메뉴 건너뛰기




Volumn 111, Issue 1, 2006, Pages 16-26

Myeloperoxidase and its contributory role in inflammatory vascular disease

Author keywords

[No Author keywords available]

Indexed keywords

3 NITROTYROSINE; FIBRONECTIN; HEMOPROTEIN; HYPOCHLOROUS ACID; LIPOPROTEIN; MATRIX METALLOPROTEINASE; MYELOPEROXIDASE; NEUTROPHIL CYTOPLASMIC ANTIBODY; NITRIC OXIDE; TYROSINE;

EID: 33646757884     PISSN: 01637258     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pharmthera.2005.06.023     Document Type: Review
Times cited : (249)

References (134)
  • 1
    • 0034534961 scopus 로고    scopus 로고
    • Nitric oxide is a physiological substrate for mammalian peroxidases
    • Abu-Soud H.M., and Hazen S.L. Nitric oxide is a physiological substrate for mammalian peroxidases. J Biol Chem 275 (2000) 37524-37532
    • (2000) J Biol Chem , vol.275 , pp. 37524-37532
    • Abu-Soud, H.M.1    Hazen, S.L.2
  • 2
    • 0034102068 scopus 로고    scopus 로고
    • Nitric oxide modulates the catalytic activity of myeloperoxidase
    • Abu-Soud H.M., and Hazen S.L. Nitric oxide modulates the catalytic activity of myeloperoxidase. J Biol Chem 275 (2000) 5425-5430
    • (2000) J Biol Chem , vol.275 , pp. 5425-5430
    • Abu-Soud, H.M.1    Hazen, S.L.2
  • 3
    • 0022971259 scopus 로고
    • Processing of a newly identified intermediate of human myeloperoxidase in isolated granules occurs at neutral pH
    • Akin D.T., and Kinkade Jr. J.M. Processing of a newly identified intermediate of human myeloperoxidase in isolated granules occurs at neutral pH. J Biol Chem 261 (1986) 8370-8375
    • (1986) J Biol Chem , vol.261 , pp. 8370-8375
    • Akin, D.T.1    Kinkade Jr., J.M.2
  • 4
    • 0034095543 scopus 로고    scopus 로고
    • Role of poly-(ADP-ribose) synthetase in lipopolysaccharide-induced vascular failure and acute lung injury in pigs
    • Albertini M., Clement M.G., Lafortuna C.L., Caniatti M., Magder S., Abdulmalek K., et al. Role of poly-(ADP-ribose) synthetase in lipopolysaccharide-induced vascular failure and acute lung injury in pigs. J Crit Care 15 (2000) 73-83
    • (2000) J Crit Care , vol.15 , pp. 73-83
    • Albertini, M.1    Clement, M.G.2    Lafortuna, C.L.3    Caniatti, M.4    Magder, S.5    Abdulmalek, K.6
  • 5
    • 0033800733 scopus 로고    scopus 로고
    • Differential host susceptibility to pulmonary infections with bacteria and fungi in mice deficient in myeloperoxidase
    • Aratani Y., Kura F., Watanabe H., Akagawa H., Takano Y., Suzuki K., et al. Differential host susceptibility to pulmonary infections with bacteria and fungi in mice deficient in myeloperoxidase. J Infect Dis 182 (2000) 1276-1279
    • (2000) J Infect Dis , vol.182 , pp. 1276-1279
    • Aratani, Y.1    Kura, F.2    Watanabe, H.3    Akagawa, H.4    Takano, Y.5    Suzuki, K.6
  • 6
    • 0032820852 scopus 로고    scopus 로고
    • Plaque erosion is a major substrate for coronary thrombosis in acute myocardial infarction
    • Arbustini E., Dal Bello B., Morbini P., Burke A.P., Bocciarelli M., Specchia G., et al. Plaque erosion is a major substrate for coronary thrombosis in acute myocardial infarction. Heart 82 (1999) 269-272
    • (1999) Heart , vol.82 , pp. 269-272
    • Arbustini, E.1    Dal Bello, B.2    Morbini, P.3    Burke, A.P.4    Bocciarelli, M.5    Specchia, G.6
  • 7
    • 0023227571 scopus 로고
    • Myeloperoxidase precursors incorporate heme
    • Arnljots K., and Olsson I. Myeloperoxidase precursors incorporate heme. J Biol Chem 262 (1987) 10430-10433
    • (1987) J Biol Chem , vol.262 , pp. 10430-10433
    • Arnljots, K.1    Olsson, I.2
  • 8
    • 0037416219 scopus 로고    scopus 로고
    • Myeloperoxidase and plasminogen activator inhibitor 1 play a central role in ventricular remodeling after myocardial infarction
    • Askari A.T., Brennan M.L., Zhou X., Drinko J., Morehead A., Thomas J.D., et al. Myeloperoxidase and plasminogen activator inhibitor 1 play a central role in ventricular remodeling after myocardial infarction. J Exp Med 197 (2003) 615-624
    • (2003) J Exp Med , vol.197 , pp. 615-624
    • Askari, A.T.1    Brennan, M.L.2    Zhou, X.3    Drinko, J.4    Morehead, A.5    Thomas, J.D.6
  • 9
    • 1642580611 scopus 로고    scopus 로고
    • Prognostic value of myeloperoxidase in patients with chest pain
    • [author reply 516-8]
    • Asselbergs F.W., Tervaert J.W., and Tio R.A. Prognostic value of myeloperoxidase in patients with chest pain. N Engl J Med 350 (2004) 516-518 [author reply 516-8]
    • (2004) N Engl J Med , vol.350 , pp. 516-518
    • Asselbergs, F.W.1    Tervaert, J.W.2    Tio, R.A.3
  • 10
    • 0034725724 scopus 로고    scopus 로고
    • Phagocytes and oxidative stress
    • Babior B.M. Phagocytes and oxidative stress. Am J Med 109 (2000) 33-44
    • (2000) Am J Med , vol.109 , pp. 33-44
    • Babior, B.M.1
  • 11
    • 0035667004 scopus 로고    scopus 로고
    • Endothelial transcytosis of myeloperoxidase confers specificity to vascular ECM proteins as targets of tyrosine nitration
    • Baldus S., Eiserich J.P., Mani A., Castro L., Figueroa M., Chumley P., et al. Endothelial transcytosis of myeloperoxidase confers specificity to vascular ECM proteins as targets of tyrosine nitration. J Clin Invest 108 (2001) 1759-1770
    • (2001) J Clin Invest , vol.108 , pp. 1759-1770
    • Baldus, S.1    Eiserich, J.P.2    Mani, A.3    Castro, L.4    Figueroa, M.5    Chumley, P.6
  • 12
    • 0036801357 scopus 로고    scopus 로고
    • Spatial mapping of pulmonary and vascular nitrotyrosine reveals the pivotal role of myeloperoxidase as a catalyst for tyrosine nitration in inflammatory diseases
    • Baldus S., Eiserich J.P., Brennan M.L., Jackson R.M., Alexander C.B., and Freeman B.A. Spatial mapping of pulmonary and vascular nitrotyrosine reveals the pivotal role of myeloperoxidase as a catalyst for tyrosine nitration in inflammatory diseases. Free Radic Biol Med 33 (2002) 1010
    • (2002) Free Radic Biol Med , vol.33 , pp. 1010
    • Baldus, S.1    Eiserich, J.P.2    Brennan, M.L.3    Jackson, R.M.4    Alexander, C.B.5    Freeman, B.A.6
  • 13
    • 0141727730 scopus 로고    scopus 로고
    • Myeloperoxidase serum levels predict risk in patients with acute coronary syndromes
    • Baldus S., Heeschen C., Meinertz T., Zeiher A.M., Eiserich J.P., Munzel T., et al. Myeloperoxidase serum levels predict risk in patients with acute coronary syndromes. Circulation 108 (2003) 1440-1445
    • (2003) Circulation , vol.108 , pp. 1440-1445
    • Baldus, S.1    Heeschen, C.2    Meinertz, T.3    Zeiher, A.M.4    Eiserich, J.P.5    Munzel, T.6
  • 14
    • 4043072706 scopus 로고    scopus 로고
    • Myeloperoxidase enhances nitric oxide catabolism during myocardial ischemia and reperfusion
    • Baldus S., Heitzer T., Eiserich J.P., Lau D., Mollnau H., Ortak M., et al. Myeloperoxidase enhances nitric oxide catabolism during myocardial ischemia and reperfusion. Free Radic Biol Med 37 (2004) 902-911
    • (2004) Free Radic Biol Med , vol.37 , pp. 902-911
    • Baldus, S.1    Heitzer, T.2    Eiserich, J.P.3    Lau, D.4    Mollnau, H.5    Ortak, M.6
  • 15
    • 0029805172 scopus 로고    scopus 로고
    • Nitric oxide, superoxide, and peroxynitrite: the good, the bad, and ugly
    • Beckman J.S., and Koppenol W.H. Nitric oxide, superoxide, and peroxynitrite: the good, the bad, and ugly. Am J Physiol 271 (1996) C1424-C1437
    • (1996) Am J Physiol , vol.271
    • Beckman, J.S.1    Koppenol, W.H.2
  • 17
    • 4444292600 scopus 로고    scopus 로고
    • The myeloperoxidase product hypochlorous acid oxidizes HDL in the human artery wall and impairs ABCA1-dependent cholesterol transport
    • Bergt C., Pennathur S., Fu X., Byun J., O'Brien K., McDonald T.O., et al. The myeloperoxidase product hypochlorous acid oxidizes HDL in the human artery wall and impairs ABCA1-dependent cholesterol transport. Proc Natl Acad Sci USA 101 (2004) 13032-13037
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 13032-13037
    • Bergt, C.1    Pennathur, S.2    Fu, X.3    Byun, J.4    O'Brien, K.5    McDonald, T.O.6
  • 18
    • 0018144790 scopus 로고
    • Characterization and quantification of the peroxidase in human monocytes
    • Bos A., Wever R., and Roos D. Characterization and quantification of the peroxidase in human monocytes. Biochim Biophys Acta 525 (1978) 37-44
    • (1978) Biochim Biophys Acta , vol.525 , pp. 37-44
    • Bos, A.1    Wever, R.2    Roos, D.3
  • 19
    • 0042626223 scopus 로고    scopus 로고
    • Emerging role of myeloperoxidase and oxidant stress markers in cardiovascular risk assessment
    • Brennan M.L., and Hazen S.L. Emerging role of myeloperoxidase and oxidant stress markers in cardiovascular risk assessment. Curr Opin Lipidol 14 (2003) 353-359
    • (2003) Curr Opin Lipidol , vol.14 , pp. 353-359
    • Brennan, M.L.1    Hazen, S.L.2
  • 21
    • 0037124020 scopus 로고    scopus 로고
    • A tale of two controversies: defining both the role of peroxidases in nitrotyrosine formation in vivo using eosinophil peroxidase and myeloperoxidase-deficient mice, and the nature of peroxidase-generated reactive nitrogen species
    • Brennan M.L., Wu W., Fu X., Shen Z., Song W., Frost H., et al. A tale of two controversies: defining both the role of peroxidases in nitrotyrosine formation in vivo using eosinophil peroxidase and myeloperoxidase-deficient mice, and the nature of peroxidase-generated reactive nitrogen species. J Biol Chem 277 (2002) 17415-17427
    • (2002) J Biol Chem , vol.277 , pp. 17415-17427
    • Brennan, M.L.1    Wu, W.2    Fu, X.3    Shen, Z.4    Song, W.5    Frost, H.6
  • 23
    • 0035190154 scopus 로고    scopus 로고
    • Immunohistochemical detection of myeloperoxidase and its oxidation products in Kupffer cells of human liver
    • Brown K.E., Brunt E.M., and Heinecke J.W. Immunohistochemical detection of myeloperoxidase and its oxidation products in Kupffer cells of human liver. Am J Pathol 159 (2001) 2081-2088
    • (2001) Am J Pathol , vol.159 , pp. 2081-2088
    • Brown, K.E.1    Brunt, E.M.2    Heinecke, J.W.3
  • 25
    • 0034665315 scopus 로고    scopus 로고
    • Bioactive proteinase 3 on the cell surface of human neutrophils: quantification, catalytic activity, and susceptibility to inhibition
    • Campbell E.J., Campbell M.A., and Owen C.A. Bioactive proteinase 3 on the cell surface of human neutrophils: quantification, catalytic activity, and susceptibility to inhibition. J Immunol 165 (2000) 3366-3374
    • (2000) J Immunol , vol.165 , pp. 3366-3374
    • Campbell, E.J.1    Campbell, M.A.2    Owen, C.A.3
  • 27
    • 0031800368 scopus 로고    scopus 로고
    • Association of myeloperoxidase with heparin: oxidative inactivation of proteins on the surface of endothelial cells by the bound enzyme
    • Daphna E.M., Michaela S., Eynat P., Irit A., and Rimon S. Association of myeloperoxidase with heparin: oxidative inactivation of proteins on the surface of endothelial cells by the bound enzyme. Mol Cell Biochem 183 (1998) 55-61
    • (1998) Mol Cell Biochem , vol.183 , pp. 55-61
    • Daphna, E.M.1    Michaela, S.2    Eynat, P.3    Irit, A.4    Rimon, S.5
  • 28
    • 0028292033 scopus 로고
    • Myeloperoxidase, a catalyst for lipoprotein oxidation, is expressed in human atherosclerotic lesions
    • Daugherty A., Dunn J.L., Rateri D.L., and Heinecke J.W. Myeloperoxidase, a catalyst for lipoprotein oxidation, is expressed in human atherosclerotic lesions. J Clin Invest 94 (1994) 437-444
    • (1994) J Clin Invest , vol.94 , pp. 437-444
    • Daugherty, A.1    Dunn, J.L.2    Rateri, D.L.3    Heinecke, J.W.4
  • 29
    • 0029159779 scopus 로고
    • Nitric oxide decreases cytokine-induced endothelial activation. Nitric oxide selectively reduces endothelial expression of adhesion molecules and proinflammatory cytokines
    • De Caterina R., Libby P., Peng H.B., Thannickal V.J., Rajavashisth T.B., Gimbrone Jr. M.A., et al. Nitric oxide decreases cytokine-induced endothelial activation. Nitric oxide selectively reduces endothelial expression of adhesion molecules and proinflammatory cytokines. J Clin Invest 96 (1995) 60-68
    • (1995) J Clin Invest , vol.96 , pp. 60-68
    • De Caterina, R.1    Libby, P.2    Peng, H.B.3    Thannickal, V.J.4    Rajavashisth, T.B.5    Gimbrone Jr., M.A.6
  • 30
    • 0039106191 scopus 로고    scopus 로고
    • Neutrophil myeloperoxidase revisited: it's role in health and disease
    • Deby-Dupont G., and Lamy M. Neutrophil myeloperoxidase revisited: it's role in health and disease. Intensivmedizin 36 (1999) 500-513
    • (1999) Intensivmedizin , vol.36 , pp. 500-513
    • Deby-Dupont, G.1    Lamy, M.2
  • 31
    • 0024009517 scopus 로고
    • Proteolytic inactivation of alpha-1-proteinase inhibitor by a neutrophil metalloproteinase
    • Desrochers P.E., and Weiss S.J. Proteolytic inactivation of alpha-1-proteinase inhibitor by a neutrophil metalloproteinase. J Clin Invest 81 (1988) 1646-1650
    • (1988) J Clin Invest , vol.81 , pp. 1646-1650
    • Desrochers, P.E.1    Weiss, S.J.2
  • 32
    • 0037024270 scopus 로고    scopus 로고
    • Effects of xanthine oxidase inhibition with allopurinol on endothelial function and peripheral blood flow in hyperuricemic patients with chronic heart failure: results from 2 placebo-controlled studies
    • Doehner W., Schoene N., Rauchhaus M., Leyva-Leon F., Pavitt D.V., Reaveley D.A., et al. Effects of xanthine oxidase inhibition with allopurinol on endothelial function and peripheral blood flow in hyperuricemic patients with chronic heart failure: results from 2 placebo-controlled studies. Circulation 105 (2002) 2619-2624
    • (2002) Circulation , vol.105 , pp. 2619-2624
    • Doehner, W.1    Schoene, N.2    Rauchhaus, M.3    Leyva-Leon, F.4    Pavitt, D.V.5    Reaveley, D.A.6
  • 33
    • 0032556905 scopus 로고    scopus 로고
    • Formation of nitric oxide-derived inflammatory oxidants by myeloperoxidase in neutrophils
    • Eiserich J.P., Hristova M., Cross C.E., Jones A.D., Freeman B.A., Halliwell B., et al. Formation of nitric oxide-derived inflammatory oxidants by myeloperoxidase in neutrophils. Nature 391 (1998) 393-397
    • (1998) Nature , vol.391 , pp. 393-397
    • Eiserich, J.P.1    Hristova, M.2    Cross, C.E.3    Jones, A.D.4    Freeman, B.A.5    Halliwell, B.6
  • 34
    • 0032992466 scopus 로고    scopus 로고
    • Microtubule dysfunction by posttranslational nitrotyrosination of alpha-tubulin: a nitric oxide-dependent mechanism of cellular injury
    • Eiserich J.P., Estevez A.G., Bamberg T.V., Ye Y.Z., Chumley P.H., Beckman J.S., et al. Microtubule dysfunction by posttranslational nitrotyrosination of alpha-tubulin: a nitric oxide-dependent mechanism of cellular injury. Proc Natl Acad Sci USA 96 (1999) 6365-6370
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 6365-6370
    • Eiserich, J.P.1    Estevez, A.G.2    Bamberg, T.V.3    Ye, Y.Z.4    Chumley, P.H.5    Beckman, J.S.6
  • 36
    • 0032076871 scopus 로고    scopus 로고
    • The structure of heme proteins compounds I and II: some misconceptions
    • Everse J. The structure of heme proteins compounds I and II: some misconceptions. Free Radic Biol Med 24 (1998) 1338-1346
    • (1998) Free Radic Biol Med , vol.24 , pp. 1338-1346
    • Everse, J.1
  • 37
    • 0023878734 scopus 로고
    • Anti-neutrophil cytoplasmic autoantibodies with specificity for myeloperoxidase in patients with systemic vasculitis and idiopathic necrotizing and crescentic glomerulonephritis
    • Falk R.J., and Jennette J.C. 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
  • 38
    • 0025345612 scopus 로고
    • Anti-neutrophil cytoplasmic autoantibodies induce neutrophils to degranulate and produce oxygen radicals in vitro
    • Falk R.J., Terrell R.S., Charles L.A., and Jennette J.C. Anti-neutrophil cytoplasmic autoantibodies induce neutrophils to degranulate and produce oxygen radicals in vitro. Proc Natl Acad Sci USA 87 (1990) 4115-4119
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 4115-4119
    • Falk, R.J.1    Terrell, R.S.2    Charles, L.A.3    Jennette, J.C.4
  • 39
    • 0029876139 scopus 로고    scopus 로고
    • Coronary plaque erosion without rupture into a lipid core. A frequent cause of coronary thrombosis in sudden coronary death
    • Farb A., Burke A.P., Tang A.L., Liang T.Y., Mannan P., Smialek J., et al. Coronary plaque erosion without rupture into a lipid core. A frequent cause of coronary thrombosis in sudden coronary death. Circulation 93 (1996) 1354-1363
    • (1996) Circulation , vol.93 , pp. 1354-1363
    • Farb, A.1    Burke, A.P.2    Tang, A.L.3    Liang, T.Y.4    Mannan, P.5    Smialek, J.6
  • 40
    • 0026467074 scopus 로고
    • Increased concentrations of nitrite in synovial fluid and serum samples suggest increased nitric oxide synthesis in rheumatic diseases
    • Farrell A.J., Blake D.R., Palmer R.M., and Moncada S. Increased concentrations of nitrite in synovial fluid and serum samples suggest increased nitric oxide synthesis in rheumatic diseases. Ann Rheum Dis 51 (1992) 1219-1222
    • (1992) Ann Rheum Dis , vol.51 , pp. 1219-1222
    • Farrell, A.J.1    Blake, D.R.2    Palmer, R.M.3    Moncada, S.4
  • 41
    • 0028853285 scopus 로고
    • Structure of the green heme in myeloperoxidase
    • Fenna R., Zeng J., and Davey C. Structure of the green heme in myeloperoxidase. Arch Biochem Biophys 316 (1995) 653-656
    • (1995) Arch Biochem Biophys , vol.316 , pp. 653-656
    • Fenna, R.1    Zeng, J.2    Davey, C.3
  • 42
    • 0024232736 scopus 로고
    • Oxidation of proteins in rat heart and lungs by polymorphonuclear leukocyte oxidants
    • Fliss H. Oxidation of proteins in rat heart and lungs by polymorphonuclear leukocyte oxidants. Mol Cell Biochem 84 (1988) 177-188
    • (1988) Mol Cell Biochem , vol.84 , pp. 177-188
    • Fliss, H.1
  • 43
    • 0028843708 scopus 로고
    • Kinetics and mechanisms of hypochlorous acid reactions
    • Folkes L.K., Candeias L.P., and Wardman P. Kinetics and mechanisms of hypochlorous acid reactions. Arch Biochem Biophys 323 (1995) 120-126
    • (1995) Arch Biochem Biophys , vol.323 , pp. 120-126
    • Folkes, L.K.1    Candeias, L.P.2    Wardman, P.3
  • 44
    • 0035798684 scopus 로고    scopus 로고
    • Hypochlorous acid oxygenates the cysteine switch domain of pro-matrilysin (MMP-7). A mechanism for matrix metalloproteinase activation and atherosclerotic plaque rupture by myeloperoxidase
    • Fu X., Kassim S.Y., Parks W.C., and Heinecke J.W. Hypochlorous acid oxygenates the cysteine switch domain of pro-matrilysin (MMP-7). A mechanism for matrix metalloproteinase activation and atherosclerotic plaque rupture by myeloperoxidase. J Biol Chem 276 (2001) 41279-41287
    • (2001) J Biol Chem , vol.276 , pp. 41279-41287
    • Fu, X.1    Kassim, S.Y.2    Parks, W.C.3    Heinecke, J.W.4
  • 46
    • 0031788693 scopus 로고    scopus 로고
    • Tissue inhibitors of metalloproteinases and metalloproteinases in atherosclerosis
    • George S.J. Tissue inhibitors of metalloproteinases and metalloproteinases in atherosclerosis. Curr Opin Lipidol 9 (1998) 413-423
    • (1998) Curr Opin Lipidol , vol.9 , pp. 413-423
    • George, S.J.1
  • 48
    • 15144339407 scopus 로고    scopus 로고
    • Diagnostic value of standardized assays for anti-neutrophil cytoplasmic antibodies in idiopathic systemic vasculitis. EC/BCR Project for ANCA Assay Standardization
    • Hagen E.C., Daha M.R., Hermans J., Andrassy K., Csernok E., Gaskin G., et al. Diagnostic value of standardized assays for anti-neutrophil cytoplasmic antibodies in idiopathic systemic vasculitis. EC/BCR Project for ANCA Assay Standardization. Kidney Int 53 (1998) 743-753
    • (1998) Kidney Int , vol.53 , pp. 743-753
    • Hagen, E.C.1    Daha, M.R.2    Hermans, J.3    Andrassy, K.4    Csernok, E.5    Gaskin, G.6
  • 49
    • 0034050692 scopus 로고    scopus 로고
    • Pathogenesis of ANCA-associated systemic vasculitis
    • Harper L., and Savage C.O. Pathogenesis of ANCA-associated systemic vasculitis. J Pathol 190 (2000) 349-359
    • (2000) J Pathol , vol.190 , pp. 349-359
    • Harper, L.1    Savage, C.O.2
  • 50
    • 3042735742 scopus 로고    scopus 로고
    • Myeloperoxidase and plaque vulnerability
    • Hazen S.L. Myeloperoxidase and plaque vulnerability. Arterioscler Thromb Vasc Biol 24 (2004) 1143-1146
    • (2004) Arterioscler Thromb Vasc Biol , vol.24 , pp. 1143-1146
    • Hazen, S.L.1
  • 51
    • 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., Zhang R., Shen Z., Wu W., Podrez E.A., MacPherson J.C., 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 (1999) 950-958
    • (1999) Circ Res , vol.85 , pp. 950-958
    • Hazen, S.L.1    Zhang, R.2    Shen, Z.3    Wu, W.4    Podrez, E.A.5    MacPherson, J.C.6
  • 52
    • 0034826857 scopus 로고    scopus 로고
    • Cyclophosphamide decreases nitrotyrosine formation and inhibits nitric oxide production by alveolar macrophages in mycoplasmosis
    • Hickman-Davis J.M., Lindsey J.R., and Matalon S. Cyclophosphamide decreases nitrotyrosine formation and inhibits nitric oxide production by alveolar macrophages in mycoplasmosis. Infect Immun 69 (2001) 6401-6410
    • (2001) Infect Immun , vol.69 , pp. 6401-6410
    • Hickman-Davis, J.M.1    Lindsey, J.R.2    Matalon, S.3
  • 53
    • 0033985973 scopus 로고    scopus 로고
    • Nitrotyrosine generation via inducible nitric oxide synthase in vascular wall in focal ischemia-reperfusion
    • Hirabayashi H., Takizawa S., Fukuyama N., Nakazawa H., and Shinohara Y. Nitrotyrosine generation via inducible nitric oxide synthase in vascular wall in focal ischemia-reperfusion. Brain Res 852 (2000) 319-325
    • (2000) Brain Res , vol.852 , pp. 319-325
    • Hirabayashi, H.1    Takizawa, S.2    Fukuyama, N.3    Nakazawa, H.4    Shinohara, Y.5
  • 54
    • 0033559312 scopus 로고    scopus 로고
    • Human immunodeficiency virus-1-infected macrophages induce inducible nitric oxide synthase and nitric oxide (NO) production in astrocytes: astrocytic NO as a possible mediator of neural damage in acquired immunodeficiency syndrome
    • Hori K., Burd P.R., Furuke K., Kutza J., Weih K.A., and Clouse K.A. Human immunodeficiency virus-1-infected macrophages induce inducible nitric oxide synthase and nitric oxide (NO) production in astrocytes: astrocytic NO as a possible mediator of neural damage in acquired immunodeficiency syndrome. Blood 93 (1999) 1843-1850
    • (1999) Blood , vol.93 , pp. 1843-1850
    • Hori, K.1    Burd, P.R.2    Furuke, K.3    Kutza, J.4    Weih, K.A.5    Clouse, K.A.6
  • 55
    • 0034748415 scopus 로고    scopus 로고
    • Serum myeloperoxidase concentration in a healthy population: biological variations, familial resemblance and new genetic polymorphisms
    • Hoy A., Tregouet D., Leininger-Muller B., Poirier O., Maurice M., Sass C., et al. Serum myeloperoxidase concentration in a healthy population: biological variations, familial resemblance and new genetic polymorphisms. Eur J Hum Genet 9 (2001) 780-786
    • (2001) Eur J Hum Genet , vol.9 , pp. 780-786
    • Hoy, A.1    Tregouet, D.2    Leininger-Muller, B.3    Poirier, O.4    Maurice, M.5    Sass, C.6
  • 56
    • 0024337245 scopus 로고
    • Leukocytic oxygen activation and microbicidal oxidative toxins
    • Hurst J.K., and Barrette Jr. W.C. Leukocytic oxygen activation and microbicidal oxidative toxins. Crit Rev Biochem Mol Biol 24 (1989) 271-328
    • (1989) Crit Rev Biochem Mol Biol , vol.24 , pp. 271-328
    • Hurst, J.K.1    Barrette Jr., W.C.2
  • 57
    • 0032147208 scopus 로고    scopus 로고
    • Biological tyrosine nitration: a pathophysiological function of nitric oxide and reactive oxygen species
    • Ischiropoulos H. Biological tyrosine nitration: a pathophysiological function of nitric oxide and reactive oxygen species. Arch Biochem Biophys 356 (1998) 1-11
    • (1998) Arch Biochem Biophys , vol.356 , pp. 1-11
    • Ischiropoulos, H.1
  • 58
    • 0027258140 scopus 로고
    • Hypercholesterolemia in low density lipoprotein receptor knockout mice and its reversal by adenovirus-mediated gene delivery
    • Ishibashi S., Brown M.S., Goldstein J.L., Gerard R.D., Hammer R.E., and Herz J. Hypercholesterolemia in low density lipoprotein receptor knockout mice and its reversal by adenovirus-mediated gene delivery. J Clin Invest 92 (1993) 883-893
    • (1993) J Clin Invest , vol.92 , pp. 883-893
    • Ishibashi, S.1    Brown, M.S.2    Goldstein, J.L.3    Gerard, R.D.4    Hammer, R.E.5    Herz, J.6
  • 60
    • 0031438748 scopus 로고    scopus 로고
    • Relative chlorinating, nitrating, and oxidizing capabilities of neutrophils determined with phagocytosable probes
    • Jiang Q., and Hurst J.K. Relative chlorinating, nitrating, and oxidizing capabilities of neutrophils determined with phagocytosable probes. J Biol Chem 272 (1997) 32767-32772
    • (1997) J Biol Chem , vol.272 , pp. 32767-32772
    • Jiang, Q.1    Hurst, J.K.2
  • 61
    • 0027193841 scopus 로고
    • Suppression of gene expression of myeloperoxidase (MPO) by gamma-interferon (IFN-gamma) in HL60 cells
    • Kawano S., Tatsumi E., Yoneda N., Nagata S., and Yamaguchi N. Suppression of gene expression of myeloperoxidase (MPO) by gamma-interferon (IFN-gamma) in HL60 cells. Lymphokine Cytokine Res 12 (1993) 81-85
    • (1993) Lymphokine Cytokine Res , vol.12 , pp. 81-85
    • Kawano, S.1    Tatsumi, E.2    Yoneda, N.3    Nagata, S.4    Yamaguchi, N.5
  • 62
    • 0031370573 scopus 로고    scopus 로고
    • Peroxynitrite and myeloperoxidase leave the same footprint in protein nitration
    • Kettle A.J., van Dalen C.J., and Winterbourn C.C. Peroxynitrite and myeloperoxidase leave the same footprint in protein nitration. Redox Rep 3 (1997) 257-258
    • (1997) Redox Rep , vol.3 , pp. 257-258
    • Kettle, A.J.1    van Dalen, C.J.2    Winterbourn, C.C.3
  • 65
    • 0037076395 scopus 로고    scopus 로고
    • Global changes in gene expression by human polymorphonuclear leukocytes during receptor-mediated phagocytosis: cell fate is regulated at the level of gene expression
    • Kobayashi S.D., Voyich J.M., Buhl C.L., Stahl R.M., and DeLeo F.R. Global changes in gene expression by human polymorphonuclear leukocytes during receptor-mediated phagocytosis: cell fate is regulated at the level of gene expression. Proc Natl Acad Sci USA 99 (2002) 6901-6906
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 6901-6906
    • Kobayashi, S.D.1    Voyich, J.M.2    Buhl, C.L.3    Stahl, R.M.4    DeLeo, F.R.5
  • 66
    • 0021920438 scopus 로고
    • Myeloperoxidase: its structure and expression during myeloid differentiation
    • Koeffler H.P., Ranyard J., and Pertcheck M. Myeloperoxidase: its structure and expression during myeloid differentiation. Blood 65 (1985) 484-491
    • (1985) Blood , vol.65 , pp. 484-491
    • Koeffler, H.P.1    Ranyard, J.2    Pertcheck, M.3
  • 67
    • 0031001754 scopus 로고    scopus 로고
    • Extensive tyrosine nitration in human myocardial inflammation: evidence for the presence of peroxynitrite
    • Kooy N.W., Lewis S.J., Royall J.A., Ye Y.Z., Kelly D.R., and Beckman J.S. Extensive tyrosine nitration in human myocardial inflammation: evidence for the presence of peroxynitrite. Crit Care Med 25 (1997) 812-819
    • (1997) Crit Care Med , vol.25 , pp. 812-819
    • Kooy, N.W.1    Lewis, S.J.2    Royall, J.A.3    Ye, Y.Z.4    Kelly, D.R.5    Beckman, J.S.6
  • 69
    • 0032880537 scopus 로고    scopus 로고
    • Oxidative damage to proteins of bronchoalveolar lavage fluid in patients with acute respiratory distress syndrome: evidence for neutrophil-mediated hydroxylation, nitration, and chlorination
    • Lamb N.J., Gutteridge J.M., Baker C., Evans T.W., and Quinlan G.J. Oxidative damage to proteins of bronchoalveolar lavage fluid in patients with acute respiratory distress syndrome: evidence for neutrophil-mediated hydroxylation, nitration, and chlorination. Crit Care Med 27 (1999) 1738-1744
    • (1999) Crit Care Med , vol.27 , pp. 1738-1744
    • Lamb, N.J.1    Gutteridge, J.M.2    Baker, C.3    Evans, T.W.4    Quinlan, G.J.5
  • 70
    • 0037058827 scopus 로고    scopus 로고
    • Vascular oxidative stress and endothelial dysfunction in patients with chronic heart failure: role of xanthine-oxidase and extracellular superoxide dismutase
    • Landmesser U., Spiekermann S., Dikalov S., Tatge H., Wilke R., Kohler C., et al. Vascular oxidative stress and endothelial dysfunction in patients with chronic heart failure: role of xanthine-oxidase and extracellular superoxide dismutase. Circulation 106 (2002) 3073-3078
    • (2002) Circulation , vol.106 , pp. 3073-3078
    • Landmesser, U.1    Spiekermann, S.2    Dikalov, S.3    Tatge, H.4    Wilke, R.5    Kohler, C.6
  • 72
    • 0031035583 scopus 로고    scopus 로고
    • Reactive nitrogen intermediates promote low density lipoprotein oxidation in human atherosclerotic intima
    • Leeuwenburgh C., Hardy M.M., Hazen S.L., Wagner P., Oh-ishi S., Steinbrecher U.P., et al. Reactive nitrogen intermediates promote low density lipoprotein oxidation in human atherosclerotic intima. J Biol Chem 272 (1997) 1433-1436
    • (1997) J Biol Chem , vol.272 , pp. 1433-1436
    • Leeuwenburgh, C.1    Hardy, M.M.2    Hazen, S.L.3    Wagner, P.4    Oh-ishi, S.5    Steinbrecher, U.P.6
  • 73
    • 0031021944 scopus 로고    scopus 로고
    • Mass spectrometric quantification of markers for protein oxidation by tyrosyl radical, copper, and hydroxyl radical in low density lipoprotein isolated from human atherosclerotic plaques
    • Leeuwenburgh C., Rasmussen J.E., Hsu F.F., Mueller D.M., Pennathur S., and Heinecke J.W. Mass spectrometric quantification of markers for protein oxidation by tyrosyl radical, copper, and hydroxyl radical in low density lipoprotein isolated from human atherosclerotic plaques. J Biol Chem 272 (1997) 3520-3526
    • (1997) J Biol Chem , vol.272 , pp. 3520-3526
    • Leeuwenburgh, C.1    Rasmussen, J.E.2    Hsu, F.F.3    Mueller, D.M.4    Pennathur, S.5    Heinecke, J.W.6
  • 74
    • 0029054734 scopus 로고
    • Molecular bases of the acute coronary syndromes
    • Libby P. Molecular bases of the acute coronary syndromes. Circulation 91 (1995) 2844-2850
    • (1995) Circulation , vol.91 , pp. 2844-2850
    • Libby, P.1
  • 75
    • 0034687333 scopus 로고    scopus 로고
    • Coronary artery injury and the biology of atherosclerosis: inflammation, thrombosis, and stabilization
    • (discussion 8J-9J)
    • Libby P. Coronary artery injury and the biology of atherosclerosis: inflammation, thrombosis, and stabilization. Am J Cardiol 86 (2000) 3J-8J (discussion 8J-9J)
    • (2000) Am J Cardiol , vol.86
    • Libby, P.1
  • 76
    • 0023255330 scopus 로고
    • Loss of granule myeloperoxidase during in vitro culture of human monocytes correlates with decay in antiprotozoa activity
    • Locksley R.M., Nelson C.S., Fankhauser J.E., and Klebanoff S.J. Loss of granule myeloperoxidase during in vitro culture of human monocytes correlates with decay in antiprotozoa activity. Am J Trop Med Hyg 36 (1987) 541-548
    • (1987) Am J Trop Med Hyg , vol.36 , pp. 541-548
    • Locksley, R.M.1    Nelson, C.S.2    Fankhauser, J.E.3    Klebanoff, S.J.4
  • 77
    • 0029862502 scopus 로고    scopus 로고
    • Nitration and inactivation of manganese superoxide dismutase in chronic rejection of human renal allografts
    • MacMillan-Crow L.A., Crow J.P., Kerby J.D., Beckman J.S., and Thompson J.A. Nitration and inactivation of manganese superoxide dismutase in chronic rejection of human renal allografts. Proc Natl Acad Sci USA 93 (1996) 11853-11858
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 11853-11858
    • MacMillan-Crow, L.A.1    Crow, J.P.2    Kerby, J.D.3    Beckman, J.S.4    Thompson, J.A.5
  • 78
    • 0031713365 scopus 로고    scopus 로고
    • Fibronectin: structure, assembly, and cardiovascular implications
    • Magnusson M.K., and Mosher D.F. Fibronectin: structure, assembly, and cardiovascular implications. Arterioscler Thromb Vasc Biol 18 (1998) 1363-1370
    • (1998) Arterioscler Thromb Vasc Biol , vol.18 , pp. 1363-1370
    • Magnusson, M.K.1    Mosher, D.F.2
  • 79
    • 0001059250 scopus 로고    scopus 로고
    • 2/halide system in human atherosclerotic lesions: colocalization of myeloperoxidase and hypochlorite-modified proteins
    • 2/halide system in human atherosclerotic lesions: colocalization of myeloperoxidase and hypochlorite-modified proteins. Eur J Biochem 267 (2000) 4495-4503
    • (2000) Eur J Biochem , vol.267 , pp. 4495-4503
    • Malle, E.1    Waeg, G.2    Schreiber, R.3    Grone, E.F.4    Sattler, W.5    Grone, H.J.6
  • 80
    • 0025265381 scopus 로고
    • Reaction of compound III of myeloperoxidase with ascorbic acid
    • Marquez L.A., and Dunford H.B. Reaction of compound III of myeloperoxidase with ascorbic acid. J Biol Chem 265 (1990) 6074-6078
    • (1990) J Biol Chem , vol.265 , pp. 6074-6078
    • Marquez, L.A.1    Dunford, H.B.2
  • 81
    • 0025240884 scopus 로고
    • Kinetic studies on the reaction of compound II of myeloperoxidase with ascorbic acid. Role of ascorbic acid in myeloperoxidase function
    • Marquez L.A., Dunford H.B., and Van Wart H. Kinetic studies on the reaction of compound II of myeloperoxidase with ascorbic acid. Role of ascorbic acid in myeloperoxidase function. J Biol Chem 265 (1990) 5666-5670
    • (1990) J Biol Chem , vol.265 , pp. 5666-5670
    • Marquez, L.A.1    Dunford, H.B.2    Van Wart, H.3
  • 82
    • 0028211341 scopus 로고
    • Spectral and kinetic studies on the formation of myeloperoxidase compounds I and II: roles of hydrogen peroxide and superoxide
    • Marquez L.A., Huang J.T., and Dunford H.B. Spectral and kinetic studies on the formation of myeloperoxidase compounds I and II: roles of hydrogen peroxide and superoxide. Biochemistry 33 (1994) 1447-1454
    • (1994) Biochemistry , vol.33 , pp. 1447-1454
    • Marquez, L.A.1    Huang, J.T.2    Dunford, H.B.3
  • 83
    • 10644253777 scopus 로고    scopus 로고
    • 2-chlorohexadecanal derived from hypochlorite-modified high-density lipoprotein-associated plasmalogen is a natural inhibitor of endothelial nitric oxide biosynthesis
    • Marsche G., Heller R., Fauler G., Kovacevic A., Nuszkowski A., Graier W., et al. 2-chlorohexadecanal derived from hypochlorite-modified high-density lipoprotein-associated plasmalogen is a natural inhibitor of endothelial nitric oxide biosynthesis. Arterioscler Thromb Vasc Biol 24 (2004) 2302-2306
    • (2004) Arterioscler Thromb Vasc Biol , vol.24 , pp. 2302-2306
    • Marsche, G.1    Heller, R.2    Fauler, G.3    Kovacevic, A.4    Nuszkowski, A.5    Graier, W.6
  • 84
    • 0030704740 scopus 로고    scopus 로고
    • Transcytosis and surface presentation of IL-8 by venular endothelial cells
    • Middleton J., Neil S., Wintle J., Clark-Lewis I., Moore H., Lam C., et al. Transcytosis and surface presentation of IL-8 by venular endothelial cells. Cell 91 (1997) 385-395
    • (1997) Cell , vol.91 , pp. 385-395
    • Middleton, J.1    Neil, S.2    Wintle, J.3    Clark-Lewis, I.4    Moore, H.5    Lam, C.6
  • 85
    • 0035476427 scopus 로고    scopus 로고
    • Hypochlorous acid stimulation of the mitogen-activated protein kinase pathway enhances cell survival
    • Midwinter R.G., Vissers M.C., and Winterbourn C.C. Hypochlorous acid stimulation of the mitogen-activated protein kinase pathway enhances cell survival. Arch Biochem Biophys 394 (2001) 13-20
    • (2001) Arch Biochem Biophys , vol.394 , pp. 13-20
    • Midwinter, R.G.1    Vissers, M.C.2    Winterbourn, C.C.3
  • 86
    • 0002157595 scopus 로고    scopus 로고
    • Neutrophils obtained from obliterative atherosclerotic patients exhibit enhanced resting respiratory burst and increased degranulation in response to various stimuli
    • Mohacsi A., Kozlovszky B., Kiss I., Seres I., and Fulop Jr. T. Neutrophils obtained from obliterative atherosclerotic patients exhibit enhanced resting respiratory burst and increased degranulation in response to various stimuli. Biochim Biophys Acta 1316 (1996) 210-216
    • (1996) Biochim Biophys Acta , vol.1316 , pp. 210-216
    • Mohacsi, A.1    Kozlovszky, B.2    Kiss, I.3    Seres, I.4    Fulop Jr., T.5
  • 87
    • 0030764896 scopus 로고    scopus 로고
    • Immunohistochemical and genetic evidence of myeloperoxidase involvement in multiple sclerosis
    • Nagra R.M., Becher B., Tourtellotte W.W., Antel J.P., Gold D., Paladino T., et al. Immunohistochemical and genetic evidence of myeloperoxidase involvement in multiple sclerosis. J Neuroimmunol 78 (1997) 97-107
    • (1997) J Neuroimmunol , vol.78 , pp. 97-107
    • Nagra, R.M.1    Becher, B.2    Tourtellotte, W.W.3    Antel, J.P.4    Gold, D.5    Paladino, T.6
  • 88
    • 0019866087 scopus 로고
    • Hydrogen peroxide metabolism in human monocytes during differentiation in vitro
    • Nakagawara A., Nathan C.F., and Cohn Z.A. Hydrogen peroxide metabolism in human monocytes during differentiation in vitro. J Clin Invest 68 (1981) 1243-1252
    • (1981) J Clin Invest , vol.68 , pp. 1243-1252
    • Nakagawara, A.1    Nathan, C.F.2    Cohn, Z.A.3
  • 90
    • 0031665631 scopus 로고    scopus 로고
    • Insights into myeloperoxidase biosynthesis from its inherited deficiency
    • Nauseef W.M. Insights into myeloperoxidase biosynthesis from its inherited deficiency. J Mol Med 76 (1998) 661-668
    • (1998) J Mol Med , vol.76 , pp. 661-668
    • Nauseef, W.M.1
  • 91
    • 0020662879 scopus 로고
    • Role of myeloperoxidase in the respiratory burst of human neutrophils
    • Nauseef W.M., Metcalf J.A., and Root R.K. Role of myeloperoxidase in the respiratory burst of human neutrophils. Blood 61 (1983) 483-492
    • (1983) Blood , vol.61 , pp. 483-492
    • Nauseef, W.M.1    Metcalf, J.A.2    Root, R.K.3
  • 92
    • 0034904840 scopus 로고    scopus 로고
    • A functional myeloperoxidase polymorphic variant is associated with coronary artery disease in French-Canadians
    • Nikpoor B., Turecki G., Fournier C., Theroux P., and Rouleau G.A. A functional myeloperoxidase polymorphic variant is associated with coronary artery disease in French-Canadians. Am Heart J 142 (2001) 336-339
    • (2001) Am Heart J , vol.142 , pp. 336-339
    • Nikpoor, B.1    Turecki, G.2    Fournier, C.3    Theroux, P.4    Rouleau, G.A.5
  • 93
    • 0033937863 scopus 로고    scopus 로고
    • Role of myeloperoxidase in the neutrophil-induced oxidation of low density lipoprotein as studied by myeloperoxidase-knockout mouse
    • Noguchi N., Nakano K., Aratani Y., Koyama H., Kodama T., and Niki E. Role of myeloperoxidase in the neutrophil-induced oxidation of low density lipoprotein as studied by myeloperoxidase-knockout mouse. J Biochem (Tokyo) 127 (2000) 971-976
    • (2000) J Biochem (Tokyo) , vol.127 , pp. 971-976
    • Noguchi, N.1    Nakano, K.2    Aratani, Y.3    Koyama, H.4    Kodama, T.5    Niki, E.6
  • 94
    • 0035937846 scopus 로고    scopus 로고
    • Transcytosis of lipoprotein lipase across cultured endothelial cells requires both heparan sulfate proteoglycans and the very low density lipoprotein receptor
    • Obunike J.C., Lutz E.P., Li Z., Paka L., Katopodis T., Strickland D.K., et al. Transcytosis of lipoprotein lipase across cultured endothelial cells requires both heparan sulfate proteoglycans and the very low density lipoprotein receptor. J Biol Chem 276 (2001) 8934-8941
    • (2001) J Biol Chem , vol.276 , pp. 8934-8941
    • Obunike, J.C.1    Lutz, E.P.2    Li, Z.3    Paka, L.4    Katopodis, T.5    Strickland, D.K.6
  • 95
    • 0037406516 scopus 로고    scopus 로고
    • A functional variant of the myeloperoxidase gene is associated with cardiovascular disease in end-stage renal disease patients
    • Pecoits-Filho R., Stenvinkel P., Marchlewska A., Heimburger O., Barany P., Hoff C.M., et al. A functional variant of the myeloperoxidase gene is associated with cardiovascular disease in end-stage renal disease patients. Kidney Int Suppl (2003) S172-S176
    • (2003) Kidney Int Suppl
    • Pecoits-Filho, R.1    Stenvinkel, P.2    Marchlewska, A.3    Heimburger, O.4    Barany, P.5    Hoff, C.M.6
  • 96
    • 5644262427 scopus 로고    scopus 로고
    • Human atherosclerotic intima and blood of patients with established coronary artery disease contain high density lipoprotein damaged by reactive nitrogen species
    • Pennathur S., Bergt C., Shao B., Byun J., Kassim S.Y., Singh P., et al. Human atherosclerotic intima and blood of patients with established coronary artery disease contain high density lipoprotein damaged by reactive nitrogen species. J Biol Chem (2004)
    • (2004) J Biol Chem
    • Pennathur, S.1    Bergt, C.2    Shao, B.3    Byun, J.4    Kassim, S.Y.5    Singh, P.6
  • 97
    • 0035677242 scopus 로고    scopus 로고
    • Anti-neutrophil cytoplasmic antibodies stabilize adhesion and promote migration of flowing neutrophils on endothelial cells
    • Radford D.J., Luu N.T., Hewins P., Nash G.B., and Savage C.O. Anti-neutrophil cytoplasmic antibodies stabilize adhesion and promote migration of flowing neutrophils on endothelial cells. Arthritis Rheum 44 (2001) 2851-2861
    • (2001) Arthritis Rheum , vol.44 , pp. 2851-2861
    • Radford, D.J.1    Luu, N.T.2    Hewins, P.3    Nash, G.B.4    Savage, C.O.5
  • 98
    • 0042570785 scopus 로고    scopus 로고
    • Neutrophil-activating potential of antineutrophil cytoplasm autoantibodies
    • Rarok A.A., Limburg P.C., and Kallenberg C.G. Neutrophil-activating potential of antineutrophil cytoplasm autoantibodies. J Leukoc Biol 74 (2003) 3-15
    • (2003) J Leukoc Biol , vol.74 , pp. 3-15
    • Rarok, A.A.1    Limburg, P.C.2    Kallenberg, C.G.3
  • 99
    • 0016595791 scopus 로고
    • Granule enzymes of polymorphonuclear neutrophils: a phylogenetic comparison
    • Rausch P.G., and Moore T.G. Granule enzymes of polymorphonuclear neutrophils: a phylogenetic comparison. Blood 46 (1975) 913-919
    • (1975) Blood , vol.46 , pp. 913-919
    • Rausch, P.G.1    Moore, T.G.2
  • 100
    • 0028308484 scopus 로고
    • M12 protein from Streptococcus pyogenes is a receptor for immunoglobulin G3 and human albumin
    • Retnoningrum D.S., and Cleary P.P. M12 protein from Streptococcus pyogenes is a receptor for immunoglobulin G3 and human albumin. Infect Immun 62 (1994) 2387-2394
    • (1994) Infect Immun , vol.62 , pp. 2387-2394
    • Retnoningrum, D.S.1    Cleary, P.P.2
  • 101
    • 0028841383 scopus 로고
    • Effect of tumor necrosis factor-induced integrin activation on Fc gamma receptor II-mediated signal transduction: relevance for activation of neutrophils by anti-proteinase 3 or anti-myeloperoxidase antibodies
    • Reumaux D., Vossebeld P.J., Roos D., and Verhoeven A.J. Effect of tumor necrosis factor-induced integrin activation on Fc gamma receptor II-mediated signal transduction: relevance for activation of neutrophils by anti-proteinase 3 or anti-myeloperoxidase antibodies. Blood 86 (1995) 3189-3195
    • (1995) Blood , vol.86 , pp. 3189-3195
    • Reumaux, D.1    Vossebeld, P.J.2    Roos, D.3    Verhoeven, A.J.4
  • 102
    • 0029894331 scopus 로고    scopus 로고
    • Nitric oxide-mediated cyclooxygenase activation. A key event in the antiplatelet effects of nitrovasodilators
    • Salvemini D., Currie M.G., and Mollace V. Nitric oxide-mediated cyclooxygenase activation. A key event in the antiplatelet effects of nitrovasodilators. J Clin Invest 97 (1996) 2562-2568
    • (1996) J Clin Invest , vol.97 , pp. 2562-2568
    • Salvemini, D.1    Currie, M.G.2    Mollace, V.3
  • 103
    • 0035186323 scopus 로고    scopus 로고
    • Reactive oxygen and nitrogen metabolites modulate fibronectin-induced fibroblast migration in vitro
    • Sato E., Koyama S., Camhi S.L., Nelson D.K., and Robbins R.A. Reactive oxygen and nitrogen metabolites modulate fibronectin-induced fibroblast migration in vitro. Free Radic Biol Med 30 (2001) 22-29
    • (2001) Free Radic Biol Med , vol.30 , pp. 22-29
    • Sato, E.1    Koyama, S.2    Camhi, S.L.3    Nelson, D.K.4    Robbins, R.A.5
  • 104
    • 0033593070 scopus 로고    scopus 로고
    • Leukocytes utilize myeloperoxidase-generated nitrating intermediates as physiological catalysts for the generation of biologically active oxidized lipids and sterols in serum
    • Schmitt D., Shen Z., Zhang R., Colles S.M., Wu W., Salomon R.G., et al. Leukocytes utilize myeloperoxidase-generated nitrating intermediates as physiological catalysts for the generation of biologically active oxidized lipids and sterols in serum. Biochemistry 38 (1999) 16904-16915
    • (1999) Biochemistry , vol.38 , pp. 16904-16915
    • Schmitt, D.1    Shen, Z.2    Zhang, R.3    Colles, S.M.4    Wu, W.5    Salomon, R.G.6
  • 105
    • 0344196903 scopus 로고    scopus 로고
    • NO-dependent protein nitration: a cell signaling event or an oxidative inflammatory response?
    • Schopfer F.J., Baker P.R., and Freeman B.A. NO-dependent protein nitration: a cell signaling event or an oxidative inflammatory response?. Trends Biochem Sci 28 (2003) 646-654
    • (2003) Trends Biochem Sci , vol.28 , pp. 646-654
    • Schopfer, F.J.1    Baker, P.R.2    Freeman, B.A.3
  • 106
    • 0031837825 scopus 로고    scopus 로고
    • The oxidative inactivation of tissue inhibitor of metalloproteinase-1 (TIMP-1) by hypochlorous acid (HOCI) is suppressed by anti-rheumatic drugs
    • Shabani F., McNeil J., and Tippett L. The oxidative inactivation of tissue inhibitor of metalloproteinase-1 (TIMP-1) by hypochlorous acid (HOCI) is suppressed by anti-rheumatic drugs. Free Radic Res 28 (1998) 115-123
    • (1998) Free Radic Res , vol.28 , pp. 115-123
    • Shabani, F.1    McNeil, J.2    Tippett, L.3
  • 107
    • 0037414194 scopus 로고    scopus 로고
    • Association of nitrotyrosine levels with cardiovascular disease and modulation by statin therapy
    • Shishehbor M.H., Aviles R.J., Brennan M.L., Fu X., Goormastic M., Pearce G.L., et al. Association of nitrotyrosine levels with cardiovascular disease and modulation by statin therapy. Jama 289 (2003) 1675-1680
    • (2003) Jama , vol.289 , pp. 1675-1680
    • Shishehbor, M.H.1    Aviles, R.J.2    Brennan, M.L.3    Fu, X.4    Goormastic, M.5    Pearce, G.L.6
  • 108
    • 0037453094 scopus 로고    scopus 로고
    • Electron spin resonance characterization of vascular xanthine and NAD(P)H oxidase activity in patients with coronary artery disease: relation to endothelium-dependent vasodilation
    • Spiekermann S., Landmesser U., Dikalov S., Bredt M., Gamez G., Tatge H., et al. Electron spin resonance characterization of vascular xanthine and NAD(P)H oxidase activity in patients with coronary artery disease: relation to endothelium-dependent vasodilation. Circulation 107 (2003) 1383-1389
    • (2003) Circulation , vol.107 , pp. 1383-1389
    • Spiekermann, S.1    Landmesser, U.2    Dikalov, S.3    Bredt, M.4    Gamez, G.5    Tatge, H.6
  • 109
    • 0025096787 scopus 로고
    • Assembly of dimeric myeloperoxidase during posttranslational maturation in human leukemic HL-60 cells
    • Taylor K.L., Guzman G.S., Burgess C.A., and Kinkade Jr. J.M. Assembly of dimeric myeloperoxidase during posttranslational maturation in human leukemic HL-60 cells. Biochemistry 29 (1990) 1533-1539
    • (1990) Biochemistry , vol.29 , pp. 1533-1539
    • Taylor, K.L.1    Guzman, G.S.2    Burgess, C.A.3    Kinkade Jr., J.M.4
  • 110
    • 0028985005 scopus 로고
    • Isolation and identification of a protoheme IX derivative released during autolytic cleavage of human myeloperoxidase
    • Taylor K.L., Strobel F., Yue K.T., Ram P., Pohl J., Woods A.S., et al. Isolation and identification of a protoheme IX derivative released during autolytic cleavage of human myeloperoxidase. Arch Biochem Biophys 316 (1995) 635-642
    • (1995) Arch Biochem Biophys , vol.316 , pp. 635-642
    • Taylor, K.L.1    Strobel, F.2    Yue, K.T.3    Ram, P.4    Pohl, J.5    Woods, A.S.6
  • 111
    • 0242467273 scopus 로고    scopus 로고
    • Physiological oxidants induce apoptosis and cell cycle arrest in a multidrug-resistant natural killer cell line, NK-YS
    • Than T.A., Ogino T., Hosako M., Omori M., Tsuchiyama J., and Okada S. Physiological oxidants induce apoptosis and cell cycle arrest in a multidrug-resistant natural killer cell line, NK-YS. Leuk Lymphoma 44 (2003) 2109-2116
    • (2003) Leuk Lymphoma , vol.44 , pp. 2109-2116
    • Than, T.A.1    Ogino, T.2    Hosako, M.3    Omori, M.4    Tsuchiyama, J.5    Okada, S.6
  • 112
    • 2442716454 scopus 로고    scopus 로고
    • Albumin mediates the transcytosis of myeloperoxidase by means of caveolae in endothelial cells
    • Tiruppathi C., Naqvi T., Wu Y., Vogel S.M., Minshall R.D., and Malik A.B. Albumin mediates the transcytosis of myeloperoxidase by means of caveolae in endothelial cells. Proc Natl Acad Sci USA 101 (2004) 7699-7704
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 7699-7704
    • Tiruppathi, C.1    Naqvi, T.2    Wu, Y.3    Vogel, S.M.4    Minshall, R.D.5    Malik, A.B.6
  • 115
    • 10744226883 scopus 로고    scopus 로고
    • Pro-thrombotic State Induced by Post-translational Modification of Fibrinogen by Reactive Nitrogen Species
    • Vadseth C., Souza J.M., Thomson L., Seagraves A., Nagaswami C., Scheiner T., et al. Pro-thrombotic State Induced by Post-translational Modification of Fibrinogen by Reactive Nitrogen Species. J Biol Chem 279 (2004) 8820-8826
    • (2004) J Biol Chem , vol.279 , pp. 8820-8826
    • Vadseth, C.1    Souza, J.M.2    Thomson, L.3    Seagraves, A.4    Nagaswami, C.5    Scheiner, T.6
  • 116
    • 0030660227 scopus 로고    scopus 로고
    • Thiocyanate and chloride as competing substrates for myeloperoxidase
    • van Dalen C.J., Whitehouse M.W., Winterbourn C.C., and Kettle A.J. Thiocyanate and chloride as competing substrates for myeloperoxidase. Biochem J 327 Pt. 2 (1997) 487-492
    • (1997) Biochem J , vol.327 , Issue.PART 2 , pp. 487-492
    • van Dalen, C.J.1    Whitehouse, M.W.2    Winterbourn, C.C.3    Kettle, A.J.4
  • 117
    • 0030909465 scopus 로고    scopus 로고
    • Formation of reactive nitrogen species during peroxidase-catalyzed oxidation of nitrite. A potential additional mechanism of nitric oxide-dependent toxicity
    • van der Vliet A., Eiserich J.P., Halliwell B., and Cross C.E. Formation of reactive nitrogen species during peroxidase-catalyzed oxidation of nitrite. A potential additional mechanism of nitric oxide-dependent toxicity. J Biol Chem 272 (1997) 7617-7625
    • (1997) J Biol Chem , vol.272 , pp. 7617-7625
    • van der Vliet, A.1    Eiserich, J.P.2    Halliwell, B.3    Cross, C.E.4
  • 119
    • 0021083079 scopus 로고
    • Inflamed fibronectin: an altered fibronectin enhances neutrophil adhesion
    • Vercellotti G.M., McCarthy J., Furcht L.T., Jacob H.S., and Moldow C.F. Inflamed fibronectin: an altered fibronectin enhances neutrophil adhesion. Blood 62 (1983) 1063-1069
    • (1983) Blood , vol.62 , pp. 1063-1069
    • Vercellotti, G.M.1    McCarthy, J.2    Furcht, L.T.3    Jacob, H.S.4    Moldow, C.F.5
  • 120
    • 0032213390 scopus 로고    scopus 로고
    • Hypochlorous acid activates the tumor suppressor protein p53 in cultured human skin fibroblasts
    • Vile G.F., Rothwell L.A., and Kettle A.J. Hypochlorous acid activates the tumor suppressor protein p53 in cultured human skin fibroblasts. Arch Biochem Biophys 359 (1998) 51-56
    • (1998) Arch Biochem Biophys , vol.359 , pp. 51-56
    • Vile, G.F.1    Rothwell, L.A.2    Kettle, A.J.3
  • 121
    • 0033564289 scopus 로고    scopus 로고
    • Protein modification during biological aging: selective tyrosine nitration of the SERCA2a isoform of the sarcoplasmic reticulum Ca2+-ATPase in skeletal muscle
    • Viner R.I., Ferrington D.A., Williams T.D., Bigelow D.J., and Schoneich C. Protein modification during biological aging: selective tyrosine nitration of the SERCA2a isoform of the sarcoplasmic reticulum Ca2+-ATPase in skeletal muscle. Biochem J 340 Pt 3 (1999) 657-669
    • (1999) Biochem J , vol.340 , Issue.PART 3 , pp. 657-669
    • Viner, R.I.1    Ferrington, D.A.2    Williams, T.D.3    Bigelow, D.J.4    Schoneich, C.5
  • 122
    • 0030997757 scopus 로고    scopus 로고
    • Hypochlorous acid disrupts the adhesive properties of subendothelial matrix
    • Vissers M.C., and Thomas C. Hypochlorous acid disrupts the adhesive properties of subendothelial matrix. Free Radic Biol Med 23 (1997) 401-411
    • (1997) Free Radic Biol Med , vol.23 , pp. 401-411
    • Vissers, M.C.1    Thomas, C.2
  • 123
    • 0019879354 scopus 로고
    • Spectral properties of myeloperoxidase and its ligand complexes
    • Wever R., and Plat H. Spectral properties of myeloperoxidase and its ligand complexes. Biochim Biophys Acta 661 (1981) 235-239
    • (1981) Biochim Biophys Acta , vol.661 , pp. 235-239
    • Wever, R.1    Plat, H.2
  • 124
    • 0032949778 scopus 로고    scopus 로고
    • Modification of type III VLDL, their remnants, and VLDL from ApoE-knockout mice by p-hydroxyphenylacetaldehyde, a product of myeloperoxidase activity, causes marked cholesteryl ester accumulation in macrophages
    • Whitman S.C., Hazen S.L., Miller D.B., Hegele R.A., Heinecke J.W., and Huff M.W. Modification of type III VLDL, their remnants, and VLDL from ApoE-knockout mice by p-hydroxyphenylacetaldehyde, a product of myeloperoxidase activity, causes marked cholesteryl ester accumulation in macrophages. Arterioscler Thromb Vasc Biol 19 (1999) 1238-1249
    • (1999) Arterioscler Thromb Vasc Biol , vol.19 , pp. 1238-1249
    • Whitman, S.C.1    Hazen, S.L.2    Miller, D.B.3    Hegele, R.A.4    Heinecke, J.W.5    Huff, M.W.6
  • 125
    • 0021807129 scopus 로고
    • Comparative reactivities of various biological compounds with myeloperoxidase-hydrogen peroxide-chloride, and similarity of the oxidant to hypochlorite
    • Winterbourn C.C. Comparative reactivities of various biological compounds with myeloperoxidase-hydrogen peroxide-chloride, and similarity of the oxidant to hypochlorite. Biochim Biophys Acta 840 (1985) 204-210
    • (1985) Biochim Biophys Acta , vol.840 , pp. 204-210
    • Winterbourn, C.C.1
  • 127
    • 0033520499 scopus 로고    scopus 로고
    • Eosinophil peroxidase nitrates protein tyrosyl residues. Implications for oxidative damage by nitrating intermediates in eosinophilic inflammatory disorders
    • Wu W., Chen Y., and Hazen S.L. Eosinophil peroxidase nitrates protein tyrosyl residues. Implications for oxidative damage by nitrating intermediates in eosinophilic inflammatory disorders. J Biol Chem 274 (1999) 25933-25944
    • (1999) J Biol Chem , vol.274 , pp. 25933-25944
    • Wu, W.1    Chen, Y.2    Hazen, S.L.3
  • 128
    • 0026625050 scopus 로고
    • X-ray crystal structure of canine myeloperoxidase at 3 A resolution
    • Zeng J., and Fenna R.E. X-ray crystal structure of canine myeloperoxidase at 3 A resolution. J Mol Biol 226 (1992) 185-207
    • (1992) J Mol Biol , vol.226 , pp. 185-207
    • Zeng, J.1    Fenna, R.E.2
  • 129
    • 0035920164 scopus 로고    scopus 로고
    • l-Arginine chlorination products inhibit endothelial nitric oxide production
    • Zhang C., Reiter C., Eiserich J.P., Boersma B., Parks D.A., Beckman J.S., et al. l-Arginine chlorination products inhibit endothelial nitric oxide production. J Biol Chem 276 (2001) 27159-27165
    • (2001) J Biol Chem , vol.276 , pp. 27159-27165
    • Zhang, C.1    Reiter, C.2    Eiserich, J.P.3    Boersma, B.4    Parks, D.A.5    Beckman, J.S.6
  • 130
    • 0035824162 scopus 로고    scopus 로고
    • Association between myeloperoxidase levels and risk of coronary artery disease
    • Zhang R., Brennan M.L., Fu X., Aviles R.J., Pearce G.L., Penn M.S., et al. Association between myeloperoxidase levels and risk of coronary artery disease. Jama 286 (2001) 2136-2142
    • (2001) Jama , vol.286 , pp. 2136-2142
    • Zhang, R.1    Brennan, M.L.2    Fu, X.3    Aviles, R.J.4    Pearce, G.L.5    Penn, M.S.6
  • 131
    • 0037195783 scopus 로고    scopus 로고
    • Myeloperoxidase functions as a major enzymatic catalyst for initiation of lipid peroxidation at sites of inflammation
    • Zhang R., Brennan M.L., Shen Z., MacPherson J.C., Schmitt D., Molenda C.E., et al. Myeloperoxidase functions as a major enzymatic catalyst for initiation of lipid peroxidation at sites of inflammation. J Biol Chem 277 (2002) 46116-46122
    • (2002) J Biol Chem , vol.277 , pp. 46116-46122
    • Zhang, R.1    Brennan, M.L.2    Shen, Z.3    MacPherson, J.C.4    Schmitt, D.5    Molenda, C.E.6
  • 132
    • 0344440801 scopus 로고    scopus 로고
    • Interaction of myeloperoxidase with vascular NAD(P)H oxidase-derived reactive oxygen species in vasculature: implications for vascular diseases
    • Zhang C., Yang J., Jacobs J.D., and Jennings L.K. Interaction of myeloperoxidase with vascular NAD(P)H oxidase-derived reactive oxygen species in vasculature: implications for vascular diseases. Am J Physiol Heart Circ Physiol 285 (2003) H2563-H2572
    • (2003) Am J Physiol Heart Circ Physiol , vol.285
    • Zhang, C.1    Yang, J.2    Jacobs, J.D.3    Jennings, L.K.4
  • 133
    • 0030054659 scopus 로고    scopus 로고
    • Cis-elements in the promoter region of the human myeloperoxidase (MPO) gene
    • Zhao W.G., Regmi A., Austin E.D., Braun J.E., Racine M., and Austin G.E. Cis-elements in the promoter region of the human myeloperoxidase (MPO) gene. Leukemia 10 (1996) 1089-1103
    • (1996) Leukemia , vol.10 , pp. 1089-1103
    • Zhao, W.G.1    Regmi, A.2    Austin, E.D.3    Braun, J.E.4    Racine, M.5    Austin, G.E.6
  • 134
    • 4344577056 scopus 로고    scopus 로고
    • Apolipoprotein A-I is a selective target for myeloperoxidase-catalyzed oxidation and functional impairment in subjects with cardiovascular disease
    • Zheng L., Nukuna B., Brennan M.L., Sun M., Goormastic M., Settle M., et al. Apolipoprotein A-I is a selective target for myeloperoxidase-catalyzed oxidation and functional impairment in subjects with cardiovascular disease. J Clin Invest 114 (2004) 529-541
    • (2004) J Clin Invest , vol.114 , pp. 529-541
    • Zheng, L.1    Nukuna, B.2    Brennan, M.L.3    Sun, M.4    Goormastic, M.5    Settle, M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.