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Gene Review

Ido1  -  indoleamine 2,3-dioxygenase 1

Mus musculus

Synonyms: IDO-1, Ido, Indo, Indoleamine 2,3-dioxygenase 1, Indoleamine-pyrrole 2,3-dioxygenase
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Disease relevance of Indo

  • Inhibition of IDO during TNBS colitis resulted in increased mortality and an augmentation of the normal inflammatory response [1].
  • The observed inhibition of IDO activity was not due to toxicity of the NO generators and was abrogated by the co-addition of oxyhemoglobin, an antagonist of NO function [2].
  • These data suggest that IDO plays a role in resolving bacterial infection in the placenta while at the same time maintaining a barrier to T cells whose presence might result in fetal rejection [3].
  • We have studied the regulation of IDO in the utero-placental unit of mice following infection with the Gram-positive, intracellular bacterium Listeria monocytogenes that has a predilection for replication in the decidua basalis [3].
  • Effect of indoleamine 2,3-dioxygenase on induction of experimental autoimmune encephalomyelitis [4].

High impact information on Indo


Chemical compound and disease context of Indo


Biological context of Indo


Anatomical context of Indo


Associations of Indo with chemical compounds


Regulatory relationships of Indo


Other interactions of Indo


Analytical, diagnostic and therapeutic context of Indo

  • IDO protein and mRNA expression were assessed by Western blotting and real-time PCR [1].
  • The depletion of an essential amino acid (aa), tryptophan, caused by interferon-gamma (IFN-gamma)-mediated induction of indoleamine 2,3-dioxygenase (IDO) in mouse allografted tumor cells, has been suggested as a reason for the allograft rejection [8].
  • Here, we identify specific subsets of splenic (CD11c+) dendritic cells competent to mediate IDO-dependent T cell suppression following CTLA4-mediated ligation of B7 molecules [13].
  • These results suggest that IDO may contribute to the regulation of T cell activity associated with the different phases of this animal model of multiple sclerosis (MS) [4].
  • Our findings suggest that Bin1 loss promotes immune escape in cancer by deregulating IDO and that IDO inhibitors may improve responses to cancer chemotherapy [5].


  1. Inhibition of indoleamine 2,3-dioxygenase augments trinitrobenzene sulfonic acid colitis in mice. Gurtner, G.J., Newberry, R.D., Schloemann, S.R., McDonald, K.G., Stenson, W.F. Gastroenterology (2003) [Pubmed]
  2. Nitric oxide inhibits indoleamine 2,3-dioxygenase activity in interferon-gamma primed mononuclear phagocytes. Thomas, S.R., Mohr, D., Stocker, R. J. Biol. Chem. (1994) [Pubmed]
  3. Indoleamine 2,3-dioxygenase is regulated by IFN-gamma in the mouse placenta during Listeria monocytogenes infection. Mackler, A.M., Barber, E.M., Takikawa, O., Pollard, J.W. J. Immunol. (2003) [Pubmed]
  4. Effect of indoleamine 2,3-dioxygenase on induction of experimental autoimmune encephalomyelitis. Sakurai, K., Zou, J.P., Tschetter, J.R., Ward, J.M., Shearer, G.M. J. Neuroimmunol. (2002) [Pubmed]
  5. Inhibition of indoleamine 2,3-dioxygenase, an immunoregulatory target of the cancer suppression gene Bin1, potentiates cancer chemotherapy. Muller, A.J., DuHadaway, J.B., Donover, P.S., Sutanto-Ward, E., Prendergast, G.C. Nat. Med. (2005) [Pubmed]
  6. 4-1BB-mediated immunotherapy of rheumatoid arthritis. Seo, S.K., Choi, J.H., Kim, Y.H., Kang, W.J., Park, H.Y., Suh, J.H., Choi, B.K., Vinay, D.S., Kwon, B.S. Nat. Med. (2004) [Pubmed]
  7. Evidence for a tumoral immune resistance mechanism based on tryptophan degradation by indoleamine 2,3-dioxygenase. Uyttenhove, C., Pilotte, L., Théate, I., Stroobant, V., Colau, D., Parmentier, N., Boon, T., Van den Eynde, B.J. Nat. Med. (2003) [Pubmed]
  8. Cloning and expression of a cDNA encoding mouse indoleamine 2,3-dioxygenase. Habara-Ohkubo, A., Takikawa, O., Yoshida, R. Gene (1991) [Pubmed]
  9. Gene expression of enzymes for tryptophan degradation pathway is upregulated in the skin lesions of patients with atopic dermatitis or psoriasis. Ito, M., Ogawa, K., Takeuchi, K., Nakada, A., Heishi, M., Suto, H., Mitsuishi, K., Sugita, Y., Ogawa, H., Ra, C. J. Dermatol. Sci. (2004) [Pubmed]
  10. Influenza-induced expression of indoleamine 2,3-dioxygenase enhances interleukin-10 production and bacterial outgrowth during secondary pneumococcal pneumonia. van der Sluijs, K.F., Nijhuis, M., Levels, J.H., Florquin, S., Mellor, A.L., Jansen, H.M., van der Poll, T., Lutter, R. J. Infect. Dis. (2006) [Pubmed]
  11. Induction of indoleamine 2,3-dioxygenase in mouse lung during virus infection. Yoshida, R., Urade, Y., Tokuda, M., Hayaishi, O. Proc. Natl. Acad. Sci. U.S.A. (1979) [Pubmed]
  12. GCN2 kinase in T cells mediates proliferative arrest and anergy induction in response to indoleamine 2,3-dioxygenase. Munn, D.H., Sharma, M.D., Baban, B., Harding, H.P., Zhang, Y., Ron, D., Mellor, A.L. Immunity (2005) [Pubmed]
  13. Specific subsets of murine dendritic cells acquire potent T cell regulatory functions following CTLA4-mediated induction of indoleamine 2,3 dioxygenase. Mellor, A.L., Chandler, P., Baban, B., Hansen, A.M., Marshall, B., Pihkala, J., Waldmann, H., Cobbold, S., Adams, E., Munn, D.H. Int. Immunol. (2004) [Pubmed]
  14. Enhancement of innate immunity against Mycobacterium avium infection by immunostimulatory DNA is mediated by indoleamine 2,3-dioxygenase. Hayashi, T., Rao, S.P., Takabayashi, K., Van Uden, J.H., Kornbluth, R.S., Baird, S.M., Taylor, M.W., Carson, D.A., Catanzaro, A., Raz, E. Infect. Immun. (2001) [Pubmed]
  15. Cells expressing indoleamine 2,3-dioxygenase inhibit T cell responses. Mellor, A.L., Keskin, D.B., Johnson, T., Chandler, P., Munn, D.H. J. Immunol. (2002) [Pubmed]
  16. Neuronal localization of indoleamine 2,3-dioxygenase in mice. Roy, E.J., Takikawa, O., Kranz, D.M., Brown, A.R., Thomas, D.L. Neurosci. Lett. (2005) [Pubmed]
  17. 3-Hydroxyanthranilic acid, one of metabolites of tryptophan via indoleamine 2,3-dioxygenase pathway, suppresses inducible nitric oxide synthase expression by enhancing heme oxygenase-1 expression. Oh, G.S., Pae, H.O., Choi, B.M., Chae, S.C., Lee, H.S., Ryu, D.G., Chung, H.T. Biochem. Biophys. Res. Commun. (2004) [Pubmed]
  18. Tryptophan availability selectively limits NO-synthase induction in macrophages. Chiarugi, A., Rovida, E., Dello Sbarba, P., Moroni, F. J. Leukoc. Biol. (2003) [Pubmed]
  19. Expression of indoleamine 2,3-dioxygenase, tryptophan degradation, and kynurenine formation during in vivo infection with Toxoplasma gondii: induction by endogenous gamma interferon and requirement of interferon regulatory factor 1. Silva, N.M., Rodrigues, C.V., Santoro, M.M., Reis, L.F., Alvarez-Leite, J.I., Gazzinelli, R.T. Infect. Immun. (2002) [Pubmed]
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