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Volumn 38, Issue 11, 2008, Pages 3060-3067

Nramp1-functionality increases iNOS expression via repression of IL-10 formation

Author keywords

Macrophage; Nitric oxide; Nramp1; Salmonella; Slc11a1

Indexed keywords

GAMMA INTERFERON; INDUCIBLE NITRIC OXIDE SYNTHASE; INTERLEUKIN 10; IRON; NATURAL RESISTANCE ASSOCIATED MACROPHAGE PROTEIN 1; NITRIC OXIDE; STAT3 PROTEIN; SUPPRESSOR OF CYTOKINE SIGNALING; TUMOR NECROSIS FACTOR ALPHA; CATION TRANSPORT PROTEIN; NATURAL RESISTANCE-ASSOCIATED MACROPHAGE PROTEIN 1; STAT3 PROTEIN, MOUSE; UNCLASSIFIED DRUG;

EID: 58149345129     PISSN: 00142980     EISSN: 15214141     Source Type: Journal    
DOI: 10.1002/eji.200838449     Document Type: Article
Times cited : (55)

References (47)
  • 1
    • 0027262167 scopus 로고
    • Natural resistance to infection with intracellular parasites: Isolation of a candidate for Bcg
    • Vidal, S. M., Malo, D., Vogan, K., Skamene, E. and Gros, P., Natural resistance to infection with intracellular parasites: Isolation of a candidate for Bcg. Cell 1993. 73: 469-485.
    • (1993) Cell , vol.73 , pp. 469-485
    • Vidal, S.M.1    Malo, D.2    Vogan, K.3    Skamene, E.4    Gros, P.5
  • 2
    • 0029092312 scopus 로고
    • The Ity/Lsh/Bcg locus: Natural resistance to infection with intracellular parasites is abrogated by disruption of the Nramp1 gene
    • Vidal, S., Tremblay, M. L., Govoni, G., Gauthier, S., Sebastiani, G., Malo, D., Skamene, E. et al., The Ity/Lsh/Bcg locus: Natural resistance to infection with intracellular parasites is abrogated by disruption of the Nramp1 gene. J. Exp. Med. 1995. 182: 655-666.
    • (1995) J. Exp. Med , vol.182 , pp. 655-666
    • Vidal, S.1    Tremblay, M.L.2    Govoni, G.3    Gauthier, S.4    Sebastiani, G.5    Malo, D.6    Skamene, E.7
  • 3
    • 4744371619 scopus 로고    scopus 로고
    • Incomplete glycosylation and defective intracellular targeting of mutant solute carrier family 11 member 1 (Slc11a1)
    • White, J. K., Stewart, A., Popoff, J. F., Wilson, S. and Blackwell, J. M., Incomplete glycosylation and defective intracellular targeting of mutant solute carrier family 11 member 1 (Slc11a1). Biochem. J. 2004. 382: 811-819.
    • (2004) Biochem. J , vol.382 , pp. 811-819
    • White, J.K.1    Stewart, A.2    Popoff, J.F.3    Wilson, S.4    Blackwell, J.M.5
  • 4
    • 0032485353 scopus 로고    scopus 로고
    • Variations in the NRAMP1 gene and susceptibility to tuberculosis in West Africans
    • Bellamy, R., Ruwende, C., Corrah, T., McAdam, K. P., Whittle, H. C. and Hill, A. V., Variations in the NRAMP1 gene and susceptibility to tuberculosis in West Africans. N. Engl. J. Med. 1998. 338: 640-644.
    • (1998) N. Engl. J. Med , vol.338 , pp. 640-644
    • Bellamy, R.1    Ruwende, C.2    Corrah, T.3    McAdam, K.P.4    Whittle, H.C.5    Hill, A.V.6
  • 6
    • 0010412593 scopus 로고    scopus 로고
    • Differential iron transport into phagosomes isolated from the RAW264.7 macrophage cell lines transfected with Nramp1Gly169 or Nramp1Asp169
    • Kuhn, D. E., Baker, B. D., Lafuse, W. P. and Zwilling, B. S., Differential iron transport into phagosomes isolated from the RAW264.7 macrophage cell lines transfected with Nramp1Gly169 or Nramp1Asp169. J. Leukoc. Biol. 1999. 66: 113-119.
    • (1999) J. Leukoc. Biol , vol.66 , pp. 113-119
    • Kuhn, D.E.1    Baker, B.D.2    Lafuse, W.P.3    Zwilling, B.S.4
  • 7
    • 0034613681 scopus 로고    scopus 로고
    • Natural resistance to intracellular infections: Natural resistance-associated macrophage protein 1 (Nramp1) functions as a pH-dependent manganese transporter at the phagosomal membrane
    • Jabado, N., Jankowski, A., Dougaparsad, S., Picard, V., Grinstein, S. and Gros, P., Natural resistance to intracellular infections: Natural resistance-associated macrophage protein 1 (Nramp1) functions as a pH-dependent manganese transporter at the phagosomal membrane. J. Exp. Med. 2000. 192: 1237-1248.
    • (2000) J. Exp. Med , vol.192 , pp. 1237-1248
    • Jabado, N.1    Jankowski, A.2    Dougaparsad, S.3    Picard, V.4    Grinstein, S.5    Gros, P.6
  • 8
    • 0035154676 scopus 로고    scopus 로고
    • Iron transport into mycobacterium avium-containing phagosomes from an Nramp1(Gly169)-transfected RAW264.7 macrophage cell line
    • Kuhn, D. E., Lafuse, W. P. and Zwilling, B. S., Iron transport into mycobacterium avium-containing phagosomes from an Nramp1(Gly169)-transfected RAW264.7 macrophage cell line. J. Leukoc. Biol. 2001. 69: 43-49.
    • (2001) J. Leukoc. Biol , vol.69 , pp. 43-49
    • Kuhn, D.E.1    Lafuse, W.P.2    Zwilling, B.S.3
  • 9
    • 0019847498 scopus 로고
    • Superoxide-dependent formation of hydroxyl radicals in the presence of iron salts. Detection of 'free' iron in biological systems by using bleomycin-dependent degradation of DNA
    • Gutteridge, J. M., Rowley, D. A. and Halliwell, B., Superoxide-dependent formation of hydroxyl radicals in the presence of iron salts. Detection of 'free' iron in biological systems by using bleomycin-dependent degradation of DNA. Biochem. J. 1981. 199: 263-265.
    • (1981) Biochem. J , vol.199 , pp. 263-265
    • Gutteridge, J.M.1    Rowley, D.A.2    Halliwell, B.3
  • 10
    • 0034945912 scopus 로고    scopus 로고
    • Nramp1 modulates iron homoeostasis in vivo and in vitro: Evidence for a role in cellular iron release involving de-acidification of intracellular vesicles
    • Biggs, T. E., Baker, S. T., Botham, M. S., Dhital, A., Barton, C. H. and Perry, V. H., Nramp1 modulates iron homoeostasis in vivo and in vitro: Evidence for a role in cellular iron release involving de-acidification of intracellular vesicles. Eur. J. Immunol. 2001. 31: 2060-2070.
    • (2001) Eur. J. Immunol , vol.31 , pp. 2060-2070
    • Biggs, T.E.1    Baker, S.T.2    Botham, M.S.3    Dhital, A.4    Barton, C.H.5    Perry, V.H.6
  • 11
    • 0036534742 scopus 로고    scopus 로고
    • Solute carrier 11a1 (Slc11a1; formerly Nramp1) regulates metabolism and release of iron acquired by phagocytic, but not transferrin-receptor-mediated, iron uptake
    • Mulero, V., Searle, S., Blackwell, J. M. and Brock, J. H., Solute carrier 11a1 (Slc11a1; formerly Nramp1) regulates metabolism and release of iron acquired by phagocytic, but not transferrin-receptor-mediated, iron uptake. Biochem. J. 2002. 363: 89-94.
    • (2002) Biochem. J , vol.363 , pp. 89-94
    • Mulero, V.1    Searle, S.2    Blackwell, J.M.3    Brock, J.H.4
  • 13
    • 0032997261 scopus 로고    scopus 로고
    • Iron loading and disease surveillance
    • Weinberg, E. D., Iron loading and disease surveillance. Emerg. Infect. Dis. 1999. 5: 346-352.
    • (1999) Emerg. Infect. Dis , vol.5 , pp. 346-352
    • Weinberg, E.D.1
  • 16
    • 0032055833 scopus 로고    scopus 로고
    • Response of monocyte iron regulatory protein activity to inflammation: Abnormal behavior in genetic hemochromatosis
    • Recalcati, S., Pometta, R., Levi, S., Conte, D. and Cairo, G., Response of monocyte iron regulatory protein activity to inflammation: abnormal behavior in genetic hemochromatosis. Blood 1998. 91: 2565-2572.
    • (1998) Blood , vol.91 , pp. 2565-2572
    • Recalcati, S.1    Pometta, R.2    Levi, S.3    Conte, D.4    Cairo, G.5
  • 17
    • 0033563095 scopus 로고    scopus 로고
    • Central role of transcription factor NF-IL6 for cytokine and iron-mediated regulation of murine inducible nitric oxide synthase expression
    • Dlaska, M. and Weiss, G., Central role of transcription factor NF-IL6 for cytokine and iron-mediated regulation of murine inducible nitric oxide synthase expression. J. Immunol. 1999. 162: 6171-6177.
    • (1999) J. Immunol , vol.162 , pp. 6171-6177
    • Dlaska, M.1    Weiss, G.2
  • 18
    • 0030911247 scopus 로고    scopus 로고
    • Functional requirement of the hypoxia-responsive element in the activation of the inducible nitric oxide synthase promoter by the iron chelator desferrioxamine
    • Melillo, G., Taylor, L. S., Brooks, A., Musso, T., Cox, G. W. and Varesio, L., Functional requirement of the hypoxia-responsive element in the activation of the inducible nitric oxide synthase promoter by the iron chelator desferrioxamine. J. Biol. Chem. 1997. 272: 12236-12243.
    • (1997) J. Biol. Chem , vol.272 , pp. 12236-12243
    • Melillo, G.1    Taylor, L.S.2    Brooks, A.3    Musso, T.4    Cox, G.W.5    Varesio, L.6
  • 20
    • 0034769118 scopus 로고    scopus 로고
    • Nitric oxide and the immune response
    • Bogdan, C., Nitric oxide and the immune response. Nat. Immunol. 2001. 2: 907-916.
    • (2001) Nat. Immunol , vol.2 , pp. 907-916
    • Bogdan, C.1
  • 22
    • 0028100281 scopus 로고
    • Nitrite production by macrophages derived from BCG-resistant and -susceptible congenic mouse strains in response to IFN-gamma and infection with BCG
    • Barrera, L. F., Kramnik, I., Skamene, E. and Radzioch, D., Nitrite production by macrophages derived from BCG-resistant and -susceptible congenic mouse strains in response to IFN-gamma and infection with BCG. Immunology 1994. 82: 457-464.
    • (1994) Immunology , vol.82 , pp. 457-464
    • Barrera, L.F.1    Kramnik, I.2    Skamene, E.3    Radzioch, D.4
  • 23
    • 0029258822 scopus 로고
    • Nramp transfection transfers Ity/Lsh/Bcg-related pleiotropic effects on macrophage activation: Influence on oxidative burst and nitric oxide pathways
    • Barton, C. H., Whitehead, S. H. and Blackwell, J. M., Nramp transfection transfers Ity/Lsh/Bcg-related pleiotropic effects on macrophage activation: Influence on oxidative burst and nitric oxide pathways. Mol. Med. 1995. 1: 267-279.
    • (1995) Mol. Med , vol.1 , pp. 267-279
    • Barton, C.H.1    Whitehead, S.H.2    Blackwell, J.M.3
  • 24
    • 0043136713 scopus 로고    scopus 로고
    • Nramp1 functionality increases inducible nitric oxide synthase transcription via stimulation of IFN regulatory factor 1 expression
    • Fritsche, G., Dlaska, M., Barton, H., Theurl, I., Garimorth, K. and Weiss, G., Nramp1 functionality increases inducible nitric oxide synthase transcription via stimulation of IFN regulatory factor 1 expression. J. Immunol. 2003. 171: 1994-1998.
    • (2003) J. Immunol , vol.171 , pp. 1994-1998
    • Fritsche, G.1    Dlaska, M.2    Barton, H.3    Theurl, I.4    Garimorth, K.5    Weiss, G.6
  • 25
    • 0029035476 scopus 로고
    • Altered immune responses in mice lacking inducible nitric oxide synthase
    • Wei, X. Q., Charles, I. G., Smith, A., Ure, J., Feng, G. J., Huang, F. P., Xu, D. et al., Altered immune responses in mice lacking inducible nitric oxide synthase. Nature 1995. 375: 408-411.
    • (1995) Nature , vol.375 , pp. 408-411
    • Wei, X.Q.1    Charles, I.G.2    Smith, A.3    Ure, J.4    Feng, G.J.5    Huang, F.P.6    Xu, D.7
  • 26
    • 0030667473 scopus 로고    scopus 로고
    • Inhibition of virulent Mycobacterium tuberculosis by Bcg(r) and Bcg(s) macrophages correlates with nitric oxide production
    • Arias, M., Rojas, M., Zabaleta, J., Rodriguez, J. I., Paris, S. C., Barrera, L. F. and Garcia, L. F., Inhibition of virulent Mycobacterium tuberculosis by Bcg(r) and Bcg(s) macrophages correlates with nitric oxide production. J. Infect. Dis. 1997. 176: 1552-1558.
    • (1997) J. Infect. Dis , vol.176 , pp. 1552-1558
    • Arias, M.1    Rojas, M.2    Zabaleta, J.3    Rodriguez, J.I.4    Paris, S.C.5    Barrera, L.F.6    Garcia, L.F.7
  • 28
    • 33646581368 scopus 로고    scopus 로고
    • Divergent mechanisms utilized by SOCS3 to mediate interleukin-10 inhibition of tumor necrosis factor alpha and nitric oxide production by macrophages
    • Qasimi, P., Ming-Lum, A., Ghanipour, A., Ong, C. J., Cox, M. E., Ihle, J., Cacalano, N. et al., Divergent mechanisms utilized by SOCS3 to mediate interleukin-10 inhibition of tumor necrosis factor alpha and nitric oxide production by macrophages. J. Biol. Chem. 2006. 281: 6316-6324.
    • (2006) J. Biol. Chem , vol.281 , pp. 6316-6324
    • Qasimi, P.1    Ming-Lum, A.2    Ghanipour, A.3    Ong, C.J.4    Cox, M.E.5    Ihle, J.6    Cacalano, N.7
  • 29
    • 34547863499 scopus 로고    scopus 로고
    • The co-ordinated regulation of iron homeostasis in murine macrophages limits the availability of iron for intracellular Salmonella typhimurium
    • Nairz, M., Theurl, I., Ludwiczek, S., Theurl, M., Mair, S. M., Fritsche, G. andWeiss, G., The co-ordinated regulation of iron homeostasis in murine macrophages limits the availability of iron for intracellular Salmonella typhimurium. Cell Microbiol. 2007. 9: 2126-2140.
    • (2007) Cell Microbiol , vol.9 , pp. 2126-2140
    • Nairz, M.1    Theurl, I.2    Ludwiczek, S.3    Theurl, M.4    Mair, S.M.5    Fritsche, G.6    andWeiss, G.7
  • 31
    • 0030062314 scopus 로고    scopus 로고
    • Gamma interferon and interleukin-10 gene expression in innately susceptible and resistant mice during the early phase of Salmonella typhimurium infection
    • Pie, S., Matsiota-Bernard, P., Truffa-Bachi, P. and Nauciel, C., Gamma interferon and interleukin-10 gene expression in innately susceptible and resistant mice during the early phase of Salmonella typhimurium infection. Infect. Immun. 1996. 64: 849-854.
    • (1996) Infect. Immun , vol.64 , pp. 849-854
    • Pie, S.1    Matsiota-Bernard, P.2    Truffa-Bachi, P.3    Nauciel, C.4
  • 32
    • 0033563093 scopus 로고    scopus 로고
    • TNF-alpha and IL-10 modulate the induction of apoptosis by virulent Mycobacterium tuberculosis in murine macrophages
    • Rojas, M., Olivier, M., Gros, P., Barrera, L. F. and Garcia, L. F., TNF-alpha and IL-10 modulate the induction of apoptosis by virulent Mycobacterium tuberculosis in murine macrophages. J. Immunol. 1999. 162: 6122-6131.
    • (1999) J. Immunol , vol.162 , pp. 6122-6131
    • Rojas, M.1    Olivier, M.2    Gros, P.3    Barrera, L.F.4    Garcia, L.F.5
  • 33
    • 0037114921 scopus 로고    scopus 로고
    • Interleukin-10, polymorphism in SLC11A1 (formerly NRAMP1), and susceptibility to tuberculosis
    • Awomoyi, A. A., Marchant, A., Howson, J. M., McAdam, K. P., Blackwell, J. M. and Newport, M. J., Interleukin-10, polymorphism in SLC11A1 (formerly NRAMP1), and susceptibility to tuberculosis. J. Infect. Dis. 2002. 186: 1808-1814.
    • (2002) J. Infect. Dis , vol.186 , pp. 1808-1814
    • Awomoyi, A.A.1    Marchant, A.2    Howson, J.M.3    McAdam, K.P.4    Blackwell, J.M.5    Newport, M.J.6
  • 35
    • 1842484338 scopus 로고    scopus 로고
    • Involvement of Salmonella pathogenicity island 2 in the up-regulation of interleukin-10 expression in macrophages: Role of protein kinase A signal pathway
    • Uchiya, K., Groisman, E. A. and Nikai, T., Involvement of Salmonella pathogenicity island 2 in the up-regulation of interleukin-10 expression in macrophages: Role of protein kinase A signal pathway. Infect. Immun. 2004. 72: 1964-1973.
    • (2004) Infect. Immun , vol.72 , pp. 1964-1973
    • Uchiya, K.1    Groisman, E.A.2    Nikai, T.3
  • 37
    • 0038119551 scopus 로고    scopus 로고
    • Effect of iron treatment on circulating cytokine levels in ESRD patients receiving recombinant human erythropoietin
    • Weiss, G., Meusburger, E., Radacher, G., Garimorth, K., Neyer, U. and Mayer, G., Effect of iron treatment on circulating cytokine levels in ESRD patients receiving recombinant human erythropoietin. Kidney Int. 2003. 64: 572-578.
    • (2003) Kidney Int , vol.64 , pp. 572-578
    • Weiss, G.1    Meusburger, E.2    Radacher, G.3    Garimorth, K.4    Neyer, U.5    Mayer, G.6
  • 38
    • 1642619148 scopus 로고    scopus 로고
    • Differential effects of iron deficiency and underfeeding on serum levels of interleukin-10, interleukin-12p40, and interferon-gamma in mice
    • Kuvibidila, S. and Warrier, R. P., Differential effects of iron deficiency and underfeeding on serum levels of interleukin-10, interleukin-12p40, and interferon-gamma in mice. Cytokine 2004. 26: 73-81.
    • (2004) Cytokine , vol.26 , pp. 73-81
    • Kuvibidila, S.1    Warrier, R.P.2
  • 40
    • 0036144434 scopus 로고    scopus 로고
    • Mycobacterium avium infection of macrophages results in progressive suppression of interleukin-12 production in vitro and in vivo
    • Wagner, D., Sangari, F. J., Kim, S., Petrofsky, M. and Bermudez, L. E., Mycobacterium avium infection of macrophages results in progressive suppression of interleukin-12 production in vitro and in vivo. J. Leukoc. Biol. 2002. 71: 80-88.
    • (2002) J. Leukoc. Biol , vol.71 , pp. 80-88
    • Wagner, D.1    Sangari, F.J.2    Kim, S.3    Petrofsky, M.4    Bermudez, L.E.5
  • 41
    • 12444344631 scopus 로고    scopus 로고
    • Elemental analysis of Mycobacterium avium-, Mycobacterium tuberculosis-, and Mycobacterium smegmatis-containing phagosomes indicates pathogen-induced microenvironments within the host cell's endosomal system
    • Wagner, D., Maser, J., Lai, B., Cai, Z., Barry, 3rd., C. E., Honer Zu Bentrup, K., Russell, D. G. et al., Elemental analysis of Mycobacterium avium-, Mycobacterium tuberculosis-, and Mycobacterium smegmatis-containing phagosomes indicates pathogen-induced microenvironments within the host cell's endosomal system. J. Immunol. 2005. 174: 1491-1500.
    • (2005) J. Immunol , vol.174 , pp. 1491-1500
    • Wagner, D.1    Maser, J.2    Lai, B.3    Cai, Z.4    Barry 3rd, C.E.5    Honer Zu Bentrup, K.6    Russell, D.G.7
  • 43
    • 26844507372 scopus 로고    scopus 로고
    • Mycobacterium bovis BCG attenuates surface expression of mature class II molecules through IL-10-dependent inhibition of cathepsin S
    • Sendide, K., Deghmane, A. E., Pechkovsky, D., Av-Gay, Y., Talal, A. and Hmama, Z., Mycobacterium bovis BCG attenuates surface expression of mature class II molecules through IL-10-dependent inhibition of cathepsin S. J. Immunol. 2005. 175: 5324-5332.
    • (2005) J. Immunol , vol.175 , pp. 5324-5332
    • Sendide, K.1    Deghmane, A.E.2    Pechkovsky, D.3    Av-Gay, Y.4    Talal, A.5    Hmama, Z.6
  • 44
    • 0041656392 scopus 로고    scopus 로고
    • Determinants of response to interleukin-10 receptor blockade immunotherapy in experimental visceral leishmaniasis
    • Murray, H. W., Moreira, A. L., Lu, C. M., DeVecchio, J. L., Matsuhashi, M., Ma, X. and Heinzel, F. P., Determinants of response to interleukin-10 receptor blockade immunotherapy in experimental visceral leishmaniasis. J. Infect. Dis. 2003. 188: 458-464.
    • (2003) J. Infect. Dis , vol.188 , pp. 458-464
    • Murray, H.W.1    Moreira, A.L.2    Lu, C.M.3    DeVecchio, J.L.4    Matsuhashi, M.5    Ma, X.6    Heinzel, F.P.7
  • 45
    • 0032927084 scopus 로고    scopus 로고
    • High level expression of Nramp1G169 in RAW264.7 cell transfectants: Analysis of intracellular iron transport
    • Atkinson, P. G. and Barton, C. H., High level expression of Nramp1G169 in RAW264.7 cell transfectants: Analysis of intracellular iron transport. Immunology 1999. 96: 656-662.
    • (1999) Immunology , vol.96 , pp. 656-662
    • Atkinson, P.G.1    Barton, C.H.2
  • 46
    • 21644454100 scopus 로고    scopus 로고
    • Regulatory networks for the control of body iron homeostasis and their dysregulation in HFE mediated hemochromatosis
    • Ludwiczek, S., Theurl, I., Bahram, S., Schumann, K. and Weiss, G., Regulatory networks for the control of body iron homeostasis and their dysregulation in HFE mediated hemochromatosis. J. Cell Physiol. 2005. 204: 489-499.
    • (2005) J. Cell Physiol , vol.204 , pp. 489-499
    • Ludwiczek, S.1    Theurl, I.2    Bahram, S.3    Schumann, K.4    Weiss, G.5
  • 47
    • 0024380087 scopus 로고
    • Rapid detection of octamer binding proteins with 'mini-extracts', prepared from a small number of cells
    • Schreiber, E., Matthias, P., Muller, M. M. and Schaffner, W., Rapid detection of octamer binding proteins with 'mini-extracts', prepared from a small number of cells. Nucleic Acids Res. 1989. 17: 6419.
    • (1989) Nucleic Acids Res , vol.17 , pp. 6419
    • Schreiber, E.1    Matthias, P.2    Muller, M.M.3    Schaffner, W.4


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