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Volumn 122, Issue 1, 1997, Pages 188-192

Effect of aromatic nitroso-compounds on superoxide-generating activity in neutrophils

Author keywords

Human and porcine neutrophils; Inhibition; Nitroso compounds; Respiratory burst

Indexed keywords

CHEMOTACTIC PEPTIDE; ENZYME INHIBITOR; N NITROSOPYRROLIDINE; NITROPHENOL; NITROSO DERIVATIVE; NITROSOBENZENE; OXYGEN; PHORBOL 13 ACETATE 12 MYRISTATE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; SUPEROXIDE; TOLUENE DERIVATIVE;

EID: 0030786450     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a021727     Document Type: Article
Times cited : (9)

References (29)
  • 1
    • 0022976736 scopus 로고
    • Stoichiometric conversion of oxygen to superoxide anion during the respiratory burst in neutrophils: Direct evidence by a new method for measurement of superoxide anion with diacetyledeutoroheme-substituted horseradish peroxidase
    • Makino, R., Tanaka, T., Iizuka, T., Ishimura, Y., and Kanegasaki, S. (1986) Stoichiometric conversion of oxygen to superoxide anion during the respiratory burst in neutrophils: direct evidence by a new method for measurement of superoxide anion with diacetyledeutoroheme-substituted horseradish peroxidase. J. Biol. Chem. 261, 11444-11447
    • (1986) J. Biol. Chem. , vol.261 , pp. 11444-11447
    • Makino, R.1    Tanaka, T.2    Iizuka, T.3    Ishimura, Y.4    Kanegasaki, S.5
  • 2
    • 0017834531 scopus 로고
    • Oxygen-dependent microbial killing by phagocytes
    • Babior, B.M. (1978) Oxygen-dependent microbial killing by phagocytes. N. Engl. J. Med. 298, 659-668
    • (1978) N. Engl. J. Med. , vol.298 , pp. 659-668
    • Babior, B.M.1
  • 3
    • 0025756918 scopus 로고
    • Enzymic mechanisms of superoxide production
    • Cross, A.R. and Jones, O.T.G. (1991) Enzymic mechanisms of superoxide production. Biochim. Biophys. Acta 1057, 281-298
    • (1991) Biochim. Biophys. Acta , vol.1057 , pp. 281-298
    • Cross, A.R.1    Jones, O.T.G.2
  • 4
    • 0025992764 scopus 로고
    • The superoxide-generating oxidase of phagocytic cells. Physiological, molecular and pathological aspects
    • Morel, F., Doussiere, J., and Vignais, P.V. (1991) The superoxide-generating oxidase of phagocytic cells. Physiological, molecular and pathological aspects. Eur. J. Biochem. 201, 523-546
    • (1991) Eur. J. Biochem. , vol.201 , pp. 523-546
    • Morel, F.1    Doussiere, J.2    Vignais, P.V.3
  • 5
    • 0027189961 scopus 로고
    • The biochemical basis of the NADPH oxidase of phagocytes
    • Segal, A.W. and Abo, A. (1993) The biochemical basis of the NADPH oxidase of phagocytes. Trends Biochem. Sci. 18, 43-47
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 43-47
    • Segal, A.W.1    Abo, A.2
  • 9
    • 0025081316 scopus 로고
    • A 63-kilodalton cytosolic polypeptide involved in superoxide generation in porcine neutrophils
    • Tanaka, T., Imajoh-Ohmi, S., Kanegasaki, S., Takagi, Y., Makino, R., and Ishimura, Y. (1990) A 63-kilodalton cytosolic polypeptide involved in superoxide generation in porcine neutrophils. J. Biol. Chem. 265, 18717-18720
    • (1990) J. Biol. Chem. , vol.265 , pp. 18717-18720
    • Tanaka, T.1    Imajoh-Ohmi, S.2    Kanegasaki, S.3    Takagi, Y.4    Makino, R.5    Ishimura, Y.6
  • 10
    • 0026537078 scopus 로고
    • Cytosolic components involved in porcine neutrophil oxidase activation. Purification of a 47-kilodalton protein and reconstitution of the activation system
    • Tanaka, T., Makino, R., and Ishimura, Y. (1992) Cytosolic components involved in porcine neutrophil oxidase activation. Purification of a 47-kilodalton protein and reconstitution of the activation system. J. Biol. Chem. 267, 1239-1244
    • (1992) J. Biol. Chem. , vol.267 , pp. 1239-1244
    • Tanaka, T.1    Makino, R.2    Ishimura, Y.3
  • 12
    • 0028299331 scopus 로고
    • rac from its inhibitory GDP/GTP exchange protein (rhoGDI) followed by its translocation to the plasma membrane
    • rac from its inhibitory GDP/GTP exchange protein (rhoGDI) followed by its translocation to the plasma membrane. Biochem. J. (London) 298, 585-591
    • (1994) Biochem. J. (London) , vol.298 , pp. 585-591
    • Abo, A.1    Webb, M.R.2    Grogan, A.3    Segal, A.W.4
  • 15
    • 0011698432 scopus 로고
    • The combining power of normal human hemoglobin for nitrosobenzene
    • Murayama, M. (1960) The combining power of normal human hemoglobin for nitrosobenzene. J. Biol. Chem. 235, 1024-1028
    • (1960) J. Biol. Chem. , vol.235 , pp. 1024-1028
    • Murayama, M.1
  • 16
    • 0018099081 scopus 로고
    • Influence of ring substituents on the binding of nitrosobenzene by ferrohemoglobin
    • Hirota, K. and Itano, H.A. (1978) Influence of ring substituents on the binding of nitrosobenzene by ferrohemoglobin. J. Biol. Chem. 253, 3477-3481
    • (1978) J. Biol. Chem. , vol.253 , pp. 3477-3481
    • Hirota, K.1    Itano, H.A.2
  • 17
    • 0023143235 scopus 로고
    • Reaction of para-substituted nitrosobenzene with human hemoglobin
    • Eyer, P. and Ascherl, M. (1987) Reaction of para-substituted nitrosobenzene with human hemoglobin. Biol. Chem. Hoppe-Seyler 368, 285-294
    • (1987) Biol. Chem. Hoppe-Seyler , vol.368 , pp. 285-294
    • Eyer, P.1    Ascherl, M.2
  • 19
    • 0025854869 scopus 로고
    • Formation of prostaglandin synthase-iron-nitrosoalkane inhibitory complexes upon in situ oxidation of N-substituted hydroxylamines
    • Mahy, J.P. and Mansuy, D. (1991) Formation of prostaglandin synthase-iron-nitrosoalkane inhibitory complexes upon in situ oxidation of N-substituted hydroxylamines. Biochemistry 30, 4165-4172
    • (1991) Biochemistry , vol.30 , pp. 4165-4172
    • Mahy, J.P.1    Mansuy, D.2
  • 20
    • 0022414641 scopus 로고
    • Studies on neutrophil b-type cytochrome in situ by low temperature absorption spectroscopy
    • Iizuka, T., Kanegasaki, S., Makino, R., Tanaka, T., and Ishimura, Y. (1985) Studies on neutrophil b-type cytochrome in situ by low temperature absorption spectroscopy. J. Biol. Chem. 260, 12049-12053
    • (1985) J. Biol. Chem. , vol.260 , pp. 12049-12053
    • Iizuka, T.1    Kanegasaki, S.2    Makino, R.3    Tanaka, T.4    Ishimura, Y.5
  • 21
    • 0015816824 scopus 로고
    • "Aromatic" substituent constants for structure-activity correlations
    • Hansch, C., Leo, A., Unger, S.H., Kim, K.H., Nikaitani, D., and Lien, E.J. (1973) "Aromatic" substituent constants for structure-activity correlations. J. Med. Chem. 16, 1207-1216
    • (1973) J. Med. Chem. , vol.16 , pp. 1207-1216
    • Hansch, C.1    Leo, A.2    Unger, S.H.3    Kim, K.H.4    Nikaitani, D.5    Lien, E.J.6
  • 22
    • 0021751316 scopus 로고
    • ADP-ribosylation of the specific membrane protein by islet-activating protein, pertussis toxin, associated with inhibition of a chemotactic peptide-induced arachidonate release in neutrophils
    • Okajima, F. and Ui, M. (1984) ADP-ribosylation of the specific membrane protein by islet-activating protein, pertussis toxin, associated with inhibition of a chemotactic peptide-induced arachidonate release in neutrophils. J. Biol. Chem. 259, 13863-13871
    • (1984) J. Biol. Chem. , vol.259 , pp. 13863-13871
    • Okajima, F.1    Ui, M.2
  • 23
    • 0022343276 scopus 로고
    • 2+ mobilization in guinea pig neutrophils
    • 2+ mobilization in guinea pig neutrophils. J. Biol. Chem. 260, 15771-15780
    • (1985) J. Biol. Chem. , vol.260 , pp. 15771-15780
    • Ohta, H.1    Okajima, F.2    Ui, M.3
  • 24
    • 0022003812 scopus 로고
    • Pertussis toxin inhibits fMet-Leu-Phe- but not phorbol ester-stimulated changes in rabbit neutrophils: Role of G proteins in excitation response coupling
    • Volpi, M., Naccache, P.H., Molski, T.F.P., Shefcyk, J., Huang, C.K., Marsh, M.L., Munoz, J., Becker, E.L., and Scha'afi, R.I. (1985) Pertussis toxin inhibits fMet-Leu-Phe- but not phorbol ester-stimulated changes in rabbit neutrophils: role of G proteins in excitation response coupling. Proc. Natl. Acad. Sci. USA 82, 2708-2712
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 2708-2712
    • Volpi, M.1    Naccache, P.H.2    Molski, T.F.P.3    Shefcyk, J.4    Huang, C.K.5    Marsh, M.L.6    Munoz, J.7    Becker, E.L.8    Scha'afi, R.I.9
  • 25
    • 0021358832 scopus 로고
    • Diacylglycerol, 1-oleoyl-2-acetyl-glycerol, stimulates superoxide-generation from human neutrophils
    • Fujita, I., Irita, K., Takeshige, K., and Minakami, S. (1984) Diacylglycerol, 1-oleoyl-2-acetyl-glycerol, stimulates superoxide-generation from human neutrophils. Biochem. Biophys. Res. Commun. 120, 318-324
    • (1984) Biochem. Biophys. Res. Commun. , vol.120 , pp. 318-324
    • Fujita, I.1    Irita, K.2    Takeshige, K.3    Minakami, S.4
  • 26
    • 0024366833 scopus 로고
    • Inhibitory effect of antibiotic cerulenin on the respiratory burst in phagocytes. I. Effects of cerulenin on active oxygen-generation and lipid metabolism in phagocytes
    • Nakata, M., Tomita, T., and Kanegasaki, S. (1989) Inhibitory effect of antibiotic cerulenin on the respiratory burst in phagocytes. I. Effects of cerulenin on active oxygen-generation and lipid metabolism in phagocytes. J. Antibiot. 42, 1171-1177
    • (1989) J. Antibiot. , vol.42 , pp. 1171-1177
    • Nakata, M.1    Tomita, T.2    Kanegasaki, S.3
  • 27
    • 0024349753 scopus 로고
    • Inhibitory effect of antibiotic cerulenin on the respiratory burst in phagocytes. II. Inhibition by cerulenin of intracellular calcium mobilization in human neutrophils
    • Nakata, M., Tomita, T., Iizuka, T., and Kanegasaki, S. (1989) Inhibitory effect of antibiotic cerulenin on the respiratory burst in phagocytes. II. Inhibition by cerulenin of intracellular calcium mobilization in human neutrophils. J. Antibiot. 42, 1178-1183
    • (1989) J. Antibiot. , vol.42 , pp. 1178-1183
    • Nakata, M.1    Tomita, T.2    Iizuka, T.3    Kanegasaki, S.4
  • 29
    • 0030873482 scopus 로고    scopus 로고
    • Mechanisms of nitroso compound-induced inhibition of superoxide generation in neutrophils
    • in press
    • Nasuda-Kouyama, A., Nakata, M., Iizuka, T., and Isogai, Y. (1997) Mechanisms of nitroso compound-induced inhibition of superoxide generation in neutrophils. J. Biochem., in press
    • (1997) J. Biochem.
    • Nasuda-Kouyama, A.1    Nakata, M.2    Iizuka, T.3    Isogai, Y.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.