Janus Kinase 3 Down-Regulates Lipopolysaccharide-Induced IL-1β-Converting Enzyme Activation by Autocrine IL-10

Journal of Immunology

Volumn 172, Issue 8, 2004, Pages 4948-4955

  Kim, Hee Jung ^a   Hart, Judy ^a   Knatz, Nina ^b   Hall, Mark W ^b   Wewers, Mark D ^a  

^a OHIO STATE UNIVERSITY   (United States)

^b OHIO STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

INTERLEUKIN 10; INTERLEUKIN 1BETA CONVERTING ENZYME; INTERLEUKIN 4; JANUS KINASE; JANUS KINASE 3; LIPOPOLYSACCHARIDE; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE P38; NEUTRALIZING ANTIBODY; PHOSPHATIDYLINOSITOL 3 KINASE; UNCLASSIFIED DRUG;

ARTICLE; AUTOCRINE EFFECT; CONCENTRATION RESPONSE; CYTOKINE PRODUCTION; CYTOKINE RELEASE; DOWN REGULATION; ENZYME ACTIVATION; HUMAN; HUMAN CELL; IMMUNOMODULATION; MACROPHAGE ACTIVATION; MONOCYTE; NORMAL HUMAN; PRIORITY JOURNAL; PROTEIN PROCESSING;

EID: 1842529222     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: 10.4049/jimmunol.172.8.4948     Document Type: Article

References (54)

1. Fantuzzi, G., and C. A. Dinarello. 1999. Interleukin-18 and interleukin-1β: two cytokine substrates for ICE (caspase-1). J. Clin. Immunol. 19:1.
2. Cao, Z., M. Tanaka, C. Regnier, M. Rothe, A. Yamit-hezi, J. D. Woronicz, M. E. Fuentes, M. H. Durnin, S. A. Dalrymple, and D. V. Goeddel. 1999. NF-κB activation by tumor necrosis factor and interleukin-1. Cold Spring Harb. Symp. Quant. Biol. 64:473.
3. Jacobs, R. F., D. R. Tabor, A. W. Burks, and G. D. Campbell. 1989. Elevated interleukin-1 release by human alveolar macrophages during the adult respiratory distress syndrome. Am. Rev. Respir. Dis. 140:1686.
4. Siler, T. M., J. E. Swierkosz, T. M. Hyers, A. A. Fowler, and R. O. Webster. 1989. Immunoreactive interleukin-1 in bronchoalveolar lavage fluid of high-risk patients and patients with the adult respiratory distress syndrome. Exp. Lung Res. 15:881.
5. Pugin, J., B. Ricou, K. P. Steinberg, P. M. Suter, and T. R. Martin. 1996. Proinflammatory activity in bronchoalveolar lavage fluids from patients with ARDS, a prominent role for interleukin-1. Am. J. Respir. Crit. Care Med. 153:1850.
6. van der Meer, J. W., M. Barza, S. M. Wolff, and C. A. Dinarello. 1988. A low dose of recombinant interleukin 1 protects granulocytopenic mice from lethal gram-negative infection. Proc. Natl. Acad. Sci. USA 85:1620.
7. Chen, W., E. A. Havell, L. L. Moldawer, K. W. McIntyre, R. A. Chizzonite, and A. G. Harmsen. 1992. Interleukin 1: an important mediator of host resistance against Pneumocystis carinii. J. Exp. Med. 176:713.
8. Cerretti, D. P., C. J. Kozlosky, B. Mosley, N. Nelson, K. Van Ness, T. A. Greenstreet, C. J. March, S. R. Kronheim, T. Druck, L. A. Cannizzaro, et al. 1992. Molecular cloning of the interleukin-1β converting enzyme. Science 256:97.
9. Thomberry, N. A., H. G. Bull, J. R. Calaycay, K. T. Chapman, A. D. Howard, M. J. Kostura, D. K. Miller, S. M. Molineaux, J. R. Weidner, J. Aunins, et al. 1992. A novel heterodimeric cysteine protease is required for interleukin-1β processing in monocytes. Nature 356:768.
10. Ghayur, T., S. Banerjee, M. Hugunin, D. Butler, L. Herzog, A. Carter, L. Quintal, L. Sekut, R. Talanian, M. Paskind, et al. 1997. Caspase-1 processes IFN-γ-inducing factor and regulates LPS-induced IFN-γ production. Nature 386:619.
11. Gu, Y., K. Kuida, H. Tsutsui, G. Ku, K. Hsiao, M. A. Fleming, N. Hayashi, K. Higashino, H. Okamura, K. Nakanishi, et al. 1997. Activation of interferon-γ inducing factor mediated by interleukin-1β converting enzyme. Science 275:206.
12. Ayala, J. M., T. T. Yamin, L. A. Egger, J. Chin, M. J. Kostura, and D. K. Miller. 1994. IL-1β-converting enzyme is present in monocytic cells as an inactive 45-kDa precursor. J Immunol. 153:2592.
13. Schumann, R. R., C. Belka, D. Reute, N. Lamping, C. J. Kirschning, J. R. Weber, and D. Pfeil. 1998. Lipopolysaccharide activates caspase-1 (interleukin-1-converting enzyme) in cultured monocytic and endothelial cells. Blood 91:577.
14. Schonbeck, U., F. Mach, J. Y. Bonnefoy, H. Loppnow, H. D. Flad, and P. Libby, 1997. Ligation of CD40 activates interleukin 1β-converting enzyme (caspase-1) activity in vascular smooth muscle and endothelial cells and promotes elaboration of active interleukin 1β. J. Biol. Chem. 272:19569.
15. Walker, N. P., R. V. Talanian, K. D. Brady, L. C. Dang, N. J. Bump, C. R. Ferenz, S. Franklin, T. Ghayur, M. C. Hackett, L. D. Hammill. et al. 1994. Crystal structure of the cysteine protease interleukin-1β-converting enzyme: a (p20/p10)2 homodimer. Cell 78:343.
16. Wilson, K. P., J. A. Black. J. A. Thomson, E. E. Kim. J. P. Griffith, M. A. Navia, M. A. Murcko, S. P. Chambers, R. A. Aldape, S. A. Raybuck, et al. 1994. Structure and mechanism of interleukin-1β converting enzyme. Nature 370:270.
17. Yamin, T. T., J. M. Ayala, and D. K. Miller. 1996. Activation of the native 45-kDa precursor form of interleukin-1-converting enzyme. J. Biol. Chem. 271:13273.
18. Mehta, V. B., J. Hart, and M. Wewers. 2001. ATP-stimulated release of interleukin (IL)-1β and IL-18 requires priming by lipopolysaccharide and is independent of caspase-1 cleavage. J. Biol. Chem. 276:3820.
19. Bouchier-Hayes, L., and S. J. Martin, 2002. CARD games in apoptosis and immunity. EMBO Rep. 3:616.
20. Weber, C. H., and C. Vincenz. 2001. The death domain superfamily: a tale of two interfaces? Trends Biochem. Sci. 26:475.
21. Martinon, F., K. Burns, and J. Tschopp. 2002. The inflammasome: a molecular platform triggering activation of inflammatory caspases and processing of proIL-β. Mol. Cell. 10:417.
22. Srinivasula, S. M., J. L. Poyet, M. Razmara, P. Datta, Z. Zhang, and E. S. Alnemri. 2002. The PYRIN-CARD protein ASC is an activating adaptor for caspase-1. J. Biol. Chem. 277:21119.
23. Imada, K., and W. J. Leonard. 2000. The Jak-STAT pathway. Mol. Immunol. 37:1.
24. Rane, S. G., and E. P. Reddy. 2000. Janus kinases: components of multiple signaling pathways. Oncogene 19:5662.
25. Leonard, W. J. 2001. Role of Jak kinases and STATs in cytokine signal transduction. Int. J. Hematol. 73:271.
26. c) is a required signaling component of the IL-21 receptor and supports IL-21-induced cell proliferation via JAK3. Biochemistry 41:8725.
27. Leonard, W. J. 2001. Cytokines and immunodeficiency diseases. Nat. Rev. Immunol. 1:200.
28. Buckley, R. H. 2000. Advances in the understanding and treatment of human severe combined immunodeficiency. Immunol. Res. 22:237.
29. Mella, P., R. F. Schumacher, T. Cranston, G. de Saint Basile. G. Savoldi, and L. D. Notarangelo. 2001. Eleven novel JAK3 mutations in patients with severe combined immunodeficiency-including the first patients with mutations in the kinase domain. Hum. Mutat. 18:355.
30. Villa, A., M. Sironi, P. Macchi, C. Matteucci, L. D. Notarangelo, P. Vezzoni, and A. Mantovani. 1996. Monocyte function in a severe combined immunodeficient patient with a donor splice site mutation in the Jak3 gene. Blood 88:817.
31. Nosaka, T., J. M. van Deursen, R. A. Tripp, W. E. Thierfelder, B. A. Witthuhn, A. P. McMickle, P. C. Doherty, G. C. Grosveld, and J. N. Ihle. 1995. Defective lymphoid development in mice lacking Jak3. Science 270:800.
32. Park, S. Y., K. Saijo, T. Takahashi, M. Osawa, H. Arase, N. Hirayama, K. Miyake, H. Nakauchi, T. Shirasawa, and T. Saito. 1995. Developmental defects of lymphoid cells in Jak3 kinase-deficient mice. Immunity 3:771.
33. Saijo, K., S. Y. Park, Y. Ishida, H. Arase, and T. Saito. 1997. Crucial role of Jak3 in negative selection of self-reactive T cells. J. Exp. Med. 185:351.
34. Musso, T., J. A. Johnston, D. Linnekin, L. Varesio, T. K. Rowe, J. J. O'Shea, and D. W. McVicar, 1995. Regulation of JAK3 expression in human monocytes: phosphorylation in response to interleukins 2, 4, and 7. J. Exp. Med. 4:1425.
35. Thornberry, N. A., T. A. Rano, E. P. Peterson, D. M. Rasper. T. Timkey, M. Garcia-Calvo, V. M. Houtzager, P. A. Nordstrom. S. Roy, J. P. Vaillancourt, et al. 1997. A combinatorial approach defines specificities of members of the caspase family and granzyme B: functional relationships established for key mediators of apoptosis. J. Biol. Chem. 272:17907.
36. Nicholson, D. W., A. Ali, N. A. Thornberry, J. P. Vaillancourt, C. K. Ding, M. Gallant, Y. Gareau, P. R. Griffin, M. Labelle, Y. A. Lazebnik, et al. 1995. Identification and inhibition of the ICE/CED-3 protease necessary for mammalian apoptosis. Nature 376:37.
37. Wewers, M. D., H. A. Dare, A. V. Winnard, J. M. Parker. and D. K. Miller. 1997. IL-1β-converting enzyme (ICE) is present and functional in human alveolar macrophages: macrophage IL-1β release limitation is ICE independent. J. Immunol. 159:5964.
38. Herzyk, D. J., A. E. Berger, J. N. Allen, J. N., and M. D. Wewers. 1992. Sandwich ELISA formats designed to detect 17 kDa IL-1β significantly underestimate 35 kDa IL-1β. J. Immunol. Methods 148:243.
39. Huberty, C. J., and. J. D. Morris. 1989. Multivariate analysis versus multiple univariate analyses. Psychol Bull. 114:145.
40. Sudbeck, E. A., X. P. Liu, R. K. Narla, S. Mahajan, S. Ghosh, C. Mao, and F. M. Uckun. 1999. Structure-based design of specific inhibitors of Janus kinase 3 as apoptosis-inducing antileukemic agents. Clin. Cancer Res. 5:1569.
41. Uckun, F. M., E. A. Sudbeck, C. Mao, S. Ghosh, X. P. Liu. A. O. Vassilev. C. S. Navara, and R. K. Narla. 2001. Structure-based design of novel anticancer agents, Curr. Cancer Drug Targets 1:59.
42. Bonder, C. S., J. J. Finlay-Jones, and P. H. Hart. 1999. Interleukin-4 regulation of human monocyte and macrophage interleukin-10 and interleukin-12 production: role of a functional interleukin-2 receptor γ-chain. Immunology 96:529.
43. Chae, J. J., H. D. Komarow, J. Cheng, G. Wood. N. Raben, P. P. Liu, and D. L. Kastner. 2003. Targeted disruption of pyrin, the FMF protein, causes heightened sensitivity to endoroxin and a defect in macrophage apoptosis. Mol. Cell. 11:591.
44. Richards, N., P. Schaner, A. Diaz, J. Stuckey, E. Shelden, A. Wadhwa, and D. L. Gumucio. 2001. Interaction between pyrin and the apoptotic speck protein (ASC) modulates ASC-induced apoptosis. J. Biol. Chem. 276:39320,
45. Wewers, M. D., and D. J. Herzyk. 1989. Alveolar macrophages differ from blood monocytes in human IL-1β release: quantitation by enzyme-linked immunoassay. J. Immunol. 143:1635.
46. Cassatella, M. A., S. Gasperini, C. Bovolenta, F. Calzetti, M. Vollebregt, P. Scapini, M. Marchi, R. Suzuki, A. Suzuki, and A. Yoshimura. 1999. Interleukin-10 (IL-10) selectively enhances CIS3/SOCS3 mRNA expression in human neutrophils: evidence for an IL-10-induced pathway that is independent of STAT protein activation. Blood 94:2880.
47. Ito, S., P. Ansari, M. Sakatsume, H. Dickensheets, N. Vazquez, R. P. Donnelly, A. C. Lamer, and D. S. Finbloom. 1999. Interleukin-10 inhibits expression of both interferon α- and interferon γ-induced genes by suppressing tyrosine phosphorylation of STAT1. Blood 93:1456.
48. Asadullah, K., W. Sterry, and H. D. Volk. 2003. Interleukin-10 therapy: review of a new approach. Pharmacol. Rev. 55:241.
49. Wang, P., P. Wu, M. I. Siegel, R. W. Egan, M. M. Billah. 1995. Interleukin (IL)-10 inhibits nuclear factor κB (NFκB) activation in human monocytes. IL-10 and IL-4 suppress cytokine synthesis by different mechanisms. J. Biol. Chem. 270:9558.
50. Schottelius, A. J., M. W. Mayo, R. B. Sartor, and A. S. Baldwin, Jr. 1999. Interleukin-10 signaling blocks inhibitor of κB kinase activity and nuclear factor κB DNA binding. J. Biol. Chem. 274:31868.
51. Dayer, J. 2003. The pivotal role of interleukin-1 in the clinical manifestations of rheumatoid arthritis. Rheumatology 42:ii3.
52. Dinarello, C. A., and G. Fantuzzi. 2003. Interleukin-18 and host defense against infection. J. Infect. Dis. 187:S370.
53. Li, P., H. Allen, S. Banerjee, S. Franklin, L. Herzog, C. Johnston, J. McDowell, M. Paskind, L. Rodman, J. Salfeld, et al. 1995. Mice deficient in IL-1β-converting enzyme are defective in production of mature IL-1β and resistant to endotoxic shock. Cell 80:401.
54. Siegmund, B., H. A. Lehr, G. Fantuzzi, and C. A. Dinarello, 2001. IL-1β-converting enzyme (caspase-1) in intestinal inflammation. Proc. Natl. Acad. Sci. USA 98:13249.