메뉴 건너뛰기




Volumn 24, Issue 4, 1989, Pages 271-328

Leukocytic oxygen activation and microbicidal oxidative toxin

Author keywords

[No Author keywords available]

Indexed keywords

HYPOCHLOROUS ACID; OXIDOREDUCTASE; OXYGEN; TOXIN;

EID: 0024337245     PISSN: 10409238     EISSN: None     Source Type: Journal    
DOI: 10.3109/10409238909082555     Document Type: Article
Times cited : (220)

References (375)
  • 2
    • 0021739838 scopus 로고
    • Oxidants from phagocytes: agents of defense and destructio
    • (1984) Blood , vol.64 , pp. 959
    • Babior, B.M.1
  • 9
    • 84966100812 scopus 로고
    • Centennial of the rise of cellular immunology: Metchnikoff's discovery at Messin
    • (1982) A.S.M. News , vol.48 , pp. 558
    • Bibel, D.J.1
  • 17
    • 0001861915 scopus 로고
    • The fate of bacteria within phagocytic cells. I. The degradation of isotopically labeled bacteria by polymorphonuclear leukocytes and macrophage
    • (1968) J. Exp. Med. , vol.117 , pp. 27
    • Cohn, Z.A.1
  • 22
    • 0018185563 scopus 로고
    • Different arrangements of phagolysosome membranes which depend upon the particles phagocytized. Observations with markers of the two sides of plasma membrane
    • (1977) Exp. Cell Res. , vol.111 , pp. 437
    • Rikihisa, Y.1    Mizuno, D.2
  • 23
    • 0017356323 scopus 로고
    • Membrane asymmetry. The nature of membrane asymmetry provides clues to the puzzle of how membranes are assemble
    • (1977) Science , vol.195 , pp. 743
    • Rothman, J.E.1    Lenard, J.2
  • 27
    • 0014962562 scopus 로고
    • Quantitative aspects of the production of superoxide anion radical by milk xanthine oxidas
    • (1970) J. Biol. Chem. , vol.245 , pp. 4053
    • Fridovich, I.1
  • 30
    • 0020816982 scopus 로고
    • Activation of guinea pig polymorphonuclear leukocytes with soluble stimulators leads to nonrandom distribution of NADPH oxidase in the plasma membran
    • (1983) J. Biochem. , vol.94 , pp. 655
    • Tsunawaki, S.1    Kaneda, M.2    Kakinuma, K.3
  • 44
  • 59
  • 62
    • 0018643333 scopus 로고
    • The subcellular distribution and some properties of the cytochrome b component of the microbicidal oxidase system of human neutrophil
    • (1979) Biochem. J. , vol.182 , pp. 181
    • Segal, A.W.1    Jones, O.T.G.2
  • 67
    • 0023175462 scopus 로고
    • -245 subunits from neutrophils in X-limited chronic granulomatous diseas
    • (1987) Nature , vol.326 , pp. 88
    • Segal, A.W.1
  • 90
    • 0019887886 scopus 로고
    • Structural implication of heme-linked ionization of horseradish peroxidase probed by the Fe-histidine stretching Raman lin
    • (1981) J. Biol. Chem. , vol.256 , pp. 3969
    • Teraoka, J.1    Kitagawa, T.2
  • 99
    • 0020537758 scopus 로고
    • Ubiquinone content and respiratory burst activity of latex-filled phagolysosomes isolated from human neutrophils and evidence for the probable involvement of a third granul
    • (1983) J. Biol. Chem. , vol.258 , pp. 5363
    • Crawford, D.R.1    Schneider, D.L.2
  • 100
    • 0021165890 scopus 로고
    • Subcellular localization of cytochrome b and ubiquinone in a tertiary granule of resting human neutrophils and evidence for a proton pump ATPas
    • (1984) J. Biol. Chem. , vol.259 , pp. 7143
    • Mollinedo, F.1    Schneider, D.L.2
  • 104
    • 84965985742 scopus 로고    scopus 로고
    • Hydride versus electron transfer in the oxidation of NADH model compound
    • Oxidases and Related Redox Systems, Proc. 4th Int. Symp., Eds. T.E. King, H.S. Mason, M. Morrison. Alan R. Liss, New York, in press
    • Powell, M.F.1    Bruice, T.C.2
  • 108
  • 120
    • 0019868223 scopus 로고
    • Intrinsic dichlorophenolindophenol reductase activity associated with the superoxide-generating oxidoreductase of human granulocyte
    • (1981) Biochemistry , vol.20 , pp. 7483
    • Green, T.R.1    Schaefer, R.E.2
  • 125
    • 0023148367 scopus 로고
    • Protein kinase C and the activation of the human neutrophil NADPH-oxidas
    • (1987) Blood , vol.69 , pp. 711
    • Tauber, A.I.1
  • 128
    • 0022828952 scopus 로고
    • Further evidence for the involvement of a phosphoprotein in the respiratory burst oxidase of human neutrophil
    • (1986) Biochem. J. , vol.239 , pp. 723
    • Heyworth, P.G.1    Segal, A.W.2
  • 133
    • 84965230905 scopus 로고
    • On the use of certain antiseptic substances in the treatment of infected wound
    • (1915) Br. Med. J. , vol.2 , pp. 318
    • Dakin, H.D.1
  • 135
    • 0020363971 scopus 로고
    • Oxidative inactivation of Escherichia coli by hypochlorous acid. Rates and differentiation of respiratory from other reaction site
    • (1982) FEBS Lett. , vol.144 , pp. 157
    • Albrich, J.M.1    Hurst, J.K.2
  • 139
    • 0018386333 scopus 로고
    • Myeloperoxidase, hydrogen peroxide, chloride antimicrobial system: nitrogen-chlorine derivatives of bacterial components in bactericidal action agains
    • (1979) Escherichia coli, Infect. Immun. , vol.23 , pp. 522
    • Thomas, E.L.1
  • 149
    • 0014559249 scopus 로고
    • Leukocyte myeloperoxidase deficiency and disseminated candidiasis: the role of myeloperoxidase in resistance to Candida infectio
    • (1969) J. Clin. Invest. , vol.48 , pp. 1478
    • Lehrer, R.I.1    Cline, M.J.2
  • 154
    • 0023250939 scopus 로고
    • Fungicidal activity of human neutrophils and monocytes on dermatophyte fungi, Trichophyton quinckanum and Trichophyton rubru
    • (1987) Immunobiology , vol.61 , pp. 289
    • Calderon, R.A.1    Hay, R.J.2
  • 159
    • 0022243379 scopus 로고
    • Spectroscopic, ligand binding, and enzymatic properties of the spleen green hemoprotei
    • (1985) J. Biol. Chem. , vol.260 , pp. 11688
    • Ikeda-Saito, M.1
  • 164
    • 0021359110 scopus 로고
    • Influence of yeast mannan on release of myeloperoxidase by human neutrophils: determination of structural features of mannan required for formation of myelo-peroxidase-mannan-neutrophil complexe
    • (1984) Infect. Immun. , vol.43 , pp. 467
    • Wright, C.D.1    Bowie, J.U.2    Nelson, R.D.3
  • 171
    • 0018821048 scopus 로고
    • Myeloperoxidase of the leukocyte of normal blood. Nature of the prosthetic grou
    • (1980) J. Biochem. , vol.87 , pp. 379
    • Odajima, T.1
  • 177
    • 0022513977 scopus 로고
    • On the analogy in the stmcture of the spleen green heme protein and granulocyte myeloperoxidas
    • (1986) FEBS Lett. , vol.202 , pp. 245
    • Ideka-Saito, M.1
  • 189
    • 84966084572 scopus 로고
    • The role of peroxide in the functional mechanism of myeloperoxidas
    • Oxidases and Related Redox Systems. Proc. 3rd Int. Symp., Eds. T.E. King, H.S. Mason, M. Morrison. Pergamon Press, Oxford
    • (1982) , pp. 717
    • Harrison, J.E.1
  • 196
  • 213
    • 0008406197 scopus 로고
    • Reversible one-electron oxidation of metallochlorines and comparison of the octaethyl-porphine and octaethylchlorine ligand
    • (1970) Z. Naturforsch , vol.25b , pp. 255
    • Fuhrhop, J.H.1
  • 225
    • 0000752259 scopus 로고
    • Kinetic studies on the chloramines. I. The rates of formation of monochloramine, N-chloromethylamine and N-chlorodimethylamin
    • (1949) J. Am. Chem. Soc. , vol.71 , pp. 1664
    • Weil, I.1    Morris, J.C.2
  • 238
    • 0022658552 scopus 로고
    • Neutrophil-mediated solubilization of the subendothelial matrix: oxidative and nonoxidative mechanisms of proteolysis used by normal and chronic granulomatous disease phagocyte
    • (1986) J. Immunol. , vol.136 , pp. 636
    • Weiss, S.J.1    Curnutte, J.T.2    Regiani, S.3
  • 252
    • 0014836733 scopus 로고
    • Metabolic control and intracellular pH during phagocytosis of polymorphonuclear leucocyte
    • (1970) J. Biochem. , vol.68 , pp. 177
    • Kakinuma, K.1
  • 260
    • 0019460785 scopus 로고
    • Mechanism of the bactericidal action of myeloperoxidase: increased permeability of the Escherichiu coli cell envelop
    • (1981) Infect. Immun. , vol.31 , pp. 11
    • Sips, H.J.1    Hamers, M.N.2
  • 285
    • 0017317997 scopus 로고
    • Reactions involving singlet oxygen and the superoxide anio
    • (1976) Nature , vol.262 , pp. 420
    • Koppenol, W.H.1
  • 288
    • 0018123211 scopus 로고
    • Superoxide-dependent formation of hydroxyl radicals in the presence of iron chelates: is it a mechanism for hydroxyl radical production in biochemical systems?
    • (1978) FEBS Lett. , vol.96 , pp. 238
    • Halliwell, B.1
  • 290
    • 33947291445 scopus 로고
    • Physical and chemical properties of singlet molecular oxyge
    • (1971) Chem. Rev. , vol.71 , pp. 395
    • Kearns, D.R.1
  • 292
  • 293
    • 49149143821 scopus 로고
    • g) molecular oxygen in chemically generated and dye-photosensitized liquid solutions at mom temperatur
    • (1980) Chem. Phys. Lett. , vol.72 , pp. 112
    • Khan, A.U.1
  • 294
    • 0021111937 scopus 로고
    • Singlet oxygen production by lactoperoxidase, evidence from 1270-nm chemiluminescenc
    • (1983) J. Biol. Chem. , vol.258 , pp. 5991
    • Kanofsky, J.R.1
  • 318
  • 323
    • 0023297560 scopus 로고
    • The reaction between ferrous polyaminocarboxylate complexes and hydrogen peroxide: an investigation of reaction intermediates by stopped flow spectrophotometr
    • (1987) J. Inorg. Biochem. , vol.29 , pp. 199
    • Rush, J.D.1    Koppenol, W.D.2
  • 337
    • 0020972548 scopus 로고
    • Thermodynamic binding constants of the zinc-human serum transfenin comple
    • (1983) Biochemistry , vol.22 , pp. 3920
    • Harris, W.R.1
  • 339
  • 340
    • 0023144940 scopus 로고
    • Superoxide-dependent and ascorbatedependent formation of hydroxyl radicals from hydrogen peroxide in the presence of iron. Are lactofemn and transfemn promoters of hydroxyl-radical generation?
    • (1987) Biochem. J. , vol.241 , pp. 273
    • Arouma, O.I.1    Halliwell, B.2
  • 342
    • 0022469346 scopus 로고
    • Iron promoters of the Fenton reaction and lipid peroxidation can be released from haemoglobin by peroxide
    • (1986) FEBS Lett. , vol.201 , pp. 291
    • Gutteridge, J.M.C.1
  • 346
    • 0023200080 scopus 로고
    • Lactofemn effects on phagocytic cell function. II. The presence of iron is required for the lactofemn molecule to stimulate intracellular killing by macrophages but not to enhance the uptake of particles and microorganism
    • (1987) J. Immunol. , vol.139 , pp. 1647
    • Lima, M.F.1    Kierszenbaum, F.2
  • 355
    • 0021100140 scopus 로고
    • Oxidative modification of glutamine synthetase. II. Characterization of the ascorbate model syste
    • (1983) J. Biol. Chem. , vol.258 , pp. 11828
    • Levine, R.L.1
  • 356
    • 0023338482 scopus 로고
    • Ferrous-salt-promoted damage to deoxyribose and benzoate. The increased effectiveness of hydroxyl-radical scavengers in the presence of EDT
    • (1987) Biochem. J. , vol.243 , pp. 709
    • Gutteridge, J.M.C.1
  • 363
    • 0345513702 scopus 로고
    • Paraquat toxicity is mediated by iron or copper: the target organelle in E. coli is the cytoplasmic membran
    • Superoxide and Superoxide Dismutase in Chemistry, Biology and Medicine, Proc. 4th Int. Conf., Ed. G. Rotilio. Elsevier, Amsterdam
    • (1986) , pp. 349
    • Kohen, R.1    Korbashi, P.2    Chevion, M.3
  • 367
    • 0022486111 scopus 로고
    • Myeloperoxidase as an effective inhibitor of hydroxyl radical production. Implications for the oxidative reactions of neutrophil
    • (1986) J. Clin. Invest. , vol.78 , pp. 545
    • Winterbourn, C.C.1
  • 370
    • 0018801379 scopus 로고
    • The oxidation-reduction potentials of compound I/compound II and compound II/ferric couples of horseradish peroxidases A. and
    • (1979) J. Biol. Chem. , vol.254 , pp. 9101
    • Hayashi, Y.1    Yamazpld, I.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.