Neuroinflammation and comorbidity of pain and depression.
Houston, United States. In Pharmacol Rev, Dec 2013
These mechanisms include direct effects of cytokines on the neuronal environment or indirect effects via downregulation of G protein-coupled receptor kinase 2, activation of the tryptophan-degrading enzyme indoleamine 2,3-dioxygenase that generates neurotropic kynurenine metabolites, increased brain extracellular glutamate, and the switch of GABAergic neurotransmission from inhibition to excitation.
Immunological Relevance of the Coevolution of IDO1 and AHR.
Boston, United States. In Front Immunol, Dec 2013
Indoleamine-2,3-dioxygenase (IDO) and tryptophan-2,3-dioxygenase (TDO) are considered rate-limiting enzymes in the tryptophan catabolism and play important roles in the regulation of the immunity.
AhR-Mediated, Non-Genomic Modulation of IDO1 Function.
Perugia, Italy. In Front Immunol, Dec 2013
The evolutionary process has conferred a dual - enzymatic and signaling - function on the ancestral metabolic enzyme indoleamine 2,3-dioxygenase 1 (IDO1), which has long been known for converting the essential amino acid tryptophan (TRP) into neuroactive and immunoactive catabolites (kynurenines).
Tryptophan-catabolizing enzymes - party of three.
Sydney, Australia. In Front Immunol, Dec 2013
Indoleamine 2,3-dioxygenase (IDO) and tryptophan 2,3-dioxygenase (TDO) are tryptophan-degrading enzymes that have independently evolved to catalyze the first step in tryptophan catabolism via the kynurenine pathway (KP).
Highlights of 10 years of immunology in Nature Reviews Immunology.
New Haven, United States. In Nat Rev Immunol, 2011
Highlights include our improved understanding of Toll-like receptor signalling, and of immune regulation mediated by regulatory T cells, indoleamine 2,3-dioxygenase, myeloid-derived suppressor cells and interleukin-10.