메뉴 건너뛰기




Volumn 217, Issue 1, 1998, Pages 81-88

Exposure of macrophages to an enzymatically inactive macrophage mannose receptor ligand augments killing of Candida albicans

Author keywords

[No Author keywords available]

Indexed keywords

MYELOPEROXIDASE;

EID: 0031973427     PISSN: 00379727     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (24)

References (37)
  • 1
    • 0025931052 scopus 로고
    • Liposomal hamycin: Reduced toxicity and improved antifungal efficacy in vitro and in vivo
    • Mehta RT, McQueen TJ, Keyhani A, Lopez-Berestein G. Liposomal hamycin: Reduced toxicity and improved antifungal efficacy in vitro and in vivo. J Infect Dis 164:1003-1006, 1991.
    • (1991) J Infect Dis , vol.164 , pp. 1003-1006
    • Mehta, R.T.1    McQueen, T.J.2    Keyhani, A.3    Lopez-Berestein, G.4
  • 2
    • 0026569695 scopus 로고
    • Interaction and intracellular killing of Candida albicans blastospores by human polymorphonuclear leukocytes, monocytes, and monocyte-derived macrophages in aerobic and anaerobic conditions
    • Thompson HL, Wilton JMA. Interaction and intracellular killing of Candida albicans blastospores by human polymorphonuclear leukocytes, monocytes, and monocyte-derived macrophages in aerobic and anaerobic conditions. Clin Exp Immunol 87:316-321, 1991.
    • (1991) Clin Exp Immunol , vol.87 , pp. 316-321
    • Thompson, H.L.1    Wilton, J.M.A.2
  • 3
    • 0028002452 scopus 로고
    • Candida species and virulence
    • Odds FC. Candida species and virulence. ASM News 60:313-318, 1994.
    • (1994) ASM News , vol.60 , pp. 313-318
    • Odds, F.C.1
  • 4
    • 0028568541 scopus 로고
    • The emerging fungal threat
    • Sternberg S. The emerging fungal threat. Science 266:1632-1634, 1994.
    • (1994) Science , vol.266 , pp. 1632-1634
    • Sternberg, S.1
  • 5
    • 0028224943 scopus 로고
    • The role of cell-mediated immunity in candidiasis
    • Fidel PL, Sobel JD. The role of cell-mediated immunity in candidiasis. Trends Microbiol 2:202-206, 1994.
    • (1994) Trends Microbiol , vol.2 , pp. 202-206
    • Fidel, P.L.1    Sobel, J.D.2
  • 7
    • 0022633452 scopus 로고
    • Immunomodulation by neutrophil myeloperoxidase and hydrogen peroxide: Differential susceptibility of human lymphocyte functions
    • El-Hag A, Lipsky PE, Bennett M, Clark RA. Immunomodulation by neutrophil myeloperoxidase and hydrogen peroxide: Differential susceptibility of human lymphocyte functions. J Immunol 136:3420-3426, 1986.
    • (1986) J Immunol , vol.136 , pp. 3420-3426
    • El-Hag, A.1    Lipsky, P.E.2    Bennett, M.3    Clark, R.A.4
  • 8
    • 0018572710 scopus 로고
    • Early degranulation of human neutrophils: Immunocytochemical studies of surface and intracellular phagocytic events
    • Pryzwansky KB, MacRae EK, Spitznagel JK, Cooney MH. Early degranulation of human neutrophils: Immunocytochemical studies of surface and intracellular phagocytic events. Cell 18:1025-1033, 1979.
    • (1979) Cell , vol.18 , pp. 1025-1033
    • Pryzwansky, K.B.1    MacRae, E.K.2    Spitznagel, J.K.3    Cooney, M.H.4
  • 9
    • 0019997889 scopus 로고
    • Cellular and extracellular myeloperoxidase in pyogenic inflammation
    • Bradley PP, Christensen RD, Rothstein G. Cellular and extracellular myeloperoxidase in pyogenic inflammation. Blood 60:618-622, 1982.
    • (1982) Blood , vol.60 , pp. 618-622
    • Bradley, P.P.1    Christensen, R.D.2    Rothstein, G.3
  • 10
    • 0025891959 scopus 로고
    • Structural and biological properties of human recombinant myeloperoxidase produced by Chinese hamster ovary cell lines
    • Moguilevsky N, Garcia-Quintana L, Jacquet A, Tournay C, Fabry L, Pierard L, Bollen A. Structural and biological properties of human recombinant myeloperoxidase produced by Chinese hamster ovary cell lines. Eur J Biochem 197:605-614, 1991.
    • (1991) Eur J Biochem , vol.197 , pp. 605-614
    • Moguilevsky, N.1    Garcia-Quintana, L.2    Jacquet, A.3    Tournay, C.4    Fabry, L.5    Pierard, L.6    Bollen, A.7
  • 11
    • 0025407762 scopus 로고
    • Clearance of neutrophil-derived myeloperoxidase by the macrophage mannose receptor
    • Shepherd VL, Hoidal J. Clearance of neutrophil-derived myeloperoxidase by the macrophage mannose receptor. Am J Respir Cell Mol Biol 2:235-340, 1990.
    • (1990) Am J Respir Cell Mol Biol , vol.2 , pp. 235-340
    • Shepherd, V.L.1    Hoidal, J.2
  • 12
    • 0040994892 scopus 로고
    • Plasma membrane markers to study differentiation, activation, and localization of murine macrophages: Ag F4/80 and the mannosyl, fucosyl receptor
    • Weir DM, Herzenberg LA, Blackwell C, Herzenberg LA, Eds. Oxford, London: Alden Press
    • Gordon S, Starkey PM, Hume D, Ezekowitz RAB, Hirsch S, Austyn J. Plasma membrane markers to study differentiation, activation, and localization of murine macrophages: Ag F4/80 and the mannosyl, fucosyl receptor. In: Weir DM, Herzenberg LA, Blackwell C, Herzenberg LA, Eds. Handbook of Experimental Immunology, 2nd edition. Oxford, London: Alden Press, pp43.1-43.15, 1986.
    • (1986) Handbook of Experimental Immunology, 2nd Edition
    • Gordon, S.1    Starkey, P.M.2    Hume, D.3    Ezekowitz, R.A.B.4    Hirsch, S.5    Austyn, J.6
  • 13
    • 0026561385 scopus 로고
    • The macrophage mannose receptor and other macrophage lectins
    • Stahl PD. The macrophage mannose receptor and other macrophage lectins. Cur Opin Immunol 4:49-52, 1992.
    • (1992) Cur Opin Immunol , vol.4 , pp. 49-52
    • Stahl, P.D.1
  • 14
    • 0026068240 scopus 로고
    • Induction of tumor necrosis factor and macrophage-mediated cytotoxicity by horseradish peroxidase and other glycosylated proteins: The role of enzymatic activity and LPS
    • Lefkowitz DL, Mills K, Castro A, Lefkowitz SS. Induction of tumor necrosis factor and macrophage-mediated cytotoxicity by horseradish peroxidase and other glycosylated proteins: The role of enzymatic activity and LPS. J Leukoc Biol 50:615-623, 1991.
    • (1991) J Leukoc Biol , vol.50 , pp. 615-623
    • Lefkowitz, D.L.1    Mills, K.2    Castro, A.3    Lefkowitz, S.S.4
  • 17
    • 0029894461 scopus 로고    scopus 로고
    • Phagocytosis and intracellular killing of Candida albicans by macrophages exposed to myeloperoxidases
    • Lefkowitz SS, Gelderman MP, Lefkowitz DL, Moguilevsky N, Bollen A. Phagocytosis and intracellular killing of Candida albicans by macrophages exposed to myeloperoxidases. J Infect Dis 173:1202-1207, 1996.
    • (1996) J Infect Dis , vol.173 , pp. 1202-1207
    • Lefkowitz, S.S.1    Gelderman, M.P.2    Lefkowitz, D.L.3    Moguilevsky, N.4    Bollen, A.5
  • 18
    • 0024600608 scopus 로고
    • Uptake of human eosinophil peroxidase and myeloperoxidase by cells involved in the inflammatory process
    • Zabucchi G, Soranzo MR, Menegazzi R, Bertoncin P, Nardon E, Patriarca P. Uptake of human eosinophil peroxidase and myeloperoxidase by cells involved in the inflammatory process. J Histochem Cytochem 37(4):449-508, 1989.
    • (1989) J Histochem Cytochem , vol.37 , Issue.4 , pp. 449-508
    • Zabucchi, G.1    Soranzo, M.R.2    Menegazzi, R.3    Bertoncin, P.4    Nardon, E.5    Patriarca, P.6
  • 19
    • 0030897090 scopus 로고    scopus 로고
    • Secretion and inactivation of myeloperoxidase by isolated neutrophils
    • King CC, Jefferson MM, Thomas EL. Secretion and inactivation of myeloperoxidase by isolated neutrophils. J Leukoc Biol 61:293-302, 1997.
    • (1997) J Leukoc Biol , vol.61 , pp. 293-302
    • King, C.C.1    Jefferson, M.M.2    Thomas, E.L.3
  • 20
    • 0023882065 scopus 로고
    • Immunological detection of myeloperoxidase in synovial fluid from patients with rheumatoid arthritis
    • Edwards SW, Hughes V, Barlow J, Bucknall R. Immunological detection of myeloperoxidase in synovial fluid from patients with rheumatoid arthritis. J Biochem 250:81-85, 1988.
    • (1988) J Biochem , vol.250 , pp. 81-85
    • Edwards, S.W.1    Hughes, V.2    Barlow, J.3    Bucknall, R.4
  • 22
    • 0021742157 scopus 로고
    • Quantitative assay for acute intestinal inflammation based on myeloperoxidase activity
    • Krawisz JE, Sharon P, Stenson WF. Quantitative assay for acute intestinal inflammation based on myeloperoxidase activity. Gastroenterology 87:1322-1350, 1984.
    • (1984) Gastroenterology , vol.87 , pp. 1322-1350
    • Krawisz, J.E.1    Sharon, P.2    Stenson, W.F.3
  • 23
    • 0022928046 scopus 로고
    • Activation of macrophages with oxidative enzymes
    • DiSabato G, Everse J, Eds. Orlando: Academic Press
    • Lefkowitz DL, Lefkowitz SS, Wei RQ, Everse J. Activation of macrophages with oxidative enzymes. In: DiSabato G, Everse J, Eds. Methods in Enzymology. Orlando: Academic Press, pp537-548, 1986.
    • (1986) Methods in Enzymology , pp. 537-548
    • Lefkowitz, D.L.1    Lefkowitz, S.S.2    Wei, R.Q.3    Everse, J.4
  • 24
    • 0018758864 scopus 로고
    • Phagocytosis and intracellular killing of pathogenic yeasts by human monocytes and neutrophils
    • Schuit KE. Phagocytosis and intracellular killing of pathogenic yeasts by human monocytes and neutrophils. Infect Immun 24:932-938, 1979.
    • (1979) Infect Immun , vol.24 , pp. 932-938
    • Schuit, K.E.1
  • 25
    • 0021866415 scopus 로고
    • Antimicrobial activities of dialysate-elicited and resident human peritoneal macrophages
    • Peterson KP, Gaziano E, Suh HJ, Devalon M, Peterson L, Keane WF. Antimicrobial activities of dialysate-elicited and resident human peritoneal macrophages. Infect Immun 49:212-218, 1985.
    • (1985) Infect Immun , vol.49 , pp. 212-218
    • Peterson, K.P.1    Gaziano, E.2    Suh, H.J.3    Devalon, M.4    Peterson, L.5    Keane, W.F.6
  • 26
    • 0023227275 scopus 로고
    • Plasmid-mediated resistance to phagocytosis in Yersinia enterolitica
    • Lian C-J, Hwang WS, Pai CH. Plasmid-mediated resistance to phagocytosis in Yersinia enterolitica. Infect Immun 55:1176-1183, 1987.
    • (1987) Infect Immun , vol.55 , pp. 1176-1183
    • Lian, C.-J.1    Hwang, W.S.2    Pai, C.H.3
  • 27
    • 0018849665 scopus 로고
    • Macrophage microbicidal activity
    • Sasada M, Johnston RB. Macrophage microbicidal activity. J Exp Med 152:85-98, 1980.
    • (1980) J Exp Med , vol.152 , pp. 85-98
    • Sasada, M.1    Johnston, R.B.2
  • 29
    • 0024438603 scopus 로고
    • Uptake and utilization of human polymorphonuclear leukocyte granule myeloperoxidase by mouse peritoneal macrophages
    • Leung K-P, Goren MB. Uptake and utilization of human polymorphonuclear leukocyte granule myeloperoxidase by mouse peritoneal macrophages. Cell Tissue Res 257:653-656, 1989.
    • (1989) Cell Tissue Res , vol.257 , pp. 653-656
    • Leung, K.-P.1    Goren, M.B.2
  • 31
    • 0020661782 scopus 로고
    • Yeast mannans inhibit binding and phagocytosis of zymosan by mouse peritoneal macrophages
    • Sung SJ, Nelson RS, Silverstein SC. Yeast mannans inhibit binding and phagocytosis of zymosan by mouse peritoneal macrophages. J Cell Biol 96:160-166, 1983.
    • (1983) J Cell Biol , vol.96 , pp. 160-166
    • Sung, S.J.1    Nelson, R.S.2    Silverstein, S.C.3
  • 32
    • 0021827129 scopus 로고
    • Fluid phase and mannose receptor-mediated uptake of horseradish peroxidase in mouse bone marrow-derived macrophages: Biochemical and ultrastructural study
    • Lang T, de Chastellier C. Fluid phase and mannose receptor-mediated uptake of horseradish peroxidase in mouse bone marrow-derived macrophages: Biochemical and ultrastructural study. Biol Cell 53:149-154, 1985.
    • (1985) Biol Cell , vol.53 , pp. 149-154
    • Lang, T.1    De Chastellier, C.2
  • 33
    • 0027963465 scopus 로고
    • Site-directed mutagenesis of human myeloperoxidase: Further identification of residues involved in catalytic activity and heme interaction
    • Jacquet A, Garcia-Quintana L, Deleersnyder V, Fenna R, Bollen A, Moguilevsky N. Site-directed mutagenesis of human myeloperoxidase: Further identification of residues involved in catalytic activity and heme interaction. Biochem Biophys Res Comm 202:73-81, 1994.
    • (1994) Biochem Biophys Res Comm , vol.202 , pp. 73-81
    • Jacquet, A.1    Garcia-Quintana, L.2    Deleersnyder, V.3    Fenna, R.4    Bollen, A.5    Moguilevsky, N.6
  • 34
    • 0026508876 scopus 로고
    • Contribution to ligand binding by multiple carbohydrate-recognition domains in the macrophage mannose receptor
    • Taylor ME, Bezouska K, Drickamer K. Contribution to ligand binding by multiple carbohydrate-recognition domains in the macrophage mannose receptor. J Biol Chem 3:1719-1726, 1992.
    • (1992) J Biol Chem , vol.3 , pp. 1719-1726
    • Taylor, M.E.1    Bezouska, K.2    Drickamer, K.3
  • 35
    • 0027535749 scopus 로고
    • Structural requirements for high affinity binding of complex ligands by the macrophage mannose receptor
    • Taylor ME, Drickamer K. Structural requirements for high affinity binding of complex ligands by the macrophage mannose receptor. J Biol Chem 1:399-404, 1993.
    • (1993) J Biol Chem , vol.1 , pp. 399-404
    • Taylor, M.E.1    Drickamer, K.2
  • 36
    • 0026165935 scopus 로고
    • Human neutrophils produce free radicals from the cell-zymosan interface during phagocytosis and from the whole plasma membrane when stimulated with calcium ionophore A23187
    • Hiral K, Moriguchi K, Wang GY. Human neutrophils produce free radicals from the cell-zymosan interface during phagocytosis and from the whole plasma membrane when stimulated with calcium ionophore A23187. Exp Cell Res 194:19-27, 1991.
    • (1991) Exp Cell Res , vol.194 , pp. 19-27
    • Hiral, K.1    Moriguchi, K.2    Wang, G.Y.3
  • 37
    • 0023223828 scopus 로고
    • Oxidative inactivation of myeloperoxidase released from human neutrophils
    • Edwards SW, Nurcombe HL, Hart CA. Oxidative inactivation of myeloperoxidase released from human neutrophils. Biochem J 245:925-928, 1987.
    • (1987) Biochem J , vol.245 , pp. 925-928
    • Edwards, S.W.1    Nurcombe, H.L.2    Hart, C.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.