메뉴 건너뛰기




Volumn 105, Issue 10, 2000, Pages 1455-1463

Eosinophils generate brominating oxidants in allergen-induced asthma

Author keywords

[No Author keywords available]

Indexed keywords

ALLERGEN; HALIDE; HYDROGEN PEROXIDE; MYELOPEROXIDASE; OXIDIZING AGENT; PEROXIDASE;

EID: 0034033812     PISSN: 00219738     EISSN: None     Source Type: Journal    
DOI: 10.1172/JCI9702     Document Type: Article
Times cited : (273)

References (67)
  • 2
    • 37049188738 scopus 로고
    • Brominating oxidants generated by human eosinophils
    • Weiss, S.J., Test, S.T., Eckmann, C.M., Ross, D., and Regiania, S. 1986. Brominating oxidants generated by human eosinophils. Science. 234:200-203.
    • (1986) Science , vol.234 , pp. 200-203
    • Weiss, S.J.1    Test, S.T.2    Eckmann, C.M.3    Ross, D.4    Regiania, S.5
  • 3
    • 0024554014 scopus 로고
    • Eosinophils preferentially use bromide to generate halogenating agents
    • Mayeno, A.N., Curran, A.J., Roberts, R.L., and Foote, C.S. 1989. Eosinophils preferentially use bromide to generate halogenating agents. J. Biol. Chem. 264:5660-5668.
    • (1989) J. Biol. Chem. , vol.264 , pp. 5660-5668
    • Mayeno, A.N.1    Curran, A.J.2    Roberts, R.L.3    Foote, C.S.4
  • 4
    • 0023149501 scopus 로고
    • The injurious effect of eosinophil peroxidase, hydrogen peroxide, and halides on pneumocytes in vitro
    • Agosti, J.M., et al. 1987. The injurious effect of eosinophil peroxidase, hydrogen peroxide, and halides on pneumocytes in vitro. J. Allergy Clin. Immunol. 79:496-504.
    • (1987) J. Allergy Clin. Immunol. , vol.79 , pp. 496-504
    • Agosti, J.M.1
  • 7
    • 0033604657 scopus 로고    scopus 로고
    • The role of allergy in the development of asthma
    • Holt, P.G., Macaubas, C., Stumbles, P.A., and Sly, P.D. 1999. The role of allergy in the development of asthma. Nature. 402:B12-B17.
    • (1999) Nature , vol.402
    • Holt, P.G.1    Macaubas, C.2    Stumbles, P.A.3    Sly, P.D.4
  • 8
    • 0017695845 scopus 로고
    • Oxidative metabolism of the human eosinophil
    • DeChatelet, L.R., et al. 1977. Oxidative metabolism of the human eosinophil. Blood. 50:525-535.
    • (1977) Blood , vol.50 , pp. 525-535
    • DeChatelet, L.R.1
  • 9
    • 0025299641 scopus 로고
    • Tumor necrosis factor alpha/cachectin stimulates eosinophil oxidant production and toxicity towards human endothelium
    • Slungaard, A., Vercellotti, G.M., Walker, G., Nelson, R.D., and Jacob, H.S. 1990. Tumor necrosis factor alpha/cachectin stimulates eosinophil oxidant production and toxicity towards human endothelium. J. Exp. Med. 171:2025-2041.
    • (1990) J. Exp. Med. , vol.171 , pp. 2025-2041
    • Slungaard, A.1    Vercellotti, G.M.2    Walker, G.3    Nelson, R.D.4    Jacob, H.S.5
  • 10
    • 0031572166 scopus 로고    scopus 로고
    • Study on the superoxide-producing enzyme of eosinophils and neutrophils-comparison of the NADPH oxidase components
    • Someya, A., Nishijima, K., Nunoi, H., Irie, S., and Nagaoka, I. 1997. Study on the superoxide-producing enzyme of eosinophils and neutrophils-comparison of the NADPH oxidase components. Arch. Biochem. Biophys. 345:207-213.
    • (1997) Arch. Biochem. Biophys. , vol.345 , pp. 207-213
    • Someya, A.1    Nishijima, K.2    Nunoi, H.3    Irie, S.4    Nagaoka, I.5
  • 11
    • 0018869987 scopus 로고
    • Bactericidal activity of eosinophil peroxidase
    • Jong, E.C., Henderson, W.R., and Klebanoff, S.J. 1980. Bactericidal activity of eosinophil peroxidase. J. Immunol. 124:1378-1382.
    • (1980) J. Immunol. , vol.124 , pp. 1378-1382
    • Jong, E.C.1    Henderson, W.R.2    Klebanoff, S.J.3
  • 12
    • 0019524195 scopus 로고
    • Peroxidase-mediated toxicity to schistosomula of Schistosoma mansoni
    • Jong, E.C., Mahmoud, A.A., and Klebanoff, S.J. 1981. Peroxidase-mediated toxicity to schistosomula of Schistosoma mansoni. J. Immunol. 126:468-471.
    • (1981) J. Immunol. , vol.126 , pp. 468-471
    • Jong, E.C.1    Mahmoud, A.A.2    Klebanoff, S.J.3
  • 13
    • 0026010936 scopus 로고
    • Bromide-dependent toxicity of eosinophil peroxidase for endothelium and isolated working rat hearts: A model for eosinophilic endocarditis
    • Slungaard, A., and Mahoney, J.R., Jr. 1991. Bromide-dependent toxicity of eosinophil peroxidase for endothelium and isolated working rat hearts: a model for eosinophilic endocarditis. J. Exp. Med. 173:117-126.
    • (1991) J. Exp. Med. , vol.173 , pp. 117-126
    • Slungaard, A.1    Mahoney J.R., Jr.2
  • 14
    • 0024384968 scopus 로고
    • Comparative toxicity of the horse eosinophil peroxidase-H2O2-halide system and granule basic proteins
    • Klebanoff, S.J., Agosti, J.M., Jorg, A., and Waltersdorph, A.M. 1989. Comparative toxicity of the horse eosinophil peroxidase-H2O2-halide system and granule basic proteins. J. Immunol. 143:239-244.
    • (1989) J. Immunol. , vol.143 , pp. 239-244
    • Klebanoff, S.J.1    Agosti, J.M.2    Jorg, A.3    Waltersdorph, A.M.4
  • 15
    • 0019474154 scopus 로고
    • Role of cell-generated hydrogen peroxide in granulocyte-mediated killing of schistosomula of Schistosoma mansoni in vitro
    • Kazura, J.W., Fanning, M.M., Blumer, J.L., and Mahmoud, A.A. 1981. Role of cell-generated hydrogen peroxide in granulocyte-mediated killing of schistosomula of Schistosoma mansoni in vitro. J. Clin. Invest. 67:93-102.
    • (1981) J. Clin. Invest. , vol.67 , pp. 93-102
    • Kazura, J.W.1    Fanning, M.M.2    Blumer, J.L.3    Mahmoud, A.A.4
  • 16
    • 0028318790 scopus 로고
    • Effects of sonicated eosinophils on the in vivo sensitivity of human lymphoma cells to glucose oxidase
    • Samoszuk, M.K., Nguyen, V., Thomas, C., and Jacobson, D. 1994. Effects of sonicated eosinophils on the in vivo sensitivity of human lymphoma cells to glucose oxidase. Cancer Res. 54:2650-2653.
    • (1994) Cancer Res. , vol.54 , pp. 2650-2653
    • Samoszuk, M.K.1    Nguyen, V.2    Thomas, C.3    Jacobson, D.4
  • 17
    • 0021942070 scopus 로고
    • Human eosinophil peroxidase: Purification and characterization
    • Carlson, M.G., Peterson, C.G., and Venge, P. 1985 Human eosinophil peroxidase: purification and characterization J. Immunol. 134:1875-1879.
    • (1985) J. Immunol. , vol.134 , pp. 1875-1879
    • Carlson, M.G.1    Peterson, C.G.2    Venge, P.3
  • 18
    • 0024508002 scopus 로고
    • Molecular cloning of the human eosinophil peroxidase. Evidence for the existence of a peroxidase multigene family
    • Ten, R.M., Pease, L.R., McKean, D.J., Bell, M.P., and Gleich, G.J. 1989. Molecular cloning of the human eosinophil peroxidase. Evidence for the existence of a peroxidase multigene family. J. Exp. Med. 169:1757-1769.
    • (1989) J. Exp. Med. , vol.169 , pp. 1757-1769
    • Ten, R.M.1    Pease, L.R.2    McKean, D.J.3    Bell, M.P.4    Gleich, G.J.5
  • 19
    • 0024447808 scopus 로고
    • Molecular cloning and characterization of a chromosomal gene for human eosinophil peroxidase
    • Sakamaki, K., Tomonaga, M., Tsukui, K., and Nagata, S. 1989. Molecular cloning and characterization of a chromosomal gene for human eosinophil peroxidase. J. Biol. Chem. 264:16828-16836.
    • (1989) J. Biol. Chem. , vol.264 , pp. 16828-16836
    • Sakamaki, K.1    Tomonaga, M.2    Tsukui, K.3    Nagata, S.4
  • 20
    • 0018827927 scopus 로고
    • Eosinophil-mediated mammalian tumor cell cytotoxicity: Role of the peroxidase system
    • Jong, E.C., and Klebanoff, S.J. 1980. Eosinophil-mediated mammalian tumor cell cytotoxicity: role of the peroxidase system. J. Immunol. 124:1949-1953.
    • (1980) J. Immunol. , vol.124 , pp. 1949-1953
    • Jong, E.C.1    Klebanoff, S.J.2
  • 21
    • 0019988650 scopus 로고
    • Chlorination of taurine by human neutrophils. Evidence for hypochlorous acid generation
    • Weiss, S.J., Klein, R., Slivka, A., and Wei, M. 1982. Chlorination of taurine by human neutrophils. Evidence for hypochlorous acid generation. J. Clin. Invest. 70:598-607.
    • (1982) J. Clin. Invest. , vol.70 , pp. 598-607
    • Weiss, S.J.1    Klein, R.2    Slivka, A.3    Wei, M.4
  • 22
    • 0020702109 scopus 로고
    • Assessment of chlorination by human neutrophils
    • Foote, G.S., Goyne, T.E., and Lehrer, R.I. 1983. Assessment of chlorination by human neutrophils. Nature. 301:715-716.
    • (1983) Nature , vol.301 , pp. 715-716
    • Foote, G.S.1    Goyne, T.E.2    Lehrer, R.I.3
  • 23
  • 24
    • 0025804535 scopus 로고
    • Thiocyanate is the major substrate for eosinophil peroxidase in physiologic fluids. Implications for cytotoxicity
    • Slungaard, A., and Mahoney, J.R., Jr. 1991. Thiocyanate is the major substrate for eosinophil peroxidase in physiologic fluids. Implications for cytotoxicity. J. Biol. Chem. 266:4903-4910.
    • (1991) J. Biol. Chem. , vol.266 , pp. 4903-4910
    • Slungaard, A.1    Mahoney J.R., Jr.2
  • 25
    • 0010220681 scopus 로고    scopus 로고
    • Drugs: Therapeutic and toxic
    • C.A. Burtis and E.R. Ashwood, editors. W.B. Saunders Co. Philadelphia, Pennsylvania, USA
    • Teitz, N.W. 1999. Drugs: therapeutic and toxic. In Teitz textbook of clinical chemistry. C.A. Burtis and E.R. Ashwood, editors. W.B. Saunders Co. Philadelphia, Pennsylvania, USA. p. 2216.
    • (1999) Teitz Textbook of Clinical Chemistry , pp. 2216
    • Teitz, N.W.1
  • 26
    • 0030053876 scopus 로고    scopus 로고
    • p-Hydroxyphenylacetaldehyde is the major product of L-tyrosine oxidation by activated human phagocytes: A chloride-dependent mechanism for the conversion of free amino acids into reactive aldehydes by myeloperoxidase
    • Hazen, S.L., Hsu, F.F., and Heinecke, J.W. 1996. p-Hydroxyphenylacetaldehyde is the major product of L-tyrosine oxidation by activated human phagocytes: a chloride-dependent mechanism for the conversion of free amino acids into reactive aldehydes by myeloperoxidase. J. Biol. Chem. 271:1861-1867.
    • (1996) J. Biol. Chem. , vol.271 , pp. 1861-1867
    • Hazen, S.L.1    Hsu, F.F.2    Heinecke, J.W.3
  • 27
    • 0029916841 scopus 로고    scopus 로고
    • Identification of eosinophils by flow cytometry
    • Thurau, A.M., Schyk U., Wolf, V., Krug, N., and Schauer, U. 1996. Identification of eosinophils by flow cytometry. Cytometry. 23:150-158.
    • (1996) Cytometry , vol.23 , pp. 150-158
    • Thurau, A.M.1    Schyk, U.2    Wolf, V.3    Krug, N.4    Schauer, U.5
  • 28
    • 0024335026 scopus 로고
    • Purification of human blood eosinophils by negative selection using immunomagnetic beads
    • Hansel, T.T., et al. 1989. Purification of human blood eosinophils by negative selection using immunomagnetic beads. J. Immunol. Methods. 122:97-103.
    • (1989) J. Immunol. Methods , vol.122 , pp. 97-103
    • Hansel, T.T.1
  • 29
    • 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. 1997. Thiocyanate and chloride as competing substrates for myeloperoxidase. Biochem. J. 327:487-492.
    • (1997) Biochem. J. , vol.327 , pp. 487-492
    • Van Dalen, C.J.1    Whitehouse, M.W.2    Winterbourn, C.C.3    Kettle, A.J.4
  • 30
    • 0015596284 scopus 로고
    • Biological defense mechanism: The production by leukocytes of superoxide, a potential bactericidal agent
    • Babior, B.M., Kipnes, R.S., and Curnutte, J.T. 1973. Biological defense mechanism: the production by leukocytes of superoxide, a potential bactericidal agent. J. Clin. Invest. 52:741-744.
    • (1973) J. Clin. Invest. , vol.52 , pp. 741-744
    • Babior, B.M.1    Kipnes, R.S.2    Curnutte, J.T.3
  • 31
    • 0030803161 scopus 로고    scopus 로고
    • Mass spectrometric quantification of 3-chlorotyrosine in human tissues with attomole sensitivity: A sensitive and specific marker for myeloperoxidase-catalyzed chlorination at sites of inflammation
    • Hazen, S.L., Crowley, J.R., Mueller, D.M., and Heinecke, J.W. 1997. Mass spectrometric quantification of 3-chlorotyrosine in human tissues with attomole sensitivity: a sensitive and specific marker for myeloperoxidase-catalyzed chlorination at sites of inflammation. Free Radic. Biol. Med. 23:909-916.
    • (1997) Free Radic. Biol. Med. , vol.23 , pp. 909-916
    • Hazen, S.L.1    Crowley, J.R.2    Mueller, D.M.3    Heinecke, J.W.4
  • 32
    • 0030979720 scopus 로고    scopus 로고
    • 3-Chlorotyrosine, a specific marker of myeloperoxidase-catalyzed oxidation, is markedly elevated in low density lipoprotein isolated from human atherosclerotic intima
    • Hazen, S.L., and Heinecke, J.W. 1997. 3-Chlorotyrosine, a specific marker of myeloperoxidase-catalyzed oxidation, is markedly elevated in low density lipoprotein isolated from human atherosclerotic intima. J. Clin. Invest. 99:2075-2081.
    • (1997) J. Clin. Invest. , vol.99 , pp. 2075-2081
    • Hazen, S.L.1    Heinecke, J.W.2
  • 33
    • 0033596905 scopus 로고    scopus 로고
    • 3-Bromotyrosine and 3,5-dibromotyrosine are major products of protein oxidation by eosinophil peroxidase: Potential markers for eosinophil-dependent tissue injury in vivo
    • Wu, W., Chen, Y., d'Avignon, A., and Hazen, S.L. 1999. 3-Bromotyrosine and 3,5-dibromotyrosine are major products of protein oxidation by eosinophil peroxidase: potential markers for eosinophil-dependent tissue injury in vivo. Biochemistry. 38:3538-3548.
    • (1999) Biochemistry , vol.38 , pp. 3538-3548
    • Wu, W.1    Chen, Y.2    D'Avignon, A.3    Hazen, S.L.4
  • 34
    • 0345683904 scopus 로고    scopus 로고
    • Detecting oxidative modification of biomolecules with isotope dilution mass spectrometry: Sensitive and quantitative assays for oxidized amino acids in proteins and tissues
    • Heinecke, J.W., et al. 1999, Detecting oxidative modification of biomolecules with isotope dilution mass spectrometry: sensitive and quantitative assays for oxidized amino acids in proteins and tissues. Methods Enzymol. 300:124-144.
    • (1999) Methods Enzymol. , vol.300 , pp. 124-144
    • Heinecke, J.W.1
  • 35
    • 0033435233 scopus 로고    scopus 로고
    • Nitric oxide regulation of asthmatic airway inflammation with segmental allergen challenge
    • Thomassen, M.J., et al. 1999. Nitric oxide regulation of asthmatic airway inflammation with segmental allergen challenge. J. Allergy Clin. Immunol. 104:1174-1182.
    • (1999) J. Allergy Clin. Immunol. , vol.104 , pp. 1174-1182
    • Thomassen, M.J.1
  • 36
    • 0003662479 scopus 로고    scopus 로고
    • National Institutes of Health. Bethesda, Maryland, USA. Publication no. 97-4051
    • National Heart, Lung, and Blood Institute. 1997. Expert panel report 2: guidelines for the diagnosis and management of asthma. National Institutes of Health. Bethesda, Maryland, USA. Publication no. 97-4051, pp. 1-86.
    • (1997) Expert Panel Report 2: Guidelines for the Diagnosis and Management of Asthma , pp. 1-86
  • 37
    • 0031772133 scopus 로고    scopus 로고
    • Modification of proteins and lipids by myeloperoxidase-derived oxidants
    • Hazen, S.L., Hsu, F.F., Gaut, J.R, Crowley, J.R., and Heinecke, J.W. 1999. Modification of proteins and lipids by myeloperoxidase-derived oxidants. Methods Enzymol. 300:88-105.
    • (1999) Methods Enzymol. , vol.300 , pp. 88-105
    • Hazen, S.L.1    Hsu, F.F.2    Gaut, J.R.3    Crowley, J.R.4    Heinecke, J.W.5
  • 38
    • 0000954438 scopus 로고
    • Autofluorescence of eosinophils: A bone marrow study
    • Fuerst, D.E., and Jannach, J.R. 1965. Autofluorescence of eosinophils: a bone marrow study. Nature. 205:1333-1335.
    • (1965) Nature , vol.205 , pp. 1333-1335
    • Fuerst, D.E.1    Jannach, J.R.2
  • 39
    • 0019489784 scopus 로고
    • Eosinophil autofluorescence and its use in isolation and analysis of human eosinophils using flow microfluorometry
    • Weil, G.J., and Chused, T.M. 1981. Eosinophil autofluorescence and its use in isolation and analysis of human eosinophils using flow microfluorometry. Blood. 57:1099-1104.
    • (1981) Blood , vol.57 , pp. 1099-1104
    • Weil, G.J.1    Chused, T.M.2
  • 40
    • 0023280087 scopus 로고
    • Deposition of autofluorescent eosinophil granules in pathologic bone marrow biopsies
    • Samoszuk, M.K., and Espinoza, F.P. 1987. Deposition of autofluorescent eosinophil granules in pathologic bone marrow biopsies. Blood. 70:597-599.
    • (1987) Blood , vol.70 , pp. 597-599
    • Samoszuk, M.K.1    Espinoza, F.P.2
  • 41
    • 0019497926 scopus 로고
    • Some enzymatic characteristics of eosinophil peroxidase from patients with eosinophilia and from healthy donors
    • Bos, A.J., Wevet, R., Hamers, M.N., and Roos, D. 1981. Some enzymatic characteristics of eosinophil peroxidase from patients with eosinophilia and from healthy donors. Infect. Immun. 32:427-431.
    • (1981) Infect. Immun. , vol.32 , pp. 427-431
    • Bos, A.J.1    Wevet, R.2    Hamers, M.N.3    Roos, D.4
  • 42
    • 0023030982 scopus 로고
    • Extensive deposition of eosinophil peroxidase in Hodgkin's and non-Hodgkin's lymphomas
    • Samoszuk, M.K., Lukes, R.J., and Nathwani, B. 1986. Extensive deposition of eosinophil peroxidase in Hodgkin's and non-Hodgkin's lymphomas. Am. J. Pathol. 125:426-429.
    • (1986) Am. J. Pathol. , vol.125 , pp. 426-429
    • Samoszuk, M.K.1    Lukes, R.J.2    Nathwani, B.3
  • 43
    • 0026485410 scopus 로고
    • Comparison of airway and blood eosinophil function after in vivo antigen challenge
    • Sedgwick, J.B., et al. 1992. Comparison of airway and blood eosinophil function after in vivo antigen challenge. J. Immunol. 149:3710-3718.
    • (1992) J. Immunol. , vol.149 , pp. 3710-3718
    • Sedgwick, J.B.1
  • 44
    • 0026648268 scopus 로고
    • Inflammatory cells and eicosanoid mediators in subjects with late asthmatic responses and increases in airway responsiveness
    • Smith, H.R., et al. 1992. Inflammatory cells and eicosanoid mediators in subjects with late asthmatic responses and increases in airway responsiveness. J. Allergy Clin. Immunol. 89:1076-1084.
    • (1992) J. Allergy Clin. Immunol. , vol.89 , pp. 1076-1084
    • Smith, H.R.1
  • 45
    • 0029018265 scopus 로고
    • Spontaneous oxygen radical production at sites of antigen challenge in allergic subjects
    • Sanders, S.P., et al. 1995. Spontaneous oxygen radical production at sites of antigen challenge in allergic subjects. Am. J. Respir. Crit. Care Med. 151:1725-1733.
    • (1995) Am. J. Respir. Crit. Care Med. , vol.151 , pp. 1725-1733
    • Sanders, S.P.1
  • 46
    • 0030926183 scopus 로고    scopus 로고
    • The immediate and late allergic response to segmental bronchopulmonary provocation in asthma
    • Jarjour, N.N., et al. 1997. The immediate and late allergic response to segmental bronchopulmonary provocation in asthma. Am J. Respir. Crit. Care Med. 155:1515-1521.
    • (1997) Am J. Respir. Crit. Care Med. , vol.155 , pp. 1515-1521
    • Jarjour, N.N.1
  • 47
    • 0010220681 scopus 로고    scopus 로고
    • Drugs: Therapeutic and toxic
    • C.A. Burtis and H.R. Ashwood, editors. W.B. Saunders Co. Philadelphia, Pennsylvania, USA
    • Teitz, N.W. 1999. Drugs: therapeutic and toxic. In Teitz textbook of clinical chemistry. C.A. Burtis and H.R. Ashwood, editors. W.B. Saunders Co. Philadelphia, Pennsylvania, USA. p. 1097.
    • (1999) Teitz Textbook of Clinical Chemistry , pp. 1097
    • Teitz, N.W.1
  • 48
    • 0032054664 scopus 로고    scopus 로고
    • Marine natural products
    • Faulkner, D.J. 1998. Marine natural products. Nat. Prod. Rep. 15:113-158.
    • (1998) Nat. Prod. Rep. , vol.15 , pp. 113-158
    • Faulkner, D.J.1
  • 49
    • 0025816433 scopus 로고
    • Two new brominated tyrosine derivatives from the sponge Druinella (Psammaplysilla) purpurea
    • James, D.M., Kunze, H.B., and Faulkner, D.J. 1991. Two new brominated tyrosine derivatives from the sponge Druinella (Psammaplysilla) purpurea. J. Nat. Prod. 54:1137-1140.
    • (1991) J. Nat. Prod. , vol.54 , pp. 1137-1140
    • James, D.M.1    Kunze, H.B.2    Faulkner, D.J.3
  • 50
    • 0021190356 scopus 로고
    • Protein brominarion by bromoperoxidase from Penicillus capitatus
    • Manthey, J.A., Hager, L.P., and McElvany, K.D. 1984. Protein brominarion by bromoperoxidase from Penicillus capitatus. Methods Enzymol. 107:439-445.
    • (1984) Methods Enzymol. , vol.107 , pp. 439-445
    • Manthey, J.A.1    Hager, L.P.2    McElvany, K.D.3
  • 51
    • 0019886915 scopus 로고
    • Synthesis of brominated heptanones and bromoform by a bromoperoxidase of marine origin
    • Beissner, R.S., Guilford, W.J., Coates, R.M., and Hager, L.P. 1981. Synthesis of brominated heptanones and bromoform by a bromoperoxidase of marine origin. Biochemistry. 20:3724-3731.
    • (1981) Biochemistry , vol.20 , pp. 3724-3731
    • Beissner, R.S.1    Guilford, W.J.2    Coates, R.M.3    Hager, L.P.4
  • 52
    • 0029089519 scopus 로고
    • Biosynthesis of brominated tyrosine metabolites by Aplysina fistularis
    • Carney, J.R., and Rinehart, K.L. 1995. Biosynthesis of brominated tyrosine metabolites by Aplysina fistularis. J. Nat. Prod. 58:971-985.
    • (1995) J. Nat. Prod. , vol.58 , pp. 971-985
    • Carney, J.R.1    Rinehart, K.L.2
  • 53
    • 0028222730 scopus 로고
    • 3-antagonist from the marine sponge Verongula gigantea
    • 3-antagonist from the marine sponge Verongula gigantea. J. Nat. Prod. 57:175-177.
    • (1994) J. Nat. Prod. , vol.57 , pp. 175-177
    • Mierezwa, R.1
  • 54
    • 0026762718 scopus 로고
    • Fistularin 3 and 11-ketofistularin 3. Feline leukemia virus active bromotyrosine metabolites from the marine sponge Aplysina archeri
    • Gunaseketa, S.P., and Cross, S.S. 1992. Fistularin 3 and 11-ketofistularin 3. Feline leukemia virus active bromotyrosine metabolites from the marine sponge Aplysina archeri. J. Nat. Prod. 55:509-512.
    • (1992) J. Nat. Prod. , vol.55 , pp. 509-512
    • Gunaseketa, S.P.1    Cross, S.S.2
  • 55
    • 0012007699 scopus 로고
    • 2Br and some N-brominated ammo acids
    • R.L. Jolley, W.A. Brungs, R.B. Cumming, and V.A. Jacobs, editors. Ann Arbor Science Publishers Inc. Ann Arbor, Michigan, USA
    • 2Br and some N-brominated ammo acids. In Water chlorination: environmental impact and health effects. R.L. Jolley, W.A. Brungs, R.B. Cumming, and V.A. Jacobs, editors. Ann Arbor Science Publishers Inc. Ann Arbor, Michigan, USA. 171-181.
    • (1980) Water Chlorination: Environmental Impact and Health Effects , pp. 171-181
    • Wajon, J.E.1    Morris, J.C.2
  • 56
    • 0028801505 scopus 로고
    • Oxidation of bromide by the human leukocyte enzymes myeloperoxidase and eosinophil peroxidase. Formation of bromamines
    • Thomas, E.L., Bozeman, P.M. Jefferson, M.M., and King, C.C. 1995. Oxidation of bromide by the human leukocyte enzymes myeloperoxidase and eosinophil peroxidase. Formation of bromamines. J. Biol. Chem. 270:2906-2913.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2906-2913
    • Thomas, E.L.1    Bozeman, P.M.2    Jefferson, M.M.3    King, C.C.4
  • 57
    • 0343920015 scopus 로고    scopus 로고
    • Rapid loss of superoxide dismutase activity during antigen-induced asthmatic response
    • Comhair, S.A., Bhathena, P., Dweik, R.A., Kavuru, M.S., and Erzurum, S.C. 2000. Rapid loss of superoxide dismutase activity during antigen-induced asthmatic response. Lancet. 355:624.
    • (2000) Lancet , vol.355 , pp. 624
    • Comhair, S.A.1    Bhathena, P.2    Dweik, R.A.3    Kavuru, M.S.4    Erzurum, S.C.5
  • 58
    • 0032570808 scopus 로고    scopus 로고
    • Human neutrophils employ the myeloperoxidase-hydrogen peroxide-chloride system to oxidize alpha-amino acids to a family of reactive aldehydes. Mechanistic studies identifying labile intermediates along the reaction pathway
    • Hazen, S.L., d'Avignon, A., Anderson, M.M., Hsu, F.F., and Heinecke, J.W. 1998. Human neutrophils employ the myeloperoxidase-hydrogen peroxide-chloride system to oxidize alpha-amino acids to a family of reactive aldehydes. Mechanistic studies identifying labile intermediates along the reaction pathway. J. Biol. Chem 273:4997-5005.
    • (1998) J. Biol. Chem , vol.273 , pp. 4997-5005
    • Hazen, S.L.1    D'Avignon, A.2    Anderson, M.M.3    Hsu, F.F.4    Heinecke, J.W.5
  • 60
    • 0024450447 scopus 로고
    • Bromine derivatives of amino acids as intermediates in the peroxidase-catalyzed formation of singlet oxygen
    • Kanofsky, J.R. 1989. Bromine derivatives of amino acids as intermediates in the peroxidase-catalyzed formation of singlet oxygen. Arch. Biochem. Biophys. 274:229-234.
    • (1989) Arch. Biochem. Biophys. , vol.274 , pp. 229-234
    • Kanofsky, J.R.1
  • 61
    • 0029887638 scopus 로고    scopus 로고
    • Effect of eosmophil peroxidase on airway epithelial permeability in the guinea pig
    • Brottman, G.M., Regelmann, W.E., Slungaard, A., and Wangensteen, O.D. 1996. Effect of eosmophil peroxidase on airway epithelial permeability in the guinea pig. Pediatr. Pulmonol. 21:159-166.
    • (1996) Pediatr. Pulmonol. , vol.21 , pp. 159-166
    • Brottman, G.M.1    Regelmann, W.E.2    Slungaard, A.3    Wangensteen, O.D.4
  • 62
    • 0027403008 scopus 로고
    • Eosinophils increase lung microvascular permeability via the peroxidase-hydrogen peroxide-halide system. Bronchoconstriction and vasoconstriction unaffected by eosinophil peroxidase inhibition
    • Yoshikawa, S., Kayes, S.G., and Parker, J.C 1993. Eosinophils increase lung microvascular permeability via the peroxidase-hydrogen peroxide-halide system. Bronchoconstriction and vasoconstriction unaffected by eosinophil peroxidase inhibition. Am. Rev. Respir. Dis. 147:914-920.
    • (1993) Am. Rev. Respir. Dis. , vol.147 , pp. 914-920
    • Yoshikawa, S.1    Kayes, S.G.2    Parker, J.C.3
  • 63
    • 0028351332 scopus 로고
    • Role of eosinophil activation in the bronchial reactivity of allergic guinea pigs
    • Pretolani, M., et al. 1994. Role of eosinophil activation in the bronchial reactivity of allergic guinea pigs. Am. J. Respir. Crit. Care Med. 149:1167-1174.
    • (1994) Am. J. Respir. Crit. Care Med. , vol.149 , pp. 1167-1174
    • Pretolani, M.1
  • 64
    • 0027371716 scopus 로고
    • Effects of activated eosinophils cultured from human umbilical cord blood on guinea pig trachealis
    • Hamann, K.J., et al. 1993. Effects of activated eosinophils cultured from human umbilical cord blood on guinea pig trachealis. Am. J. Physiol. 265:L301-L307.
    • (1993) Am. J. Physiol. , vol.265
    • Hamann, K.J.1
  • 65
    • 0027933215 scopus 로고
    • Eosinophil granule proteins increase microvascular macromolecular transport in the hamster cheek pouch
    • Minnicozzi, M., Duran, W.N., Gleich, G.J., and Egan, R.W. 1994. Eosinophil granule proteins increase microvascular macromolecular transport in the hamster cheek pouch. J. Immunol. 153:2664-2670.
    • (1994) J. Immunol. , vol.153 , pp. 2664-2670
    • Minnicozzi, M.1    Duran, W.N.2    Gleich, G.J.3    Egan, R.W.4
  • 66
    • 0025828705 scopus 로고
    • Human eosinophil major basic protein induces airway constriction and airway hyperresponsiveness in primates
    • Gundel, R.H., Letts, L.G., and Gleich, G.J. 1991. Human eosinophil major basic protein induces airway constriction and airway hyperresponsiveness in primates. J. Clin. Invest. 87:1470-1473.
    • (1991) J. Clin. Invest. , vol.87 , pp. 1470-1473
    • Gundel, R.H.1    Letts, L.G.2    Gleich, G.J.3
  • 67
    • 0016422847 scopus 로고
    • Synthesis and microbiological activities of some monohalogenated analogs of tyrosine
    • McCord, T.J., et al. 1975. Synthesis and microbiological activities of some monohalogenated analogs of tyrosine. J. Med. Chem. 18:26-29.
    • (1975) J. Med. Chem. , vol.18 , pp. 26-29
    • McCord, T.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.