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Volumn 42, Issue 5, 2009, Pages 286-292

Inhibition of LPS-induced nitric oxide production by transduced Tat-arginine deiminase fusion protein in Raw 264.7 cells

Author keywords

Arginine deiminase (ADI); HIV 1 Tat peptide; Inflammation; Nitric oxide synthase; Protein transduction

Indexed keywords

BACTERIA (MICROORGANISMS); HUMAN IMMUNODEFICIENCY VIRUS; HUMAN IMMUNODEFICIENCY VIRUS 1;

EID: 66549086521     PISSN: 19766696     EISSN: 1976670X     Source Type: Journal    
DOI: 10.5483/BMBRep.2009.42.5.286     Document Type: Article
Times cited : (3)

References (46)
  • 2
    • 0022531132 scopus 로고
    • Biosynthesis and metabolism of arginine in bacteria
    • Cumin, R., Glansdorff, N., Pierard, A. and Stalon, V. (1986) Biosynthesis and metabolism of arginine in bacteria. Microbiol. Rev. 50, 314-352.
    • (1986) Microbiol. Rev. , vol.50 , pp. 314-352
    • Cumin, R.1    Glansdorff, N.2    Pierard, A.3    Stalon, V.4
  • 3
    • 0342748603 scopus 로고    scopus 로고
    • Arginine deiminase inhibits proliferation of human leukemia cells more potently than asparaginase by inducing cell cycle arrest and apoptosis
    • Gong, H., Zolzer, F., von Recklinghausen, G., Havers, W. and Schweigerer, L. (2000) Arginine deiminase inhibits proliferation of human leukemia cells more potently than asparaginase by inducing cell cycle arrest and apoptosis. Leukemia 14, 826-829.
    • (2000) Leukemia , vol.14 , pp. 826-829
    • Gong, H.1    Zolzer, F.2    von Recklinghausen, G.3    Havers, W.4    Schweigerer, L.5
  • 4
    • 0031081394 scopus 로고    scopus 로고
    • Apoptotic cell death of human T lymphoblastoid cells induced by arginine deiminase
    • Komada, Y., Zhang, X. L., Zhou, Y. W., Ido, M. and Azuma, E. (1997) Apoptotic cell death of human T lymphoblastoid cells induced by arginine deiminase. Int. J. Hematol. 65, 129-141.
    • (1997) Int. J. Hematol. , vol.65 , pp. 129-141
    • Komada, Y.1    Zhang, X.L.2    Zhou, Y.W.3    Ido, M.4    Azuma, E.5
  • 5
    • 0026608575 scopus 로고
    • In vivo anti-tumor activity of arginine deiminase purified from Mycoplasma arginini
    • Takaku, H., Takase, M., Abe, S., Hayashi, H. and Miyazaki, K. (1992) In vivo anti-tumor activity of arginine deiminase purified from Mycoplasma arginini. Int. J. Cancer 51, 244-249.
    • (1992) Int. J. Cancer , vol.51 , pp. 244-249
    • Takaku, H.1    Takase, M.2    Abe, S.3    Hayashi, H.4    Miyazaki, K.5
  • 6
    • 0036792124 scopus 로고    scopus 로고
    • Pegylated arginine deiminase (ADI-SSPEG 20,000 MW) inhibits human melanomas and hepatocellular carcinomas in vitro and in vivo
    • Ensor, C. M., Holtsberg, F. W., Bomalaski, J. S. and Clark, M. A. (2002) Pegylated arginine deiminase (ADI-SSPEG 20,000 MW) inhibits human melanomas and hepatocellular carcinomas in vitro and in vivo. Cancer Res. 62, 5443-5450.
    • (2002) Cancer Res. , vol.62 , pp. 5443-5450
    • Ensor, C.M.1    Holtsberg, F.W.2    Bomalaski, J.S.3    Clark, M.A.4
  • 7
    • 0034733165 scopus 로고    scopus 로고
    • Cytoprotective effect of arginine deiminase on taxol-induced apoptosis in DU145 human prostate cancer cells
    • Kang, S. W., Kang, H., Park, I. S., Choi, S. H., Shin, K. H., Chun, Y. S., Chun, B. G. and Min, B. H. (2000) Cytoprotective effect of arginine deiminase on taxol-induced apoptosis in DU145 human prostate cancer cells. Mol. Cells 10, 331-337.
    • (2000) Mol. Cells , vol.10 , pp. 331-337
    • Kang, S.W.1    Kang, H.2    Park, I.S.3    Choi, S.H.4    Shin, K.H.5    Chun, Y.S.6    Chun, B.G.7    Min, B.H.8
  • 8
    • 0037187008 scopus 로고    scopus 로고
    • Characterization of mycoplasma arginine deiminase expressed in E. coli and its inhibitory regulation of nitric oxide synthesis
    • Noh, E. J., Kang, S. W., Shin, Y. J., Kim, D. C., Park, I. S., Kim, M. Y., Chun, B. G. and Min, B. H. (2002) Characterization of mycoplasma arginine deiminase expressed in E. coli and its inhibitory regulation of nitric oxide synthesis. Mol. Cells 13, 137-143.
    • (2002) Mol. Cells , vol.13 , pp. 137-143
    • Noh, E.J.1    Kang, S.W.2    Shin, Y.J.3    Kim, D.C.4    Park, I.S.5    Kim, M.Y.6    Chun, B.G.7    Min, B.H.8
  • 9
    • 0032145202 scopus 로고    scopus 로고
    • Use of L-asparaginase in childhood ALL
    • Muller, H. J. and Boos, J. (1998) Use of L-asparaginase in childhood ALL. Crit. Rev. Oncol. Hematol. 28, 97-113.
    • (1998) Crit. Rev. Oncol. Hematol. , vol.28 , pp. 97-113
    • Muller, H.J.1    Boos, J.2
  • 10
    • 0141763633 scopus 로고    scopus 로고
    • Regeneration of hepatocellular cancer in a patient treated with arginine deiminase
    • Curley, S. A., Bomalaski, J. S., Ensor, C. M., Holtsberg, F. W. and Clark, M. A. (2003) Regeneration of hepatocellular cancer in a patient treated with arginine deiminase. Hepatogastroenterol. 50, 1214-1216.
    • (2003) Hepatogastroenterol. , vol.50 , pp. 1214-1216
    • Curley, S.A.1    Bomalaski, J.S.2    Ensor, C.M.3    Holtsberg, F.W.4    Clark, M.A.5
  • 11
    • 28844493579 scopus 로고    scopus 로고
    • Modulation of arginine metabolic pathways as the potential anti-tumor mechanism of recombinant arginine deimiase
    • Shen, L. J., Beloussow, K. and Shen, W. C. (2006) Modulation of arginine metabolic pathways as the potential anti-tumor mechanism of recombinant arginine deimiase. Cancer Lett. 231, 30-35.
    • (2006) Cancer Lett. , vol.231 , pp. 30-35
    • Shen, L.J.1    Beloussow, K.2    Shen, W.C.3
  • 12
    • 39149099417 scopus 로고    scopus 로고
    • Arginine deiminase, a potential anti-tumor drug
    • Ni, Y., Schwaneberg, U. and Sun, Z. H. (2008) Arginine deiminase, a potential anti-tumor drug. Cancer Lett. 261, 1-11.
    • (2008) Cancer Lett. , vol.261 , pp. 1-11
    • Ni, Y.1    Schwaneberg, U.2    Sun, Z.H.3
  • 13
    • 57049153966 scopus 로고    scopus 로고
    • Recombinant arginine deiminase reduces inducible nitric oxide synthase iNOS-mediated neurotoxicity in a co-culture of neurons and microglia
    • Yu, H. H., Wu, F. L., Lin, S. E. and Shen, L. J. (2008) Recombinant arginine deiminase reduces inducible nitric oxide synthase iNOS-mediated neurotoxicity in a co-culture of neurons and microglia. J. Neurosci. Res. 86, 2963-2972.
    • (2008) J. Neurosci. Res. , vol.86 , pp. 2963-2972
    • Yu, H.H.1    Wu, F.L.2    Lin, S.E.3    Shen, L.J.4
  • 15
    • 0029927787 scopus 로고    scopus 로고
    • Resistance to neurotoxicity in cortical cultures from neuronal nitric oxide synthase-deficient mice
    • Dawson, V. L., Kizushi, V. M., Huang, P. L., Snyder, S. H. and Dawson, T. M. (1996) Resistance to neurotoxicity in cortical cultures from neuronal nitric oxide synthase-deficient mice. J. Neurosci. 16, 2479-2487.
    • (1996) J. Neurosci. , vol.16 , pp. 2479-2487
    • Dawson, V.L.1    Kizushi, V.M.2    Huang, P.L.3    Snyder, S.H.4    Dawson, T.M.5
  • 17
    • 0027945658 scopus 로고
    • Effects of cerebral ischemia in mice deficient in neuronal nitric oxide synthase
    • Huang, Z., Huang, P. L., Panahian, N., Dalkara, T., Fishman M. C. and Moskowitz, M. A. (1994) Effects of cerebral ischemia in mice deficient in neuronal nitric oxide synthase. Science 265, 1883-1885.
    • (1994) Science , vol.265 , pp. 1883-1885
    • Huang, Z.1    Huang, P.L.2    Panahian, N.3    Dalkara, T.4    Fishman, M.C.5    Moskowitz, M.A.6
  • 18
    • 0030664096 scopus 로고    scopus 로고
    • Delayed reduction of ischemic brain injury and neurological deficits in mice lacking the inducible nitric oxide synthase gene
    • Iadecola, C., Zhang, F., Casey, R., Nagayama, M. and Ross, M. E. (1997) Delayed reduction of ischemic brain injury and neurological deficits in mice lacking the inducible nitric oxide synthase gene. J. Neurosci. 17, 9157-9164.
    • (1997) J. Neurosci. , vol.17 , pp. 9157-9164
    • Iadecola, C.1    Zhang, F.2    Casey, R.3    Nagayama, M.4    Ross, M.E.5
  • 19
    • 33845361630 scopus 로고    scopus 로고
    • Motor neuron degeneration in amyotrophic lateral sclerosis mutant superoxide dismutase-1 transgenic mice: mechanism of mitochondriopathy and cell death
    • Martin, L. J., Liu, Z., Chen, K., Price, A. C., Pan, Y., Swa by, J. A. and Golden, W. C. (2007) Motor neuron degeneration in amyotrophic lateral sclerosis mutant superoxide dismutase-1 transgenic mice: mechanism of mitochondriopathy and cell death. J. Comp. Neurol. 500, 20-46.
    • (2007) J. Comp. Neurol. , vol.500 , pp. 20-46
    • Martin, L.J.1    Liu, Z.2    Chen, K.3    Price, A.C.4    Pan, Y.5    Swa by, J.A.6    Golden, W.C.7
  • 20
    • 0032998811 scopus 로고    scopus 로고
    • Nitric oxide synthase and cyclooxygenases: distribution, regulation, and intervention in arthritis
    • Amin, A. R., Attur, M. and Abramson, S. B. (1999) Nitric oxide synthase and cyclooxygenases: distribution, regulation, and intervention in arthritis. Curr. Opin. Rheumatol. 11, 202-209.
    • (1999) Curr. Opin. Rheumatol. , vol.11 , pp. 202-209
    • Amin, A.R.1    Attur, M.2    Abramson, S.B.3
  • 22
    • 0023079312 scopus 로고
    • Endotoxins and disease mechanisms
    • Morrison, D. C. and Ryan, J. L. (1987) Endotoxins and disease mechanisms. Annu. Rev. Med. 38, 417-432.
    • (1987) Annu. Rev. Med. , vol.38 , pp. 417-432
    • Morrison, D.C.1    Ryan, J.L.2
  • 23
    • 0021564388 scopus 로고
    • The cell biology of macrophage activation
    • Adams, D. O. and Hamilton, T. A. (1984) The cell biology of macrophage activation. Annu. Rev. Immunol. 2, 283-318.
    • (1984) Annu. Rev. Immunol. , vol.2 , pp. 283-318
    • Adams, D.O.1    Hamilton, T.A.2
  • 24
  • 25
    • 0035204427 scopus 로고    scopus 로고
    • A peptide carrier for the delivery of biologically active proteins into mammalian cells
    • Morris, M. C., Depollier, J., Mery, J., Heitz, F. and Divita, G. (2001) A peptide carrier for the delivery of biologically active proteins into mammalian cells. Nat. Biotechnol. 19, 1173-1176.
    • (2001) Nat. Biotechnol. , vol.19 , pp. 1173-1176
    • Morris, M.C.1    Depollier, J.2    Mery, J.3    Heitz, F.4    Divita, G.5
  • 26
    • 0033520487 scopus 로고    scopus 로고
    • In vivo protein transduction: delivery of a biologically active protein into the mouse
    • Schwarze, S. R., Ho, A., Vocero-Akbani, A. and Dowdy, S. R. (1999) In vivo protein transduction: delivery of a biologically active protein into the mouse. Science 285, 1569-1572.
    • (1999) Science , vol.285 , pp. 1569-1572
    • Schwarze, S.R.1    Ho, A.2    Vocero-Akbani, A.3    Dowdy, S.R.4
  • 27
    • 0033948268 scopus 로고    scopus 로고
    • Messenger proteins: homeoproteins, TAT and others
    • Prochiantz, A. (2000) Messenger proteins: homeoproteins, TAT and others. Curr. Opin. Cell Biol. 12, 400-406.
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 400-406
    • Prochiantz, A.1
  • 28
    • 0034711454 scopus 로고    scopus 로고
    • Transduction of Cu, Zn-superoxide dismutase mediated by an HIV-1 Tat protein basic domain into mammalian cells
    • Kwon, H. Y., Eum, W. S., Jang, H. W., Kang, J. H., Ryu, J. Y., Lee, B. R., Jin, L. H., Park, J. and Choi, S. Y. (2000) Transduction of Cu,Zn-superoxide dismutase mediated by an HIV-1 Tat protein basic domain into mammalian cells. FEBS Lett. 485, 163-167.
    • (2000) FEBS Lett. , vol.485 , pp. 163-167
    • Kwon, H.Y.1    Eum, W.S.2    Jang, H.W.3    Kang, J.H.4    Ryu, J.Y.5    Lee, B.R.6    Jin, L.H.7    Park, J.8    Choi, S.Y.9
  • 29
    • 3042679656 scopus 로고    scopus 로고
    • HIV-1 Tat mediated protein transduction of Cu, Zn-superoxide dismutase into pancreatic β cells in vitro and in vivo
    • Eum W. S., Choung, I. S., Li, M. Z., Kang, J. H., Kim, D. W., Park, J., Kwon, H. Y. and Choi, S. Y. (2004) HIV-1 Tat mediated protein transduction of Cu,Zn-superoxide dismutase into pancreatic β cells in vitro and in vivo. Free Radic. Biol. Med. 37, 339-349.
    • (2004) Free Radic. Biol. Med. , vol.37 , pp. 339-349
    • Eum, W.S.1    Choung, I.S.2    Li, M.Z.3    Kang, J.H.4    Kim, D.W.5    Park, J.6    Kwon, H.Y.7    Choi, S.Y.8
  • 36
    • 0043201343 scopus 로고    scopus 로고
    • Evidence of protein transduction but not intracellular by protein fused to HIV Tat in retinal cell culture and in vivo
    • Cashman, S. M., Morris, D. J., and Kuman-Singh, R. (2003). Evidence of protein transduction but not intracellular by protein fused to HIV Tat in retinal cell culture and in vivo. Mol. Ther. 8, 130-142.
    • (2003) Mol. Ther. , vol.8 , pp. 130-142
    • Cashman, S.M.1    Morris, D.J.2    Kuman-Singh, R.3
  • 37
    • 0036652959 scopus 로고    scopus 로고
    • Biochemical characterization of the arginine degrading enzymes arginase and arginine deiminase and their effect on nitric oxide production
    • Dillon, B. J., Holtsberq, F. W., Ensor, C. M., Bomalaski, J. S. and Clark, M. A. (2002) Biochemical characterization of the arginine degrading enzymes arginase and arginine deiminase and their effect on nitric oxide production. Med. Sci. Monit. 8, BR248-253.
    • (2002) Med. Sci. Monit. , vol.8
    • Dillon, B.J.1    Holtsberq, F.W.2    Ensor, C.M.3    Bomalaski, J.S.4    Clark, M.A.5
  • 38
    • 0037430556 scopus 로고    scopus 로고
    • Resistance to the anti-proliferative activity of recombinant arginine deiminase in cell culture correlates with the endogenous enzyme, argininosuccinate synthetase
    • Shen, L. J., Lin, W. C., Beloussow, K. and Shen, W. C. (2003) Resistance to the anti-proliferative activity of recombinant arginine deiminase in cell culture correlates with the endogenous enzyme, argininosuccinate synthetase. Cancer Lett. 191, 165-170.
    • (2003) Cancer Lett , vol.191 , pp. 165-170
    • Shen, L.J.1    Lin, W.C.2    Beloussow, K.3    Shen, W.C.4
  • 39
    • 33744908869 scopus 로고    scopus 로고
    • Drug evaluation: ADIPEG-20-a PEGylated arginine deiminase for arginine-auxotrophic cencers
    • Shen, L. J. and Shen, W. C. (2006) Drug evaluation: ADIPEG-20-a PEGylated arginine deiminase for arginine-auxotrophic cencers. Curr. Opin. Mol. Ther. 8, 240-248.
    • (2006) Curr. Opin. Mol. Ther. , vol.8 , pp. 240-248
    • Shen, L.J.1    Shen, W.C.2
  • 40
    • 0043025225 scopus 로고    scopus 로고
    • Arginine deiminase and other antiangiogenic agents inhibit unfavorable neuroblastoma growth: potentiation by irradiation
    • Gong, H., Pottgen, C., Stuben, G., Havers, W., Stuschke, M. and Schweigerer, L. (2003) Arginine deiminase and other antiangiogenic agents inhibit unfavorable neuroblastoma growth: potentiation by irradiation. Int. J. Cancer 106, 723-728.
    • (2003) Int. J. Cancer , vol.106 , pp. 723-728
    • Gong, H.1    Pottgen, C.2    Stuben, G.3    Havers, W.4    Stuschke, M.5    Schweigerer, L.6
  • 41
    • 3342988480 scopus 로고    scopus 로고
    • Induction of hyperammonia in irradiated hepatoma cells: a recapitulation and possible explanation of the phenomenon
    • van Rijn, J., van den Berg, J., Schipper, R. G., de Jong, S., Cuijpers, V., Verhofstad, A. A. and Teerlink, T. (2004) Induction of hyperammonia in irradiated hepatoma cells: a recapitulation and possible explanation of the phenomenon. Br. J. Cancer 91, 150-152.
    • (2004) Br. J. Cancer , vol.91 , pp. 150-152
    • van Rijn, J.1    van den Berg, J.2    Schipper, R.G.3    de Jong, S.4    Cuijpers, V.5    Verhofstad, A.A.6    Teerlink, T.7
  • 42
    • 44949240553 scopus 로고    scopus 로고
    • Arginine deiminase enhances MCF-7 cell radiosensitivity by inducing changes in the expression of cell cycle-related proteins
    • Park, H., Lee, J. B., Shim, Y. J., Shin, Y. J., Jeong, S. Y., Oh, J., Park, G. H., Lee, K. H. and Min, B. H. (2008) Arginine deiminase enhances MCF-7 cell radiosensitivity by inducing changes in the expression of cell cycle-related proteins. Mol. Cells 25, 305-311.
    • (2008) Mol. Cells , vol.25 , pp. 305-311
    • Park, H.1    Lee, J.B.2    Shim, Y.J.3    Shin, Y.J.4    Jeong, S.Y.5    Oh, J.6    Park, G.H.7    Lee, K.H.8    Min, B.H.9
  • 43
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities utilizing the principle of protein-dye binding
    • Bradford, M. (1976) A rapid and sensitive method for the quantitation of microgram quantities utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.1
  • 44
    • 0019170507 scopus 로고
    • Optimization of conditions for the colorimetic determination of citrulline, using deacetyl monoxime
    • Boyde, T. R. and Mohammed, R. (1980) Optimization of conditions for the colorimetic determination of citrulline, using deacetyl monoxime. Anal. Biochem. 107, 424-431.
    • (1980) Anal. Biochem. , vol.107 , pp. 424-431
    • Boyde, T.R.1    Mohammed, R.2
  • 45
    • 0027527363 scopus 로고
    • A fluorometric assay for the measurement of nitrite in biological samples
    • Misko, T. P., Schilling, R. J., Salvemini, D., Moore, W. M. and Currie, M. G. (1993) A fluorometric assay for the measurement of nitrite in biological samples. Anal Biochem. 214, 11-16.
    • (1993) Anal Biochem. , vol.214 , pp. 11-16
    • Misko, T.P.1    Schilling, R.J.2    Salvemini, D.3    Moore, W.M.4    Currie, M.G.5
  • 46
    • 35348837342 scopus 로고    scopus 로고
    • Anti-inflammatory effects of recombinant arginine deiminase originating from Lactococus lactis ssp.lactis ATCC 7962
    • Kim, J. E., Hur, H. J., Lee, K. W. and Lee, H. J. (2007) Anti-inflammatory effects of recombinant arginine deiminase originating from Lactococus lactis ssp.lactis ATCC 7962. J. Microbiol. Biotechnol. 17, 1491-1497.
    • (2007) J. Microbiol. Biotechnol. , vol.17 , pp. 1491-1497
    • Kim, J.E.1    Hur, H.J.2    Lee, K.W.3    Lee, H.J.4


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