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Volumn 272, Issue 12, 2005, Pages 3120-3131

Regulation of arginase II by interferon regulatory factor 3 and the involvement of polyamines in the antiviral response

Author keywords

Antiviral response; Arginase II; Interferon regulatory factor 3 (IRF 3); Polyamine; Spermine

Indexed keywords

ARGINASE; ARGINASE II; BETA INTERFERON; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INTERFERON REGULATORY FACTOR 3; POLYAMINE DERIVATIVE; PUTRESCINE; SPERMIDINE; SPERMINE; TRANSCRIPTION FACTOR AP 1; UNCLASSIFIED DRUG;

EID: 21344447738     PISSN: 1742464X     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2005.04726.x     Document Type: Article
Times cited : (33)

References (56)
  • 1
    • 0034767753 scopus 로고    scopus 로고
    • Antiviral actions of interferons
    • Samuel CE (2001) Antiviral actions of interferons. Clin Microbiol Rev 14, 778-809.
    • (2001) Clin Microbiol Rev , vol.14 , pp. 778-809
    • Samuel, C.E.1
  • 2
    • 0034769960 scopus 로고    scopus 로고
    • Viruses and interferons
    • Sen GC (2001) Viruses and interferons. Annu Rev Microbiol 55, 255-281.
    • (2001) Annu Rev Microbiol , vol.55 , pp. 255-281
    • Sen, G.C.1
  • 3
    • 0036710523 scopus 로고    scopus 로고
    • Multiple signaling pathways leading to the activation of interferon regulatory factor 3
    • Servant MJ, Grandvaux N & Hiscott J (2002) Multiple signaling pathways leading to the activation of interferon regulatory factor 3. Biochem Pharmacol 64, 985-992.
    • (2002) Biochem Pharmacol , vol.64 , pp. 985-992
    • Servant, M.J.1    Grandvaux, N.2    Hiscott, J.3
  • 5
    • 0033970937 scopus 로고    scopus 로고
    • Activation of p38 mitogen-activated protein kinase and c-Jun NH(2)-terminal kinase by double-stranded RNA and encephalomyocarditis virus: Involvement of RNase L, protein kinase R, and alternative pathways
    • Iordanov MS, Paranjape JM, Zhou A, Wong J, Williams BR, Meurs EF, Silverman RH & Magun BE (2000) Activation of p38 mitogen-activated protein kinase and c-Jun NH(2)-terminal kinase by double-stranded RNA and encephalomyocarditis virus: involvement of RNase L, protein kinase R, and alternative pathways. Mol Cell Biol 20, 617-627.
    • (2000) Mol Cell Biol , vol.20 , pp. 617-627
    • Iordanov, M.S.1    Paranjape, J.M.2    Zhou, A.3    Wong, J.4    Williams, B.R.5    Meurs, E.F.6    Silverman, R.H.7    Magun, B.E.8
  • 6
    • 0038363463 scopus 로고    scopus 로고
    • Triggering the interferon antiviral response through an IKK-related pathway
    • Sharma S, tenOever BR, Grandvaux N, Zhou GP, Lin R & Hiscott J (2003) Triggering the interferon antiviral response through an IKK-related pathway. Science 300, 1148-1151.
    • (2003) Science , vol.300 , pp. 1148-1151
    • Sharma, S.1    Tenoever, B.R.2    Grandvaux, N.3    Zhou, G.P.4    Lin, R.5    Hiscott, J.6
  • 9
    • 0032538891 scopus 로고    scopus 로고
    • Differential viral induction of distinct interferon-alpha genes by positive feedback through interferon regulatory factor-7
    • Marie I, Durbin JE & Levy DE (1998) Differential viral induction of distinct interferon-alpha genes by positive feedback through interferon regulatory factor-7. EMBO J 17, 6660-6669.
    • (1998) EMBO J , vol.17 , pp. 6660-6669
    • Marie, I.1    Durbin, J.E.2    Levy, D.E.3
  • 11
    • 0033842515 scopus 로고    scopus 로고
    • Selective DNA binding and association with the CREB binding protein coactivator contribute to differential activation of alpha/beta interferon genes by interferon regulatory factors 3 and 7
    • Lin R, Genin P, Mamane Y & Hiscott J (2000) Selective DNA binding and association with the CREB binding protein coactivator contribute to differential activation of alpha/beta interferon genes by interferon regulatory factors 3 and 7. Mol Cell Biol 20, 6342-6353.
    • (2000) Mol Cell Biol , vol.20 , pp. 6342-6353
    • Lin, R.1    Genin, P.2    Mamane, Y.3    Hiscott, J.4
  • 12
    • 0033833398 scopus 로고    scopus 로고
    • Activation of cellular interferon-responsive genes after infection of human cells with herpes simplex virus type 1
    • Nicholl MJ, Robinson LH & Preston CM (2000) Activation of cellular interferon-responsive genes after infection of human cells with herpes simplex virus type 1. J Gen Virol 81, 2215-2218.
    • (2000) J Gen Virol , vol.81 , pp. 2215-2218
    • Nicholl, M.J.1    Robinson, L.H.2    Preston, C.M.3
  • 14
    • 0036092049 scopus 로고    scopus 로고
    • Transcriptional profiling of interferon regulatory factor 3 target genes: Direct involvement in the regulation of interferon-stimulated genes
    • Grandvaux N, Servant MJ, tenOever B, Sen GC, Balachandran S, Barber GN, Lin R & Hiscott J (2002) Transcriptional profiling of interferon regulatory factor 3 target genes: direct involvement in the regulation of interferon-stimulated genes. J Virol 76, 5532-5539.
    • (2002) J Virol , vol.76 , pp. 5532-5539
    • Grandvaux, N.1    Servant, M.J.2    Tenoever, B.3    Sen, G.C.4    Balachandran, S.5    Barber, G.N.6    Lin, R.7    Hiscott, J.8
  • 15
    • 0032915860 scopus 로고    scopus 로고
    • Structural and functional analysis of interferon regulatory factor 3: Localization of the transactivation and autoinhibitory domains
    • Lin R, Mamane Y & Hiscott J (1999) Structural and functional analysis of interferon regulatory factor 3: localization of the transactivation and autoinhibitory domains. Mol Cell Biol 19, 2465-2474.
    • (1999) Mol Cell Biol , vol.19 , pp. 2465-2474
    • Lin, R.1    Mamane, Y.2    Hiscott, J.3
  • 17
    • 0028919209 scopus 로고
    • Arginase induction by suppressors of nitric oxide synthesis (IL-4, IL-10 and PGE2) in murine bone-marrow-derived macrophages
    • Corraliza IM, Soler G, Eichmann K & Modolell M (1995) Arginase induction by suppressors of nitric oxide synthesis (IL-4, IL-10 and PGE2) in murine bone-marrow-derived macrophages. Biochem Biophys Res Commun 206, 667-673.
    • (1995) Biochem Biophys Res Commun , vol.206 , pp. 667-673
    • Corraliza, I.M.1    Soler, G.2    Eichmann, K.3    Modolell, M.4
  • 18
    • 0032799629 scopus 로고    scopus 로고
    • Regulation of the genes for arginase isoforms and related enzymes in mouse macrophages by lipopolysaccharide
    • Salimuddin Nagasaki A, Gotoh T, Isobe H & Mori M (1999) Regulation of the genes for arginase isoforms and related enzymes in mouse macrophages by lipopolysaccharide. Am J Physiol 277, E110-E117.
    • (1999) Am J Physiol , vol.277
    • Salimuddin Nagasaki, A.1    Gotoh, T.2    Isobe, H.3    Mori, M.4
  • 19
    • 0030597114 scopus 로고    scopus 로고
    • Molecular cloning of cDNA for nonhepatic mitochondrial arginase (arginase II) and comparison of its induction with nitric oxide synthase in a murine macrophage-like cell line
    • Gotoh T, Sonoki T, Nagasaki A, Terada K, Takiguchi M & Mori M (1996) Molecular cloning of cDNA for nonhepatic mitochondrial arginase (arginase II) and comparison of its induction with nitric oxide synthase in a murine macrophage-like cell line. FEBS Lett 395, 119-122.
    • (1996) FEBS Lett , vol.395 , pp. 119-122
    • Gotoh, T.1    Sonoki, T.2    Nagasaki, A.3    Terada, K.4    Takiguchi, M.5    Mori, M.6
  • 21
    • 0035099627 scopus 로고    scopus 로고
    • Polyamine in cell growth and cell death: Molecular mechanisms and therapeutic applications
    • Thomas T & Thomas TJ (2001) Polyamine in cell growth and cell death: molecular mechanisms and therapeutic applications. Cell Mol Life Sci 58, 244-258.
    • (2001) Cell Mol Life Sci , vol.58 , pp. 244-258
    • Thomas, T.1    Thomas, T.J.2
  • 22
    • 0034045972 scopus 로고    scopus 로고
    • Involvement of polyamine in apoptosis. Facts and controversies: Effectors or protectors?
    • Schipper RG, Penning LC & Verhofstad AA (2000) Involvement of polyamine in apoptosis. Facts and controversies: effectors or protectors? Semin Cancer Biol 10, 55-68.
    • (2000) Semin Cancer Biol , vol.10 , pp. 55-68
    • Schipper, R.G.1    Penning, L.C.2    Verhofstad, A.A.3
  • 23
    • 0031893220 scopus 로고    scopus 로고
    • Virus dependent phosphorylation of the IRF-3 transcription factor regulates nuclear translocation, transactivation potential and proteasome mediated degradation
    • Lin R, Heylbroeck C, Pitha PM & Hiscott J (1998) Virus dependent phosphorylation of the IRF-3 transcription factor regulates nuclear translocation, transactivation potential and proteasome mediated degradation. Mol Cell Biol 18, 2986-2996.
    • (1998) Mol Cell Biol , vol.18 , pp. 2986-2996
    • Lin, R.1    Heylbroeck, C.2    Pitha, P.M.3    Hiscott, J.4
  • 25
    • 0034685624 scopus 로고    scopus 로고
    • Polyamine: Mysterious modulators of cellular functions
    • Igarashi K & Kashiwagi K (2000) Polyamine: mysterious modulators of cellular functions. Biochem Biophys Res Commun 271, 559-564.
    • (2000) Biochem Biophys Res Commun , vol.271 , pp. 559-564
    • Igarashi, K.1    Kashiwagi, K.2
  • 26
    • 0037026720 scopus 로고    scopus 로고
    • Spermine increases phosphatidylinositol 4,5-bisphosphate content in permeabilized and non-permeabilized HL60 cells
    • Coburn RF, Jones DH, Morgan CP, Baron CB & Cockcroft S (2002) Spermine increases phosphatidylinositol 4,5-bisphosphate content in permeabilized and non-permeabilized HL60 cells. Biochim Biophys Acta 1584, 20-30.
    • (2002) Biochim Biophys Acta , vol.1584 , pp. 20-30
    • Coburn, R.F.1    Jones, D.H.2    Morgan, C.P.3    Baron, C.B.4    Cockcroft, S.5
  • 27
    • 0035128587 scopus 로고    scopus 로고
    • Apoptosis is promoted by the dsRNA-activated factor (DRAF1) during viral infection independent of the action of interferon or p53
    • Weaver BK, Ando O, Kumar KP & Reich NC (2001) Apoptosis is promoted by the dsRNA-activated factor (DRAF1) during viral infection independent of the action of interferon or p53. FASEB J 15, 501-515.
    • (2001) FASEB J , vol.15 , pp. 501-515
    • Weaver, B.K.1    Ando, O.2    Kumar, K.P.3    Reich, N.C.4
  • 29
    • 0033535039 scopus 로고    scopus 로고
    • Arginase II downregulates nitric oxide (NO) production and prevents NO-mediated apoptosis in murine macrophage-derived RAW 264.7 cells
    • Gotoh T & Mori M (1999) Arginase II downregulates nitric oxide (NO) production and prevents NO-mediated apoptosis in murine macrophage-derived RAW 264.7 cells. J Cell Biol 144, 427-434.
    • (1999) J Cell Biol , vol.144 , pp. 427-434
    • Gotoh, T.1    Mori, M.2
  • 31
    • 0035889228 scopus 로고    scopus 로고
    • Lipopolysaccharide stimulates the MyD88-independent pathway and results in activation of IFN-regulatory factor 3 and the expression of a subset of lipopolysaccharide-inducible genes
    • Kawai T, Takeuchi O, Fujita T, Inoue J, Muhlradt PF, Sato S, Hoshino K & Akira S (2001) Lipopolysaccharide stimulates the MyD88-independent pathway and results in activation of IFN-regulatory factor 3 and the expression of a subset of lipopolysaccharide-inducible genes. J Immunol 167, 5887-5894.
    • (2001) J Immunol , vol.167 , pp. 5887-5894
    • Kawai, T.1    Takeuchi, O.2    Fujita, T.3    Inoue, J.4    Muhlradt, P.F.5    Sato, S.6    Hoshino, K.7    Akira, S.8
  • 32
    • 0037378718 scopus 로고    scopus 로고
    • Toll-like receptor 3 mediates a more potent antiviral response than Toll-like receptor 4
    • Doyle SE, O'Connell R, Vaidya SA, Chow EK, Yee K & Cheng G (2003) Toll-like receptor 3 mediates a more potent antiviral response than Toll-like receptor 4. J Immunol 170, 3565-3571.
    • (2003) J Immunol , vol.170 , pp. 3565-3571
    • Doyle, S.E.1    O'Connell, R.2    Vaidya, S.A.3    Chow, E.K.4    Yee, K.5    Cheng, G.6
  • 33
    • 0034671570 scopus 로고    scopus 로고
    • A new pathway of translational regulation mediated by eukaryotic initiation factor 3
    • Guo J, Hui DJ, Merrick WC & Sen GC (2000) A new pathway of translational regulation mediated by eukaryotic initiation factor 3. EMBO J 19, 6891-6899.
    • (2000) EMBO J , vol.19 , pp. 6891-6899
    • Guo, J.1    Hui, D.J.2    Merrick, W.C.3    Sen, G.C.4
  • 34
    • 1342316075 scopus 로고    scopus 로고
    • A comprehensive view of regulation of gene expression by double-stranded RNA-mediated cell signaling
    • Geiss G, Jin G, Guo J, Bumgarner R, Katze MG & Sen GC (2001) A comprehensive view of regulation of gene expression by double-stranded RNA-mediated cell signaling. J Biol Chem 30, 30.
    • (2001) J Biol Chem , vol.30 , pp. 30
    • Geiss, G.1    Jin, G.2    Guo, J.3    Bumgarner, R.4    Katze, M.G.5    Sen, G.C.6
  • 35
    • 0033539573 scopus 로고    scopus 로고
    • Activation of nuclear factor kappaB by polyamine in breast cancer cells
    • Shah N, Thomas T, Shirahata A, Sigal LH & Thomas TJ (1999) Activation of nuclear factor kappaB by polyamine in breast cancer cells. Biochemistry 38, 14763-14774.
    • (1999) Biochemistry , vol.38 , pp. 14763-14774
    • Shah, N.1    Thomas, T.2    Shirahata, A.3    Sigal, L.H.4    Thomas, T.J.5
  • 36
    • 0035967111 scopus 로고    scopus 로고
    • Regulation of estrogenic and nuclear factor kappa B functions by polyamine and their role in polyamine analog-induced apoptosis of breast cancer cells
    • Shah N, Thomas TJ, Lewis JS, Klinge CM, Shirahata A, Gelinas C & Thomas T (2001) Regulation of estrogenic and nuclear factor kappa B functions by polyamine and their role in polyamine analog-induced apoptosis of breast cancer cells. Oncogene 20, 1715-1729.
    • (2001) Oncogene , vol.20 , pp. 1715-1729
    • Shah, N.1    Thomas, T.J.2    Lewis, J.S.3    Klinge, C.M.4    Shirahata, A.5    Gelinas, C.6    Thomas, T.7
  • 38
    • 0142213140 scopus 로고    scopus 로고
    • Polyamines are required for activation of c-Jun NH2-terminal kinase and apoptosis in response to TNF-alpha in IEC-6 cells
    • Bhattacharya S, Ray RM, Viar MJ & Johnson LR (2003) Polyamines are required for activation of c-Jun NH2-terminal kinase and apoptosis in response to TNF-alpha in IEC-6 cells. Am J Physiol Gastrointest Liver Physiol 285, G980-G991.
    • (2003) Am J Physiol Gastrointest Liver Physiol , vol.285
    • Bhattacharya, S.1    Ray, R.M.2    Viar, M.J.3    Johnson, L.R.4
  • 39
    • 0019953046 scopus 로고
    • Inhibitors of polyamine biosynthesis block human cytomegalovirus replication
    • Tyms AS & Williamson JD (1982) Inhibitors of polyamine biosynthesis block human cytomegalovirus replication. Nature 297, 690-691.
    • (1982) Nature , vol.297 , pp. 690-691
    • Tyms, A.S.1    Williamson, J.D.2
  • 40
    • 0021358189 scopus 로고
    • D,L-alpha-Difluoromethylornithine inhibits human cytomegalovirus replication
    • Gibson W, van Breemen R, Fields A, LaFemina R & Irmiere A (1984) D,L-alpha-Difluoromethylornithine inhibits human cytomegalovirus replication. J Virol 50, 145-154.
    • (1984) J Virol , vol.50 , pp. 145-154
    • Gibson, W.1    Van Breemen, R.2    Fields, A.3    Lafemina, R.4    Irmiere, A.5
  • 41
    • 0016608296 scopus 로고
    • Polyamine metabolism in cells infected with herpes simplex virus
    • McCormick FP & Newton AA (1975) Polyamine metabolism in cells infected with herpes simplex virus. J Gen Virol 27, 25-33.
    • (1975) J Gen Virol , vol.27 , pp. 25-33
    • McCormick, F.P.1    Newton, A.A.2
  • 42
    • 0043206229 scopus 로고    scopus 로고
    • Lytic infection of pseudorabies virus in the presence of spermine, spermidine, or DFMO
    • Wang HC & Wong ML (2003) Lytic infection of pseudorabies virus in the presence of spermine, spermidine, or DFMO. Virus Res 94, 121-127.
    • (2003) Virus Res , vol.94 , pp. 121-127
    • Wang, H.C.1    Wong, M.L.2
  • 43
    • 0023742380 scopus 로고
    • Polyamine depletion of cells reduces the infectivity of herpes simplex virus but not the infectivity of Sindbis virus
    • Pohjanpelto P, Sekki A, Hukkanen V & von Bonsdorff CH (1988) Polyamine depletion of cells reduces the infectivity of herpes simplex virus but not the infectivity of Sindbis virus. Life Sci 42, 2011-2018.
    • (1988) Life Sci , vol.42 , pp. 2011-2018
    • Pohjanpelto, P.1    Sekki, A.2    Hukkanen, V.3    Von Bonsdorff, C.H.4
  • 44
    • 0025766094 scopus 로고
    • Polyamine biosynthesis in cells infected with different clinical isolates of human cytomegalovirus
    • Clarke JR & Tyms AS (1991) Polyamine biosynthesis in cells infected with different clinical isolates of human cytomegalovirus. J Med Virol 34, 212-216.
    • (1991) J Med Virol , vol.34 , pp. 212-216
    • Clarke, J.R.1    Tyms, A.S.2
  • 45
    • 0035125111 scopus 로고    scopus 로고
    • Induction of arginases I and II in cornea during herpes simplex virus infection
    • Mistry SK, Zheng M, Rouse BT & Morris SM Jr (2001) Induction of arginases I and II in cornea during herpes simplex virus infection. Virus Res 73, 177-182.
    • (2001) Virus Res , vol.73 , pp. 177-182
    • Mistry, S.K.1    Zheng, M.2    Rouse, B.T.3    Morris Jr., S.M.4
  • 46
    • 0019975618 scopus 로고
    • Inhibition of herpes simplex virus multiplication by activated macrophages: A role for arginase?
    • Wildy P, Gell PG, Rhodes J & Newton A (1982) Inhibition of herpes simplex virus multiplication by activated macrophages: a role for arginase? Infect Immun 37, 40-45.
    • (1982) Infect Immun , vol.37 , pp. 40-45
    • Wildy, P.1    Gell, P.G.2    Rhodes, J.3    Newton, A.4
  • 47
    • 0021089231 scopus 로고
    • Contribution of macrophage arginase in the intrinsic restriction of herpes simplex virus replication in permissive macrophage cultures induced by gamma-interferon containing products of activated spleen cells
    • Sethi KK (1983) Contribution of macrophage arginase in the intrinsic restriction of herpes simplex virus replication in permissive macrophage cultures induced by gamma-interferon containing products of activated spleen cells. Immunobiology 165, 459-474.
    • (1983) Immunobiology , vol.165 , pp. 459-474
    • Sethi, K.K.1
  • 48
    • 0031925465 scopus 로고    scopus 로고
    • Mice lacking inducible nitric-oxide synthase are more susceptible to herpes simplex virus infection despite enhanced Th1 cell responses
    • MacLean A, Wei XQ, Huang FP, Al-Alem UA, Chan WL & Liew FY (1998) Mice lacking inducible nitric-oxide synthase are more susceptible to herpes simplex virus infection despite enhanced Th1 cell responses. J Gen Virol 79, 825-830.
    • (1998) J Gen Virol , vol.79 , pp. 825-830
    • MacLean, A.1    Wei, X.Q.2    Huang, F.P.3    Al-Alem, U.A.4    Chan, W.L.5    Liew, F.Y.6
  • 49
    • 0032720135 scopus 로고    scopus 로고
    • Nitric oxide and macrophage antiviral extrinsic activity
    • Benencia F & Courreges MC (1999) Nitric oxide and macrophage antiviral extrinsic activity. Immunology 98, 363-370.
    • (1999) Immunology , vol.98 , pp. 363-370
    • Benencia, F.1    Courreges, M.C.2
  • 50
    • 0035347173 scopus 로고    scopus 로고
    • Constitutive expression of arginase in microvascular endothelial cells counteracts nitric oxide-mediated vasodilatory function
    • Zhang C, Hein TW, Wang W, Chang CI & Kuo L (2001) Constitutive expression of arginase in microvascular endothelial cells counteracts nitric oxide-mediated vasodilatory function. FASEB J 15, 1264-1266.
    • (2001) FASEB J , vol.15 , pp. 1264-1266
    • Zhang, C.1    Hein, T.W.2    Wang, W.3    Chang, C.I.4    Kuo, L.5
  • 53
    • 0031013624 scopus 로고    scopus 로고
    • Coinduction of nitric-oxide synthase and arginase I in cultured rat peritoneal macrophages and rat tissues in vivo by lipopolysaccharide
    • Sonoki T, Nagasaki A, Gotoh T, Takiguchi M, Takeya M, Matsuzaki H & Mori M (1997) Coinduction of nitric-oxide synthase and arginase I in cultured rat peritoneal macrophages and rat tissues in vivo by lipopolysaccharide. J Biol Chem 272, 3689-3693.
    • (1997) J Biol Chem , vol.272 , pp. 3689-3693
    • Sonoki, T.1    Nagasaki, A.2    Gotoh, T.3    Takiguchi, M.4    Takeya, M.5    Matsuzaki, H.6    Mori, M.7
  • 54
    • 0027934360 scopus 로고
    • Determination of arginase activity in macrophages: A micromethod
    • Corraliza IM, Campo ML, Soler G & Modolell M (1994) Determination of arginase activity in macrophages: a micromethod. J Immunol Methods 174, 231-235.
    • (1994) J Immunol Methods , vol.174 , pp. 231-235
    • Corraliza, I.M.1    Campo, M.L.2    Soler, G.3    Modolell, M.4
  • 55
    • 0014726925 scopus 로고
    • Use of the dansyl reaction in biochemical analysis
    • Seiler N (1970) Use of the dansyl reaction in biochemical analysis. Methods Biochem Anal 18, 259-337.
    • (1970) Methods Biochem Anal , vol.18 , pp. 259-337
    • Seiler, N.1
  • 56
    • 0038581602 scopus 로고    scopus 로고
    • Atmospheric pressure chemical ionization-mass spectrometry method to improve the determination of dansylated polyamine
    • Gaboriau F, Havouis R, Moulinoux JP & Delcros JG (2003) Atmospheric pressure chemical ionization-mass spectrometry method to improve the determination of dansylated polyamine. Anal Biochem 318, 212-220.
    • (2003) Anal Biochem , vol.318 , pp. 212-220
    • Gaboriau, F.1    Havouis, R.2    Moulinoux, J.P.3    Delcros, J.G.4


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