Differential Regulation of Indoleamine 2,3-Dioxygenase Expression by Nitric Oxide and Inflammatory Mediators in IFN-γ-Activated Murine Macrophages and Microglial Cells

Journal of Immunology

Volumn 159, Issue 1, 1997, Pages 419-426

  Alberati Giani, Daniela ^a   Malherbe, Pari ^a   Ricciardi Castagnoli, Paola ^b   Köhler, Christer ^a   Denis Donini, Suzanne ^b   Cesura, Andrea M ^a  

^a F HOFFMANN LA ROCHE LTD   (Switzerland)

^b UNIVERSITY OF MILAN   (Italy)

Author keywords

[No Author keywords available]

Indexed keywords

ENZYME INHIBITOR; GAMMA INTERFERON; INDOLEAMINE 2,3 DIOXYGENASE; LIPOPOLYSACCHARIDE; NITRIC OXIDE; PICOLINIC ACID; PICOLINIC ACID DERIVATIVE; TRYPTOPHAN 2,3 DIOXYGENASE;

ANIMAL; ARTICLE; BAGG ALBINO MOUSE; CELL LINE; DRUG ANTAGONISM; DRUG EFFECT; ENZYMOLOGY; IMMUNOLOGY; MACROPHAGE; MACROPHAGE ACTIVATION; METABOLISM; MICROGLIA; MOUSE;

ANIMALS; CELL LINE; ENZYME INHIBITORS; INDOLEAMINE-PYRROLE 2,3,-DIOXYGENASE; INTERFERON TYPE II; LIPOPOLYSACCHARIDES; MACROPHAGE ACTIVATION; MACROPHAGES; MICE; MICE, INBRED BALB C; MICROGLIA; NITRIC OXIDE; PICOLINIC ACIDS; TRYPTOPHAN OXYGENASE;

EID: 0031179511     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (47)

1. Landolfo, S., and G. Garotta. 1991. IFN-γ, a lymphokine that modulates immunological and inflammatory responses. J. Immunol Res. 3:81.
2. Taylor, M. W., and G. Feng. 1991. Relationship between Interferon-γ, indoleamine 2,3-dioxygenase, and tryptophan cutabolism. FASEB J. 5:2516.
3. Habara-Ohkubo, A., T. Shirahata, O. Takikawa, and R. Yoshida. 1993. Establishment of an antitoxoplasma state by stable expression of mouse indoleamine 2,3-dioxygenase. Infect. Immunol. 61:1810.
4. Christen, S., E. Peterhans, and K. Stocker. 1990. Antioxidant activities of some tryptophan metabolites: possible implication for inflammatory diseases. Proc. Natl. Acad. Sci. USA 87:2506.
5. Heyes, M. P., K. Saito, E. O. Major, S. Milstein, S. P. Markey, and J. H. Vickers. 1993. A mechanism of quinolinic acid formation by brain in inflammatory neurological disease. Brain 116:1425.
6. Blight, A. R., T. I. Cohen, K. Saito, and M. P. Heyes. 1995. Quinolinic acid accumulation and functional deficits following experimental spinal cord injury. Brain 118:735.
7. Moncada, S., R. M. J. Palmer, and E. A. Higgs. 1991. Nitric oxide: physiology, pathophysiology, and pharmacology. Pharmacol. Rev. 43:109.
8. Bredt, D. S., and S. H. Snyder. 1992. Nitric oxide, a novel neuronal messenger. Neuron 8:3.
9. Nathan, C., and Q-W. Xie. 1994. Nitric oxide synthases: roles, tolls, and controls. Cell 78:915.
10. Nathan, C., and J. B. Hibbs, Jr. 1991. Role of nitric oxide synthesis in macrophage antimicrobial activity. Curr. Opin. Immunol. 3:65.
11. Beckmann, J. S., and J. P. Crow. 1993. Pathological implications of nitric oxide, Superoxide and peroxynitrite formation. Biochem. Soc. Trans. 21:330.
12. Dugas, B., M. D. Mossalayi, C. Damais, and J. P. Kolb. 1995. Nitric oxide production by human monocytes: evidence for a role of CD23. Immunol. Today 16:574.
13. Vouldoukis, I., V. Riveros-Moreno, B. Dugas, F. Ouaaz, P. Bécherel, P. Debré, S. Moncada, and M. D. Mossalayi. 1995. The killing of Leishmania major by human macrophages is mediated by nitric oxide FcεRII/CD23 surface antigen. Proc. Natl. Acad. Sci USA 92:7804.
14. Bukrinsky, M. I., H. S. L. M. Nottet, H. Schmidtmayerova, L. Dubrovsky, C. R. Flanagan, M. E. Mullins, S. A. Lipton, and H. E. Gendelman. 1995. Regulation of nitric oxide synthase activity in human immunodeficiency virus type 1 (HIV-1)-infected monocytes: implications for HIV-associated neurological disease. J. Exp. Med. 181:733.
15. De Maria, R., M. G. Cifone, R. Trotta, M. R. Rippo, C. Festuccia, A. Santoni, and R. Testi. 1994. Triggering of human monocyte activation through CD69, a member of the natural killer cell gene complex family of signal transducing receptors. J. Exp. Med. 180:1999.
16. Melillo, G., G. W. Cox, A. Biragyn, L. A. Sheffler, and L. Varesio. 1994. Regulation of nitric-oxide synthase mRNA expression by Interferon-γ and picolinic acid. J. Biol. Chem. 269:8128.
17. Thomas, S. R., D. Mohr, and R. Stocker. 1994. Nitric oxide inhibits indoleamine 2,3-dioxygenase activity in interferon-γ-primed mononuclear phagocytes. J. Biol. Chem. 269:14457.
18. Lutz, M. B., F. Granucci, C. Winzler, G. Marconi, P. Paglia, M. Foti, C. U. Assmann, L. Cirns, M. Resigno, and P. Ricciardi-Castagnoli. 1994. Retroviral immortalization of phagocytic and dendritic cell clones as a tool to investigate functional heterogeneity. J. Immunol. Methods 174:269.
19. Sassano, M., F. Granucci, M. Seveso, G. Marconi, M. Foti, and P. Ricciardi-Castagnoli. 1994. Molecular cloning of a recombinant retrovirus currying a mutated envAKR-mycMH2 fusion gene immortalizing cells of the monocytic-macrophage lineage. Oncogene 9:1473.
20. Righi, M., L. Mori, G. De Libero, M. Sironi, A. Biondi, A. Mantovani, S. D. Donini, and P. Ricciardi-Castagnoli. 1989. Monokine production by microglial cell clones. Eur. J. Immunol. 19:1443.
21. Pirami, L., B. Stockinger, S. Betz Corradin, M. Sironi, M. Sassano, P. Valsasnini, M. Righi, and P. Ricciardi-Caslagnoli. 1991. Mouse macrophage clones immortalized by retrovirus are functionally heterogeneous. Proc. Natl. Acad. Sci. USA 88:7543.
22. Betz-Corradin, S., J. Manuel, S. D. Donini, E. Quattrocchi, and P. Ricciardi-Castagnoli. 1993. Inducible nitric oxide synthase activity of cloned murine microglial cells. Glia 7:255.
23. Denis-Donini, S., J. Glowinsky, and A. Prochiants. 1984. Glial heterogeinity may define the three-dimensional shape of mouse mesencephalic dopaminergic neurons. Nature 307:641.
24. Sacerdote, P., S. Denis-Donini, P. Paglai, F. Granucci, A. E. Panerai, and P. Ricciardi-Castagnoli. 1993. Cloned microglial cells but not macrophages synthetize β-endorphin in response to CRH activation. Glia 9:305.
25. Takikawa, O., T. Kuroiwa, F. Yamazaki, and R. Kido. 1988. Mechanism of Interferon-γ action. Characterization of indoleamine 2,3-dioxygenase in cultured human cells induced by interferon-γ and evaluation of the enzyme-mediated tryptophan degradation in its anticellular activity. J. Biol. Chem. 263:2041.
26. Alberati-Giani, D., P. Ricciardi-Castagnoli, C. Köhler, and A. M. Cesura. 1996. Regulation of the kynurenine metabolic pathway by Interferon-γ in murine cloned macrophages and microglial cells. J. Neurochem. 66:996.
27. Ding, A. H., C. F. Nathan, and D. J. Stuehr. 1988. Release of reactive nitrogen intermediates and reactive oxygen intermediates from mouse peritoneal macrophages: comparison of activating cytokines and evidence for independent production. J. Immunol. 141:2407.
28. Habara-Hohkubo, A., O. Takikawa, and R. Yoshida. 1991. Cloning and expression of a cDNA encoding mouse indoleamine 2,3-dioxygenase. Gene 105:221.
29. Sambrook, J., E. F. Fritsch, and T. Maniatis. 1989. Molecular Cloning: A Laboratory Manual, 2nd Ed. Cold Spring Harbor Laboratory, Cold Spring Harbor, NY.
30. Ehrard, P. B., U. Ganter, J. Bauer, and U. Otten. 1993. Expression of functional trK protooncogene in human monocytes. Proc. Natl. Acad. Sci. USA 90:5423.
31. Murray, H. W., A. Szuro-Sudol, D. Wellner, M. J. Oca, A. M. Granger, D. M. Libby, C. D. Rothermel, and B. Rubin. 1989. Role of tryptophan degradation in respiratory burst-independent antimicrobial activity of gamma Interferon-stimulated human macrophages. Infect. Immunol. 57:845.
32. Varesio, L., M. Clayton, E. Blasi, R. Ruffman, and D. Radzioch. 1990. Picolinic acid, a catabolite of tryptophan, as the second signal in the activation of IFN-γ-primed macrophages. J. Immunol. 145:4265.
33. Blasi, E., A. Bartoli, R. Barluzzi, R. Mazzolla, and F. Bistoni. 1994. Pattern of cytokine gene expression in brains of mice protected by picolinic acid against lethal intracerebral infection with Candida albicans. J. Neuroimmunol. 52:205.
34. Beninger, R. J., A. M. Colton, J. L. Ingles, K. Jhamandas, and R. J. Boegman. 1994. Picolinic acid blocks the neurotoxic but not the neuroexcitant properties of quinolinic acid in the rat brain: evidence from turning behaviour and tyrosine hydroxylase immunohistochemistry. Neuroscience 61:603.
35. Melillo, G., T. Musso, A. Sica, L. S. Taylor, G. W. Cox, and L. Varesio. 1995. A hypoxia-responsive element mediates a novel pathway of activation of the inducible nitric oxide synthase promoter. J. Exp. Med. 182:1683.
36. Venkateshan, C. N., R. Narayanan, M. G. Espey, J. R. Moffet, D. C. Gajdusek, C. J. Gibbs, Jr. and M. A. A. Namboodiri. 1996. Immunocytochemical localization of the endogenous neuroexcitotoxin quinolinate in human peripheral blood monocytes/macrophages and the effect of human T-cell lymphotropic virus type I infection. Proc. Natl. Acad. Sci. USA 93:1636.
37. Koide, Y., and A. Yoshida. 1994. The signal transduction mechanism responsible for gamma interferon-induced indoleamine 2,3-dioxygenase gene expression. Infect. Immunol. 62:948.
38. Stamler, J. S. 1994. Redox signaling: nitrosylation and related target interactions of nitric oxide. Cell 78:931.
39. Chon, S. Y., H. H. Hassanain, R. Pine, and S. L. Gupta. 1995. Involvement of two regulatory elements in interferon-γ-regulated expression of human indoleamine 2,3-dioxygenase gene. J. Interferon Cytokine Res. 15:517.
40. Dai, W., and S. L. Gupta. 1990. Regulation of indoleamine 2,3-dioxygenase gene expression in human fibroblasts by interferon-γ. Biochem. Biophys. Res. Commun. 168:1.
41. Chu, S. C., H.-P. Wu, T. C. Banks, N. T. Eissa, and J. Moss. 1995. Structural diversity in the 5′-untranslated region of cytokine-stimulated human inducible nitric oxide synthase mRNA. J. Biol. Chem. 270:10625.
42. Hu, B., B. D. Hissong, and J. M. Carlin. 1995. Interleukin-1 enhances indoleamine 2,3-dioxygenase activity by increasing specific mRNA expression in human mononuclear phagocytes. J. Interferon Cytokine Res. 15:617.
43. Kozak, M. 1991. Structural features in eukaryotic mRNAs that modulates the initiation of translation. J. Biol. Chem. 266:19867.
44. Peng, H.-B., P. Libby, and J. K. Liao. 1995. Induction and stabilization of lκBα by nitric oxide mediates inhibition of NF-κB. J. Biol. Chem. 270:14214.
45. Schreck, R., K. Albermann, and P. A. Bueuerle. 1992. Nuclear factor κB: an oxidative stress-responsive transcription factor of eukaryotic cells (a review). Free Radical Res. Commun. 17:221.
46. Rutherford, M. S., A. Witsell, and L. B. Schook. 1993. Mechanisms generating functionally heterogeneous macrophages: chaos revisited. J. Leukocyte Biol. 53:602.
47. Mallat, M., and B. Chumak. 1994. Brain macrophages: neurotoxic or neurotrophic effector cells? J. Leukocyte Biol. 56:416.