Indoleamine 2,3-dioxygenase is a signaling protein in long-term tolerance by dendritic cells
By M. T. Pallotta, C. Orabona, C. Volpi, C. Vacca, M. L. Belladonna, R. Bianchi, G. Servillo, Cinzia Brunacci, M. Calvitti, S. Bicciato and 7 more. Nature Immunology, 2011
685 citations recorded by the source corpus.
Regulation of tryptophan metabolism by indoleamine 2,3-dioxygenase (IDO) in dendritic cells (DCs) is a highly versatile modulator of immunity. In inflammation, interferon-γ is the main inducer of IDO for the prevention of hyperinflammatory responses, yet IDO is also responsible for self-tolerance effects in the longer term. Here we show that treatment of mouse plasmacytoid DCs (pDCs) with transforming growth factor-β (TGF-β) conferred regulatory effects on IDO that were mechanistically separable from its enzymic activity. We found that IDO was involved in intracellular signaling events responsible for the self-amplification and maintenance of a stably regulatory phenotype in pDCs. Thus, IDO has a tonic, nonenzymic function that contributes to TGF-β-driven tolerance in noninflammatory contexts.
Subfields: Behavioral Neuroscience, Biological Psychiatry, Neurology
View Paper: https://www.semanticscholar.org/paper/8d3b20d17a467dfa47c4282ecc536a81b59a4817
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Citations in the corpus
- IDO in the Tumor Microenvironment: Inflammation, Counter-regulation and Tolerance (2016, positive): “Indeed, IDO appears to have certain inherent signaling functions in DCs that are distinct from its tryptophan-catabolizing enzymatic function [106], such that expression of IDO may render the DC more tolerogenic in a cell-intrinsic fashion [107].”
- Transforming Grown Factor-β Signaling in Immunity and Cancer (2019, positive): “The tolerogenic program of DCs is in part mediated by induction of immunosuppressing molecules indoleamine 2,3-dioxygenase (IDO) and arginase by TGF-β signaling (Belladonna et al., 2008; Pallotta et al., 2011).”
- Tryptophan catabolism in cancer: beyond IDO and tryptophan depletion. (2012, background): “Posttranslational regulation may also take place, and phosphorylation of IDO was described and found to regulate its turnover and signaling activity (12, 13).”