Regulation of B7.1 costimulatory molecule is mediated by the IFN regulatory factor-7 through the activation of JNK in lipopolysaccharide-stimulated human monocytic cells

Journal of Immunology

Volumn 175, Issue 9, 2005, Pages 5690-5700

  Lim, Wilfred ^a   Gee, Katrina ^a   Mishra, Sasmita ^a   Kumar, Ashaok ^a,b  

^a UNIVERSITY OF OTTAWA   (Canada)

^b CHILDREN S HOSPITAL OF EASTERN ONTARIO   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

ANTHRA[1,9 CD]PYRAZOL 6(2H) ONE; B7 ANTIGEN; BACTERIUM LIPOPOLYSACCHARIDE; CD14 ANTIGEN; CD28 ANTIGEN; CYTOTOXIC T LYMPHOCYTE ANTIGEN 4; DEXAMETHASONE; INTERFERON REGULATORY FACTOR 7; LUCIFERASE; MITOGEN ACTIVATED PROTEIN KINASE P38; SMALL INTERFERING RNA; STRESS ACTIVATED PROTEIN KINASE 1;

ANTIGEN EXPRESSION; APOPTOSIS; ARTICLE; BINDING SITE; CELL DIFFERENTIATION; CELL PROLIFERATION; CONTROLLED STUDY; DNA TRANSFECTION; ENZYME ACTIVATION; FLOW CYTOMETRY; GEL MOBILITY SHIFT ASSAY; HUMAN; HUMAN CELL; MONOCYTE; PERIPHERAL BLOOD MONONUCLEAR CELL; PRIORITY JOURNAL; PROMOTER REGION; REVERSE TRANSCRIPTION POLYMERASE CHAIN REACTION; T LYMPHOCYTE ACTIVATION; TRANSCRIPTION INITIATION SITE; TRANSCRIPTION REGULATION; WESTERN BLOTTING;

EID: 27144517972     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: 10.4049/jimmunol.175.9.5690     Document Type: Article

References (61)

1. Carreno, B. M., and M. Collins. 2002. The B7 family of ligands and its receptors: new pathways for costimulation and inhibition of immune responses. Annu. Rev. Immunol 20: 29-53.
2. Sharpe, A. H., and G. J. Freeman. 2002. The B7-CD28 superfamily. Nat. Rev. Immunol. 2: 116-126.
3. Fraser, J. D., B. A. Irving, G. R. Crabtree, and A. Weiss. 1991. Regulation of interleukin-2 gene enhancer activity by the T cell accessory molecule CD28. Science 251: 313-316.
4. Wells, A. D., H. Gudmundsdottir, and L. A. Turka. 1997. Following the fate of individual T cells throughout activation and clonal expansion: signals from T cell receptor and CD28 differentially regulate the induction and duration of a proliferative response. J. Clin. Invest. 100: 3173-3183.
5. Prilliman, K. R., E. E. Lemmens, G. Palioungas, T. G. Wolfe, J. P. Allison, A. H. Sharpe, and S. P. Schoenberger. 2002. Cutting edge: a crucial role for B7-CD28 in transmitting T help from APC to CTL. J. Immunol. 169: 4094-4097.
6. Chang, T. T., C. Jabs, R. A. Sobel, V. K. Kuchroo, and A. H. Sharpe. 1999. Studies in B7-deficient mice reveal a critical role for B7 costimulation in both induction and effector phases of experimental autoimmune encephalomyelitis. J. Exp. Med. 190: 733-740.
7. Guerder, S., J. Meyerhoff, and R. Flavell. 1994. The role of the T cell costimulator B7-1 in autoimmunity and the induction and maintenance of tolerance to peripheral antigen. Immunity 1: 155-166.
8. Salomon, B., and J. A. Bluestone. 2001. Complexities of CD28/B7: CTLA-4 costimulatory pathways in autoimmunity and transplantation. Annu. Rev. Immunol. 19: 225-252.
9. Kuchroo, V. K., M. P. Das, J. A. Brown, A. M. Ranger, S. S. Zamvil, R. A. Sobel, H. L. Weiner, N. Nabavi, and L. H. Glimcher. 1995. B7-1 and B7-2 costimulatory molecules activate differentially the Th1/Th2 developmental pathways: application to autoimmune disease therapy. Cell 80: 707-718.
10. Lenschow, D. J., S. C. Ho, H. Sattar, L. Rhee, G. Gray, N. Nabavi, K. C. Herold, and J. A. Bluestone. 1995. Differential effects of anti-B7-1 and anti-B7-2 monoclonal antibody treatment on the development of diabetes in the nonobese diabetic mouse. J. Exp. Med. 181: 1145-1155.
11. + tumor cells are potent vaccines for stimulating tumor rejection in tumor-bearing mice. J. Exp. Med. 181: 619-629:
12. Gao, J. X., H. Zhang, X. F. Bai, J. Wen, X. Zheng, J. Liu, P. Zheng, and Y. Liu. 2002. Perinatal blockade of B7-1 and B7-2 inhibits clonal deletion of highly pathogenic autoreactive T cells. J. Exp. Med. 195: 959-971.
13. Boussiotis, V. A., G. J. Freeman, J. G. Gribben, J. Daley, G. Gray, and L. M. Nadler. 1993. Activated human B lymphocytes express three CTLA-4 counterreceptors that costimulate T-cell activation. Proc. Natl. Acad. Sci. USA 90: 11059-11063.
14. Freeman, G. J., J. G. Gribben, V. A. Boussiotis, J. W. Ng, V. A. J. Restivo, L. A. Lombard, G. S. Gray, and L. M. Nadler. 1993. Cloning of B7-2: a CTLA-4 counter-receptor that costimulates human T cell proliferation. Science 262: 909-911.
15. Creery, W. D., F. Diaz-Mitoma, L. Filion, and A. Kumar. 1996. Differential modulation of B7-1 and B7-2 isoform expression on human monocytes by cytokines which influence the development of T helper cell phenotype. Eur. J. Immunol. 26: 1273-1277.
16. Hathcock, K. S., G. Laszlo, C. Pucillo, P. Linsley, and R. J. Hodes. 1994. Comparative analysis of B7-1 and B7-2 costimulatory ligands: expression and function. J. Exp. Med. 180: 631-640.
17. Paust, S., L. Lu, N. McCarty, and H. Cantor. 2004. Engagement of B7 on effector T cells by regulatory T cells prevents autoimmune disease. Proc. Natl. Acad. Sci. USA 101: 10398-10403
18. Curiel, R. E., C. S. Garcia, S. Rottschafer, M. C. Bosco, and I. Espinoza-Delgado. 1999. Enhanced B7-2 gene expression by interferon-γ in human monocytic cells is controlled through transcriptional and posttranscriptional mechanisms. Blood 94: 1782-1789.
19. Thompson, C. B. 1995. Distinct roles for the costimulatory ligands B7-1 and B7-2 in T helper cell differentiation? Cell 81: 979-982.
20. Suvas, S., V. Singh, S. Sahdev, H. Vohra, and J. N. Agrewala. 2002. Distinct role of CD80 and CD86 in the regulation of the activation of B cell and B cell lymphoma. J. Biol. Chem. 277: 7766-7775.
21. Schweitzer, A. N., and A. H. Sharpe. 1998. Studies using antigen-presenting cells lacking expression of both B7-1 (CD80) and B7-2 (CD86) show distinct requirements for B7 molecules during priming versus restimulation of Th2 but not Th1 cytokine production. J. Immunol. 161: 2762-2771.
22. Collins, A. V., D. W. Brodie, R. J. Gilbert, A. Iaboni, R. Manso-Sancho, B. Walse, D. I. Stuart, P. A. van der Merwe, and S. J. Davis. 2002. The interaction properties of costimulatory molecules revisited. Immunity 17: 201-210.
23. Linsley, P. S., J. L. Greene, W. Brady, J. Bajorath, J. A. Ledbetter, and R. Peach. 1994. Human B7-1 (CD80) and B7-2 (CD86) bind with similar avidities but distinct kinetics to CD28 and CTLA-4 receptors. Immunity 1: 793-801.
24. van der Merwe, P. A., D. L. Bodian, S. Daenke, P. Linsley, and S. J. Davis. 1997. CD80 (B7-1) binds both CD28 and CTLA-4 with a low affinity and very fast kinetics. J. Exp. Med. 185: 393-403.
25. Waterhouse, P., J. M. Penninger, E. Timms, A. Wakeham, A. Shahinian, K. P. Lee, C. B. Thompson, H. Griesser, and T. W. Mak. 1995. Lymphoproliferative disorders with early lethality in mice deficient in Ctla-4. Science 270: 985-988.
26. Zheng, Y., C. N. Manzotti, M. Liu, F. Burke, K. I. Mead, and D. M. Sansom. 2004. CD86 and CD80 differentially modulate the suppressive function of human regulatory T cells. J. Immunol. 172: 2778-2784.
27. Liu, L., V. K. Kuchroo, and H. L. Weiner. 1999. B7.2 (CD86) but not B7.1 (CD80) costimulation is required for the induction of low dose oral tolerance. J. Immunol 163: 2284-2290.
28. Zhao, J., G. J. Freeman, G. S. Gray, L. M. Nadler, and L. H. Glimcher. 1996. A cell type-specific enhancer in the human B7.1 gene regulated by NF-κB. J. Exp. Med. 183: 777-789.
29. Fong, T. C., Y. Wu, and T. J. Kipps. 1996. Identification of a promoter element that regulates tissue-specific expression of the human CD80 (B7.1) gene. J. Immunol. 157: 4442-4450.
30. Lewis, T. S., P. S. Shapiro, and N. G. Ahn. 1998. Signal transduction through MAP kinase cascades. Adv. Cancer Res. 74: 49-139.
31. Liu, M. K., P. Herrera-Velit, R. W. Brownsey, and N. E. Reiner. 1994. CD14-dependent activation of protein kinase C and mitogen-activated protein kinases (p42 and p44) in human monocytes treated with bacterial lipopolysaccharide. J. Immunol. 153: 2642-2652.
32. Ma, W., W. Lim, K. Gee, S. Aucoin, D. Nandan, M. Kozlowski, F. Diaz-Mitoma, and A. Kumar. 2001. The p38 mitogen activated kinase pathway regulates the human IL-10 promoter via the activation of Sp1 transcription factor in lipopolysaccharide-stimulated human macrophages. J. Biol. Chem. 276: 13664-13674.
33. Dudley, D. T., L. Pang, S. J. Decker, A. J. Bridges, and A. R. Saltiel. 1995. A synthetic inhibitor of the mitogen-activated protein kinase cascade. Proc. Natl. Acad. Sci. USA 92: 7686-7689.
34. Lee, J. C., and P. R. Young. 1996. Role of CSB/p38/RK stress response kinase in LPS and cytokine signaling mechanisms. J. Leukocyte Biol. 59: 152-157.
35. Bennett, B. L., D. T. Sasaki, B. W. Murray, E. C. O'Leary, S. T. Sakata, W. Xu, J. C. Leisten, A. Motiwala, S. Pierce, Y. Satoh, et al. 2001. SP600125, an anthrapyrazolone inhibitor of Jun N-terminal kinase. Proc. Natl. Acad. Sci. USA 98: 13681-13686.
36. Lim, W., W. Ma, K. Gee, S. Aucoin, D. Nandan, F. Diaz-Mitoma, M. Kozlowski, and A. Kumar. 2002. Distinct role of p38 and c-Jun N-terminal kinases in IL-10-dependent and IL-10-independent regulation of the costimulatory molecule B7.2 in lipopolysaccharide-stimulated human monocytic cells. J. Immunol. 168: 1759-1769.
37. Kumar, A., J. B. Angel, S. Aucoin, W. D. Creery, M. P. Daftarian, D. W. Cameron, L. Filion, and F. Diaz-Mitoma. 1999. Dysregulation of B7.2 (CD86) expression on monocytes of HIV-infected individuals is associated with altered production of IL-2. Clin. Exp. Immunol. 117: 84-91.
38. Chen, Y. R., and T. H. Tan. 1998. Inhibition of the c-Jun N-terminal kinase (JNK) signaling pathway by curcumin. Oncogene 17: 173-178.
39. Shalom-Barak, T., J. Quach, and M. Lotz. 1998. Interleukin-17-induced gene expression in articular chondrocytes is associated with activation of mitogen-activated protein kinases and NF-κB. J. Biol. Chem. 273: 27467-27473.
40. Ma, W., K. Gee, W. Lim, K. Chambers, J. B. Angel, M. Kozlowski, and A. Kumar. 2004. Dexamethasone inhibits IL-12p40 production in lipopolysaccharide- stimulated human monocytic cells by down-regulating the activity of c-Jun N-terminal kinase, the activation protein-1, and NF-κB transcription factors. J. Immunol. 172: 318-330.
41. Lin, R., P. Genin, Y. Mamane, and J. Hiscott. 2000. Selective DNA binding and association with the CREB binding protein coactivator contribute to differential activation of α/β Interferon genes by interferon regulatory factors 3 and 7. Mol. Cell. Biol. 20: 6342-6353.
42. Takeuchi, O., K. Hoshino, T. Kawai, H. Sanjo, H. Takada, T. Ogawa, K. Takeda, and S. Akira. 1999. Differential roles of TLR2 and TLR4 in recognition of Gram-negative and Gram-positive bacterial cell wall components. Immunity 11: 443-451.
43. Reyes-Moreno, C., J. Girouard, R. Lapointe, A. Darveau, and W. Mourad. 2004. CD40/CD40 homodimers are required for CD40-induced phosphatidylinositol 3-kinase-dependent expression of B7.2 by human B lymphocytes. J. Biol. Chem. 279: 7799-7806.
44. Yang, H., C. H. Lin, G. Ma, M. O. Baffi, and M. G. Wathelet. 2003. Interferon regulatory factor-7 synergizes with other transcription factors through multiple interactions with p300/CBP coactivators. J. Biol. Chem. 278: 15495-15504.
45. Zhang, L., and J. S. Pagano. 2002. Structure and function of IRF-7. J. Interferon Cytokine Res. 22: 95-101.
46. Taniguchi, T., K. Ogasawara, A. Takaoka, and N. Tanaka. 2001. IRF family of transcription factors as regulators of host defense. Annu. Rev. Immunol. 19: 623-655.
47. Au, W. C., P. A. Moore, D. W. LaFleur, B. Tombal, and P. M. Pitha. 1998. Characterization of the interferon regulatory factor-7 and its potential role in the transcription activation of interferon A genes. J. Biol Chem. 273: 29210-29217.
48. Lu, R., and P. M. Pitha. 2001. Monocyte differentiation to macrophage requires interferon regulatory factor 7. J. Biol. Chem. 276: 45491-45496.
49. Zhang, L., and J. S. Pagano. 2001. Interferon regulatory factor 7 mediates activation of Tap-2 by Epstein-Barr virus latent membrane protein 1. J. Virol. 75: 341-350.
50. Lin, R., Y. Mamane, and J. Hiscott. 2000. Multiple regulatory domains control IRF-7 activity in response to virus infection. J. Biol. Chem. 275: 34320-34327.
51. Smith, E. J., I. Marie, A. Prakash, A. Garcia-Sastre, and D. E. Levy. 2001. IRF3 and IRF7 phosphorylation in virus-infected cells does not require double-stranded RNA-dependent protein kinase R or IκB kinase but is blocked by vaccinia virus E3L protein. J. Biol Chem. 276: 8951-8957.
52. Kim, T. K., T. Kim, T. Y. Kim, W. G. Lee, and J. Yim. 2000. Chemotherapeutic DNA-damaging drugs activate Interferon regulatory factor-7 by the mitogen-activated protein kinase kinase-4-cJun NH2-terminal kinase pathway. Cancer Res. 60: 1153-1156.
53. Gupta, S., T. Barrett, A. J. Whitmarsh, J. Cavanagh, H. K. Sluss, B. Derijard, and R. J. Davis. 1996. Selective interaction of JNK protein kinase isoforms with transcription factors. EMBO J. 15: 2760-2770.
54. Yang, D. D., C. Y. Kuan, A. J. Whitmarsh, M. Rincon, T. S. Zheng, R. J. Davis, P. Rakic, and R. A. Flavell. 1997. Absence of excitotoxicity-induced apoptosis in the hippocampus of mice lacking the Jnk3 gene. Nature 389: 865-870.
55. Dong, C., D. D. Yang, C. Tournier, A. J. Whitmarsh, J. Xu, R. J. Davis, and R. A. Ravell. 2000. JNK is required for effector T-cell function but not for T-cell activation. Nature 405: 91-94.
56. + T cells to Th1 cells requires MAP kinase JNK2. Immunity 9: 575-585.
57. Constant, S. L., C. Dong, D. D. Yang, M. Wysk, R. J. Davis, and R. A. Flavell. 2000. JNK1 is required for T cell-mediated immunity against Leishmania major infection. J. Immunol. 165:2671-2676.
58. + thymocytes. J. Exp. Med. 188: 1817-1830.
59. + T cells. Immunol. Rev. 192: 131-142.
60. Sabapathy, K., and E. F. Wagner. 2004. JNK2: a negative regulator of cellular proliferation. Cell Cycle 3: 1520-1523.
61. Jaeschke, A., M. Rincon, B. Doran, J. Reilly, D. Neuberg, D. L. Greiner, L. D. Shultz, A. A. Rossini, R. A. Flavell, and R. J. Davis. 2005. Disruption of the Jnk2 (Mapk9) gene reduces destructive insulitis and diabetes in a mouse model of type I diabetes. Proc. Natl. Acad. Sci. USA 102: 6931-6935.