IL-10 inhibits CD28 and ICOS costimulations of T cells via src homology 2 domain-containing protein tyrosine phosphatase 1

Journal of Allergy and Clinical Immunology

Volumn 120, Issue 1, 2007, Pages 76-83

  Taylor, Alison ^a,b   Akdis, Mübeccel ^a   Joss, Andrea ^a   Akkoç, Tunç ^a,c   Wenig, Renate ^d   Colonna, Marco ^e   Daigle, Isabelle ^a   Flory, Egbert ^d   Blaser, Kurt ^a   Akdis, Cezmi A ^a  

^a SWISS INSTITUTE OF ALLERGY AND ASTHMA RESEARCH SIAF   (Switzerland)

^b UNIVERSITY OF EAST ANGLIA   (United Kingdom)

^c MARMARA UNIVERSITY   (Turkey)

^d PAUL EHRLICH INSTITUT   (Germany)

^e WASHINGTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

anergy; costimulation; IL 10; inhibition; phosphorylation; SHP 1; suppression; T cell; tolerance

Indexed keywords

CD28 ANTIGEN; INTERLEUKIN 10; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN; PROTEIN INDUCIBLE COSTIMULATOR; PROTEIN SH2; PROTEIN TYROSINE PHOSPHATASE; PROTEIN TYROSINE PHOSPHATASE 1; T LYMPHOCYTE RECEPTOR; UNCLASSIFIED DRUG;

ANIMAL EXPERIMENT; ARTICLE; BINDING AFFINITY; CELL PROLIFERATION; CONTROLLED STUDY; DRUG MECHANISM; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN PHOSPHORYLATION; T LYMPHOCYTE ACTIVATION;

1-PHOSPHATIDYLINOSITOL 3-KINASE; ANIMALS; ANTIGENS, CD28; ANTIGENS, DIFFERENTIATION, T-LYMPHOCYTE; CELLS, CULTURED; HUMANS; INTERLEUKIN-10; LYMPHOCYTE ACTIVATION; MICE; MUTATION; RNA INTERFERENCE; SHP1 PROTEIN TYROSINE PHOSPHATASE; T-LYMPHOCYTES;

EID: 34250843152     PISSN: 00916749     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jaci.2007.04.004     Document Type: Article

References (33)

1. Baxter A.G., and Hodgkin P.D. Activation rules: the two-signal theories of immune activation. Nat Rev Immunol 2 (2002) 439-446
2. Boussiotis V.A., Gribben J.G., Freeman G.J., and Nadler L.M. Blockade of the CD28 co-stimulatory pathway: a means to induce tolerance. Curr Opin Immunol 6 (1994) 797-807
3. Yoshinaga S.K., Whoriskey J.S., Khare S.D., Sarmiento U., Guo J., Horan T., et al. T-cell co-stimulation through B7RP-1 and ICOS. Nature 402 (1999) 827-832
4. Harding F.A., McArthur J.G., Gross J.A., Raulet D.H., and Allison J.P. CD28-mediated signalling co-stimulates murine T cells and prevents induction of anergy in T-cell clones. Nature 356 (1992) 607-609
5. Dhand R., Hara K., Hiles I., Bax B., Gout I., Panayotou G., et al. PI 3-kinase: structural and functional analysis of intersubunit interactions. EMBO J 13 (1994) 511-521
6. Prasad K.V., Cai Y.C., Raab M., Duckworth B., Cantley L., Shoelson S.E., et al. T-cell antigen CD28 interacts with the lipid kinase phosphatidylinositol 3-kinase by a cytoplasmic Tyr(P)-Met-Xaa-Met motif. Proc Natl Acad Sci U S A 91 (1994) 2834-2838
7. Coyle A.J., Lehar S., Lloyd C., Tian J., Delaney T., Manning S., et al. The CD28-related molecule ICOS is required for effective T cell-dependent immune responses. Immunity 13 (2000) 95-105
8. Cong Y., Weaver C.T., Lazenby A., and Elson C.O. Bacterial-reactive T regulatory cells inhibit pathogenic immune responses to the enteric flora. J Immunol 169 (2002) 6112-6119
9. Akdis M., Verhagen J., Taylor A., Karamloo F., Karagiannidis C., Crameri R., et al. Immune responses in healthy and allergic individuals are characterized by a fine balance between allergen-specific T regulatory 1 and T helper 2 cells. J Exp Med 199 (2004) 1567-1575
10. Kuhn R., Lohler J., Rennick D., Rajewsky K., and Muller W. Interleukin-10-deficient mice develop chronic enterocolitis. Cell 75 (1993) 263-274
11. Wehinger J., Gouilleux F., Groner B., Finke J., Mertelsmann R., and Weber-Nordt R.M. IL-10 induces DNA binding activity of three STAT proteins (Stat1, Stat3, and Stat5) and their distinct combinatorial assembly in the promoters of selected genes. FEBS Lett 394 (1996) 365-370
12. Stefanova I., Hemmer B., Vergelli M., Martin R., Biddison W.E., and Germain R.N. TCR ligand discrimination is enforced by competing ERK positive and SHP-1 negative feedback pathways. Nat Immunol 4 (2003) 248-254
13. Yang J., Liu L., He D., Song X., Liang X., Zhao Z.J., et al. 2003 Crystal structure of human protein-tyrosine phosphatase SHP-1. J Biol Chem 278 (2003) 6516-6520
14. Akdis C.A., Joss A., Akdis M., Faith A., and Blaser K. A molecular basis for T cell suppression by IL-10: CD28-associated IL-10 receptor inhibits CD28 tyrosine phosphorylation and phosphatidylinositol 3-kinase binding. FASEB J 14 (2000) 1666-1668
15. Shultz L.D., Schweitzer P.A., Rajan T.V., Yi T., Ihle J.N., Matthews R.J., et al. Mutations at the murine motheaten locus are within the hematopoietic cell protein-tyrosine phosphatase (Hcph) gene. Cell 73 (1993) 1445-1454
16. Steidl S., Stitz J., Schmitt I., Konig R., Flory E., Schweizer M., et al. Coreceptor switch of [MLV(SIVagm)] pseudotype vectors by V3-loop exchange. Virology 300 (2002) 205-216
17. Riley J.L., Blair P.J., Musser J.T., Abe R., Tezuka K., Tsuji T., et al. ICOS costimulation requires IL-2 and can be prevented by CTLA-4 engagement. J Immunol 166 (2001) 4943-4948
18. Viola A., and Lanzavecchia A. T cell activation determined by T cell receptor number and tunable thresholds. Science 273 (1996) 104-106
19. Ou L.S., Goleva E., Hall C., and Leung D.Y. T regulatory cells in atopic dermatitis and subversion of their activity by superantigens. J Allergy Clin Immunol 113 (2004) 756-763
20. Pages F., Ragueneau M., Rottapel R., Truneh A., Nunes J., Imbert J., et al. Binding of phosphatidylinositol-3-OH kinase to CD28 is required for T-cell signalling. Nature 369 (1994) 327-329
21. Cuevas B., Lu Y., Watt S., Kumar R., Zhang J., Siminovitch K.A., et al. SHP-1 regulates Lck-induced phosphatidylinositol 3-kinase phosphorylation and activity. J Biol Chem 274 (1999) 27583-27589
22. Jin Y.J., Yu C.L., and Burakoff S.J. Human 70-kDa SHP-1L differs from 68-kDa SHP-1 in its C-terminal structure and catalytic activity. J Biol Chem 274 (1999) 28301-28307
23. Finbloom D.S., and Winestock K.D. IL-10 induces the tyrosine phosphorylation of tyk2 and Jak1 and the differential assembly of STAT1 alpha and STAT3 complexes in human T cells and monocytes. J Immunol 155 (1995) 1079-1090
24. + T cells ICAM-1 or B7-1 can costimulate naive CD4 T cell activation but both are required for optimum response. J Immunol 155 (1995) 45-57
25. Wang L.L., Blasioli J., Plas D.R., Thomas M.L., and Yokoyama W.M. Specificity of the SH2 domains of SHP-1 in the interaction with the immunoreceptor tyrosine-based inhibitory motif-bearing receptor gp49B. J Immunol 162 (1999) 1318-1323
26. Brockdorff J., Williams S., Couture C., and Mustelin T. Dephosphorylation of ZAP-70 and inhibition of T cell activation by activated SHP1. Eur J Immunol 29 (1999) 2539-2550
27. Gavrieli M., Watanabe N., Loftin S.K., Murphy T.L., and Murphy K.M. Characterization of phosphotyrosine binding motifs in the cytoplasmic domain of B and T lymphocyte attenuator required for association with protein tyrosine phosphatases SHP-1 and SHP-2. Biochem Biophys Res Commun 312 (2003) 1236-1243
28. Burshtyn D.N., Yang W., Yi T., and Long E.O. A novel phosphotyrosine motif with a critical amino acid at position -2 for the SH2 domain-mediated activation of the tyrosine phosphatase SHP-1. J Biol Chem 272 (1997) 13066-13072
29. Campbell K.S., and Colonna M. DAP12: a key accessory protein for relaying signals by Natural Killer cell receptors. Int J Biochem Cell Biol 31 (1999) 631-636
30. Yetter A., Uddin S., Krolewski J.J., Jiao H., Yi T., and Platanias L.C. Association of the interferon-dependent tyrosine kinase Tyk-2 with the hematopoietic cell phosphatase. J Biol Chem 270 (1995) 18179-18182
31. Yang J., Cheng Z., Niu T., Liang X., Zhao Z.J., and Zhou G.W. Structural basis for substrate specificity of protein-tyrosine phosphatase SHP-1. J Biol Chem 275 (2000) 4066-4071
32. Miller M.J., Wei S.H., Parker I., and Cahalan M.D. Two-photon imaging of lymphocyte motility and antigen response in intact lymph node. Science 296 (2002) 1869-1873
33. Egen J.G., Kuhns M.S., and Allison J.P. CTLA-4: new insights into its biological function and use in tumor immunotherapy. Nat Immunol 3 (2002) 611-618