IDO inhibits T-cell function through suppressing Vav1 expression and activation

Cancer Biology and Therapy

Volumn 8, Issue 14, 2009, Pages 1402-1408

  Li, Runmei ^a   Wei, Feng ^a   Yu, Jinpu ^a   Li, Hui ^a   Ren, Xiubao ^a   Hao, Xishan ^a  

^a TIANJIN MEDICAL UNIVERSITY   (China)

Author keywords

Apoptosis; Indoleamine 2,3 dioxygenase (IDO); mRNA; Phosphorylation; Proliferation; Protein expression; T cell; Vav1

Indexed keywords

1 METHYL LEVO TRYPTOPHAN; CELL PROTEIN; INDOLEAMINE 2,3 DIOXYGENASE; INTERLEUKIN 2; PROTEIN VAV1; RNA; TRYPTOPHAN DERIVATIVE; UNCLASSIFIED DRUG; 1 METHYL TRYPTOPHAN; 1-METHYL-TRYPTOPHAN; DRUG DERIVATIVE; HYBRID PROTEIN; LYMPHOCYTE ANTIGEN RECEPTOR; MESSENGER RNA; TRYPTOPHAN; VAV PROTEIN; VAV1 PROTEIN, HUMAN;

ANIMAL CELL; ARTICLE; CELL FUNCTION; CELL PROLIFERATION; CHO CELL; GENE EXPRESSION; HUMAN; HUMAN CELL; NONHUMAN; ONCOGENE; PROTEIN EXPRESSION; PROTEIN PHOSPHORYLATION; T LYMPHOCYTE; VAV1 GENE; ANIMAL; APOPTOSIS; BIOSYNTHESIS; CELL CULTURE; COCULTURE; CRICETULUS; CYTOLOGY; DRUG ANTAGONISM; GENETICS; HAMSTER; IMMUNOLOGY; IMMUNOSUPPRESSIVE TREATMENT; LYMPHOCYTE ACTIVATION; METABOLISM; PHOSPHORYLATION; PHYSIOLOGY; PROTEIN PROCESSING; TUMOR ESCAPE;

ANIMALS; APOPTOSIS; CELLS, CULTURED; CHO CELLS; COCULTURE TECHNIQUES; CRICETINAE; CRICETULUS; HUMANS; IMMUNOSUPPRESSION; INDOLEAMINE-PYRROLE 2,3,-DIOXYGENASE; INTERLEUKIN-2; LYMPHOCYTE ACTIVATION; PHOSPHORYLATION; PROTEIN PROCESSING, POST-TRANSLATIONAL; PROTO-ONCOGENE PROTEINS C-VAV; RECEPTORS, ANTIGEN, T-CELL; RECOMBINANT FUSION PROTEINS; RNA, MESSENGER; T-LYMPHOCYTES; TRYPTOPHAN; TUMOR ESCAPE;

EID: 76249111086     PISSN: 15384047     EISSN: 15558576     Source Type: Journal    
DOI: 10.4161/cbt.8.14.8882     Document Type: Article

References (22)

1. Prendergast GC, Jaffee EM. Cancer immunologists and cancer biologists: why didn't talk then but need to now. Cancer Res 2007; 67:3500-4.
2. Uyttenhove C, Pilotte L, Théate I, Stroobant V, Colau D, Parmentier N, et al. Evidence for a tumoral immune resistance mechanism based on tryptophan degradation by indoleamine 2,3-dioxygenase. Nat Med 2003; 9:1269-74.
3. Martin FA, Sebastiani S, Höpken UE, Uguccioni M, Lipp M, Lanzavecchia A, et al. Regulation of dendritic cell migration to the draining lymphnode: impact on T lymphocyte traffic priming. J Exp Med 2003; 198:615-21.
4. Grohmann U, Fallarino F, Puccetti P. Tolerance, DCs and tryptophan: much ado about IDO. Trends Immunol 2003; 24:242-8.
5. Fallarino F, Grohmann U, Vacca C, Bianchi R, Orabona C, Spreca A, et al. T cell apoptosis by tryptophan catabolism. Cell Death Differ 2002; 9:1069-77.
6. Frumento G, Rotondo R, Tonetti M, Damonte G, Benatti U, Ferrara GB. Tryptophan-derived catabolites are responsible for inhibition of T and natural killer cell proliferation induced by indoleamine 2,3-dioxygenase. J Exp Med 2002; 196:459-68.
7. Terness P, Bauer TM, Röse L, Dufter C, Watzlik A, Simon H, et al. Inhibition of allogeneic T cell proliferation by indoleamine 2,3-dioxygenase-expressing dendritic cells: mediation of suppression by tryptophan metabolites. J Exp Med 2002; 196:447-57.
8. + T cells induced by TCR triggering or homeostatic cytokines. Eur J Immunol 2006; 36:296-304.
9. Mellor AL, Munn DH. Tryptophan catabolism and regulation of adaptive immunity. J Immunol 2003; 170:5809-13.
10. Lee GK, Park HJ, Macleod M, Chandler P, Munn DH, Mellor AL. Tryptophan deprivation sensitizes activated T cells to apoptosis prior to cell division. Immunology 2002; 107:452-60.
11. + T regulatory cells. Blood 2007; 109:2871-7.
12. Munn DH, Mellor AL. Indoleamine 2,3-dioxygenase and tumor-induced tolerance. J Clin Invest 2007; 117:1147-54.
13. Coppola S, Bryant S, Koda T, Conway D, Barbacid M. Mechanism of activation of the vav protooncogene. Cell Growth Differ 1991; 2:95-105.
14. Crespo P, Schuebel KE, Ostrom AA, Gutkind JS, Bustelo XR. Phosphotyrosine-dependent activation of Rac-1 GDP/GTP exchange by the vav proto-oncogene product. Nature 1997; 385:169-72.
15. Tybulewicz VL. Vav-family proteins in T-cell signalling. Curr Opin Immunol 2005; 17:267-74.
16. Tybulewicz VL, Ardouin L, Prisco A, Reynolds LF. Vav1: a key signal transducer downstream of the TCR. Immunol Rev 2003; 192:42-52.
17. Costello PS, Walters AE, Mee PJ, Turner M, Reynolds LF, Prisco A, et al. The Rho-family GTP exchange factor Vav is a critical transducer of T cell receptor signals to the calcium, ERK and NFkappaB pathways. Proc Natl Acad Sci USA 1999; 96:3035-40.
18. + T-cells in cytokine-induced killers might favor the antitumor cytotoxicity of cytokine-induced killers in vivo. Cancer Biother Radiopharm 2006; 21:276-84.
19. Mellor AL, Keskin DB, Johnson T, Chandler P, Munn DH. Cells expressing indoleamine 2,3-dioxygenase inhibit T cell responses. J Immunol 2002; 168:3771-6.
20. Gogishvili T, Elias F, Emery JL, McPherson K, Okkenhaug K, Hünig T, et al. Proliferative signals mediated by CD28 superagonists require the exchange factor Vav1 but not phosphoinositide 3-kinase in primary peripheral T cells. Eur J Immunol 2008; 38:2528-33.
21. Tuosto L, Marinari B, Piccolella E. CD4-Lck through TCR and in the absence of Vav exchange factor induces Bax increase and mitochondrial damage. J Immunol 2002; 168:6106-12.
22. Raberger J, Boucheron N, Sakaguchi S, Penninger JM, Ellmeier W, Raberger J, et al. Impaired T-cell development in the absence of Vav1 and Itk. Eur J Immunol 2008; 38:3530-42.