properties of phagocytin
    • J.G. Hirsch Further studies on preparation and properties of phagocytin J. Exp. Med. 111 1960 323 337
    • (1960) J. Exp. Med. , vol.111 , pp. 323-337
    • Hirsch, J.G.1
  • 28
    • 79251594822 scopus 로고    scopus 로고
    • Conformational and thermal stability of mature dimeric human myeloperoxidase and a recombinant monomeric form from CHO cells
    • S. Banerjee, J. Stampler, P.G. Furtmuller, and C. Obinger Conformational and thermal stability of mature dimeric human myeloperoxidase and a recombinant monomeric form from CHO cells Biochim. Biophys. Acta 1814 2011 375 387
    • (2011) Biochim. Biophys. Acta , vol.1814 , pp. 375-387
    • Banerjee, S.1    Stampler, J.2    Furtmuller, P.G.3    Obinger, C.4
  • 29
    • 0030910381 scopus 로고    scopus 로고
    • Autocatalytic processing of heme by lactoperoxidase produces the native protein-bound prosthetic group
    • DOI 10.1074/jbc.272.14.8857
    • G.D. DePillis, S. Ozaki, J.M. Kuo, D.A. Maltby, and P.R. Ortiz de Montellano Autocatalytic processing of heme by lactoperoxidase produces the native protein-bound prosthetic group J. Biol. Chem. 272 1997 8857 8860 (Pubitemid 27154877)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.14 , pp. 8857-8860
    • DePillis, G.D.1    Ozaki, S.-I.2    Kuo, J.M.3    Maltby, D.A.4    Ortiz De Montellano, P.R.5
  • 30
    • 0037898944 scopus 로고    scopus 로고
    • Autocatalytic radical reactions in physiological prosthetic heme modification
    • C. Colas, and P.R. Ortiz de Montellano Autocatalytic radical reactions in physiological prosthetic heme modification Chem. Rev. 103 2003 2305 2332
    • (2003) Chem. Rev. , vol.103 , pp. 2305-2332
    • Colas, C.1    Ortiz De Montellano, P.R.2
  • 31
    • 0022495926 scopus 로고
    • Molecular forms of myeloperoxidase in human plasma
    • R.L. Olsen, T.K. Steigen, T. Holm, and C. Little Molecular forms of myeloperoxidase in human plasma Biochem. J. 237 1986 559 565 (Pubitemid 16043716)
    • (1986) Biochemical Journal , vol.237 , Issue.2 , pp. 559-565
    • Olsen, R.L.1    Steigen, T.K.2    Holm, T.3    Little, C.4
  • 33
    • 0022259915 scopus 로고
    • Production of the superoxide adduct of myeloperoxidase (compound III) by stimulated human neutrophils and its reactivity with hydrogen peroxide and chloride
    • C.C. Winterbourn, R.C. Garcia, and A.W. Segal Production of the superoxide adduct of myeloperoxidase (compound III) by stimulated human neutrophils and its reactivity with hydrogen peroxide and chloride Biochem. J. 228 1985 583 592 (Pubitemid 15011507)
    • (1985) Biochemical Journal , vol.228 , Issue.3 , pp. 583-592
    • Winterbourn, C.C.1    Garcia, R.C.2    Segal, A.W.3
  • 34
    • 33845997473 scopus 로고    scopus 로고
    • Modeling the reactions of superoxide and myeloperoxidase in the neutrophil phagosome: Implications for microbial killing
    • DOI 10.1074/jbc.M605898200
    • C.C. Winterbourn, M.B. Hampton, J.H. Livesey, and A.J. Kettle Modeling the reactions of superoxide and myeloperoxidase in the neutrophil phagosome: implications for microbial killing J. Biol. Chem. 281 2006 39860 39869 (Pubitemid 46041789)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.52 , pp. 39860-39869
    • Winterbourn, C.C.1    Hampton, M.B.2    Livesey, J.H.3    Kettle, A.J.4
  • 35
    • 0033695425 scopus 로고    scopus 로고
    • Plasma hydrogen peroxide production in human essential hypertension: Role of heredity, gender, and ethnicity
    • F. Lacy, M.T. Kailasam, D.T. O'Connor, G.W. Schmid-Schonbein, and R.J. Parmer Plasma hydrogen peroxide production in human essential hypertension: role of heredity, gender, and ethnicity Hypertension 36 2000 878 884
    • (2000) Hypertension , vol.36 , pp. 878-884
    • Lacy, F.1    Kailasam, M.T.2    O'Connor, D.T.3    Schmid-Schonbein, G.W.4    Parmer, R.J.5


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