Increased cAMP in monocytes augments notch signaling mechanisms by elevating RBP-J and transducin-like enhancer of split (TLE)

Journal of Biological Chemistry

Volumn 288, Issue 30, 2013, Pages 21526-21536

  Larabee, Jason L ^a   Shakir, Salika M ^a   Barua, Soumitra ^a   Ballard, Jimmy D ^a  

^a UNIVERSITY OF OKLAHOMA COLLEGE OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACILLUS ANTHRACIS; BACTERIAL PATHOGENS; HUMAN MONOCYTES; IMMUNE RESPONSE; INNATE IMMUNE RESPONSE; NOTCH SIGNALING; SIGNALING MECHANISMS; SIGNALING PATHWAYS;

BODY FLUIDS; IMMUNE SYSTEM;

SIGNALING;

BACILLUS ANTHRACIS EDEMA TOXIN; BACTERIAL TOXIN; CCAAT ENHANCER BINDING PROTEIN BETA; CYCLIC AMP; IMMUNOGLOBULIN J RECOMBINATION SIGNAL SEQUENCE BINDING PROTEIN; NOTCH RECEPTOR; TOLL LIKE RECEPTOR; TRANSDUCIN; TRANSDUCIN LIKE ENHANCER OF SPLIT; UNCLASSIFIED DRUG;

ANIMAL CELL; ARTICLE; BACILLUS ANTHRACIS; CELL ISOLATION; CONTROLLED STUDY; GENE; GENE INDUCTION; HES1 GENE; HEY1 GENE; HUMAN; HUMAN CELL; IL2RA GENE; IL7R GENE; IMMUNOBLOTTING; IMMUNOPRECIPITATION; MACROPHAGE; MONOCYTE; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; REVERSE TRANSCRIPTION POLYMERASE CHAIN REACTION; SIGNAL TRANSDUCTION; UPREGULATION;

BACTERIAL PATHOGENESIS; BACTERIAL TOXINS; CYCLIC AMP (CAMP); MONOCYTES; NOTCH PATHWAY;

ANIMALS; ANTIGENS, BACTERIAL; BACTERIAL TOXINS; BASIC HELIX-LOOP-HELIX TRANSCRIPTION FACTORS; BUCLADESINE; CCAAT-ENHANCER-BINDING PROTEIN-BETA; CELL LINE; CELLS, CULTURED; CYCLIC AMP; GENE EXPRESSION; HEK293 CELLS; HOMEODOMAIN PROTEINS; HUMANS; IMMUNOBLOTTING; IMMUNOGLOBULIN J RECOMBINATION SIGNAL SEQUENCE-BINDING PROTEIN; LIPOPOLYSACCHARIDES; LUCIFERASES; MACROPHAGES; MICE; MICE, INBRED C57BL; MONOCYTES; PROTEIN BINDING; RECEPTOR, NOTCH1; REPRESSOR PROTEINS; REVERSE TRANSCRIPTASE POLYMERASE CHAIN REACTION; SIGNAL TRANSDUCTION;

EID: 84881256774     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.465120     Document Type: Article

References (28)

1. McDonough, K. A., and Rodriguez, A. (2012) The myriad roles of cyclic AMP in microbial pathogens. From signal to sword. Nat. Rev. Microbiol. 10, 27-38
2. Leppla, S. H. (1982) Anthrax toxin edema factor. A bacterial adenylate cyclase that increases cyclic AMP concentrations of eukaryotic cells. Proc. Natl. Acad. Sci. 79, 3162-3166
3. Young, J. A., and Collier, R. J. (2007) Anthrax toxin. Receptor binding, internalization, pore formation, and translocation. Annu. Rev. Biochem. 76, 243-265
4. Liu, S., Miller-Randolph, S., Crown, D., Moayeri, M., Sastalla, I., Okugawa, S., and Leppla, S. H. (2010) Anthrax toxin targeting of myeloid cells through the CMG2 receptor is essential for establishment of Bacillus anthracis infections in mice. Cell Host Microbe 8, 455-462
5. Kim, C., Wilcox-Adelman, S., Sano, Y., Tang, W.-J., Collier, R. J., and Park, J. M. (2008) Antiinflammatory cAMP signaling and cell migration genes co-opted by the anthrax bacillus. Proc. Natl. Acad. Sci. 105, 6150-6155
6. Larabee, J. L., Shakir, S. M., Hightower, L., and Ballard, J. D. (2011) Adenomatous polyposis coli protein associates with C/EBP beta and increases Bacillus anthracis edema toxin-stimulated gene expression in macrophages. J. Biol. Chem. 286, 19364-19372
7. Larabee, J. L., Maldonado-Arocho, F. J., Pacheco, S., France, B., DeGiusti, K., Shakir, S. M., Bradley, K. A., and Ballard, J. D. (2011) Glycogen synthase kinase 3 activation is important for anthrax edema toxin-induced dendritic cell maturation and anthrax toxin receptor 2 expression in macrophages. Infect. Immun. 79, 3302-3308
8. Guichard, A., McGillivray, S. M., Cruz-Moreno, B., van Sorge, N. M., Nizet, V., and Bier, E. (2010) Anthrax toxins cooperatively inhibit endocytic recycling by the Rab11/Sec15 exocyst. Nature 467, 854-858
9. Maillard, I., Adler, S. H., and Pear, W. S. (2003) Notch and the immune system. Immunity 19, 781-791
10. Lewis, J., Hanisch, A., and Holder, M. (2009) Notch signaling, the segmentation clock, and the patterning of vertebrate somites. J. Biol. 8, 44
11. Bray, S. J. (2006) Notch signalling. A simple pathway becomes complex. Nat. Rev. Mol. Cell Biol. 7, 678-689
12. Fischer, A., and Gessler, M. (2007) Delta, Notch, and then? Protein interactions and proposed modes of repression by Hes and Hey bHLH factors. Nucleic Acids Res. 35, 4583-4596
13. Hu, X., Chung, A. Y., Wu, I., Foldi, J., Chen, J., Ji, J. D., Tateya, T., Kang, Y. J., Han, J., Gessler, M., Kageyama, R., and Ivashkiv, L. B. (2008) Integrated regulation of Toll-like receptor responses by Notch and interferon-α pathways. Immunity 29, 691-703
14. Foldi, J., Chung, A. Y., Xu, H., Zhu, J., Outtz, H. H., Kitajewski, J., Li, Y., Hu, X., and Ivashkiv, L. B. (2010) Autoamplification of Notch signaling in macrophages by TLR-induced and RBP-J-dependent induction of Jagged1. J. Immunol. 185, 5023-5031
15. Xu, H., Zhu, J., Smith, S., Foldi, J., Zhao, B., Chung, A. Y., Outtz, H., Kitajewski, J., Shi, C., Weber, S., Saftig, P., Li, Y., Ozato, K., Blobel, C. P., Ivashkiv, L. B., and Hu, X. (2012) Notch-RBP-J signaling regulates the transcription factor IRF8 to promote inflammatory macrophage polarization. Nat. Immunol. 13, 642-650
16. Zhang, Q., Wang, C., Liu, Z., Liu, X., Han, C., Cao, X., and Li, N. (2012) Notch signal suppresses Toll-like receptor-triggered inflammatory responses in macrophages by inhibiting extracellular signal-regulated kinase 1/2-mediated nuclear factor κB activation. J. Biol. Chem. 287, 6208-6217
17. Palaga, T., Buranaruk, C., Rengpipat, S., Fauq, A. H., Golde, T. E., Kaufmann, S. H., and Osborne, B. A. (2008) Notch signaling is activated by TLR stimulation and regulates macrophage functions. Eur. J. Immunol. 38, 174-183
18. Campeau, E., Ruhl, V. E., Rodier, F., Smith, C. L., Rahmberg, B. L., Fuss, J. O., Campisi, J., Yaswen, P., Cooper, P. K., and Kaufman, P. D. (2009) A versatile viral system for expression and depletion of proteins in mammalian cells. PLoS ONE 4, e6529
19. Grbavec, D., and Stifani, S. (1996) Molecular interaction between TLE1 and the carboxyl-terminal domain of HES-1 containing theWRPWmotif. Biochem. Biophys. Res. Commun. 223, 701-705
20. Chen, G., and Courey, A. J. (2000) Groucho/TLE family proteins and transcriptional repression. Gene 249, 1-16
21. Grbavec, D., Lo, R., Liu, Y., and Stifani, S. (1998) Transducin-like Enhancer of split 2, a mammalian homologue of Drosophila Groucho, acts as a transcriptional repressor, interacts with Hairy/Enhancer of split proteins, and is expressed during neuronal development. Eur. J. Biochem. 258, 339-349
22. Sharif, M. N., Sosic, D., Rothlin, C. V., Kelly, E., Lemke, G., Olson, E. N., and Ivashkiv, L. B. (2006) Twist mediates suppression of inflammation by type I IFNs and Axl. J. Exp. Med. 203, 1891-1901
23. Šoši, D., Richardson, J. A., Yu, K., Ornitz, D. M., and Olson, E. N. (2003) Twist regulates cytokine gene expression through a negative feedback loop that represses NF-B activity. Cell 112, 169-180
24. Peters-Golden, M. (2009) Putting on the Brakes. Cyclic AMP as a multipronged controller of macrophage function. Sci. Signal. 2, pe37
25. Serezani, C. H., Ballinger, M. N., Aronoff, D. M., and Peters-Golden, M. (2008) Cyclic AMP. Master regulator of innate immune cell function. Am. J. Respir. Cell Mol. Biol. 39, 127-132
26. Tetsuka, T., Uranishi, H., Imai, H., Ono, T., Sonta, S., Takahashi, N., Asamitsu, K., and Okamoto, T. (2000) Inhibition of nuclear factor-Bmediated Transcription by association with the amino-terminal enhancer of Split, a Groucho-related protein lacking WD40 repeats. J. Biol. Chem. 275, 4383-4390
27. Alvarez, Y., Municio, C., Hugo, E., Zhu, J., Alonso, S., Hu, X., Fernández, N., and Sánchez Crespo, M. (2011) Notch-and transducin-like enhancer of split (TLE)-dependent histone deacetylation explain interleukin 12 (IL-12) p70 inhibition by zymosan. J. Biol. Chem. 286, 16583-16595
28. Caolo, V., van den Akker, N. M., Verbruggen, S., Donners, M. M., Swennen, G., Schulten, H., Waltenberger, J., Post, M. J., and Molin, D. G. (2010) Feed-forward signaling by membrane-bound ligand receptor circuit. The case of Notch Delta-like 4 ligand in endothelial cells. J. Biol. Chem. 285, 40681-40689