메뉴 건너뛰기




Volumn 34, Issue 1, 2004, Pages 200-209

Arginase induction promotes Trypanosoma cruzi intracellular replication of Cruzipain-treated J774 cells through the activation of multiple signaling pathways

Author keywords

Arginase; Macrophage; Parasite antigen; Protein kinase; Trypanosoma cruzi

Indexed keywords

2 (2 AMINO 3 METHOXYPHENYL)CHROMONE; 4 (4 FLUOROPHENYL) 2 (4 METHYLSULFINYLPHENYL) 5 (4 PYRIDYL)IMIDAZOLE; ARGINASE; ARGININE; CALPHOSTIN C; CARBAZOLE DERIVATIVE; CRUZIPAIN; CYCLIC AMP DEPENDENT PROTEIN KINASE; CYCLIC AMP DEPENDENT PROTEIN KINASE INHIBITOR; CYSTEINE PROTEINASE; DRUG DERIVATIVE; GENISTEIN; GROWTH INHIBITOR; IMIDAZOLE DERIVATIVE; INDOLE DERIVATIVE; KT 5720; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE INHIBITOR; MITOGEN ACTIVATED PROTEIN KINASE P38; N(G) HYDROXYARGININE; N(OMEGA) HYDROXYARGININE; N(OMEGA)-HYDROXYARGININE; NITRIC OXIDE; PARASITE ANTIGEN; PROTEIN KINASE C INHIBITOR; PROTEIN P42; PROTEIN P44; PROTEIN TYROSINE KINASE; PROTEIN TYROSINE KINASE INHIBITOR; PYRIDINE DERIVATIVE; PYRROLE DERIVATIVE; UNCLASSIFIED DRUG; UREA;

EID: 1642554787     PISSN: 00142980     EISSN: None     Source Type: Journal    
DOI: 10.1002/eji.200324313     Document Type: Article
Times cited : (52)

References (45)
  • 2
    • 0027742271 scopus 로고
    • The biology of macrophage: I. General principles and properties
    • Seljelid, R. and Eskeland, T., The biology of macrophage: I. General principles and properties. Eur. J. Haematol. 1993. 51: 267-275.
    • (1993) Eur. J. Haematol. , vol.51 , pp. 267-275
    • Seljelid, R.1    Eskeland, T.2
  • 4
    • 0034680145 scopus 로고    scopus 로고
    • Toll-like receptors in the induction of the innate immune response
    • Aderem, A. and Ulevitch, R. J., Toll-like receptors in the induction of the innate immune response. Nature 2000. 406: 782-787.
    • (2000) Nature , vol.406 , pp. 782-787
    • Aderem, A.1    Ulevitch, R.J.2
  • 5
    • 0033082935 scopus 로고    scopus 로고
    • Other functions, other genes: Alternative activation of antigen-presenting cells
    • Goerdt, S. and Orfanos, C. E., Other functions, other genes: alternative activation of antigen-presenting cells. Immunity 1999. 10: 137-142.
    • (1999) Immunity , vol.10 , pp. 137-142
    • Goerdt, S.1    Orfanos, C.E.2
  • 6
    • 0037265240 scopus 로고    scopus 로고
    • Alternative activation of macrophages
    • Gordon, S., Alternative activation of macrophages. Nat. Rev. Immunol. 2003. 3: 23-35.
    • (2003) Nat. Rev. Immunol. , vol.3 , pp. 23-35
    • Gordon, S.1
  • 8
    • 0018694269 scopus 로고
    • Regulation of urea synthesis in rat liver
    • Saheki, T., Sato, Y., Takada, S. and Katsunuma, T., Regulation of urea synthesis in rat liver. J. Biochem. 1979. 86: 745-750.
    • (1979) J. Biochem. , vol.86 , pp. 745-750
    • Saheki, T.1    Sato, Y.2    Takada, S.3    Katsunuma, T.4
  • 9
    • 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. and Mori, M., 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. 1996. 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
  • 11
    • 0026697780 scopus 로고
    • Arginase distribution in tissues of domestic animals
    • Aminlari, M. and Vaseghi, T., Arginase distribution in tissues of domestic animals. Comp. Biochem. Physiol. B. 1992. 103: 385-389.
    • (1992) Comp. Biochem. Physiol. B. , vol.103 , pp. 385-389
    • Aminlari, M.1    Vaseghi, T.2
  • 13
    • 0031013624 scopus 로고    scopus 로고
    • Coinduction of nitric-oxide synthase and arginase I in cultured rat peritoneal macrophages and rat tissues in vitro by lipopolysaccharide
    • Sonoki, T., Nagasaki, A., Gotoh, T., Takiguchi, M., Takeya, M., Matsuzaki, H. and Mori, M., Coinduction of nitric-oxide synthase and arginase I in cultured rat peritoneal macrophages and rat tissues in vitro by lipopolysaccharide. J. Biol. Chem. 1997. 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
  • 14
    • 0028979170 scopus 로고
    • Transforming growth factor beta stimulates arginase activity in macrophages: Implications for the regulation of macrophage cytotoxicity
    • Boutard, V., Havouis, R., Fouqueray, B., Philippe, C., Moulinoux, J. P. and Baud, L., Transforming growth factor beta stimulates arginase activity in macrophages: implications for the regulation of macrophage cytotoxicity. J. Immunol. 1995. 155: 2077-2084.
    • (1995) J. Immunol. , vol.155 , pp. 2077-2084
    • Boutard, V.1    Havouis, R.2    Fouqueray, B.3    Philippe, C.4    Moulinoux, J.P.5    Baud, L.6
  • 15
    • 0031895498 scopus 로고    scopus 로고
    • Arginase activity is modulated by IL-4 and HOArg in nephritic glomeruli and mesangial cells
    • Waddington, S. N., Tam F. W. K., Cook, H. T. and Cattell, V., Arginase activity is modulated by IL-4 and HOArg in nephritic glomeruli and mesangial cells. Am. J. Physiol. Renal Physiol. 1998. 274: 473-480.
    • (1998) Am. J. Physiol. Renal Physiol. , vol.274 , pp. 473-480
    • Waddington, S.N.1    Tam, F.W.K.2    Cook, H.T.3    Cattell, V.4
  • 16
    • 0028919209 scopus 로고
    • Arginase induction by suppressors of nitric oxide synthesis (IL-4, IL-10 and PGE2) in murine bone-marrow-derived macrophages
    • Corraliza, I. M., Soler, G., Eichmann, K. and Modolell, M., Arginase induction by suppressors of nitric oxide synthesis (IL-4, IL-10 and PGE2) in murine bone-marrow-derived macrophages. Biochem. Biophys. Res. Comm. 1995. 206: 667-673.
    • (1995) Biochem. Biophys. Res. Comm. , vol.206 , pp. 667-673
    • Corraliza, I.M.1    Soler, G.2    Eichmann, K.3    Modolell, M.4
  • 17
    • 0028916297 scopus 로고
    • Reciprocal regulation of the nitric oxide synthase/arginase balance in mouse bone marrow-derived macrophages by Th1 and Th2 cytokines
    • Modolell, M., Corraliza, I. M., Link, F., Soler, G. and Eichmann, K., Reciprocal regulation of the nitric oxide synthase/arginase balance in mouse bone marrow-derived macrophages by Th1 and Th2 cytokines. Eur. J. Immunol. 1995. 25: 1101-1104.
    • (1995) Eur. J. Immunol. , vol.25 , pp. 1101-1104
    • Modolell, M.1    Corraliza, I.M.2    Link, F.3    Soler, G.4    Eichmann, K.5
  • 19
    • 0034663958 scopus 로고    scopus 로고
    • The involvement of tyrosine kinases, cyclic AMP/protein kinase A, and p38 mitogen-activated protein kinase in IL-13-mediated arginase I induction in macrophages: Its implications in IL-13-inhibited nitric oxide production
    • Chang, C. I., Zoghi, B., Liao, J. C. and Kuo, L., The involvement of tyrosine kinases, cyclic AMP/protein kinase A, and p38 mitogen-activated protein kinase in IL-13-mediated arginase I induction in macrophages: its implications in IL-13-inhibited nitric oxide production. J. Immunol. 2000. 165: 2134-2141.
    • (2000) J. Immunol. , vol.165 , pp. 2134-2141
    • Chang, C.I.1    Zoghi, B.2    Liao, J.C.3    Kuo, L.4
  • 20
    • 0033214545 scopus 로고    scopus 로고
    • Th1/Th2-regulated expression of arginase isoforms in murine macrophages and dendritic cells
    • Munder, M., Eichmann, K., Morán, J. M., Centeno, F., Soler, G. and Modolell, M., Th1/Th2-regulated expression of arginase isoforms in murine macrophages and dendritic cells. J. Immunol. 1999. 163: 3771-3777.
    • (1999) J. Immunol. , vol.163 , pp. 3771-3777
    • Munder, M.1    Eichmann, K.2    Morán, J.M.3    Centeno, F.4    Soler, G.5    Modolell, M.6
  • 21
    • 0036826843 scopus 로고    scopus 로고
    • Alternative activation and increase of Trypanosoma cruzi survival in murine macrophages stimulated by cruzipain, a parasite antigen
    • Stempin, C., Giordanengo, L., Gea, S. and Cerbán, F., Alternative activation and increase of Trypanosoma cruzi survival in murine macrophages stimulated by cruzipain, a parasite antigen. J. Leukoc. Biol. 2002. 72: 727-734.
    • (2002) J. Leukoc. Biol. , vol.72 , pp. 727-734
    • Stempin, C.1    Giordanengo, L.2    Gea, S.3    Cerbán, F.4
  • 22
    • 0030021084 scopus 로고    scopus 로고
    • Leishmania promastigotes selectively inhibit interleukin-12 induction in bone-marrow-derived macrophages from susceptible and resistant mice
    • Carrera, L., Gazzinelli, R. T., Badolato, R., Hieny, S., Muller, W., Jun, R. and Sacks, D. L., Leishmania promastigotes selectively inhibit interleukin-12 induction in bone-marrow-derived macrophages from susceptible and resistant mice. J. Exp. Med. 1996. 183: 515-526.
    • (1996) J. Exp. Med. , vol.183 , pp. 515-526
    • Carrera, L.1    Gazzinelli, R.T.2    Badolato, R.3    Hieny, S.4    Muller, W.5    Jun, R.6    Sacks, D.L.7
  • 23
    • 0035881856 scopus 로고    scopus 로고
    • Toxoplasma gondii tachyzoites inhibit proinflamatory cytokine induction in infected macrophages by prevening nuclear translocation of the transcription factor NFkB
    • Butcher, B. A., Kim, L., Johnson, P. F. and Denkers, E. Y., Toxoplasma gondii tachyzoites inhibit proinflamatory cytokine induction in infected macrophages by prevening nuclear translocation of the transcription factor NFkB. J. Immunol. 2001. 167: 2193-2201.
    • (2001) J. Immunol. , vol.167 , pp. 2193-2201
    • Butcher, B.A.1    Kim, L.2    Johnson, P.F.3    Denkers, E.Y.4
  • 24
    • 0037303310 scopus 로고    scopus 로고
    • In the belly of the beast: Subversion of macrophage proinflamatory signaling cascades during Toxoplasma gondii infection
    • Denkers, E. Y., Kim, L. and Butcher, B. A., In the belly of the beast: subversion of macrophage proinflamatory signaling cascades during Toxoplasma gondii infection. Cell. Microbiol. 2003. 5: 75-83.
    • (2003) Cell. Microbiol. , vol.5 , pp. 75-83
    • Denkers, E.Y.1    Kim, L.2    Butcher, B.A.3
  • 25
    • 0036263080 scopus 로고    scopus 로고
    • Differential regulation of the mitogen-activated protein kinases by pathogenic and nonpathogenic mycobacteria
    • Roach, S. K. and Schorey, J. S., Differential regulation of the mitogen-activated protein kinases by pathogenic and nonpathogenic mycobacteria. Infect. Immun. 2002. 70: 3040-3052.
    • (2002) Infect. Immun. , vol.70 , pp. 3040-3052
    • Roach, S.K.1    Schorey, J.S.2
  • 26
    • 0037346775 scopus 로고    scopus 로고
    • Macrophage signaling upon mycobacterial infection: The MAP kinases lead the way
    • Schorey, J. S. and Cooper, A. M., Macrophage signaling upon mycobacterial infection: the MAP kinases lead the way. Cell. Microbiol. 2003. 5: 133-142.
    • (2003) Cell Microbiol. , vol.5 , pp. 133-142
    • Schorey, J.S.1    Cooper, A.M.2
  • 27
    • 0033838607 scopus 로고    scopus 로고
    • Inhibition of extracellular signal-regulated kinase suppresses endotoxin-induced nitric oxide synthesis in mouse macrophages and in human colon epithelial cells
    • Lahti, A., Lahde, M., Kankaanranta, H. and Moilanen, E., Inhibition of extracellular signal-regulated kinase suppresses endotoxin-induced nitric oxide synthesis in mouse macrophages and in human colon epithelial cells. J. Pharmacol. Exp. Ther. 2000. 294: 1188-1194.
    • (2000) J. Pharmacol. Exp. Ther. , vol.294 , pp. 1188-1194
    • Lahti, A.1    Lahde, M.2    Kankaanranta, H.3    Moilanen, E.4
  • 28
    • 0028270719 scopus 로고
    • Regulation of biosynthesis of nitric oxide
    • Nathan, C. and Xie, Q. W., Regulation of biosynthesis of nitric oxide. J. Biol. Chem. 1994. 269: 13725-13728.
    • (1994) J. Biol. Chem. , vol.269 , pp. 13725-13728
    • Nathan, C.1    Xie, Q.W.2
  • 29
    • 0029437226 scopus 로고
    • Nitric oxide synthases: Gene structure and regulation
    • Wang, Y. and Marsden, P. A., Nitric oxide synthases: gene structure and regulation. Adv. Pharmacol. 1995. 34: 71-90.
    • (1995) Adv. Pharmacol. , vol.34 , pp. 71-90
    • Wang, Y.1    Marsden, P.A.2
  • 30
    • 0035911231 scopus 로고    scopus 로고
    • The inhibition of arginase by N-omega-hydroxy-L-arginine controls the growth of Leishmania inside macrophages
    • Iniesta, V., Gomez Nieto, C. and Corraliza, I., The inhibition of arginase by N-omega-hydroxy-L-arginine controls the growth of Leishmania inside macrophages. J. Exp. Med. 2001. 193: 777-783.
    • (2001) J. Exp. Med. , vol.193 , pp. 777-783
    • Iniesta, V.1    Gomez Nieto, C.2    Corraliza, I.3
  • 32
    • 0036072438 scopus 로고    scopus 로고
    • Pyridinylimidazole p38 mitogen-activated protein kinase inhibitors block intracellular Toxoplasma gondii replication
    • Wei, S., Marches, F., Daniel, B., Sonda, S., Heidenreich, K. and Curiel, T., Pyridinylimidazole p38 mitogen-activated protein kinase inhibitors block intracellular Toxoplasma gondii replication. Int. J. Parasitol. 2002. 32: 969-977.
    • (2002) Int. J. Parasitol. , vol.32 , pp. 969-977
    • Wei, S.1    Marches, F.2    Daniel, B.3    Sonda, S.4    Heidenreich, K.5    Curiel, T.6
  • 33
    • 0036717724 scopus 로고    scopus 로고
    • Activation of p38 mitogen-activated protein kinase attenuates Leishmania donovani infection in macrophages
    • Junghae, M. and Raynes, J. G., Activation of p38 mitogen-activated protein kinase attenuates Leishmania donovani infection in macrophages. Infect. Immun. 2002. 70: 5026-5035.
    • (2002) Infect. Immun. , vol.70 , pp. 5026-5035
    • Junghae, M.1    Raynes, J.G.2
  • 34
    • 0029019017 scopus 로고
    • Interleukin-13 signal transduction in lymphohemopoietic cells. Similarities and differences in signal transduction with interleukin-4 and insulin
    • Welham, M. J., Learmonth, L., Bone, H. and Schrader, J. W., Interleukin-13 signal transduction in lymphohemopoietic cells. Similarities and differences in signal transduction with interleukin-4 and insulin. J. Biol. Chem. 1995. 270: 12286-12296.
    • (1995) J. Biol. Chem. , vol.270 , pp. 12286-12296
    • Welham, M.J.1    Learmonth, L.2    Bone, H.3    Schrader, J.W.4
  • 35
    • 0030051528 scopus 로고    scopus 로고
    • MKK3- and MKK6-regulated gene expression is mediated by the p38 mitogen-activated protein kinase signal transduction pathway
    • Raingeaud, J., Whitmarsh, A. J., Barrett, T., Derijard, B. and Davis, R. J., MKK3- and MKK6-regulated gene expression is mediated by the p38 mitogen-activated protein kinase signal transduction pathway. Mol. Cell. Biol. 1996. 16: 247-255.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 247-255
    • Raingeaud, J.1    Whitmarsh, A.J.2    Barrett, T.3    Derijard, B.4    Davis, R.J.5
  • 36
    • 0031964698 scopus 로고    scopus 로고
    • Involvement of p38 mitogen-activated protein kinase signaling pathway in the rapid induction of the 78-kDa glucose-regulated protein in 9L rat brain tumor cells
    • Chen, K. D., Chen, L. Y., Huang, H. L., Lieu, C. H., Chang, Y. N., Chang, M. D. and Lai, Y. K., Involvement of p38 mitogen-activated protein kinase signaling pathway in the rapid induction of the 78-kDa glucose-regulated protein in 9L rat brain tumor cells. J. Biol. Chem. 1998. 273: 749-755.
    • (1998) J. Biol. Chem. , vol.273 , pp. 749-755
    • Chen, K.D.1    Chen, L.Y.2    Huang, H.L.3    Lieu, C.H.4    Chang, Y.N.5    Chang, M.D.6    Lai, Y.K.7
  • 38
    • 0035576207 scopus 로고    scopus 로고
    • Differential regulation of nitric oxide synthase-2 and arginase-1 by type 1/type 2 cytokines in vivo: Granulomatous pathology is shaped by the pattern of L-arginine metabolism
    • Hesse, M., Modollel, M., La Flamme, A. C., Schito, M., Fuentes, J. M., Cheever, A. W., Pearce, E. J. and Wynn, T. A., Differential regulation of nitric oxide synthase-2 and arginase-1 by type 1/type 2 cytokines in vivo: granulomatous pathology is shaped by the pattern of L-arginine metabolism. J. Immunol. 2001. 167: 6533-6544.
    • (2001) J. Immunol. , vol.167 , pp. 6533-6544
    • Hesse, M.1    Modollel, M.2    La Flamme, A.C.3    Schito, M.4    Fuentes, J.M.5    Cheever, A.W.6    Pearce, E.J.7    Wynn, T.A.8
  • 39
    • 0034842685 scopus 로고    scopus 로고
    • Arginase expression in peritoneal macrophages and increase in circulating polyamine levels in mice infected with Schistosoma mansoni
    • Abdallahi, O. M., Bensalem, H., Augier, R., Diagana, M., De Reggi, M. and Gharib, B., Arginase expression in peritoneal macrophages and increase in circulating polyamine levels in mice infected with Schistosoma mansoni. Cell. Mol. Life Sci. 2001. 58: 1350-1357.
    • (2001) Cell Mol. Life Sci. , vol.58 , pp. 1350-1357
    • Abdallahi, O.M.1    Bensalem, H.2    Augier, R.3    Diagana, M.4    De Reggi, M.5    Gharib, B.6
  • 40
    • 0035107942 scopus 로고    scopus 로고
    • Alternative versus classical macrophage activation during experimental African trypanosomosis
    • Namangala, B., De Baetselier, P., Noël, W., Brys, L. and Beschin, A., Alternative versus classical macrophage activation during experimental African trypanosomosis. J. Leukoc. Biol. 2001. 69: 387-396.
    • (2001) J. Leukoc. Biol. , vol.69 , pp. 387-396
    • Namangala, B.1    De Baetselier, P.2    Noël, W.3    Brys, L.4    Beschin, A.5
  • 41
    • 0036232437 scopus 로고    scopus 로고
    • Cruzipain, a major Trypanosoma cruzi antigen, conditions the host immune response in favor of parasite
    • Giordanengo, L., Guiñazu, N., Stempin, C., Fretes, R., Cerban, F. and Gea, S., Cruzipain, a major Trypanosoma cruzi antigen, conditions the host immune response in favor of parasite. Eur. J. Immunol. 2002. 32: 1003-1011.
    • (2002) Eur. J. Immunol. , vol.32 , pp. 1003-1011
    • Giordanengo, L.1    Guiñazu, N.2    Stempin, C.3    Fretes, R.4    Cerban, F.5    Gea, S.6
  • 42
    • 0027818526 scopus 로고
    • Purification of the major cystein proteinase (cruzipain) from Trypanosoma cruzi by affinity chromatography
    • Labriola, C., Souza, M. and Cazzulo, J. J., Purification of the major cystein proteinase (cruzipain) from Trypanosoma cruzi by affinity chromatography. Biol. Res. 1993. 26: 101-107.
    • (1993) Biol. Res. , vol.26 , pp. 101-107
    • Labriola, C.1    Souza, M.2    Cazzulo, J.J.3
  • 43
    • 0025707153 scopus 로고
    • A major cystein proteinase is developmentally regulated in Trypanosoma cruzi
    • Campetella, O., Martinez, J. and Cazzulo, J. J., A major cystein proteinase is developmentally regulated in Trypanosoma cruzi. FEMS Microbiol. Lett. 1990. 55: 145-149.
    • (1990) FEMS Microbiol. Lett. , vol.55 , pp. 145-149
    • Campetella, O.1    Martinez, J.2    Cazzulo, J.J.3
  • 44
    • 0024491490 scopus 로고
    • Further characterization and partial amino acid sequence of a cystein proteinase from Trypanosoma cruzi
    • Cazzulo, J. J., Couso, R., Raimondi, A., Wernstedt, C. and Hellman, U., Further characterization and partial amino acid sequence of a cystein proteinase from Trypanosoma cruzi. Mol. Biochem. Parasitol. 1989. 33: 33-42.
    • (1989) Mol. Biochem. Parasitol. , vol.33 , pp. 33-42
    • Cazzulo, J.J.1    Couso, R.2    Raimondi, A.3    Wernstedt, C.4    Hellman, U.5
  • 45
    • 0027934360 scopus 로고
    • Determination of arginase activity in macrophages: A micro-method
    • Corraliza, I. M., Campo, M. L., Soler, G. and Modollel, M., Determination of arginase activity in macrophages: a micro-method. J. Immunol. Methods 1994. 174: 231-235.
    • (1994) J. Immunol. Methods , vol.174 , pp. 231-235
    • Corraliza, I.M.1    Campo, M.L.2    Soler, G.3    Modollel, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.