A prominent role for Sp1 during lipopolysaccharide-mediated induction of the IL-10 promoter in macrophages

Journal of Immunology

Volumn 164, Issue 4, 2000, Pages 1940-1951

  Brightbill, Hans D ^a   Plevy, Scott E ^c   Modlin, Robert L ^a,b   Smale, Stephen T ^a,b  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

^c MOUNT SINAI SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CCAAT ENHANCER BINDING PROTEIN; CYCLIC AMP RESPONSIVE ELEMENT BINDING PROTEIN; INTERLEUKIN 10; LIPOPOLYSACCHARIDE; TRANSCRIPTION FACTOR AP 1; TRANSCRIPTION FACTOR SP1;

ANIMAL CELL; ARTICLE; CONSENSUS SEQUENCE; CONTROLLED STUDY; CYTOKINE PRODUCTION; CYTOKINE RELEASE; DOWN REGULATION; GENE EXPRESSION REGULATION; GENE INDUCTION; GENE TARGETING; INFLAMMATION; MACROPHAGE ACTIVATION; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROMOTER REGION; SIGNAL TRANSDUCTION; TH2 CELL;

EID: 0034651850     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: 10.4049/jimmunol.164.4.1940     Document Type: Article

References (77)

1. Fiorentino, D. F., M. W. Bond, and T. R. Mosmann. 1989. Two types of mouse T helper cell. IV. Th2 clones secrete a factor that inhibits cytokine production by Th1 clones. J. Exp. Med. 170:2081.
2. Barnes, P. F., S. Lu, J. S. Abrams, E. Wang, M. Yamamura, and R. L. Modlin. 1993. Cytokine production at the site of disease of human tuberculosis. Infect. Immun. 61:3482.
3. Caceres-Dittmar, G., F. J. Tapia, M. A. Sanchez, M. Yamamura, K. Uyemura, R. L. Modlin, B. R. Bloom, and J. Convit. 1993. Determination of the cytokine profile in American cutaneous leishmaniasis using the polymerase chain reaction. Clin. Exp. Immunol. 91:500.
4. Gong, J.-H., M. Zhang, R. L. Modlin, P. S. Linsley, D. Iyer, Y. Lin, and P. F. Barnes. 1996. Interleukin-10 down-regulates Mycobacterium tuberculosis induced Th1 responses and CTLA-4 expression. Infect. Immun. 64:913.
5. Sieling, P. A., J. S. Abrams, M. Yamamura, P. Salgame, B. R. Bloom, T. H. Rea, and R. L. Modlin. 1993. Immunosuppressive roles of IL-10 and IL-4 in human infection: in vitro modulation of T cell responses in leprosy. J. Immunol. 150: 5501.
6. Schols, D., and E. De Clercq. 1996. Human immunodeficiency virus type 1 gp120 induces anergy in human peripheral blood lymphocytes by inducing interleukin-10 production. J. Virol. 70:4953.
7. Giambartolomei, G. H., V. A. Dennis, B. L. Lasater, and M. T. Philipp. 1999. Induction of pro-and anti-inflammatory cytokines by Borrelia burgdorferi lipoproteins in monocytes is mediated by CD14. Infect. Immun. 67:140.
8. Van Furth, A. M., E. M. Verhard-Seijmonsbergen, J. A. Langermans, J. T. van Dissel, and R. van Furth. 1999. Anti-CD14 monoclonal antibodies inhibit the production of tumor necrosis factor α and interleukin-10 by human monocytes stimulated with killed and live Haemophilus influenzae or Streptococcus pneumoniae organisms. Infect. Immun. 67:3714.
9. Libraty, D. H., L. E. Airan, K. Uyemura, D. Jullien, B. Spellberg, T. H. Rea, and R. L. Modlin. 1997. Interferon γ differentially regulates interleukin-12 and interleukin-10 production in leprosy. J. Clin. Invest. 99:336.
10. Daftarian, P. M., A. Kumar, M. Kryworuchko, and F. Diaz-Mitoma. 1996. IL-10 production is enhanced in human T cells by IL-12 and IL-6 and in monocytes by tumor necrosis factor-α. J. Immunol. 157:12.
11. Mosmann, T. R. 1994. Properties and functions of interleukin-10. Adv. Immunol. 56:1.
12. Groux, H., F. Cottrez, M. Rouleau, S. Mauze, S. Antonenko, S. Hurst, T. McNeil, M. Bigler, M. G. Roncarolo, and R. L. Coffman. 1999. A transgenic model to analyze the immunoregulatory role of IL-10 secreted by antigen-presenting cells. J. Immunol. 162:1723.
13. Moore, K. W., A. O'Garra, R. de Waal Malefyt, P. Vieira, and T. R. Mosmann. 1993. Interleukin-10. Annu. Rev. Immunol. 11:165.
14. Mosmann, T. R., and K. W. Moore. 1991. The role of IL-10 in crossregulation of Th1 and Th2 responses. Immunol. Today 12:A49.
15. De Waal Malefyt, R., J. Abrams, B. Bennett, C. G. Figdor, and J. E. de Vries. 1991. Interleukin-10 (IL-10) inhibits cytokine synthesis by human monocytes: an autoregulatory role of IL-10 produced by monocytes. J. Exp. Med. 174:1209.
16. Fiorentino, D. F., A. Zlotnik, T. R. Mosmann, M. Howard, and A. O'Garra. 1991. IL-10 inhibits cytokine production by activated macrophages. J. Immunol. 147: 3815.
17. Silva, J. S., P. J. Morrissey, K. H. Grabstein, K. M. Mohler, D. Anderson, and S. G. Reed. 1992. Interleukin-10 and interferon-γ regulation of experimental Trypanosoma cruzi infection. J. Exp. Med. 175:169.
18. D'Andrea, A., M. Aste-Amezaga, N. M. Valiante, X. Ma, M. Kubin, and G. Trinchieri. 1993. Interleukin-10 (IL-10) inhibits human lymphocyte interferon γ-production by suppressing natural killer cell stimulatory factor/IL-12 synthesis in accessory cells. J. Exp. Med. 178:1041.
19. Tripp, C. S., S. F. Wolf, and E. R. Unanue. 1993. Interleukin-12 and tumor necrosis factor α are costimulators of interferon γ production by natural killer cells in severe combined immunodeficiency mice with listeriosis, and interleukin-10 is a physiologic antagonist. Proc. Natl. Acad. Sci. USA 90:3725.
20. Kuhn, R., J. Lohler, D. Rennick, K. Rajewsky, and W. Muller. 1993. Interleukin-10-deficient mice develop chronic enterocolitis. Cell 75:263.
21. -/- mice: an overview. J. Leukocyte Biol. 61:389.
22. Eskdale, J., P. Wordsworth, S. Bowman, M. Field, and G. Gallagher. 1997. Association between polymorphisms at the human IL-10 locus and systemic lupus erythematosus. Tissue Antigens 49:635.
23. Lazarus, M., A. H. Hajeer, D. Turner, P. Sinnott, J. Worthington, W. E. Ollier, and I. V. Hutchinson. 1997. Genetic variation in the interleukin-10 gene promoter and systemic lupus erythematosus. J. Rheum. 24:2314.
24. Mok, C. C., J. S. Lanchbury, D. W. Chan, and C. S. Lau. 1998. Interleukin-10 promoter polymorphisms in southern Chinese patients with systemic lupus erythematosus. Arthritis Rheum. 41:1090.
25. Hajeer, A. H., M. Lazarus, D. Turner, R. A. Mageed, J. Vencovsky, P. Sinnott, I. V. Hutchinson, and W. E. Ollier. 1998. IL-10 gene promoter polymorphisms in rheumatoid arthritis. Scand. J. Rheum. 27:142.
26. Kim, J., R. L. Modlin, R. L. Moy, S. M. Dubinett, T. McHugh, B. J. Nickoloff, and K. Uyemura. 1995. IL-10 production in cutaneous basal and squamous cell carcinomas: a mechanism for evading the local T cell immune response. J. Immunol. 155:2240.
27. Yamamura, M., R. L. Modlin, J. D. Ohmen, and R. L. Moy. 1993. Local expression of anti-inflammatory cytokines in cancer. J. Clin. Invest. 91:1005.
28. Gastl, G. A., J. S. Abrams, D. M. Nanus, R. Oosterkamp, J. Silver, F. Liu, M Chen, A. P. Albino, and N. H. Bander. 1993. Interleukin-10 production by human carcinoma cell lines and its relationship to interleukin-6 expression. Int. J. Cancer 55:96.
29. Huang, M., J. Wang, P. Lee, S. Sharma, J. T. Mao, H. Meissner, K. Uyemura, R. Modlin, J. Wollman, and S. M. Dubinett. 1995. Human non-small cell lung cancer cells express a type 2 cytokine pattern. Cancer Res. 55:3847.
30. Murray, P. J., L. Wang, C. Onufryk, R. I. Tepper, and R. A. Young. 1997. T cell-derived IL-10 antagonizes macrophage function in mycobacterial infection. J. Immunol. 158:315.
31. Murray, P. J., and R. A. Young. 1999. Increased antimycobacterial immunity in interleukin-10-deficient mice. Infect. Immun. 67:3087.
32. Akira, S., and T. Kishimoto. 1997. NF-IL6 and NF-κB in cytokine gene regulation. Adv. Immunol. 65:1.
33. Hamilton, T. A., J. M. Ohmori, S. Tebo, S. Narumi, and C. S. Tannenbaum. 1993. Transmembrane and intracellular signaling events in lipopolysaccharide-stimulated macrophages. In Macrophage-Pathogen Interactions. B. S. Zwilling and T. K. Eisenstein, eds. Marcel Dekker, New York, p.83.
34. Hamilton, T. A., and Y. Ohmori. 1996. Intracellular signaling pathways regulating inflammatory gene expression in mononuclear phagocytes. In Signal Transduction in Leukocytes: Role of G Proteins and Other Pathways. P. M. Lad, J. S. Kapstein, and C. K. Lin, eds. CRC Press, Boca Raton, p.325.
35. Ohmori, Y., and T. A. Hamilton. 1994. Regulation of macrophage gene expression by T cell derived lymphokines. Pharmacol. Ther. 63:235.
36. Murphy, T. L., M. G. Cleveland, P. Kulesza, J. Magram, and K. M. Murphy. 1995. Regulation of interleukin 12 p40 expression through an NF-κB half-site. Mol. Cell. Biol. 15:5258.
37. Plevy, S. E., J. H. Gemberling, S. Hsu, A. J. Dorner, and S. T. Smale. 1997. Multiple control elements mediate activation of the murine and human interleukin-12 p40 promoters: evidence of functional synergy between C/EBP and Rel proteins. Mol. Cell. Biol. 17:4572.
38. Grove, M., and M. Plumb. 1993. C/EBP, NF-κB and c-Ets family members and transcriptional regulation of the cell-specific and inducible macrophage inflammatory protein 1α immediate early gene. Mol. Cell. Biol. 13:5276.
39. Matsusaka, T., K. Fujikawa, Y. Nishio, N. Mukaida, K. Matsushima, T. Kishimoto, and S. Akira. 1993. Transcription factors NF-IL-6 and NF-κB synergistically activate transcription of the inflammatory cytokines, interleukin 6 and interleukin 8. Proc. Natl. Acad. Sci. USA 90:10193.
40. Stein, B., and A. S. Baldwin Jr. 1993. Distinct mechanisms for regulation of the interleukin-8 gene involve synergism and cooperativity between C/EBP and NF-κB. Mol. Cell. Biol. 13:7191.
41. Bondeson, J., K. A. Browne, F. M. Brennan, B. M. Foxwell, and M. Feldmann. 1999. Selective regulation of cytokine induction by adenoviral gene transfer of I-κB α into human macrophages: lipopolysaccharide-induced, but not zymosan-induced, proinflammatory cytokines are inhibited, but IL-10 is nuclear factor-κB independent. J. Immunol. 162:2939.
42. Nemeth, Z. H., G. Hasko, and E. S. Vizi. 1998. Pyrrolidine dithiocarbamate augments IL-10, inhibits TNF-α. MIP-1α, IL-12 and nitric oxide production and protects from the lethal effects of endotoxin. Shock 10:49.
43. Kim, J. M., C. I. Brennan, N. G. Copeland, N. A. Jenkins, T. A. Khan, and K. W. Moore. 1992. Structure of the mouse IL-10 gene and chromosomal localization of the mouse and human genes. J. Immunol. 148:3618.
44. Ho, S. N., H. D. Hunt, R. M. Horton, J. K. Pullen, and L. R. Pease. 1989. Site directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 77:51.
45. Emami, K. H., and M. Carey. 1992. A synergistic increase in potency of a multimerized VP16 transcriptional activation domain. EMBO J. 11:5005.
46. Blau, J., H. Xiao, S. McCracken, P. O'Hare, J. Greenblatt, and D. Bentley. 1996. Three functional classes of transcriptional activation domain. Mol. Cell. Biol. 16:2044.
47. 11110 component of the Drosophila TFIID complex and mediates transcriptional activation. Proc. Natl. Acad. Sci. USA 91:192.
48. Emami, K. H., W. W. Navarre, and S. T. Smale. 1995. Core promoter specificities of the Sp1 and VP16 transcriptional activation domains. Mol. Cell. Biol. 15:5906.
49. Li, Y. S., K. Hayakawa, and R. R. Hardy. 1993. The regulated expression of B lineage associated genes during B cell differentiation in bone marrow and fetal liver. J. Exp. Med. 178:951.
50. Dignam, J. D., R. M. Lebovitz, and R. G. Roeder. 1983. Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei. Nucleic Acids Res. 11:1475.
51. Lo, K., N. R. Landau, and S. T. Smale. 1991. LyF-1, a transcriptional regulator that interacts with a novel class of promoters for lymphocyte specific genes. Mol. Cell. Biol. 11:5229.
52. Hasko, G., C. Szabo, Z. H. Nemeth, V. Kvetan, S. M. Pastores, and E. S. Vizi. 1996. Adenosine receptor agonists differentially regulate IL-10, TNF-α and nitric oxide production in RAW264.7 macrophages and in endotoxemic mice. J. Immunol. 157:4634.
53. Hodge, M. R., H. J. Chun, J. Rengarajan, A. Alt, R. Lieberson, and L. H. Glimcher. 1996. NF-AT-driven interleukin-4 transcription potentiated by NIP45. Science 274:1903.
54. Northrop, J. P., S. N. Ho, L. Chen, D. J. Thomas, L. A. Timmerman, G. P. Nolan, A. Admon, and G. R. Crabtree. 1994. NF-AT components define a family of transcription factors targeted in T cell activation. Nature 369:497.
55. Husmann, M., P. Jehnichen, B. Jahn, D. Schlosshan, E. Romahn, and J. Marx. 1996. A novel Sp1 site in the human interleukin-1βpromoter confers preferential transcription activity in keratinocytes. Eur. J. Immunol. 26:3008.
56. Li, J.-M., M. A. Nicholas, S. Chandrasekharan, Y. Xiong, and X.-F. Wang. 1995. Transforming growth factor-β activates the promoter of cyclin-dependent kinase inhibitor p15INK4B through an Sp1 consensus site. J. Biol. Chem. 270:26750.
57. Li, J.-M., M. B. Datto, X. Shen, P. P. Hu, Y. Yu, and X.-F. Wang. 1998. Sp1, but not Sp3, functions to mediate promoter activation by TGF-β through canonical Sp1 binding sites. Nucleic Acids Res. 26:2449.
58. Ihn, H., and M. Trojanowska. 1997. Sp3 is a transcriptional activator of the human α 2(I) collagen gene. Nucleic Acids Res. 25:3712.
59. Ihn, H., E. C. LeRoy, and M. Trojanowska. 1997. Oncostatin M stimulates transcription of human α 2(I) collagen gene via the Sp1/Sp3 binding site. J. Biol. Chem. 272:24666.
60. Bethea, J. R., Y. Ohmori, and T. A. Hamilton. 1997. A tandem GC box motif is necessary for lipopolysaccharide-induced transcription of the type II TNF receptor gene. J. Immunol. 158:5815.
61. Dynan, W. S., and R. Tjian. 1983. The promoter-specific transcription factor Sp1 binds to upstream sequences in the SV40 early promoter. Cell 35:79.
62. Dynan, W. S., and R. Tjian. 1983 Isolation of transcription factors that discriminate between different promoters recognized by RNA polymerase II. Cell 32: 669.
63. Smale, S. T., M. C. Schmidt, A. J. Berk, and D. Baltimore. 1990. Transcriptional activation by Sp1 as directed through TATA or initiator: specific requirement for mammalian transcription factor IID. Proc. Natl. Acad. Sci. USA 87:4509.
64. Jarvis, B. W., and N. Qureshi. 1997. Inhibition of lipopolysaccharide-induced transcription factor Sp1 binding by spectrally pure diphosphoryl lipid A from Rhodobacter sphaeroides, protein kinase inhibitor H-8. and dexamethasone. Infect. Immun. 65:1640.
65. Courey, A. J., and R. Tjian. 1988. Analysis of Sp1 in vivo reveals multiple transcriptional domains, including a novel glutamine-rich activation motif. Cell 55:887.
66. Smith, C. L., and G. L. Hager. 1997. Transcriptional regulation of mammalian genes in vivo: a tale of two templates. J. Biol. Chem. 272:27493.
67. Inagaki, Y., S. Truter, and F. Ramirez. 1994. Transforming growth factor-β stimulates α 2(I) collagen gene expression through a cis-acting element that contains a Sp1-binding site. J. Biol. Chem. 269:14828.
68. Jackson, S. P., J. J. MacDonald, S. Lees-Miller, and R. Tjian. 1990. GC box binding induces phosphorylation of Sp1 by a DNA-dependent protein kinase. Cell 63:155.
69. Han, I., and J. E. Kudlow. 1997. Reduced O glycosylation of Sp1 is associated with increased proteasome susceptibility. Mol. Cell. Biol. 17:2550.
70. Roos, M. D., K. Su, J. R, Baker, and J. E. Kudlow. 1997. O glycosylation of an Sp1-derived peptide blocks known Sp1 protein interactions. Mol. Cell. Biol. 17: 6472.
71. Pugh, B. F., and R. Tjian. 1990. Mechanism of transcriptional activation by Sp1: evidence for coactivators. Cell 61:1187.
72. Ryu, S., S. Zhou, A. G. Ladurner, and R. Tijan. 1999. The transcriptional cofactor complex CRSP is required for activity of the enhancer-binding protein Sp1. Nature 397:446.
73. Kim, S. J., U. S. Onwuta, Y. I. Lee, R. Li, M. R. Botchan, and P. D. Robbins. 1992. The retinoblastoma gene product regulates Sp1-mediated transcription. Mol. Cell. Biol. 12:2455.
74. Hoey, T., R. O. Weinzierl, G. Gill, J. L. Chen, B. D. Dynlacht, and R. Tjian. 1993. Molecular cloning and functional analysis of Drosophila TAF110 reveal properties expected of coactivators. Cell 72:247.
75. II130 are required for interactions with glutamine-rich transcriptional activators. Mol. Cell. Biol. 18:5734.
76. + T cell clones and peripheral blood T cells. J. Immunol. 149:2378.
77. De Waal Malefyt, R., J. Haanen, H. Spits, M.-G. Roncarolo, A. te Velde, C. Figdor, K. Johnson, R. Kastelein, H. Yssel, and J. E. de Vries. 1991. Interleukin 10 (1L-10) and viral IL-10 strongly reduce antigen-specific human T cell proliferation by diminishing the antigen-presenting capacity of monocytes via down-regulation of class II major histocompatibility complex expression. J. Exp. Med. 174:915.