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Volumn 23, Issue , 2005, Pages 197-223

How neutrophils kill microbes

Author keywords

Bacteria; Enzyme; Free radical; Ion channel; Microbicidal; Protease

Indexed keywords

CATHEPSIN G; FREE RADICAL; GELATINASE; GLYCOPROTEIN GP 91; HALIDE; ION CHANNEL; MYELOPEROXIDASE; NITRIC OXIDE; POTASSIUM CHANNEL; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE 2;

EID: 17644377258     PISSN: 07320582     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.immunol.23.021704.115653     Document Type: Review
Times cited : (1416)

References (126)
  • 1
    • 18244401270 scopus 로고
    • The influence of phagocytosis on the intracellular distribution of granule-associated components of polymorphonuclear leucocytes
    • Cohn ZA, Hirsch JG. 1960. The influence of phagocytosis on the intracellular distribution of granule-associated components of polymorphonuclear leucocytes. J. Exp. Med. 112:1015-22
    • (1960) J. Exp. Med. , vol.112 , pp. 1015-1022
    • Cohn, Z.A.1    Hirsch, J.G.2
  • 3
    • 0014124339 scopus 로고
    • Studies of the metabolic activity of leukocytes from patients with a genetic abnormality of phagocyte function
    • Holmes B, Page AR, Good RA. 1967. Studies of the metabolic activity of leukocytes from patients with a genetic abnormality of phagocyte function. J. Clin. Invest. 46:1422-32
    • (1967) J. Clin. Invest. , vol.46 , pp. 1422-1432
    • Holmes, B.1    Page, A.R.2    Good, R.A.3
  • 4
    • 0014692442 scopus 로고
    • Iodination defect in the leukocytes of a patient with chronic granulomatous disease of childhood
    • Klebanoff SJ, White LR. 1969. Iodination defect in the leukocytes of a patient with chronic granulomatous disease of childhood. N. Engl. J. Med. 280:460-66
    • (1969) N. Engl. J. Med. , vol.280 , pp. 460-466
    • Klebanoff, S.J.1    White, L.R.2
  • 5
    • 0015596284 scopus 로고
    • Biological defence mechanisms: The production by leukocytes of superoxide, a potential bactericidal agent
    • Babior BM, Kipnes RS, Curnutte JT. 1973. Biological defence mechanisms: the production by leukocytes of superoxide, a potential bactericidal agent. J. Clin. Invest. 52:741-44
    • (1973) J. Clin. Invest. , vol.52 , pp. 741-744
    • Babior, B.M.1    Kipnes, R.S.2    Curnutte, J.T.3
  • 7
    • 0141963140 scopus 로고    scopus 로고
    • Infections in patients with cancer undergoing chemotherapy: Aetiology, prevention, and treatment
    • Vento S, Cainelli F. 2003. Infections in patients with cancer undergoing chemotherapy: aetiology, prevention, and treatment. Lancet Oncol. 4:595-604
    • (2003) Lancet Oncol. , vol.4 , pp. 595-604
    • Vento, S.1    Cainelli, F.2
  • 9
    • 0020467279 scopus 로고
    • The action of cells from patients with chronic granulomatous disease on Staphylococcus aureus
    • Segal AW, Harper AM, Garcia RC, Merzbach D. 1982. The action of cells from patients with chronic granulomatous disease on Staphylococcus aureus. J. Med. Microbiol. 15:441-49
    • (1982) J. Med. Microbiol. , vol.15 , pp. 441-449
    • Segal, A.W.1    Harper, A.M.2    Garcia, R.C.3    Merzbach, D.4
  • 11
    • 0015975763 scopus 로고
    • Bactericidal activity of aerobic and anaerobic polymorphonuclear neutrophils
    • Mandell GL. 1974. Bactericidal activity of aerobic and anaerobic polymorphonuclear neutrophils. Infect. Immun. 9:337-41
    • (1974) Infect. Immun. , vol.9 , pp. 337-341
    • Mandell, G.L.1
  • 12
    • 3042527868 scopus 로고    scopus 로고
    • The NADPH oxidase of professional phagocytes-prototype of the NOX electron transport chain systems
    • Cross AR, Segal AW. 2004. The NADPH oxidase of professional phagocytes-prototype of the NOX electron transport chain systems. Biochem. Biophysica Acta-Bioenergetics 1657:1-22
    • (2004) Biochem. Biophysica Acta-Bioenergetics , vol.1657 , pp. 1-22
    • Cross, A.R.1    Segal, A.W.2
  • 13
    • 0036710445 scopus 로고    scopus 로고
    • The superoxide-generating NADPH oxidase: Structural aspects and activation mechanism
    • Vignais PV. 2002. The superoxide-generating NADPH oxidase: structural aspects and activation mechanism. Cell. Mol. Life Sci. 59:1428-59
    • (2002) Cell. Mol. Life Sci. , vol.59 , pp. 1428-1459
    • Vignais, P.V.1
  • 16
    • 0019815612 scopus 로고
    • A variant of chronic granulomatous disease: Deficient oxidative metabolism due to a low-affinity NADPH oxidase
    • Lew PD, Southwick FS, Stossel TP, Whitin JC, Simons E, Cohen HJ. 1981. A variant of chronic granulomatous disease: deficient oxidative metabolism due to a low-affinity NADPH oxidase. N. Engl. J. Med. 305:1329-33
    • (1981) N. Engl. J. Med. , vol.305 , pp. 1329-1333
    • Lew, P.D.1    Southwick, F.S.2    Stossel, T.P.3    Whitin, J.C.4    Simons, E.5    Cohen, H.J.6
  • 17
    • 0019191385 scopus 로고
    • Kinetics of fusion of the cytoplasmic granules with phagocytic vacuoles in human polymorphonuclear leukocytes. Biochemical and morphological studies
    • Segal AW, Dorling J, Coade S. 1980. Kinetics of fusion of the cytoplasmic granules with phagocytic vacuoles in human polymorphonuclear leukocytes. Biochemical and morphological studies. J. Cell Biol. 85:42-59
    • (1980) J. Cell Biol. , vol.85 , pp. 42-59
    • Segal, A.W.1    Dorling, J.2    Coade, S.3
  • 18
    • 0022457012 scopus 로고
    • Superoxide production by polymorphonuclear leukocytes. A cytochemical approach
    • Briggs RT, Robinson JM, Karnovsky ML, Karnovsky MJ. 1986. Superoxide production by polymorphonuclear leukocytes. A cytochemical approach. Histochemistry 84:371-78
    • (1986) Histochemistry , vol.84 , pp. 371-378
    • Briggs, R.T.1    Robinson, J.M.2    Karnovsky, M.L.3    Karnovsky, M.J.4
  • 19
    • 0018425538 scopus 로고
    • Production of superoxide by neutrophils: A reappraisal
    • Segal AW, Meshulam T. 1979. Production of superoxide by neutrophils: a reappraisal. FEBS Lett. 100:27-32
    • (1979) FEBS Lett. , vol.100 , pp. 27-32
    • Segal, A.W.1    Meshulam, T.2
  • 20
    • 0026628863 scopus 로고
    • Superoxide generation by the human polymorphonuclear leukocyte in response to latex beads
    • Thomas MJ, Hedrick CC, Smith S, Pang J, Jerome WG, et al. 1992. Superoxide generation by the human polymorphonuclear leukocyte in response to latex beads. J. Leukoc. Biol. 51:591-96
    • (1992) J. Leukoc. Biol. , vol.51 , pp. 591-596
    • Thomas, M.J.1    Hedrick, C.C.2    Smith, S.3    Pang, J.4    Jerome, W.G.5
  • 21
    • 0014691242 scopus 로고
    • Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein)
    • McCord JM, Fridovich I. 1969. Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein). J. Biol. Chem. 244:6049-55
    • (1969) J. Biol. Chem. , vol.244 , pp. 6049-6055
    • McCord, J.M.1    Fridovich, I.2
  • 22
    • 0032213375 scopus 로고    scopus 로고
    • Inside the neutrophil phagosome: Oxidants, myeloperoxidase, and bacterial killing
    • Hampton MB, Kettle AJ, Winterbourn CC. 1998. Inside the neutrophil phagosome: oxidants, myeloperoxidase, and bacterial killing. Blood 92:3007-17
    • (1998) Blood , vol.92 , pp. 3007-3017
    • Hampton, M.B.1    Kettle, A.J.2    Winterbourn, C.C.3
  • 24
    • 0016590865 scopus 로고
    • Biological defense mechanisms. Evidence for the participation of superoxide in bacterial killing by xanthine oxidase
    • Babior BM, Curnutte JT, Kipnes RS. 1975. Biological defense mechanisms. Evidence for the participation of superoxide in bacterial killing by xanthine oxidase. J. Lab. Clin. Med. 85:235-44
    • (1975) J. Lab. Clin. Med. , vol.85 , pp. 235-244
    • Babior, B.M.1    Curnutte, J.T.2    Kipnes, R.S.3
  • 25
    • 0018777193 scopus 로고
    • Bactericidal activity of a superoxide anion-generating system. A model for the polymorphonuclear leukocyte
    • Rosen H, Klebanoff SJ. 1979. Bactericidal activity of a superoxide anion-generating system. A model for the polymorphonuclear leukocyte. J. Exp. Med. 149:27-39
    • (1979) J. Exp. Med. , vol.149 , pp. 27-39
    • Rosen, H.1    Klebanoff, S.J.2
  • 26
    • 0019474039 scopus 로고
    • Lactoferrin enhances hydroxyl radical production by human neutrophils, neutrophil paniculate fractions, and an enzymatic generating system
    • Ambruso DR, Johnston RB Jr. 1981. Lactoferrin enhances hydroxyl radical production by human neutrophils, neutrophil paniculate fractions, and an enzymatic generating system. J. Clin. Invest. 67:352-60
    • (1981) J. Clin. Invest. , vol.67 , pp. 352-360
    • Ambruso, D.R.1    Johnston Jr., R.B.2
  • 27
    • 0019252015 scopus 로고
    • Role of hydroxyl radical in polymorphonuclear leukocyte-mediated bactericidal activity
    • Rosen H. 1980. Role of hydroxyl radical in polymorphonuclear leukocyte-mediated bactericidal activity. Agents Actions Suppl. 7:180-84
    • (1980) Agents Actions Suppl. , vol.7 , pp. 180-184
    • Rosen, H.1
  • 28
    • 0026054083 scopus 로고
    • Application of spin trapping to human phagocytic cells: Insight into conditions for formation and limitation of hydroxyl radical
    • Cohen MS, Britigan BE, Pou S, Rosen GM. 1991. Application of spin trapping to human phagocytic cells: insight into conditions for formation and limitation of hydroxyl radical. Free Radic. Res. Commun. 12-13(Pt. 1):17-25
    • (1991) Free Radic. Res. Commun. , vol.12-13 , Issue.PART 1 , pp. 17-25
    • Cohen, M.S.1    Britigan, B.E.2    Pou, S.3    Rosen, G.M.4
  • 29
    • 0019774854 scopus 로고
    • Inhibition of lipid peroxidation by the iron-binding protein lactoferrin
    • Gutteridge JM, Paterson SK, Segal AW, Halliwell B. 1981. Inhibition of lipid peroxidation by the iron-binding protein lactoferrin. Biochem. J. 199:259-61
    • (1981) Biochem. J. , vol.199 , pp. 259-261
    • Gutteridge, J.M.1    Paterson, S.K.2    Segal, A.W.3    Halliwell, B.4
  • 30
    • 0020681037 scopus 로고
    • Lactoferrin-catalysed hydroxyl radical production. Additional requirement for a chelating agent
    • Winterbourn CC. 1983. Lactoferrin-catalysed hydroxyl radical production. Additional requirement for a chelating agent. Biochem. J. 210:15-19
    • (1983) Biochem. J. , vol.210 , pp. 15-19
    • Winterbourn, C.C.1
  • 31
    • 0024828694 scopus 로고
    • Neutrophil degranulation inhibits potential hydroxyl-radical formation. Relative impact of myeloperoxidase and lactoferrin release on hydroxyl-radical production by iron-supplemented neutrophils assessed by spin-trapping techniques
    • Britigan BE, Hassett DJ, Rosen GM, Hamill DR, Cohen MS. 1989. Neutrophil degranulation inhibits potential hydroxyl-radical formation. Relative impact of myeloperoxidase and lactoferrin release on hydroxyl-radical production by iron-supplemented neutrophils assessed by spin-trapping techniques. Biochem. J. 264:447-55
    • (1989) Biochem. J. , vol.264 , pp. 447-455
    • Britigan, B.E.1    Hassett, D.J.2    Rosen, G.M.3    Hamill, D.R.4    Cohen, M.S.5
  • 33
    • 0041766196 scopus 로고    scopus 로고
    • The many faces of vitamin B12: Catalysis by cobalamin-dependent enzymes
    • Banerjee R, Ragsdale SW. 2003. The many faces of vitamin B12: catalysis by cobalamin-dependent enzymes. Annu. Rev. Biochem. 72:209-47
    • (2003) Annu. Rev. Biochem. , vol.72 , pp. 209-247
    • Banerjee, R.1    Ragsdale, S.W.2
  • 34
    • 0037073888 scopus 로고    scopus 로고
    • Evidence for antibody-catalyzed ozone formation in bacterial killing and inflammation
    • Wentworth P Jr, McDunn JE, Wentworth AD, Takeuchi C, Nieva J, et al. 2002. Evidence for antibody-catalyzed ozone formation in bacterial killing and inflammation. Science 298:2195-99
    • (2002) Science , vol.298 , pp. 2195-2199
    • Wentworth Jr., P.1    McDunn, J.E.2    Wentworth, A.D.3    Takeuchi, C.4    Nieva, J.5
  • 36
    • 2442611988 scopus 로고    scopus 로고
    • Superoxide converts indigo carmine to isatin sulfonic acid: Implications for the hypothesis that neutrophils produce ozone
    • Kettle AJ, Clark BM, Winterbourn CC. 2004. Superoxide converts indigo carmine to isatin sulfonic acid: implications for the hypothesis that neutrophils produce ozone. J. Biol. Chem. 279:18521-25
    • (2004) J. Biol. Chem. , vol.279 , pp. 18521-18525
    • Kettle, A.J.1    Clark, B.M.2    Winterbourn, C.C.3
  • 37
    • 0034697020 scopus 로고    scopus 로고
    • X-ray crystal structure and characterization of halide-binding sites of human myeloperoxidase at 1.8 Å resolution
    • Fiedler TJ, Davey CA, Fenna RE. 2000. X-ray crystal structure and characterization of halide-binding sites of human myeloperoxidase at 1.8 Å resolution. J. Biol. Chem. 275:11964-71
    • (2000) J. Biol. Chem. , vol.275 , pp. 11964-11971
    • Fiedler, T.J.1    Davey, C.A.2    Fenna, R.E.3
  • 38
    • 0014292067 scopus 로고
    • Myeloperoxidase-halide-hydrogen peroxide antibacterial system
    • Klebanoff SJ. 1968. Myeloperoxidase-halide-hydrogen peroxide antibacterial system. J. Bacteriol. 95:2131-38
    • (1968) J. Bacteriol. , vol.95 , pp. 2131-2138
    • Klebanoff, S.J.1
  • 39
    • 0016746318 scopus 로고
    • Antimicrobial mechanisms in neutrophilic polymorphonuclear leukocytes
    • Klebanoff SJ. 1975. Antimicrobial mechanisms in neutrophilic polymorphonuclear leukocytes. Semin. Hematol. 12:117-42
    • (1975) Semin. Hematol. , vol.12 , pp. 117-142
    • Klebanoff, S.J.1
  • 40
    • 0014167106 scopus 로고
    • Iodination of bacteria: A bactericidal mechanism
    • Klebanoff SJ. 1967. Iodination of bacteria: a bactericidal mechanism. J. Exp. Med. 126:1063-78
    • (1967) J. Exp. Med. , vol.126 , pp. 1063-1078
    • Klebanoff, S.J.1
  • 41
    • 0029846572 scopus 로고    scopus 로고
    • Involvement of superoxide and myeloperoxidase in oxygen-dependent killing of Staphylococcus aureus by neutrophils
    • Hampton MB, Kettle AJ, Winterbourn CC. 1996. Involvement of superoxide and myeloperoxidase in oxygen-dependent killing of Staphylococcus aureus by neutrophils. Infect. Immun. 64:3512-17
    • (1996) Infect. Immun. , vol.64 , pp. 3512-3517
    • Hampton, M.B.1    Kettle, A.J.2    Winterbourn, C.C.3
  • 42
    • 0014664980 scopus 로고
    • Defective bactericidal activity in myeloperoxidase-deficient human neutrophils
    • Lehrer RI, Hanifin J, Cline MJ. 1969. Defective bactericidal activity in myeloperoxidase-deficient human neutrophils. Nature 223:78-79
    • (1969) Nature , vol.223 , pp. 78-79
    • Lehrer, R.I.1    Hanifin, J.2    Cline, M.J.3
  • 43
    • 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, et al. 2000. Differential host susceptibility to pulmonary infections with bacteria and fungi in mice deficient in myeloperoxidase. J. Infect. Dis. 182:1276-79
    • (2000) J. Infect. Dis. , vol.182 , pp. 1276-1279
    • Aratani, Y.1    Kura, F.2    Watanabe, H.3    Akagawa, H.4    Takano, Y.5
  • 44
    • 0035834065 scopus 로고    scopus 로고
    • Neutrophils employ the myeloperoxidase system to generate antimicrobial brominating and chlorinating oxidants during sepsis
    • Gaut JP, Yeh GC, Tran HD, Byun J, Henderson JP, et al. 2001. Neutrophils employ the myeloperoxidase system to generate antimicrobial brominating and chlorinating oxidants during sepsis. Proc. Natl. Acad. Sci. USA 98:11961-66
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 11961-11966
    • Gaut, J.P.1    Yeh, G.C.2    Tran, H.D.3    Byun, J.4    Henderson, J.P.5
  • 45
    • 0033041907 scopus 로고    scopus 로고
    • Severe impairment in early host defense against Candida albicans in mice deficient in myeloperoxidase
    • Aratani Y, Koyama H, Nyui S, Suzuki K, Kura F, Maeda N. 1999. Severe impairment in early host defense against Candida albicans in mice deficient in myeloperoxidase. Infect. Immun. 67:1828-36
    • (1999) Infect. Immun. , vol.67 , pp. 1828-1836
    • Aratani, Y.1    Koyama, H.2    Nyui, S.3    Suzuki, K.4    Kura, F.5    Maeda, N.6
  • 47
    • 0038392936 scopus 로고    scopus 로고
    • Inducible nitric oxide synthase and control of intracellular bacterial pathogens
    • Chakravortty D, Hensel M. 2003. Inducible nitric oxide synthase and control of intracellular bacterial pathogens. Microbes. Infect. 5:621-27
    • (2003) Microbes. Infect. , vol.5 , pp. 621-627
    • Chakravortty, D.1    Hensel, M.2
  • 48
    • 0000646464 scopus 로고
    • On a remarkable bacteriolytic element found in tissues and secretions
    • Fleming A. 1922. On a remarkable bacteriolytic element found in tissues and secretions. Proc. R. Soc. London 93:306-317
    • (1922) Proc. R. Soc. London , vol.93 , pp. 306-317
    • Fleming, A.1
  • 49
    • 0000617857 scopus 로고
    • Phagocytin: A bactericidal substance from polymorphonuclear leucocytes
    • Hirsch JG. 1956. Phagocytin: a bactericidal substance from polymorphonuclear leucocytes. J. Exp. Med. 103:589-611
    • (1956) J. Exp. Med. , vol.103 , pp. 589-611
    • Hirsch, J.G.1
  • 50
    • 0014288898 scopus 로고
    • Arginine-rich proteins of polymorphonuclear leukocyte lysosomes. Antimicrobial specificity and biochemical heterogeneity
    • Zeya HI, Spitznagel JK. 1968. Arginine-rich proteins of polymorphonuclear leukocyte lysosomes. Antimicrobial specificity and biochemical heterogeneity. J. Exp. Med. 127:927-41
    • (1968) J. Exp. Med. , vol.127 , pp. 927-941
    • Zeya, H.I.1    Spitznagel, J.K.2
  • 51
    • 0030997435 scopus 로고    scopus 로고
    • Granules of the human neutrophilic polymorphonuclear leukocyte
    • Borregaard N, Cowland JB. 1997. Granules of the human neutrophilic polymorphonuclear leukocyte. Blood 89:3503-21
    • (1997) Blood , vol.89 , pp. 3503-3521
    • Borregaard, N.1    Cowland, J.B.2
  • 53
    • 0027144720 scopus 로고
    • Neutrophilic leukocyte granules: From structure to function
    • Bainton DF. 1993. Neutrophilic leukocyte granules: from structure to function. Adv. Exp. Med. Biol. 336:17-33
    • (1993) Adv. Exp. Med. Biol. , vol.336 , pp. 17-33
    • Bainton, D.F.1
  • 54
    • 0014465369 scopus 로고
    • Resolution of granules from rabbit heterophil leukocytes into distinct populations by zonal sedimentation
    • Baggiolini M, Hirsch JG, De Duve C. 1969. Resolution of granules from rabbit heterophil leukocytes into distinct populations by zonal sedimentation. J. Cell Biol. 40:529-41
    • (1969) J. Cell Biol. , vol.40 , pp. 529-541
    • Baggiolini, M.1    Hirsch, J.G.2    De Duve, C.3
  • 55
    • 0016428571 scopus 로고
    • Partial characterization and purification of a rabbit granulocyte factor that increases permeability of Escherichia coli
    • Weiss J, Franson RC, Beckerdite S, Schmeidler K, Elsbach P. 1975. Partial characterization and purification of a rabbit granulocyte factor that increases permeability of Escherichia coli. J. Clin. Invest. 55:33-42
    • (1975) J. Clin. Invest. , vol.55 , pp. 33-42
    • Weiss, J.1    Franson, R.C.2    Beckerdite, S.3    Schmeidler, K.4    Elsbach, P.5
  • 56
    • 0017804093 scopus 로고
    • Purification and characterization of a potent bactericidal and membrane active protein from the granules of human polymorphonuclear leukocytes
    • Weiss J, Elsbach P, Olsson I, Odeberg H. 1978. Purification and characterization of a potent bactericidal and membrane active protein from the granules of human polymorphonuclear leukocytes. J. Biol. Chem. 253:2664-72
    • (1978) J. Biol. Chem. , vol.253 , pp. 2664-2672
    • Weiss, J.1    Elsbach, P.2    Olsson, I.3    Odeberg, H.4
  • 57
    • 0025883775 scopus 로고
    • Endotoxin-neutralizing properties of the 25 kD N-terminal fragment and a newly isolated 30 kD C-terminal fragment of the 55-60 kD bactericidal/ permeability-increasing protein of human neutrophils
    • Ooi CE, Weiss J, Doerfler ME, Elsbach P. 1991. Endotoxin-neutralizing properties of the 25 kD N-terminal fragment and a newly isolated 30 kD C-terminal fragment of the 55-60 kD bactericidal/ permeability-increasing protein of human neutrophils. J. Exp. Med. 174:649-55
    • (1991) J. Exp. Med. , vol.174 , pp. 649-655
    • Ooi, C.E.1    Weiss, J.2    Doerfler, M.E.3    Elsbach, P.4
  • 58
    • 0141799911 scopus 로고    scopus 로고
    • Defensins: Antimicrobial peptides of innate immunity
    • Ganz T. 2003. Defensins: antimicrobial peptides of innate immunity. Nat. Rev. Immunol. 3:710-20
    • (2003) Nat. Rev. Immunol. , vol.3 , pp. 710-720
    • Ganz, T.1
  • 60
    • 0020432801 scopus 로고
    • Internal pH of human neutrophil lysosomes
    • Styrt B, Klempner MS. 1982. Internal pH of human neutrophil lysosomes. FEBS Lett. 149:113-16
    • (1982) FEBS Lett. , vol.149 , pp. 113-116
    • Styrt, B.1    Klempner, M.S.2
  • 61
    • 0018326718 scopus 로고
    • The role of lactoferrin in the bactericidal function of polymorphonuclear leucocytes
    • Bullen JJ, Armstrong JA. 1979. The role of lactoferrin in the bactericidal function of polymorphonuclear leucocytes. Immunology 36:781-91
    • (1979) Immunology , vol.36 , pp. 781-791
    • Bullen, J.J.1    Armstrong, J.A.2
  • 62
    • 0028065442 scopus 로고
    • Molecular cloning and expression of a cDNA encoding NGAL: A lipocalin expressed in human neutrophils
    • Bundgaard JR, Sengelov H, Borregaard N, Kjeldsen L. 1994. Molecular cloning and expression of a cDNA encoding NGAL: a lipocalin expressed in human neutrophils. Biochem. Biophys. Res. Commun. 202:1468-75
    • (1994) Biochem. Biophys. Res. Commun. , vol.202 , pp. 1468-1475
    • Bundgaard, J.R.1    Sengelov, H.2    Borregaard, N.3    Kjeldsen, L.4
  • 63
    • 0018643333 scopus 로고
    • The subcellular distribution and some properties of the cytochrome b component of the microbicidal oxidase system of human neutrophils
    • Segal AW, Jones OT. 1979. The subcellular distribution and some properties of the cytochrome b component of the microbicidal oxidase system of human neutrophils. Biochem. J. 182:181-88
    • (1979) Biochem. J. , vol.182 , pp. 181-188
    • Segal, A.W.1    Jones, O.T.2
  • 64
    • 0024425765 scopus 로고
    • Human neutrophil gelatinase is a component of specific granules
    • Hibbs MS, Bainton DF. 1989. Human neutrophil gelatinase is a component of specific granules. J. Clin. Invest 84:1395-402
    • (1989) J. Clin. Invest. , vol.84 , pp. 1395-1402
    • Hibbs, M.S.1    Bainton, D.F.2
  • 66
    • 0014807909 scopus 로고
    • Further biochemical and morphological studies of granule fractions from rabbit heterophil leukocytes
    • Baggiolini M, Hirsch JG, De Duve C. 1970. Further biochemical and morphological studies of granule fractions from rabbit heterophil leukocytes. J. Cell Biol. 45:586-97
    • (1970) J. Cell Biol. , vol.45 , pp. 586-597
    • Baggiolini, M.1    Hirsch, J.G.2    De Duve, C.3
  • 67
    • 0028233280 scopus 로고
    • Secretory vesicles are the intracellular reservoir of complement receptor 1 in human neutrophils
    • Sengelov H, Kjeldsen L, Kroeze W, Berger M, Borregaard N. 1994. Secretory vesicles are the intracellular reservoir of complement receptor 1 in human neutrophils. J. Immunol. 153:804-10
    • (1994) J. Immunol. , vol.153 , pp. 804-810
    • Sengelov, H.1    Kjeldsen, L.2    Kroeze, W.3    Berger, M.4    Borregaard, N.5
  • 68
    • 0019480640 scopus 로고
    • The respiratory burst of phagocytic cells is associated with a rise in vacuolar pH
    • Segal AW, Geisow M, Garcia R, Harper A, Miller R. 1981. The respiratory burst of phagocytic cells is associated with a rise in vacuolar pH. Nature 290:406-9
    • (1981) Nature , vol.290 , pp. 406-409
    • Segal, A.W.1    Geisow, M.2    Garcia, R.3    Harper, A.4    Miller, R.5
  • 69
    • 0014005822 scopus 로고
    • Fatal granulomatous disease of childhood. An inborn abnormality of phagocytic function
    • Holmes B, Quie PG, Windhorst DB, Good RA. 1966. Fatal granulomatous disease of childhood. An inborn abnormality of phagocytic function. Lancet 1:1225-28
    • (1966) Lancet , vol.1 , pp. 1225-1228
    • Holmes, B.1    Quie, P.G.2    Windhorst, D.B.3    Good, R.A.4
  • 70
    • 0021355213 scopus 로고
    • Phagocytosing macrophages exclude proteins from the zones of contact with opsonized targets
    • Wright SD, Silverstein SC. 1984. Phagocytosing macrophages exclude proteins from the zones of contact with opsonized targets. Nature 309:359-61
    • (1984) Nature , vol.309 , pp. 359-361
    • Wright, S.D.1    Silverstein, S.C.2
  • 71
    • 0015832477 scopus 로고
    • Sequential degranulation of the two types of polymorphonuclear leukocyte granules during phagocytosis of microorganisms
    • Bainton DF. 1973. Sequential degranulation of the two types of polymorphonuclear leukocyte granules during phagocytosis of microorganisms. J. Cell Biol. 58:249-64
    • (1973) J. Cell Biol. , vol.58 , pp. 249-264
    • Bainton, D.F.1
  • 72
    • 0015581231 scopus 로고
    • Temporal changes in pH within the phagocytic vacuole of the polymorphonuclear neutrophilic leukocyte
    • Jensen MS, Bainton DF. 1973. Temporal changes in pH within the phagocytic vacuole of the polymorphonuclear neutrophilic leukocyte. J. Cell Biol. 56:379-88
    • (1973) J. Cell Biol. , vol.56 , pp. 379-388
    • Jensen, M.S.1    Bainton, D.F.2
  • 73
    • 0021336071 scopus 로고
    • Phagolysosomal pH of human neutrophils
    • Cech P, Lehrer RI. 1984. Phagolysosomal pH of human neutrophils. Blood 63:88-95
    • (1984) Blood , vol.63 , pp. 88-95
    • Cech, P.1    Lehrer, R.I.2
  • 75
    • 0031836105 scopus 로고    scopus 로고
    • Mice lacking neutrophil elastase reveal impaired host defense against Gram negative bacterial sepsis
    • Belaaouaj A, McCarthy R, Baumann M, Gao Z, Ley TJ, et al. 1998. Mice lacking neutrophil elastase reveal impaired host defense against Gram negative bacterial sepsis. Nat. Med. 4:615-18
    • (1998) Nat. Med. , vol.4 , pp. 615-618
    • Belaaouaj, A.1    McCarthy, R.2    Baumann, M.3    Gao, Z.4    Ley, T.J.5
  • 76
    • 0034144636 scopus 로고    scopus 로고
    • Impaired immunity and enhanced resistance to endotoxin in the absence of neutrophil elastase and cathepsin G
    • Tkalcevic J, Novelli M, Phylactides M, Iredale JP, Segal AW, Roes J. 2000. Impaired immunity and enhanced resistance to endotoxin in the absence of neutrophil elastase and cathepsin G. Immunity 12:201-10
    • (2000) Immunity , vol.12 , pp. 201-210
    • Tkalcevic, J.1    Novelli, M.2    Phylactides, M.3    Iredale, J.P.4    Segal, A.W.5    Roes, J.6
  • 79
    • 0026567207 scopus 로고
    • +-conducting pathway in the membrane of neutrophils
    • +-conducting pathway in the membrane of neutrophils. Biochem. J. 281:697-701
    • (1992) Biochem. J. , vol.281 , pp. 697-701
    • Kapus, A.1    Szaszi, K.2    Ligeti, E.3
  • 80
    • 0027375484 scopus 로고
    • Potential, pH, and arachidonate gate hydrogen ion currents in human neutrophils
    • DeCoursey TE, Cherny VV. 1993. Potential, pH, and arachidonate gate hydrogen ion currents in human neutrophils. Biophys. J. 65:1590-98
    • (1993) Biophys. J. , vol.65 , pp. 1590-1598
    • DeCoursey, T.E.1    Cherny, V.V.2
  • 81
    • 0032537190 scopus 로고    scopus 로고
    • Electron currents generated by the human phagocyte NADPH oxidase
    • Schrenzel J, Serrander L, Banfi B, Nusse O, Fouyouzi R, et al. 1998. Electron currents generated by the human phagocyte NADPH oxidase. Nature 392:734-37
    • (1998) Nature , vol.392 , pp. 734-737
    • Schrenzel, J.1    Serrander, L.2    Banfi, B.3    Nusse, O.4    Fouyouzi, R.5
  • 83
    • 0037417274 scopus 로고    scopus 로고
    • The voltage dependence of NADPH oxidase reveals why phagocytes need proton channels
    • DeCoursey TE, Morgan D, Cherny VV. 2003. The voltage dependence of NADPH oxidase reveals why phagocytes need proton channels. Nature 422:531-34
    • (2003) Nature , vol.422 , pp. 531-534
    • DeCoursey, T.E.1    Morgan, D.2    Cherny, V.V.3
  • 84
    • 0029970757 scopus 로고    scopus 로고
    • Paxilline inhibition of the alpha-subunit of the high-conductance calcium-activated potassium channel
    • Sanchez M, McManus OB. 1996. Paxilline inhibition of the alpha-subunit of the high-conductance calcium-activated potassium channel. Neuropharmacology 35:963-68
    • (1996) Neuropharmacology , vol.35 , pp. 963-968
    • Sanchez, M.1    McManus, O.B.2
  • 85
    • 0025299607 scopus 로고
    • Purification and characterization of a unique, potent, peptidyl probe for the high conductance calcium-activated potassium channel from venom of the scorpion Buthus tamulus
    • Galvez A, Gimenez-Gallego G, Reuben JP, Roy-Contancin L, Feigenbaum P, et al. 1990. Purification and characterization of a unique, potent, peptidyl probe for the high conductance calcium-activated potassium channel from venom of the scorpion Buthus tamulus. J. Biol. Chem. 265:11083-90
    • (1990) J. Biol. Chem. , vol.265 , pp. 11083-11090
    • Galvez, A.1    Gimenez-Gallego, G.2    Reuben, J.P.3    Roy-Contancin, L.4    Feigenbaum, P.5
  • 86
    • 0033945753 scopus 로고    scopus 로고
    • Potassium channel openers as potential therapeutic weapons in ion channel disease
    • Lawson K. 2000. Potassium channel openers as potential therapeutic weapons in ion channel disease. Kidney Int. 57:838-45
    • (2000) Kidney Int. , vol.57 , pp. 838-845
    • Lawson, K.1
  • 88
    • 0033543695 scopus 로고    scopus 로고
    • A non-invasive fluorimetric procedure for measurement of membrane potential. Quantification of the NADPH oxidase-induced depolarization in activated neutrophils
    • Jankowski A, Grinstein S. 1999. A non-invasive fluorimetric procedure for measurement of membrane potential. Quantification of the NADPH oxidase-induced depolarization in activated neutrophils. J. Biol. Chem. 274:26098-104
    • (1999) J. Biol. Chem. , vol.274 , pp. 26098-26104
    • Jankowski, A.1    Grinstein, S.2
  • 89
    • 0021203722 scopus 로고
    • Proton secretion by stimulated neutrophils. Significance of hexose monophosphate shunt activity as source of electrons and protons for the respiratory burst
    • Borregaard N, Schwartz JH, Tauber AI. 1984. Proton secretion by stimulated neutrophils. Significance of hexose monophosphate shunt activity as source of electrons and protons for the respiratory burst. J. Clin. Invest. 74:455-59
    • (1984) J. Clin. Invest. , vol.74 , pp. 455-459
    • Borregaard, N.1    Schwartz, J.H.2    Tauber, A.I.3
  • 90
    • 0026460154 scopus 로고
    • Activation of vacuolar-type proton pumps by protein kinase C. Role in neutrophil pH regulation
    • Nanda A, Gukovskaya A, Tseng J, Grinstein S. 1992. Activation of vacuolar-type proton pumps by protein kinase C. Role in neutrophil pH regulation. J. Biol. Chem. 267:22740-46
    • (1992) J. Biol. Chem. , vol.267 , pp. 22740-22746
    • Nanda, A.1    Gukovskaya, A.2    Tseng, J.3    Grinstein, S.4
  • 91
    • 0023901674 scopus 로고
    • Proton release associated with respiratory burst of polymorphonuclear leukocytes
    • Takanaka K, O'Brien PJ. 1988. Proton release associated with respiratory burst of polymorphonuclear leukocytes. J. Biochem. (Tokyo) 103:656-60
    • (1988) J. Biochem. (Tokyo) , vol.103 , pp. 656-660
    • Takanaka, K.1    O'Brien, P.J.2
  • 93
    • 0022381691 scopus 로고
    • + exchange in human neutrophils. II. Intracellular pH changes
    • + exchange in human neutrophils. II. Intracellular pH changes. J. Biol. Chem. 260:13248-55
    • (1985) J. Biol. Chem. , vol.260 , pp. 13248-13255
    • Simchowitz, L.1
  • 94
    • 0022502137 scopus 로고
    • Cytoplasmic pH regulation in phorbol ester-activated human neutrophils
    • Grinstein S, Furuya W. 1986. Cytoplasmic pH regulation in phorbol ester-activated human neutrophils. Am. J. Physiol. 251(Pt. 1):C55-65
    • (1986) Am. J. Physiol. , vol.251 , Issue.PART 1
    • Grinstein, S.1    Furuya, W.2
  • 96
    • 0025720460 scopus 로고
    • + (equivalent) conductance in the plasma membrane of human neutrophils
    • + (equivalent) conductance in the plasma membrane of human neutrophils. Proc. Natl. Acad. Sci. USA 88:10816-20
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 10816-10820
    • Nanda, A.1    Grinstein, S.2
  • 97
    • 0023718702 scopus 로고
    • Superoxide generation by the electrogenic NADPH oxidase of human neutrophils is limited by the movement of a compensating charge
    • Henderson LM, Chappell JB, Jones OT. 1988. Superoxide generation by the electrogenic NADPH oxidase of human neutrophils is limited by the movement of a compensating charge. Biochem. J. 255:285-90
    • (1988) Biochem. J. , vol.255 , pp. 285-290
    • Henderson, L.M.1    Chappell, J.B.2    Jones, O.T.3
  • 98
  • 102
    • 0019936907 scopus 로고
    • Hydrogen ion currents and intracellular pH in depolarized voltage-clamped snail neurones
    • Thomas RC, Meech RW. 1982. Hydrogen ion currents and intracellular pH in depolarized voltage-clamped snail neurones. Nature 299:826-28
    • (1982) Nature , vol.299 , pp. 826-828
    • Thomas, R.C.1    Meech, R.W.2
  • 104
    • 4043080713 scopus 로고    scopus 로고
    • During the respiratory burst, do phagocytes need proton channels or potassium channels, or both?
    • DeCoursey TE. 2004. During the respiratory burst, do phagocytes need proton channels or potassium channels, or both? Sci. STKE 2004:E21
    • (2004) Sci. STKE , vol.2004
    • DeCoursey, T.E.1
  • 105
    • 0023024325 scopus 로고
    • Antimicrobial properties of hydrogen peroxide and sodium bicarbonate individually and in combination against selected oral, gram-negative, facultative bacteria
    • Miyasaki KT, Genco RJ, Wilson ME. 1986. Antimicrobial properties of hydrogen peroxide and sodium bicarbonate individually and in combination against selected oral, gram-negative, facultative bacteria. J. Dent. Res. 65:1142-48
    • (1986) J. Dent. Res. , vol.65 , pp. 1142-1148
    • Miyasaki, K.T.1    Genco, R.J.2    Wilson, M.E.3
  • 106
    • 0020555623 scopus 로고
    • Increased respiratory burst in myeloperoxidase-deficient monocytes
    • Locksley RM, Wilson CB, Klebanoff SJ. 1983. Increased respiratory burst in myeloperoxidase-deficient monocytes. Blood 62:902-9
    • (1983) Blood , vol.62 , pp. 902-909
    • Locksley, R.M.1    Wilson, C.B.2    Klebanoff, S.J.3
  • 107
    • 0020455711 scopus 로고
    • Hydrogen peroxide mediated killing of bacteria
    • Clifford DP, Repine JE. 1982. Hydrogen peroxide mediated killing of bacteria. Mol. Cell Biochem. 49:143-49
    • (1982) Mol. Cell Biochem. , vol.49 , pp. 143-149
    • Clifford, D.P.1    Repine, J.E.2
  • 109
    • 0015381405 scopus 로고
    • Laboratory models of chronic granulomatous disease
    • Holmes B, Good RA. 1972. Laboratory models of chronic granulomatous disease. J. Reticuloendothel. Soc. 12:216-37
    • (1972) J. Reticuloendothel. Soc. , vol.12 , pp. 216-237
    • Holmes, B.1    Good, R.A.2
  • 110
    • 0015966682 scopus 로고
    • Role of peroxide in phagocytic killing of pneumococci
    • Pitt J, Bernheimer HP. 1974. Role of peroxide in phagocytic killing of pneumococci. Infect. Immun. 9:48-52
    • (1974) Infect. Immun. , vol.9 , pp. 48-52
    • Pitt, J.1    Bernheimer, H.P.2
  • 111
    • 0016660853 scopus 로고
    • Catalase, superoxide dismutase, and virulence of Staphylococcus aureus. In vitro and in vivo studies with emphasis on staphylococcal-leukocyte interaction
    • Mandell GL. 1975. Catalase, superoxide dismutase, and virulence of Staphylococcus aureus. In vitro and in vivo studies with emphasis on staphylococcal-leukocyte interaction. J. Clin. Invest. 55:561-66
    • (1975) J. Clin. Invest. , vol.55 , pp. 561-566
    • Mandell, G.L.1
  • 112
    • 0032080869 scopus 로고    scopus 로고
    • phox-/- mice. Implications for fungal pathogenicity and host defense in chronic granulomatous disease
    • phox-/- mice. Implications for fungal pathogenicity and host defense in chronic granulomatous disease. J. Clin. Invest. 101:1843-50
    • (1998) J. Clin. Invest. , vol.101 , pp. 1843-1850
    • Chang, Y.C.1
  • 113
    • 0037042203 scopus 로고    scopus 로고
    • Catalase negative Staphylococcus aureus retain virulence in mouse model of chronic granulomatous disease
    • Messina CG, Reeves EP, Roes J, Segal AW. 2002. Catalase negative Staphylococcus aureus retain virulence in mouse model of chronic granulomatous disease. FEBS Lett. 518:107-10
    • (2002) FEBS Lett. , vol.518 , pp. 107-110
    • Messina, C.G.1    Reeves, E.P.2    Roes, J.3    Segal, A.W.4
  • 114
    • 0018389875 scopus 로고
    • Utilization of liposomes for correction of the metabolic and bactericidal deficiencies in chronic granulomatous disease
    • Ismail G, Boxer LA, Baehner RL. 1979. Utilization of liposomes for correction of the metabolic and bactericidal deficiencies in chronic granulomatous disease. Pediatr. Res. 13:769-73
    • (1979) Pediatr. Res. , vol.13 , pp. 769-773
    • Ismail, G.1    Boxer, L.A.2    Baehner, R.L.3
  • 115
    • 0035892133 scopus 로고    scopus 로고
    • Reconstitution of bactericidal activity in chronic granulomatous disease cells by glucose-oxidase-containing liposomes
    • Gerber CE, Bruchelt G, Falk UB, Kimpfler A, Hauschild O, et al. 2001. Reconstitution of bactericidal activity in chronic granulomatous disease cells by glucose-oxidase-containing liposomes. Blood 98:3097-105
    • (2001) Blood , vol.98 , pp. 3097-3105
    • Gerber, C.E.1    Bruchelt, G.2    Falk, U.B.3    Kimpfler, A.4    Hauschild, O.5
  • 116
    • 0042028316 scopus 로고    scopus 로고
    • Reassessment of the microbicidal activity of reactive oxygen species and hypochlorous acid with reference to the phagocytic vacuole of the neutrophil granulocyte
    • Reeves EP, Nagl M, Godovac-Zimmermann J, Segal AW. 2003. Reassessment of the microbicidal activity of reactive oxygen species and hypochlorous acid with reference to the phagocytic vacuole of the neutrophil granulocyte. J. Med. Microbiol. 52:643-51
    • (2003) J. Med. Microbiol. , vol.52 , pp. 643-651
    • Reeves, E.P.1    Nagl, M.2    Godovac-Zimmermann, J.3    Segal, A.W.4
  • 117
    • 17644373989 scopus 로고    scopus 로고
    • Deleted in proof
    • Deleted in proof
  • 118
    • 0017618735 scopus 로고
    • Iodination by human polymorphonuclear leukocytes: A re-evaluation
    • Klebanoff SJ, Clark RA. 1977. Iodination by human polymorphonuclear leukocytes: a re-evaluation. J. Lab. Clin. Med. 89:675-86
    • (1977) J. Lab. Clin. Med. , vol.89 , pp. 675-686
    • Klebanoff, S.J.1    Clark, R.A.2
  • 119
    • 0020672123 scopus 로고
    • Iodination by stimulated human neutrophils. Studies on its stoichiometry, subcellular localization and relevance to microbial killing
    • Segal AW, Garcia RC, Harper AM, Banga JP. 1983. Iodination by stimulated human neutrophils. Studies on its stoichiometry, subcellular localization and relevance to microbial killing. Biochem. J. 210:215-25
    • (1983) Biochem. J. , vol.210 , pp. 215-225
    • Segal, A.W.1    Garcia, R.C.2    Harper, A.M.3    Banga, J.P.4
  • 120
    • 0037155914 scopus 로고    scopus 로고
    • Chlorination of bacterial and neutrophil proteins during phagocytosis and killing of Staphylococcus aureus
    • Chapman AL, Hampton MB, Senthilmohan R, Winterbourn CC, Kettle AJ. 2002. Chlorination of bacterial and neutrophil proteins during phagocytosis and killing of Staphylococcus aureus. J. Biol. Chem. 277:9757-62
    • (2002) J. Biol. Chem. , vol.277 , pp. 9757-9762
    • Chapman, A.L.1    Hampton, M.B.2    Senthilmohan, R.3    Winterbourn, C.C.4    Kettle, A.J.5
  • 122
    • 0037947142 scopus 로고
    • Chicken neutrophils: Oxidative metabolism in phagocytic cells devoid of myeloperoxidase
    • Penniall R, Spitznagel JK. 1975. Chicken neutrophils: oxidative metabolism in phagocytic cells devoid of myeloperoxidase. Proc. Natl. Acad. Sci. USA 72:5012-15
    • (1975) Proc. Natl. Acad. Sci. USA , vol.72 , pp. 5012-5015
    • Penniall, R.1    Spitznagel, J.K.2
  • 124
    • 0035964384 scopus 로고    scopus 로고
    • A kinetic analysis of the catalase activity of myeloperoxidase
    • Kettle AJ, Winterbourn CC. 2001. A kinetic analysis of the catalase activity of myeloperoxidase. Biochemistry 40:10204-12
    • (2001) Biochemistry , vol.40 , pp. 10204-10212
    • Kettle, A.J.1    Winterbourn, C.C.2
  • 125
    • 0022259915 scopus 로고
    • Production of the superoxide adduct of myeloperoxidase (compound III) by stimulated human neutrophils and its reactivity with hydrogen peroxide and chloride
    • Winterbourn CC, Garcia RC, Segal AW. 1985. Production of the superoxide adduct of myeloperoxidase (compound III) by stimulated human neutrophils and its reactivity with hydrogen peroxide and chloride. Biochem. J. 228:583-92
    • (1985) Biochem. J. , vol.228 , pp. 583-592
    • Winterbourn, C.C.1    Garcia, R.C.2    Segal, A.W.3
  • 126
    • 0037097791 scopus 로고    scopus 로고
    • Critical role of myeloperoxidase and nicotinamide adenine dinucleotide phosphate-oxidase in high-burden systemic infection of mice with Candida albicans
    • Aratani Y, Kura F, Watanabe H, Akagawa H, Takano Y, et al. 2002. Critical role of myeloperoxidase and nicotinamide adenine dinucleotide phosphate-oxidase in high-burden systemic infection of mice with Candida albicans. J. Infect. Dis. 185:1833-37
    • (2002) J. Infect. Dis. , vol.185 , pp. 1833-1837
    • Aratani, Y.1    Kura, F.2    Watanabe, H.3    Akagawa, H.4    Takano, Y.5


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