Abstract
The respiratory burst of neutrophilic granulocytes is a metabolic response of these cells to signals of infection. This metabolic pathway starts with markedly increased oxygen uptake,1,2 resulting in production of primary and secondary products, harmful to invaders.3,4
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References
Baldridge CW, Gerard RW: The extrarespiration of phagocytosis. Am J Physiol 103: 235–236, 1933.
Sbarra AJ, Karnovsky ML: The biochemical basis of phagocytosis. I. Metabolic changes during the ingestion of particles by polymorphonuclear leukocytes. J Biol Chem 234: 1355–1362, 1959.
Babior BM: Oxygen-dependent microbial killing by phagocytes. N Engl J Med 298: 659–668, 1978.
Badwey JA, Karnovsky ML: Active oxygen species and the functions of phagocytic leukocytes. Annu Rev Biochem 49: 695–726, 1980.
Schiffman E, Corcoran BA, Wahl SM: Af-formyl-methionyl peptides as chemoattractants for leukocytes. Proc Natl Acad Sci USA 72: 1059–1065, 1975.
English D, Rozoff JS, Lukens JN: Regulation of human polymorphonuclear leukocyte superoxide release by cellular responses to chemotactic peptides. J Immunol 126: 165–173, 1981.
Goldstein JM, Ross D, Kaplan HB, et al: Complement and immunoglobulins stimulate superoxide production by human leukocytes independently of phagocytosis. J Clin Invest 56: 1155–1163, 1975.
Klebanoff SJ, Clark RA: The Neutrophil: Function and Clinical Disorders. Amsterdam, Elsevier/North-Holland, 1978, pp 172–183.
Curnutte JT, Babior BM: Biological defense mechanisms. The effect of bacteria and serum on superoxide production by granulocytes. J Clin Invest 53: 1662–1672, 1974.
Messner RP, Jelinek J: Receptors for human yG globulin on human neutrophils. J Clin Invest 49: 2165–2171, 1970.
Sajnani AN, Ranadive NS, Movat HZ: The visualization of receptors for the Fc portion of the IgG molecule on human neutrophil leukocytes. Life Sci 14: 2427–2430, 1974.
Borgeat P. Samuelsson B: Transformation of arachidonic acid by rabbit polymorphonuclear leukocytes. Formation of a novel dihydroxyeicosatetraenoic acid. J Biol Chem 254: 2643–2646, 1979.
Najjar VA: Biochemistry and physiology of tuftsin Thr-Lys-Pro-Arg, in Sbarra AJ, Strauss RR (eds): The Reticuloendothelial System, A Comprehensive Treatise. New York, Plenum, 1980, vol 2, pp 45–71.
Gay JC, Beckman JK, Brash AR, et al: Enhancement of chemotactic factor-stimulated neutrophil oxidative metabolism by leukotriene B4. Blood 64: 780–785, 1984.
Spirer Z, Zakuth V, Golander A, et al: The effect of tuftsin on the nitrous blue tetrazolium reduction of normal human polymorphonuclear leukocytes. J Clin Invest 55: 198–201, 1975.
Fletcher MP, Galin JI: Degranulating stimuli increase the availability of receptors on human neutrophils for the chemoattractant f Met-Leu-Phe. J Immunol 124: 1585–1588, 1980.
Dahlgren C, Magnusson KE, Stendahl O, et al: Modulation of polymorphonuclear leukocyte chemiluminescent response to the chemoattractant f-Met-Leu-Phe. Int Arch Allergy Appl Immunol 68: 79–83, 1982.
Targowski SP, Niemialtowski M: Appearance of Fc receptors on polymorphonuclear leucocytes after migration and their role in phagocytosis. Infect Immun 52: 798–802, 1986.
McPhail LC, Snyderman R: Activation of the respiratory burst enzyme in human polymorphonuclear leukocytes by chemoattractants and other soluble stimuli. Evidence that the same oxidase is activated by different transductional mechanisms. J Clin Invest 72: 192–200, 1983.
Harber MJ, Topley N: Factors affecting the measurement of chemiluminescence in stimulated human polymorphonuclear leukocytes. J Bioluminescence Chemiluminescence 1: 15–27, 1986.
Barbour AG, Allred CD, Solberg CO, et al: Chemiluminescence by polymorphonuclear leukocytes from patients with acute bacterial infections. J Infect Dis 141: 14–26, 1980.
Bass DA, Olbrantz P, Szejda P, et al: Subpopulations of neutrophils with increased oxidative product formation in blood of patients with infection. J Immunol 136: 860–866, 1986.
Selvaraj RJ, Sbarra AJ, Thomas GB, et al: A microtechnique for studying chemiluminescence response of phagocytes using whole blood and its application to the evaluation of phagocytes in pregnancy. J Reticuloendothel Soc 31: 3–16, 1982.
Tono-Oka T, Ueno N, Matsumoto I, et al: Chemiluminescence in whole blood. 1. A simple and rapid method for the estimation of phagocytic function of granulocytes and opsonic activity in whole blood. Clin Immunol Immunopathol 26: 66–75, 1983.
Allen RC, Stjernholm RL, Steele RH: Evidence for the generation of an electronic excitation state(s) in the human polymorphonuclear leukocytes and its participation in bactericidal activity. Biochem Biophys Res Commun 47: 679–684, 1972.
Zgliczynski JM, Olszowski S, Olszowska E, et al: The influence of plasma factors on chem- iluminescence of polymorphonuclear granulocytes. Postqpy Biologii Komorki 11: 459–462, 1984.
Patriarca P, Cramer R, Moncalvo S, et al: Enzymatic basis of metabolic stimulation in leukocytes during phagocytosis: The role of activated NADPH oxidase. Arch Biochem Biophys 145: 255–262, 1971.
Babior BM, Curnutte JT, McMurrich BJ; The particulate superoxide-forming system from human neutrophils. Properties of the system and further evidence supporting its participation in the respiratory burst. J Clin Invest 56: 1035–1042, 1976.
Suzuki H, Kakinuma K: Evidence that NADPH is the actual substrate of the oxidase responsible for the “respiratory burst” of phagocytosing polymorphonuclear leukocytes. J. Biochem 93: 709–715, 1983.
Doussiere J. Vignais PV: Purification and properties of an Of • generating oxidase from bovine polymorphonuclear neutrophils. Biochemistry 24: 7231–7239, 1985.
Iyer GYN, Islam MF, Quastel JG: Biochemical aspects of phagocytosis. Nature (Lond) 192:535– 541, 1961.
Roos D. Voetman AA and Meerhof LJ: Functional activity of enucleated human polymorpho-nuclear leucocytes. J Cell Biol 97: 368–377, 1983.
Korchak HM, Roos D, Giedd KN, Et Al: Granulocytes without degranulation: Neutrophil function in granule-depleted cytoplasts. Proc Natl Acad Sci USA 80: 4968–4972.
Segal AW, Jones OTG: Novel cytochrome b system in phagocytic vacuoles of human gran-ulocytes. Nature (Lond) 276: 515–517, 1978.
Segal AW, Jones OTG: Absence of cytochrome b reduction in stimulated neutrophils from both female and male patients with chronic granulomatous disease. FEBS Lett 110: 111–114, 1980.
Babior BM, Kipness RS: Superoxide-forming enzyme from human neutrophils: Evidence for a flavin requirement. Blood 50: 517–524, 1977.
Gabig GT: The NADPH-dependent O2- generating oxidase from human neutrophils: Identifica-tion of a flavoprotein component that is deficient in a patient with chronic granulomatous disease. J Biol Chem 258: 6352–6356, 1983.
Gerard C, McPhail LC, Marfat A, et al: Role of protein kinase in stimulation of human poly-morphonuclear leukocyte oxidative metabolism by various agonists. J Clin Invest 77: 61–65, 1986.
Babior MB, Kipnes RS and Curnutte JT: Biological defense mechanisms. The production by leukocytes of superoxide, a potential bactericidal agent. J Clin Invest 52: 741–744, 1973.
McCord JM, Fridovich I: Superoxide dismutase: An enzymatic function for erythrocuprein (hemo- cuprein). J Biol Chem 244: 6049–6055, 1969.
DeChatelet LR, McCall CE, McPhail LC, et al: Superoxide dismutase activity in leukocytes. J Clin Invest 53: 1197–1201, 1973.
Segal AW, Geisgow M, Garcia R, et al: The respiratory burst of phagocytic cells is associated with a rise in vacuolar pH. Nature (Lond) 290: 406–409, 1981.
Khan AU: Singlet molecular oxygen from superoxide anion and sensitized fluorescence of organic molecules. Science 168: 476–477, 1970.
Arudi RL, Bielski BHJ, Allen AO: Search for singlet oxygen luminescence in the disproportiona– tion of HO2/O2- •. Photochem Photobiol 39: 703–706, 1984.
Paul B, Sbarra AJ: The role of the phagocyte in host parasite interactions. XIII. The direct quantitative estimation of H202 in phagocytozing cells. Biochim Biophys Acta 156: 168–178, 1968.
Root RK, Metcalf J, Oshino N, et al: H202 release from human granulocytes during phagocytosis. J Clin Invest 55: 945–955, 1975.
Homan-Muller JWT, Weening RS, Roos D: Production of hydrogen peroxide by phagocytizing human granulocytes. J Lab Clin Med 85: 198–207, 1975.
Root RK, Metcalf JA: H202 release from human granulocytes during phagocytosis: Relationship to superoxide anion formation and cellular catabolism of H202: Studies with normal and cytochalasin B-treated cells. J Clin Invest 60: 1266–1279, 1977.
Kakinuma K, Kaneda M: Apparent Km of leukocyte O2- and H202 forming enzyme for oxygen, in Rossi F, Patriarca P (eds): Biochemistry and Function of Phagocytes. New York, Plenum, 1982, pp 351–359.
Agner K: Verdoperoxidase. A ferment isolated from leukocytes. Acta Physiol Scand 2: 1–62, 1941.
Bainton DF, Farquhar MG: Differences in enzyme content of azurophil and specific granules of polymorphonuclear leukocytes. II. Cytochemistry and electron microscopy of bone marrow cells. J Cell Biol 39: 299–317, 1968.
Wilson DL, Manery JF: The permeability of rabbit leukocytes to sodium, potassium and chloride. J Cell Comp Physiol 34: 493–519, 1949.
Baron DN, Ahmed SA: Intracellular concentration of water and of the principal electrolytes determined by the analysis of isolated human leukocytes. Clin Sci 37: 205–219, 1969.
Klebanoff SJ, Clark RA: The Neutrophil: Function and Clinical Disorders. New York, Else- vier/North–Holland Biomedical Press, 1978, pp 410 - 434.
Klebanoff SJ: Iodination of bacteria: A bactericidal mechanism. J Exp Med 126: 1063–1978, 1967.
Stelmaszyriska T, Zgliczyriski JM: Myeloperoxidase of human neutrophilic granulocytes as chlorinating enzyme. Eur J Biochem 45: 305–312, 1974.
Zgliczynski JM, Stelmaszyriska T: Chlorinating ability of human phagocytosing leukocytes. Eur J Biochem 56: 157–162, 1975.
Weiss SJ, Klein R, Slivka A, et al: Chlorination of taurine by human neutrophils. Evidence for hypochlorous acid generation. J Clin Invest 70: 598–607, 1982.
Thomas EL, Grisham MB, Jefferson MM: Myeloperoxidase-dependent effect of amines on functions of isolated neutrophils. J Clin Invest 72: 441–454, 1983.
Foote CS, Goyne TE and Lehrer RI: Assessment of chlorination by human neutrophils. Nature (Lond) 301: 715–716, 1983.
Agner K: Biological effects of hypochlorous acid formed by “MPO” peroxidation in the presence of chloride ions, in Akeson A, Ehrenberg A (eds): Structure and Function of Oxidation-Reduction Enzymes, Oxford, Pergamon, 1972, pp 329–335.
Zgliczynski JM, Stelmaszyriska T, Domariski J, et al: Chloramines as intermediates of oxidation reaction of amino acids by myeloperoxidase. Biochim Biophys Acta 235: 419–424, 1971.
Selvaraj RJ, Paul BB, Strauss RR, et al: Oxidative peptide cleavage and decarboxylation by the MP0-H202-C1 anti-microbial system. Infect Immun 9: 255–260, 1974.
Stelmaszyriska T, Zgliczyriski JM: N-(2-oxoacyl)amino acids and nitriles as final products of dipeptide chlorination mediated by the myeloperoxidase/H2O2/Cl - system. Eur J Biochem 92: 301–308, 1978.
Thomas EL: Myeloperoxidase, hydrogen peroxide, chloride antimicrobial system: Nitrogen-chlorine derivatives of bacterial components in bactericidal action against Escherichia coli. Infect Immun 23: 522–531, 1979.
Thomas EL, Jefferson MM, Grisham MB: Myeloperoxidase-catalyzed incorporation of amines into proteins: Role of hypochlorous acid and dichloramines. Biochemistry 24: 6299–6308, 1982.
Zgliczyriski JM: Characteristics of myeloperoxidase from neutrophils and other peroxidases from different cell types, in Sbarra AJ, Strauss RR (eds): The Reticuloendothelial System. A Comprehensive Treatise. New York, Plenum, 1980, pp 255–278.
Albrich JM, McCarthy CA, Hurst JK: Biological reactivity of hypochlorous acid: Implications for microbicidal mechanisms of leucocyte myeloperoxidase. Proc Natl Acad Sci USA 78: 210–214, 1981.
Winterbourn CC: Comparative reactivites of various biological compounds with myeloperoxidase- hydrogen peroxide-chloride, and similarity of the oxidant to hypochlorite. Biochim Biophys Acta 840: 204–210, 1985.
Onishi M, Odajima T: On the product of prostaglandin Ej oxidized by the myeloperoxidase- H202-chloride system. Jpn J Oral Biol 27: 291–298, 1985.
Zgliczynski JM, Stelmaszynska T, Ostrowski W, et al: Myeloperoxidase of human leukaemic leukocytes: Oxidation of amino acids in the presence of hydrogen peroxide. Eur J Biochem 56: 157–162, 1968.
McMenamy RW, Lund CC, Neville GJ, et al: Studies of unbound amino acid distributions in plasma, erythrocytes, leukocytes and urine of normal human subjects. J Clin Invest 39: 1675–1687, 1960.
Weiss SJ, Lampert MB, Test ST: Long-lived oxidants generated by human neutrophils: Characterization and bioactivity. Science 222: 625–628, 1983.
Test ST, Lampert MB, Ossanna PJ, et al: Generation of nitrogen-chlorine oxidants by human phagocytes. J Clin Invest 74: 1341–1349, 1984.
Grisham MB, Jefferson MM, Melton DF, et al: Chlorination of endogenous amines by isolated neutrophils. Ammonia-dependent bactericidal, cytotoxic, and cytolytic activities of the chlo- ramines. J Biol Chem 259: 10404–10413, 1984.
Slivka A, LoBuglio AF, Weiss SJ: A potential role for hypochlorous acid in granulocyte-mediated tumor cell cytotoxicity. Blood 55: 347–350, 1980.
Thomas EL, Grisham MB, Melton DF, et al: Evidence for a role of taurine in the in vitro oxidative toxicity of neutrophils towards erythrocytes. J Biol Chem 260: 3321–3329, 1985.
Dallegri F, Patrone F, Ballestrero A, et al: Inhibition of neutrophil cytolysin production by target cells. Blood 67: 1266–1272, 1986.
Pereira WE, Hoyano Y, Summons RE, et al: Chlorination studies. II. The reaction of aqueous hypochlorous acid with a-amino acids and peptides. Biochim Biophys Acta 313: 170–180, 1973.
Zgliczynski JM, Stelmaszynska T: Hydrogen cyanide and cyanogen chloride formation by the myeloperoxidase-H2O2-Cl ~ system. Biochim Biophys Acta 567: 309–314, 1979.
Stelmaszynska T: Formation of HCN by human neutrophils. 1. Chlorination of Staphylococcus epidermidis as a source of HCN. Int J Biochem 17: 373–379, 1985.
Tipper DJ, Berman MF: Structures of the cell wall peptidoglycans of Staphylococcus epidermidis Texas 26 and Staphylococcus aureus Copenhagen I. Chain length and average sequence of cross- bridge peptides. Biochemistry 8: 2183–2191, 1969.
Tipper DJ, Strominger JL: Mechanism of action of penicillins: A proposal based on their structural similarity to acyl-D-alanyl-D-alanine. Proc Natl Acad Sei USA 54: 1133–1141, 1965.
Root RK, Isturiz R, Molavi A, et al: Interactions between antibiotics and human neutrophils in the killing of staphylococci: Studies with normal and cytochalasin B-treated cells. J Clin Invest 67: 247–259, 1981.
Stelmaszynska T: Formation of HCN and its chlorination to C1CN by stimulated human neutrophils. 2. Oxidation of thiocyanate as a source of HCN. Int J. Biochem 18: 1107–1114, 1986.
Weuffen W, Kramer A, Jülich WD: Vorkommen bei Mensch und Tier, in Weuffen W (ed): Medizinische und biologische Bedeutung der Thiocyanate (Rhodanide). Berlin, VEB Verlag Volk und Gesundheit, 1982, p 123.
Wever R, Kast WM, Kasinoedin JH, et al: The peroxidation of thiocyanate catalysed by myeloperoxidase and lactoperoxidase. Biochim Biophys Acta 709: 212–219, 1982.
Thomas EL: Peroxidase-catalysed oxidation of thiocyanate, in Weuffen W (ed): Medizinische und biologische Bedeutung der Thiocyanate (Rhodanide). Berlin, VEB Verlag Volk und Gesundheit, 1982. pp 89–102.
Stelmaszynska T, Zgliczynski JM: The role of myeloperoxidase in phagocytosis, with special regard to HCN formation, in Vennesland B, Conn E, Knowles CJ, et al (eds): Cyanide in Biology. London, Academic, 1981, pp 371–383.
Zgliczynski JM, Stelmaszynska T, Olszowska E, et al: Peroxidative oxidation of halides catalysed by myeloperoxidase. Effect of fluoride on halide oxidation. Acta Biochim Biophys 30: 213–222, 1983.
Bolscher BG, Wever R: A kinetic study of the reaction between human myeloperoxidase, hydroperoxides and cyanide. Inhibition by chloride and thiocyanate. Biochim Biophys Acta 788: 1–10, 1984.
Epstein J: Estimation of microquantities of cyanide. Anal Chem 19: 272–274, 1947.
Aldridge WN: The conversion of cyanogen chloride to cyanide in the presence of blood proteins and sulphhydryl compounds. Biochem J 48: 271–276, 1951.
Thomas EL: Myeloperoxidase-hydrogen peroxide-chloride antimicrobial system: Effect of exogenous amines on antibacterial action against Escherichia coli. Infect Immun 25: 110–116, 1979.
Grisham MB, Jefferson MM, Thomas EL: Role of monochloramine in the oxidation of erythrocyte hemoglobin by stimulated neutrophils. J Biol Chem 259: 6757–6765, 1984.
Allen RC: Free-radical production by reticuloendothelial cells, in Sbarra AJ, Strauss RR (eds): The Reticuloendothelial System. A Comprehensive Treatise. New York, Plenum, 1980, vol 2, pp 309– 338.
Halliwell B: Metal ions, free radical reactions and inflammation; an assessment of current status, in Venge P, Lindbom A (eds): Inflammation. Stockholm, Almquist and Wiksell, 1985, pp 271–287.
Arneson RM: Substrate-induced chemiluminescence of xanthine oxidase and aldehyde oxidase. Arch Biochem Biophys 136: 352–360, 1970.
Haber F, Weiss J: The catalytic decomposition of hydrogen peroxide by iron salts. Proc R Soc LondA 147: 332–351, 1934.
Kellog EW, Fridovich I: Superoxide, hydrogen peroxide and singlet oxygen in lipid peroxidation by a xanthine oxidase system. J Biol Chem 250: 8812–8817, 1975.
Long CA, Bielski BHJ: Rate of reaction of superoxide radical with chloride-containing species. J Phys Chem 84: 554–557, 1980.
Tauber AI, Babior BM: Evidence for hydroxyl radical production by human neutrophils. J Clin Invest 60: 374–379, 1977.
Weiss SJ, Rustagi PK, LoBuglio AF: Human granulocyte generation of hydroxyl radical. J Exp Med 147: 316–323, 1978.
Green MR, Hill HAO, Okolow-Zubkowska MJ, et al: The production of hydroxyl and superoxide radicals by stimulated human neutrophils—Measurements by EPR spectroscopy. FEBS Lett 100: 23–27, 1979.
Sagone AL, Decker MA, Wells RM, et al: A new method for the detection of hydroxyl radical production by phagocytic cells. Biochim Biophys Acta 628: 90–97, 1980.
Cheson BD, Christensen RL, Sperling R, et al: The origin of the chemiluminescence of pha- gocytosing granulocytes. J Clin Invest 58: 789–796, 1976.
Held AM, Hurst JK: Ambiguity associated with use of singlet oxygen trapping agents in my- eloperoxidase-catalyzed oxidations. Biochem Biophys Res Commun 81: 878–885, 1978.
Klebanoff SJ, Rosen H: The role of myeloperoxidase in the microbicidal activity of polymorphonuclear leukocytes, in Oxygen Free Radicals and Tissue Damage. Ciba Foundation Symposium 65. Amsterdam, Excerpta Medica, 1979, pp 263–282.
Zgliczyñski JM, Olszowska E, Olszowski S, et al: A possible origin of chemiluminescence in phagocytosing neutrophils. Reaction between chloramines and H202. Int J Biochem 17: 515–519, 1985.
DeChatelet WR, Long GD, Shirley PS, et al: Mechanism of the luminol-dependent chemiluminescence of human neutrophils. J. Immunol 129: 1589–1593, 1982.
Dahlgren C, Stendahl O: Role of myeloperoxidase in luminol-dependent chemiluminescence of polymorphonuclear leukocytes. Infect Immun 39: 736–741, 1983.
Zgliczyñski JM, Olszowska E, Olszowski S, et al: A possible origin of chemiluminescence in phagocytosing neutrophils. Myeloperoxidase-mediated chlorination of proteins and tryptophan. Int J Biochem 17: 393–397, 1985.
Ushijima Y, Nakano M: Excitation of indole analogs by phagocytosing leukocytes. Biochem Biophys Res Commun 82: 835–858, 1978.
Weiss SJ, Young J, LoBuglio, Et Al: Role of hydrogen peroxide in neutrophil-mediated destruction of cultured endothelial cells. J Clin Invest 68: 714–719, 1981.
Ward PA, Till GO, Kunkel R, et al: Evidence for role of hydroxyl radical in complement and neutrophil-dependent tissue injury. J Clin Invest 72: 789–795, 1983.
Varani J, Fligiel SEG, Till GO, et al: Pulmonary endothelial cell killing by human neutrophils. Possible involvement of hydroxyl radical. Lab Invest 53: 656–663, 1985.
Clark RA, Klebanoff SJ: Neutrophil-mediated tumor cell cytotoxicity. Role of the peroxidase system. J Exp Med 141: 1442–1450, 1975.
Weiss SJ, Slivka A: Monocyte and granulocyte-mediated tumor cell destruction. A role for the hydrogen peroxide-myeloperoxidase-chloride system. J Clin Invest 69: 255–262, 1982.
Jacobs AA, Paul BB, Strauss RR, et al: The role of the phagocyte in host-parasite interactions. XXIII. Relation of bactericidal activity to peroxidase-associated decarboxylation and deamination. Biochem Biophys Res Commun 39: 284–289, 1970.
Clark RA, Szot S, Williams MA, et al: Oxidation of lysine side chains of elastin by the my-eloperoxidase system and by stimulated human neutrophils. Biochem Biophys Res Commun 135: 451–457, 1986.
Drozdz R: Modification of proteins by the MPO-H2O2-C1- system, doctoral thesis, 1985.
Tsan MF, Chen JW: Oxidation of methionine by human polymorphonuclear leukocytes. J Clin Invest 65: 1041–1050, 1980.
Tsan MF: Myeloperoxidase-mediated oxidation of methionine and amino acid decarboxylation. Infect Immun 36: 136–141, 1982.
Silverstein RM, Hager LP: The chloroperoxidase-catalyzed oxidation of thiols and disulphides to sulfenyl chloride. Biochemistry 13: 5069–5073, 1974.
Matheson NR, Wong PS, Travis J: Enzymatic inactivation of human alpha-1-proteinase inhibitor by neutrophil myeloperoxidase. Biochem Biophys Res Commun 88: 402–409, 1979.
Matheson NR, Wong PS, Schuyler M, et al: Interaction of human a-1-proteinase inhibitor with neutrophil myeloperoxidase. Biochemistry 20: 331–336, 1981.
Alexander NM: Oxidative cleavage of tryptophanyl peptide bonds during chemical and peroxidase catalyzed iodinations. J Biol Chem 249: 1946–1952, 1974.
Rudie NG, Porter DJT, Bright HJ: Chlorination of an active site tyrosyl residue in D-amino acid oxidase by N-chloro-D-leucine. J Biol Chem 255: 498–506, 1980.
Weiss SJ, Peppin G, Ortiz X et al: Oxidative autoactivation of latent collagenase by human neutrophils. Science 227: 747–749, 1985.
Mello-Filho AC, Meneghini R: In vivo formation of single strand breaks in DNA by hydrogen peroxide is mediated by the Haber-Weiss reaction. Biochim Biophys Acta 781: 56–61, 1984.
Greenwald RA, Moy WW: Effect of oxygen-derived free radicals on hyaluronic acid. Arthritis Rheum 23: 455–458, 1980.
Sepe SM, Clark RA: Oxidant membrane injury by the neutrophil myeloperoxidase system. I. Characterization of a liposome model and injury by myeloperoxidase, hydrogen peroxide, and halides. J Immunol 134: 1888–1895, 1985.
Sepe SM, Clark RA: Oxidant membrane injury by the neutrophil myeloperoxidase system. II. Injury by stimulated neutrophils and protection by lipid-soluble antioxidants. J Immunol 134: 1896–1901, 1985.
Slater FF, Benedetto C: Free radical reactions in relation to lipid peroxidation, inflammation and prostaglandin metabolism, in Berti F, Velo GP (eds): The Prostaglandin System. New York, Plenum, 1981, pp 109–126.
Schauenstein E, Esterbauer H, Zollner R: Aldehydes in Biological Systems. London, Pion, 1977.
Selvaraj RJ, Zgliczynski JM, Paul BB et al: Chlorination of reduced nicotinamide adenine dinucle- otides by myeloperoxidase: A novel bactericidal mechanism. J Reticuloendothel Soc 27: 31 - 38, 1980.
Rosen H, Klebanoff SJ: Oxidation of Escherichia coli iron centers by the myeloperoxidase– mediated microbicidal system. J Biol Chem 257: 13731–13735, 1982.
Rosen H, Klebanoff SJ: Oxidation of microbial iron sulfur centers by the myeloperoxidase-H2O2- halide antimicrobial system. Infect Immun 47: 613–618, 1985.
Odajima T, Onishi M, Sato N: Metabolism of steroids by myeloperoxidase. Jpn J Oral Biol 23: 489–497, 1981.
Paredes JM, Weiss S: Human neutrophils transform prostaglandins by a myeloperoxidase-depen- dent mechanism. J Biol Chem 257: 2738–2740, 1982.
Onishi M, Odajima T: On the product of prostaglandin Ej oxidized by the myeloperoxidase- H2O2-chloride system. Jpn J Oral Biol 27: 291–298, 1985.
Henderson WR, Klebanoff SJ: Leukotriene production and inactivation by normal, chronic granulomatous disease and myeloperoxidase deficient neutrophils. J Biol Chem 258: 13522 - 13527, 1983.
Lee CW, Lewis RA, Tauber AI, et al: The myeloperoxidase-dependent metabolism of leukotrienes C4, D4 and E4 to 6-trans leukotriene B4 diastereoisomers and the subclass-specific S-di- astereoisomeric sulfoxides. J Biol Chem 258: 15004 - 15009, 1983.
Clark RA, Klebanoff SJ: Chemotactic factor inactivation by the myeloperoxidase-H202-halide system. J Clin Invest 64: 913 - 919, 1979.
Tsan MF, Denison RC: Oxidation of «-formyl methionine chemotactic peptide by human neutrophils. J Immunol 126: 1387 - 1389, 1981.
Hakanson L: Antiinflammatory effects of myeloperoxidase and eosinophil peroxidase, in Venge P, Lindbom A (eds): Inflammation. Stockholm, Almquist and Wiksell, 1985, pp 319 - 323.
Klebanoff SJ, Clark RA: The Neutrophil: Function and Clinical Disorders. Amsterdam, Elsevier- North Holland, 1978, pp 217 - 488.
Kobayashi M, Tanaka T, Usui T: Inactivation of lysosomal enzymes by the respiratory burst of PMN leukocytes. Possible involvement of myeloperoxidase-H202-halide system. J Lab Clin Med 100: 896 - 907, 1982.
Clark RA, Stone PJ, ElHag A, et al: Myeloperoxidase-catalyzed inactivation of a!-protease inhibitor by human neutrophils. J Biol Chem 256: 3348 - 3353, 1981.
Carp H, Janoff A: In vitro suppression of serum elastase-inhibitory capacity by reactive oxygen species generated by phagocytosing polymorphonuclear leukocytes. J Clin Invest 63: 793–797, 1979.
Lieberman J: Elastase, collagenase, emphysema and ai-antitrypsin deficiency. Chest 70: 62–67, 1976.
Adeniyi-Jones SK, Karnovsky ML: Oxidative decarboxylation of free and peptide-linked amino acids in phagocytizing guinea pig granulocytes. J Clin Invest 68: 365–373, 1981.
Wolff SP, Garner A, Dean RT: Free radicals, lipids and protein degradation. Trends Biochem Sci 11: 27–31, 1986.
Stadtman ER: Oxidation of proteins by mixed-function oxidation systems: implication in protein turnover, ageing and neutrophil function. Trends Biochem Sci 11: 11–12, 1986.
Payne JW, Tuffnell JM: Cleavage of peptide-bound methionine sulphoxide and methionine sul- phone: Possible role in enhanced proteolysis in Escherichia coli. FEMS Microbiol Lett 12:279– 282, 1981.
Bernlohr DA, Switzer RL: Reaction of Bacillus subtilis glutamine phosphoribosylpyrophosphate amidotransferase with oxygen. Chemistry and regulation by ligands. Biochemistry 20: 5675–5681, 1981.
Rivett AJ: Preferential degradation of the oxidatively modified form of glutamine synthetase by intracellular mammalian proteases. J Biol Chem 260: 300–305, 1985.
Offerman MK, McKay MJ, Marsh MW, Et Al: Glutathione disulphide inactivates, destabilizes and enhances proteolytic susceptibility of fructose 1,6-bis-phosphate aldolase. J Biol Chem 259:8886– 8891, 1984.
Sagone AL, Husney RM, O’Dorisio MS, et al: Mechanisms for the oxidation of reduced glutathione by stimulated granulocytes. Blood 63: 96–104, 1984.
Olszowska E, Olszowski S, Zgliczynski JM: Enhanced Susceptibility of chlorinated proteins to proteolysis, unpublished.
Devraede GJ, Taylor WF, Sauer WG, et al: Cancer risk and life expectancy of children with ulcerative colitis. N Engl J Med 285: 17–21, 1971.
Wlodkowski TJ, Rosenkranz HS: Mutagenicity of sodium hypochlorite for salmonella ty- phimurium. Mutat Res 31: 39–43, 1975.
Shih KL, Lederberg J: Chloramine mutagenesis in Bacillus subtilis. Science 192: 1141–1143, 1976.
Cheh AM, Skochdopole J, Koski P, et al: Nonvolatile mutagens in drinking water: Production by chlorination and destruction by sulfite. Science 207: 90–92, 1980.
Weitzman SA and Stossel TP: Mutation caused by human phagocytes. Science 212: 546–547, 1981.
Weitberg AB, Weitzman SA, Destrempes M, et al: Stimulated human phagocytes produce cytogenetic changes in cultured mammalian cells. N Engl J Med 308: 26–30, 1983.
Birnboim HC: DNA strand breakage in human leukocytes exposed to a tumor promoter, phorbol myristate acetate. Science 215: 1247–1249, 1982.
Dean RT, Roberts CR, Forni LG: Oxygen-centered free radicals can efficiently degrade the polypeptide of proteoglycans in whole cartilage. Biosci Rep 4: 1017–1021, 1984.
Dean RT, Wolff SP: Free radical damage to proteoglycans and proteins, in Venge P, Lindbom A (eds): Inflammation. Stockholm, Almquist and Wiskell, 1985, pp 289–297.
Clark RA, Szot S: The myeloperoxidase-hydrogen peroxidase-halide system as effector of neu- trophil-mediated tumor cell cytotoxicity. J Immunol 126: 1295–1301, 1982.
Gale RP, Zighelboim J: Polymorphonuclear leukocytes in antibody-dependent cellular cytotoxicity. J. Immunol 114: 1047–1052, 1975.
Zighelboim J, Gale RP, Kedar E: Polymorphonuclear leukocyte Fc receptors in antibody-dependent cellular cytotoxicity (ADCC). Transplantation 21: 524–530, 1976.
Clark RA, Klebanoff SJ: Studies on the mechanism of antibody-dependent polymorphonuclear leukocyte-mediated cytotoxicity. J Immunol 119: 1413–1418, 1977.
Hafeman DG, Lucas ZJ: Polymorphonuclear leukocyte-mediated, antibody-dependent, cellular cytotoxicity against tumor cells: Dependence on oxygen and the respiratory burst. J Immunol 123: 55–62, 1979.
Dallegri F, Frumento G, Minervini F: Role of the oxidative metabolic burst in the antibody- dependent cellular cytotoxicity mediated by neutrophil polymorphonuclears. Exp Hematol 10:859– 866, 1982.
Eaton JW, Kolpin CF, Swofford HS, et al: Chlorinated urban water: A cause of dialysis-induced hemolytic anemia. Science 181: 463–464, 1973.
Klebanoff SJ and Pincus SH: Hydrogen peroxide utilization in myeloperoxidase-deficient leucocytes: A possible microbicidal control mechanism. J Clin Invest 50: 2226–2229, 1971.
Rosen H, Klebanoff SJ: Chemiluminescence and superoxide production by myeloperoxidase- deficient leukocytes. J Clin Invest 58: 50–60, 1976.
Dri P, Soranzo MR, Cramer R, et al: Role of myeloperoxidase in respiratory burst of human polymorphonuclear leukocytes. Studies with myeloperoxidase-deficient subjects. Inflammation 9: 21–31, 1985.
Stendahl O, Coble BI, Dahlgren C, et al: Myeloperoxidase modulates the phagocytic activity of polymorphonuclear neutrophil leukocytes. Studies with cells from a myeloperoxidase-deficient patient. J Clin Invest 73: 366–373, 1984.
Coble BI, Dahlgren C, Hed J, et al: Myeloperoxidase reduces the opsonizing activity of immunoglobulin G and complement component C3b. Biochim Biophys Acta 802: 501–505, 1984.
Klebanoff SJ and Hamon CB: Role of myeloperoxidase-mediated antimicrobial systems in intact leucocytes. J Reticuloendothel Soc 12: 170–196, 1972.
DeChatelet LR, McPhail LC, Shirley PS: Effect of cyanide on NADPH oxidation by granules from human polymorphonuclear leucocytes. Blood 49: 445–454, 1977.
Cohen HJ, Chowaniec ME: Superoxide production by digitonin-stimulated guinea pig granulocytes. The effects of N-ethylmaleimide, divalent cations and glycolytic and mitochondrial inhibitors on the activation of the superoxide generating system. J Clin Invest 61: 1088–1096, 1978.
Beswick PH, Slater TF: Modification by metals, sulphydryl reagents and cyanide of the particle stimulated enhancement of oxygen consumption in bovine granulocytes. Chem Biol Interact 20: 373–382, 1978.
Reed PW: Glutathione and the hexose monophosphate shunt in phagocytizing and H202-treated rat leucocytes. J Biol Chem 244: 2459–2464, 1969.
Strauss RR, Paul BB, Jacobs AA, et al: The role of the phagocyte in host-parasite interactions. XIX. Leucocytic glutathione reductase and its involvement in phagocytosis. Arch Biochem Biophys 135: 265–271, 1969.
Hendricks SB, Taylorson RB: Breaking of seed dormancy by catalase inhibition. Proc Natl Acad Sci USA 72: 306–309, 1975.
Suzuki H, Kakinuma K: Evidence that NADPH is the actual substrate of the oxidase responsible for the “respiratory burst” of phagocytosing polymorphonuclear leukocytes. J Biochem 93: 709–715, 1983.
Cohen HJ, Chowaniec ME, Davies WE: Activation of the guinea pig granulocyte NAD(P)H- dependent superoxide generating enzyme: Localization in a plasma membrane enriched particle and kinetics of activation. Blood 55: 355–363, 1980.
Klebanoff SJ: Myeloperoxidase: Contribution to the microbicidal activity of intact leukocytes. Science 169: 1095–1097, 1970.
Edwards SW, Hallett MB, Campbell AK: Oxygen-radical production during inflammation may be limited by oxygen concentration. Biochem J 217: 851–854, 1984.
Britigan BE, Cohen MS: Effects of human serum on bacterial competition with neutrophils for molecular oxygen. Infect Immun 52: 657–663, 1986.
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© 1988 Plenum Press, New York
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Zgliczyński, J.M., Stelmaszyńska, T. (1988). The Respiratory Burst of Neutrophilic Granulocytes and Its Influence on Infected Tissues. In: Sbarra, A.J., Strauss, R.R. (eds) The Respiratory Burst and Its Physiological Significance. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-5496-3_15
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