Inhibitory role of IFN-γ-inducible lysosomal thiol reductase in T cell activation

Journal of Immunology

Volumn 177, Issue 7, 2006, Pages 4369-4375

  Barjaktarević, Igor ^a   Rahman, Ayman ^b   Radoja, Sasa ^a   Bogunović, Branka ^b   Vollmer, Alison ^a   Vukmanović, Stanislav ^a   Marić, Maja ^b  

^a CHILDREN S RESEARCH INSTITUTE   (United States)

^b GEORGETOWN UNIVERSITY MEDICAL CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

GAMMA INTERFERON INDUCIBLE LYSOSOMAL THIOL REDUCTASE; OXIDOREDUCTASE; UNCLASSIFIED DRUG;

ANIMAL CELL; ARTICLE; CELL NUCLEUS; CELLULAR DISTRIBUTION; CONTROLLED STUDY; CYTOPLASM; ENZYME INDUCTION; ENZYME LOCALIZATION; FEMALE; IN VITRO STUDY; LYMPHOCYTE MEMBRANE; LYMPHOCYTE PROLIFERATION; LYMPHOCYTOTOXICITY; LYSOSOME; MALE; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; SIGNAL TRANSDUCTION; T LYMPHOCYTE ACTIVATION; WILD TYPE;

EID: 33749150751     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: 10.4049/jimmunol.177.7.4369     Document Type: Article

References (31)

1. Raina, S., and D. Missiakas. 1997. Making and breaking disulfide bonds. Annu. Rev. Microbiol. 51: 179-202.
2. Luster, A. D., R.L. Weinshank, R. Feinman, and J.V. Ravetch. 1988. Molecular and biochemical characterization of a novel interferon-γ- inducible protein. J. Biol. Chem. 263: 12036-12043.
3. Arunachalam, B., M. Pan, and P. Cresswell. 1998. Intracellular formation and cell surface expression of a complex of an intact lysosomal protein and MHC class II molecules. J. Immunol. 160: 5797-5806.
4. Arunachalam, B., U. T. Phan, H. J. Geuze, and P. Cresswell. 2000. Enzymatic reduction of disulfide bonds in lysosomes: characterization of a interferon-γ-inducible lysosomal thiol reductase (GILT). Proc. Natl. Acad. Sci. USA 97: 745-750.
5. Phan, U. T., B. Arunachalam, and P. Cresswell. 2000. Gamma-interferon- γ-inducible lysosomal thiol reductase (GILT): maturation, activity, and mechanism of action. J. Biol. Chem. 275: 25907-25914.
6. Maric, M., B. Arunachalam, U. T. Phan, C. Dong, W. S. Garrett, K. S. Cannon, C. Alfonso, L. Karlsson, R. A. Flavell, and P. Cresswell. 2001. Defective antigen processing in GILT-free mice. Science 294: 1361-1365.
7. d-restricted epitopes from influenza hemagglutinin. J. Immunol. 172: 6607-6614.
8. Haque, M. A., P. Li, S. K. Jackson, H. M. Zarour, J. W. Hawes, U. T. Phan, M. Marić, P. Cresswell, and J. S. Blum. 2002. Absence of interferon-γ-inducible lysosomal thiol reductase in melanomas disrupts T cell recognition of select immunodominant epitopes. J. Exp. Med. 195: 1267-1277.
9. Phan, U. T., M. Marić, T. Dick, and P. Cresswell. 2001. Multiple species express thiol oxidoreductases related to GILT. Immunogenetics 53: 342-346.
10. Finkel, T. 2003. Oxidant signals and oxidative stress. Curr. Opin. Cell Biol. 15: 247-254.
11. Williams, M. S., and J. Kwon. 2004. T cell receptor stimulation, reactive oxygen species, and cell signaling. Free Radic. Biol. Med. 37: 1144-1151.
12. + cells. Int. Immunol. 9: 1423-1430.
13. Testi, R., D. D'Ambrosio, R. De Maria, and A. Santoni. 1994. The CD69 receptor: a multipurpose cell-surface trigger for hematopoietic cells. Immunol Today 15: 479-483.
14. Marzio, R., J. Mauel, and S. Betz-Corradin. 1999. CD69 and regulation of the immune function. Immunopharmacol. Immunotoxicol. 21: 565-582.
15. Sancho, D., M. Gomez, and F. Sanchez-Madrid. 2005. CD69 is an immunoregulatory molecule induced following activation. Trends Immunol. 26: 136-140.
16. Davey, G. M., S. L. Schober, B. T. Endrizzi, A. K. Dutcher, S. C. Jameson, and K. A. Hogquist. 1998. Preselection thymocytes are more sensitive to T cell receptor stimulation than mature T cells. J. Exp. Med. 188: 1867-1874.
17. Malek, T. R., J. D. Ashwell, R. N. Germain, E. M. Shevach, and J. Miller. 1986. The murine interleukin-2 receptor: biochemical structure and regulation of expression. Immunol. Rev. 92: 81-101.
18. Valitutti, S., S. Muller, M. Cella, E. Padovan, and A. Lanzavecchia. 1995. Serial triggering of many T cell receptors by a few peptide-MHC complexes. Nature 375: 148-151.
19. + T cells. J. Exp. Med. 185: 641-651.
20. Salio, M., S. Valitutti, and A. Lanzavecchia. 1998. Agonist-induced T cell receptor downregulation: molecular requirements and dissociation from T cell activation. Eur. J. Immunol. 27: 1769-1773.
21. Hogg, P. J. 2003. Disulfide bonds as switches for protein function. Trends Biochem. Sci. 28: 210-214.
22. Matthias, L. J., P. T. Yam, X. M. Jiang, N. Vandegraaff, P. Li, P. Poumbourios, N. Donoghue, and P.J. Hogg. 2002. Disulfide exchange in domain 2 of CD4 is required for entry of HIV-1. Nat. Immunol. 3: 727-732.
23. Angelini, G., S. Gardella, M. Ardy, M. R. Ciriolo, G. Filomeni, G. Di Trapani, F. Clarke, R. Sitia, and A. Rubartelli. 2002. Antigen-presenting dendritic cells provide the reducing extracellular microenvironment required for T lymphocyte activation. Proc. Natl. Acad. Sci. USA 99: 1491-1496.
24. Allison, J. P., B. W. McIntyre, and D. Bloch. 1982. Tumor-specific antigen of murine T-lymphoma defined with monoclonal antibody. J. Immunol. 129: 2293-2300.
25. Haskins, K., R. Kubo, J. White, M. Pigeon, J. Kappler, and P. Marrack. 1983. The major histocompatibility complex-restricted antigen receptor on T cells. I. Isolation with a monoclonal antibody. J. Exp. Med. 157: 1149-1169.
26. Devadas, S., L. Zaritskaya, S. G. Rhee, L. Oberley, and M. S. Williams. 2002. Discrete generation of superoxide and hydrogen peroxide by T cell receptor stimulation: selective regulation of mitogen-activated protein kinase activation and fas ligand expression. J. Exp. Med. 195: 59-70.
27. Kwon, J., C. K. Qu, J. S. Maeng, R. Falahati, C. Lee, and M. S. Williams. 2005. Receptor-stimulated oxidation of SHP-2 promotes T-cell adhesion through SLP-76-ADAP. EMBO J. 24: 2331-2341.
28. Frey, A. B., and N. Monu. 2006. Effector-phase tolerance: another mechanism of how cancer escapes antitumor immune response. J. Leukocyte Biol. 79: 652-662.
29. MacDonald, T. J., K. M. Brown, B. LaFleur, K. Peterson, C. Lawlor, Y. Chen, R. J. Packer, P. H. Cogen, and D. A. Stephan. 2001. Expression profiling of medulloblastoma: PDGFRA and the RAS/MAPK pathway as therapeutic targets for metastatic disease. Nat. Genet. 29: 143-152.
30. Huang, E., S. H. Cheng, H. Dressman, J. Pittman, M. H. Tsou, C. F. Horng, A. Bild, E. S. Iversen, M. Liao, C. M. Chen, et al. 2003. Gene expression predictors of breast cancer outcomes. Lancet 361: 1590-1596.
31. Monti, S., K. J. Savage, J. L. Kutok, F. Feuerhake, P. Kurtin, M. Mihm, B. Wu, L. Pasqualucci, D. Neuberg, R. C. Aguiar, et al. 2005. Molecular profiling of diffuse large B-cell lymphoma identifies robust subtypes including one characterized by host inflammatory response. Blood 105: 1851-1861.