메뉴 건너뛰기




Volumn 46, Issue 6, 2009, Pages 289-297

Free iron ions decrease indoleamine 2,3-dioxygenase expression and reduce IFNγ-induced inhibition of Chlamydia trachomatis infection

Author keywords

Chlamydia trachomatis; Indoleamine 2,3 dioxygenase; Interferon ; Iron

Indexed keywords

DEFEROXAMINE; FERROUS ION; FERROUS SULFATE; GAMMA INTERFERON; INDOLEAMINE 2,3 DIOXYGENASE; MESSENGER RNA; TRYPTOPHAN;

EID: 67349199663     PISSN: 08824010     EISSN: 10961208     Source Type: Journal    
DOI: 10.1016/j.micpath.2009.03.001     Document Type: Article
Times cited : (8)

References (43)
  • 1
    • 27544490285 scopus 로고    scopus 로고
    • Indoleamine 2,3 dioxygenase and regulation of T cell immunity
    • Mellor A. Indoleamine 2,3 dioxygenase and regulation of T cell immunity. Biochem Biophys Res Commun 338 (2005) 20-24
    • (2005) Biochem Biophys Res Commun , vol.338 , pp. 20-24
    • Mellor, A.1
  • 2
    • 0038215374 scopus 로고    scopus 로고
    • Tolerance, DCs and tryptophan: much ado about IDO
    • Grohmann U., Fallarino F., and Puccetti P. Tolerance, DCs and tryptophan: much ado about IDO. Trends Immunol 24 (2003) 242-248
    • (2003) Trends Immunol , vol.24 , pp. 242-248
    • Grohmann, U.1    Fallarino, F.2    Puccetti, P.3
  • 3
    • 2942595706 scopus 로고    scopus 로고
    • Human bone marrow stromal cells inhibit allogeneic T-cell responses by indoleamine 2,3-dioxygenase-mediated tryptophan degradation
    • Meisel R., Zibert A., Laryea M., Gobel U., Daubener W., and Dilloo D. Human bone marrow stromal cells inhibit allogeneic T-cell responses by indoleamine 2,3-dioxygenase-mediated tryptophan degradation. Blood 103 (2004) 4619-4621
    • (2004) Blood , vol.103 , pp. 4619-4621
    • Meisel, R.1    Zibert, A.2    Laryea, M.3    Gobel, U.4    Daubener, W.5    Dilloo, D.6
  • 5
    • 45949130970 scopus 로고
    • The immunobiology of Chlamydia
    • Levitt D., and Barol J. The immunobiology of Chlamydia. Immunol Today 8 (1987) 246-251
    • (1987) Immunol Today , vol.8 , pp. 246-251
    • Levitt, D.1    Barol, J.2
  • 6
    • 0027946866 scopus 로고
    • Persistent chlamydiae: from cell culture to a paradigm for chlamydial pathogenesis
    • Beatty W.L., Morrison R.P., and Byrne G.I. Persistent chlamydiae: from cell culture to a paradigm for chlamydial pathogenesis. Microbiol Rev 58 (1994) 686-699
    • (1994) Microbiol Rev , vol.58 , pp. 686-699
    • Beatty, W.L.1    Morrison, R.P.2    Byrne, G.I.3
  • 8
    • 0142153570 scopus 로고    scopus 로고
    • Synovial Chlamydia trachomatis in patients with reactive arthritis/Reiter's syndrome are viable but show aberrant gene expression
    • Gerard H.C., Branigan P.J., Schumacher Jr. H.R., and Hudson A.P. Synovial Chlamydia trachomatis in patients with reactive arthritis/Reiter's syndrome are viable but show aberrant gene expression. J Rheumatol 25 (1998) 734-742
    • (1998) J Rheumatol , vol.25 , pp. 734-742
    • Gerard, H.C.1    Branigan, P.J.2    Schumacher Jr., H.R.3    Hudson, A.P.4
  • 9
    • 0034004429 scopus 로고    scopus 로고
    • Analysis of transcription factors regulating induction of indoleamine 2,3-dioxygenase by IFN-gamma
    • Du M.X., Sotero-Esteva W.D., and Taylor M.W. Analysis of transcription factors regulating induction of indoleamine 2,3-dioxygenase by IFN-gamma. J Interferon Cytokine Res 20 (2000) 133-142
    • (2000) J Interferon Cytokine Res , vol.20 , pp. 133-142
    • Du, M.X.1    Sotero-Esteva, W.D.2    Taylor, M.W.3
  • 10
    • 34548863106 scopus 로고    scopus 로고
    • Noncanonical NF-kappaB signaling in dendritic cells is required for indoleamine 2,3-dioxygenase (IDO) induction and immune regulation
    • Tas S.W., Vervoordeldonk M.J., Hajji N., Schuitemaker J.H., van der Sluijs K.F., May M.J., et al. Noncanonical NF-kappaB signaling in dendritic cells is required for indoleamine 2,3-dioxygenase (IDO) induction and immune regulation. Blood 110 (2007) 1540-1549
    • (2007) Blood , vol.110 , pp. 1540-1549
    • Tas, S.W.1    Vervoordeldonk, M.J.2    Hajji, N.3    Schuitemaker, J.H.4    van der Sluijs, K.F.5    May, M.J.6
  • 11
    • 0035873436 scopus 로고    scopus 로고
    • Antioxidants inhibit indoleamine 2,3-dioxygenase in IFN-gamma-activated human macrophages: posttranslational regulation by pyrrolidine dithiocarbamate
    • Thomas S.R., Salahifar H., Mashima R., Hunt N.H., Richardson D.R., and Stocker R. Antioxidants inhibit indoleamine 2,3-dioxygenase in IFN-gamma-activated human macrophages: posttranslational regulation by pyrrolidine dithiocarbamate. J Immunol 166 (2001) 6332-6340
    • (2001) J Immunol , vol.166 , pp. 6332-6340
    • Thomas, S.R.1    Salahifar, H.2    Mashima, R.3    Hunt, N.H.4    Richardson, D.R.5    Stocker, R.6
  • 12
    • 34548204420 scopus 로고    scopus 로고
    • Post-translational regulation of human indoleamine 2,3-dioxygenase activity by nitric oxide
    • Thomas S.R., Terentis A.C., Cai H., Takikawa O., Levina A., Lay P.A., et al. Post-translational regulation of human indoleamine 2,3-dioxygenase activity by nitric oxide. J Biol Chem 282 (2007) 23778-23787
    • (2007) J Biol Chem , vol.282 , pp. 23778-23787
    • Thomas, S.R.1    Terentis, A.C.2    Cai, H.3    Takikawa, O.4    Levina, A.5    Lay, P.A.6
  • 13
    • 33746062067 scopus 로고    scopus 로고
    • Interactions between nitric oxide and indoleamine 2,3-dioxygenase
    • Samelson-Jones B.J., and Yeh S.R. Interactions between nitric oxide and indoleamine 2,3-dioxygenase. Biochemistry 45 (2006) 8527-8538
    • (2006) Biochemistry , vol.45 , pp. 8527-8538
    • Samelson-Jones, B.J.1    Yeh, S.R.2
  • 14
    • 0027938009 scopus 로고
    • Abrogation of gamma interferon-induced inhibition of Ehrlichia chaffeensis infection in human monocytes with iron-transferrin
    • Barnewall R.E., and Rikihisa Y. Abrogation of gamma interferon-induced inhibition of Ehrlichia chaffeensis infection in human monocytes with iron-transferrin. Infect Immun 62 (1994) 4804-4810
    • (1994) Infect Immun , vol.62 , pp. 4804-4810
    • Barnewall, R.E.1    Rikihisa, Y.2
  • 15
    • 0031831108 scopus 로고    scopus 로고
    • Interferon-gamma-activated primary enterocytes inhibit Toxoplasma gondii replication: a role for intracellular iron
    • Dimier I.H., and Bout D.T. Interferon-gamma-activated primary enterocytes inhibit Toxoplasma gondii replication: a role for intracellular iron. Immunology 94 (1998) 488-495
    • (1998) Immunology , vol.94 , pp. 488-495
    • Dimier, I.H.1    Bout, D.T.2
  • 17
    • 0030786743 scopus 로고    scopus 로고
    • Response of Chlamydia trachomatis serovar E to iron restriction in vitro and evidence for iron-regulated chlamydial proteins
    • Raulston J.E. Response of Chlamydia trachomatis serovar E to iron restriction in vitro and evidence for iron-regulated chlamydial proteins. Infect Immun 65 (1997) 4539-4547
    • (1997) Infect Immun , vol.65 , pp. 4539-4547
    • Raulston, J.E.1
  • 18
    • 27244449295 scopus 로고    scopus 로고
    • Inhibition of Chlamydia trachomatis growth by human interferon-alpha: mechanisms and synergistic effect with interferon-gamma and tumor necrosis factor-alpha
    • Ishihara T., Aga M., Hino K., Ushio C., Taniguchi M., Iwaki K., et al. Inhibition of Chlamydia trachomatis growth by human interferon-alpha: mechanisms and synergistic effect with interferon-gamma and tumor necrosis factor-alpha. Biomed Res 26 (2005) 179-185
    • (2005) Biomed Res , vol.26 , pp. 179-185
    • Ishihara, T.1    Aga, M.2    Hino, K.3    Ushio, C.4    Taniguchi, M.5    Iwaki, K.6
  • 19
    • 0028024570 scopus 로고
    • Tryptophan depletion as a mechanism of gamma interferon-mediated chlamydial persistence
    • Beatty W.L., Belanger T.A., Desai A.A., Morrison R.P., and Byrne G.I. Tryptophan depletion as a mechanism of gamma interferon-mediated chlamydial persistence. Infect Immun 62 (1994) 3705-3711
    • (1994) Infect Immun , vol.62 , pp. 3705-3711
    • Beatty, W.L.1    Belanger, T.A.2    Desai, A.A.3    Morrison, R.P.4    Byrne, G.I.5
  • 20
    • 0021950218 scopus 로고
    • Inhibition of growth of Chlamydia trachomatis by human gamma interferon
    • Shemer Y., and Sarov I. Inhibition of growth of Chlamydia trachomatis by human gamma interferon. Infect Immun 48 (1985) 592-596
    • (1985) Infect Immun , vol.48 , pp. 592-596
    • Shemer, Y.1    Sarov, I.2
  • 21
    • 0034466510 scopus 로고    scopus 로고
    • IFN-gamma activated indoleamine 2,3-dioxygenase activity in human cells is an antiparasitic and an antibacterial effector mechanism
    • Daubener W., and MacKenzie C.R. IFN-gamma activated indoleamine 2,3-dioxygenase activity in human cells is an antiparasitic and an antibacterial effector mechanism. Adv Exp Med Biol 467 (1999) 517-524
    • (1999) Adv Exp Med Biol , vol.467 , pp. 517-524
    • Daubener, W.1    MacKenzie, C.R.2
  • 22
    • 0027472853 scopus 로고
    • Low-nutrient induction of abnormal chlamydial development: a novel component of chlamydial pathogenesis?
    • Coles A.M., Reynolds D.J., Harper A., Devitt A., and Pearce J.H. Low-nutrient induction of abnormal chlamydial development: a novel component of chlamydial pathogenesis?. FEMS Microbiol Lett 106 (1993) 193-200
    • (1993) FEMS Microbiol Lett , vol.106 , pp. 193-200
    • Coles, A.M.1    Reynolds, D.J.2    Harper, A.3    Devitt, A.4    Pearce, J.H.5
  • 23
    • 0000056144 scopus 로고
    • Interferon gamma blocks the growth of Toxoplasma gondii in human fibroblasts by inducing the host cells to degrade tryptophan
    • Pfefferkorn E.R. Interferon gamma blocks the growth of Toxoplasma gondii in human fibroblasts by inducing the host cells to degrade tryptophan. Proc Natl Acad Sci U S A 81 (1984) 908-912
    • (1984) Proc Natl Acad Sci U S A , vol.81 , pp. 908-912
    • Pfefferkorn, E.R.1
  • 24
    • 0025944659 scopus 로고
    • Relationship between interferon-gamma, indoleamine 2,3-dioxygenase, and tryptophan catabolism
    • Taylor M.W., and Feng G.S. Relationship between interferon-gamma, indoleamine 2,3-dioxygenase, and tryptophan catabolism. FASEB J 5 (1991) 2516-2522
    • (1991) FASEB J , vol.5 , pp. 2516-2522
    • Taylor, M.W.1    Feng, G.S.2
  • 25
    • 0016683921 scopus 로고
    • Competition between Chlamydia psittaci and L cells for host isoleucine pools: a limiting factor in chlamydial multiplication
    • Hatch T.P. Competition between Chlamydia psittaci and L cells for host isoleucine pools: a limiting factor in chlamydial multiplication. Infect Immun 12 (1975) 211-220
    • (1975) Infect Immun , vol.12 , pp. 211-220
    • Hatch, T.P.1
  • 26
    • 0022367489 scopus 로고
    • Influence of cysteine deprivation on chlamydial differentiation from reproductive to infective life-cycle forms
    • Allan I., Hatch T.P., and Pearce J.H. Influence of cysteine deprivation on chlamydial differentiation from reproductive to infective life-cycle forms. J Gen Microbiol 131 (1985) 3171-3177
    • (1985) J Gen Microbiol , vol.131 , pp. 3171-3177
    • Allan, I.1    Hatch, T.P.2    Pearce, J.H.3
  • 27
    • 19044389821 scopus 로고    scopus 로고
    • Iron and immunity: a double-edged sword
    • Weiss G. Iron and immunity: a double-edged sword. Eur J Clin Invest 32 Suppl. 1 (2002) 70-78
    • (2002) Eur J Clin Invest , vol.32 , Issue.SUPPL. 1 , pp. 70-78
    • Weiss, G.1
  • 28
    • 3843097333 scopus 로고    scopus 로고
    • New and emerging theories of cardiovascular disease: infection and elevated iron
    • Alpert P.T. New and emerging theories of cardiovascular disease: infection and elevated iron. Biol Res Nurs 6 (2004) 3-10
    • (2004) Biol Res Nurs , vol.6 , pp. 3-10
    • Alpert, P.T.1
  • 30
    • 0021932310 scopus 로고
    • Listeriosis in patients with long-term hemodialysis and transfusional iron overload
    • Mossey R.T., and Sondheimer J. Listeriosis in patients with long-term hemodialysis and transfusional iron overload. Am J Med 79 (1985) 397-400
    • (1985) Am J Med , vol.79 , pp. 397-400
    • Mossey, R.T.1    Sondheimer, J.2
  • 32
    • 0029883690 scopus 로고    scopus 로고
    • Associations of iron overload in Africa with hepatocellular carcinoma and tuberculosis: Strachan's 1929 thesis revisited
    • Gordeuk V.R., McLaren C.E., MacPhail A.P., Deichsel G., and Bothwell T.H. Associations of iron overload in Africa with hepatocellular carcinoma and tuberculosis: Strachan's 1929 thesis revisited. Blood 87 (1996) 3470-3476
    • (1996) Blood , vol.87 , pp. 3470-3476
    • Gordeuk, V.R.1    McLaren, C.E.2    MacPhail, A.P.3    Deichsel, G.4    Bothwell, T.H.5
  • 35
    • 22844443827 scopus 로고    scopus 로고
    • Iron and iron chelating agents modulate Mycobacterium tuberculosis growth and monocyte-macrophage viability and effector functions
    • Cronje L., Edmondson N., Eisenach K.D., and Bornman L. Iron and iron chelating agents modulate Mycobacterium tuberculosis growth and monocyte-macrophage viability and effector functions. FEMS Immunol Med Microbiol 45 (2005) 103-112
    • (2005) FEMS Immunol Med Microbiol , vol.45 , pp. 103-112
    • Cronje, L.1    Edmondson, N.2    Eisenach, K.D.3    Bornman, L.4
  • 36
    • 0033806469 scopus 로고    scopus 로고
    • Gallium disrupts iron metabolism of mycobacteria residing within human macrophages
    • Olakanmi O., Britigan B.E., and Schlesinger L.S. Gallium disrupts iron metabolism of mycobacteria residing within human macrophages. Infect Immun 68 (2000) 5619-5627
    • (2000) Infect Immun , vol.68 , pp. 5619-5627
    • Olakanmi, O.1    Britigan, B.E.2    Schlesinger, L.S.3
  • 38
    • 0033795434 scopus 로고    scopus 로고
    • Frequent contamination of Chlamydia trachomatis and Chlamydia pneumoniae strains with mycoplasma. Biological relevance and selective eradication of mycoplasma from chlamydial cultures with mupirocin
    • Krausse-Opatz B., Dollmann P., Zeidler H., Kuipers J.G., and Kohler L. Frequent contamination of Chlamydia trachomatis and Chlamydia pneumoniae strains with mycoplasma. Biological relevance and selective eradication of mycoplasma from chlamydial cultures with mupirocin. Med Microbiol Immunol (Berl) 189 (2000) 19-26
    • (2000) Med Microbiol Immunol (Berl) , vol.189 , pp. 19-26
    • Krausse-Opatz, B.1    Dollmann, P.2    Zeidler, H.3    Kuipers, J.G.4    Kohler, L.5
  • 39
    • 0019514724 scopus 로고
    • Purification and partial characterization of the major outer membrane protein of Chlamydia trachomatis
    • Caldwell H.D., Kromhout J., and Schachter J. Purification and partial characterization of the major outer membrane protein of Chlamydia trachomatis. Infect Immun 31 (1981) 1161-1176
    • (1981) Infect Immun , vol.31 , pp. 1161-1176
    • Caldwell, H.D.1    Kromhout, J.2    Schachter, J.3
  • 40
    • 0034762867 scopus 로고    scopus 로고
    • The reprogrammed host: Chlamydia trachomatis-induced up-regulation of glycoprotein 130 cytokines, transcription factors, and antiapoptotic genes
    • Hess S., Rheinheimer C., Tidow F., Bartling G., Kaps C., Lauber J., et al. The reprogrammed host: Chlamydia trachomatis-induced up-regulation of glycoprotein 130 cytokines, transcription factors, and antiapoptotic genes. Arthritis Rheum 44 (2001) 2392-2401
    • (2001) Arthritis Rheum , vol.44 , pp. 2392-2401
    • Hess, S.1    Rheinheimer, C.2    Tidow, F.3    Bartling, G.4    Kaps, C.5    Lauber, J.6
  • 41
    • 0242317675 scopus 로고    scopus 로고
    • Experimental validation of novel and conventional approaches to quantitative real-time PCR data analysis
    • Peirson S.N., Butler J.N., and Foster R.G. Experimental validation of novel and conventional approaches to quantitative real-time PCR data analysis. Nucleic Acids Res 31 (2003) e73
    • (2003) Nucleic Acids Res , vol.31
    • Peirson, S.N.1    Butler, J.N.2    Foster, R.G.3
  • 42
    • 0023926018 scopus 로고
    • Mechanism of interferon-gamma action. Characterization of indoleamine 2,3-dioxygenase in cultured human cells induced by interferon-gamma and evaluation of the enzyme-mediated tryptophan degradation in its anticellular activity
    • Takikawa O., Kuroiwa T., Yamazaki F., and Kido R. Mechanism of interferon-gamma action. Characterization of indoleamine 2,3-dioxygenase in cultured human cells induced by interferon-gamma and evaluation of the enzyme-mediated tryptophan degradation in its anticellular activity. J Biol Chem 263 (1988) 2041-2048
    • (1988) J Biol Chem , vol.263 , pp. 2041-2048
    • Takikawa, O.1    Kuroiwa, T.2    Yamazaki, F.3    Kido, R.4
  • 43
    • 0019988401 scopus 로고
    • Determination of specific IGA antibodies to varicella zoster virus by immunoperoxidase assay
    • Haikin H., and Sarov I. Determination of specific IGA antibodies to varicella zoster virus by immunoperoxidase assay. J Clin Pathol 35 (1982) 645-649
    • (1982) J Clin Pathol , vol.35 , pp. 645-649
    • Haikin, H.1    Sarov, I.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.