Role of indoleamine 2,3-dioxygenase in health and disease.
Sydney, Australia. In Clin Sci (lond), 01 Nov 2015
IDO1 (indoleamine 2,3-dioxygenase 1) is a member of a unique class of mammalian haem dioxygenases that catalyse the oxidative catabolism of the least-abundant essential amino acid, L-Trp (L-tryptophan), along the kynurenine pathway.
PD-L1 blockade for cancer treatment: MEDI4736.
Cambridge, United Kingdom. In Semin Oncol, Jun 2015
In addition, multiple phase I combination studies are ongoing with different agents, including those targeting MEK/BRAF in melanoma, epidermal growth factor receptor, programmed cell death-1, cytotoxic T-lymphocyte antigen-4, OX40, chemokine (C-C motif) receptor 4, and indoleamine 2,3-dioxygenase.
Cancer prevention and therapy through the modulation of the tumor microenvironment.
Stanford, United States. In Semin Cancer Biol, May 2015
Specifically, we describe how inhibition of targets such as cholesterol synthesis and metabolites, reactive oxygen species and hypoxia, macrophage activation and conversion, indoleamine 2,3-dioxygenase regulation of dendritic cells, vascular endothelial growth factor regulation of angiogenesis, fibrosis inhibition, endoglin, and Janus kinase signaling emerge as examples of important potential nexuses in the regulation of tumorigenesis and the tumor microenvironment that can be targeted.
Immunomodulatory effects mediated by serotonin.
Mexico. In J Immunol Res, Dec 2014
Three classes of genes regulating 5-HT function are constitutively expressed or induced in these cells: (a) membrane proteins that regulate the response to 5-HT, such as SERT, 5HTR-GPCR, and the 5HT3-ion channels; (b) downstream signaling transduction proteins; and (c) enzymes controlling 5-HT metabolism, such as IDO and MAO, which can generate biologically active catabolites, including melatonin, kynurenines, and kynurenamines.
Tryptophan Catabolism in Chronic Viral Infections: Handling Uninvited Guests.
Montréal, Canada. In Int J Tryptophan Res, Dec 2014
UNASSIGNED: l-Tryptophan (l-Trp) is an essential amino acid that possesses diverse metabolic, neurological, and immunological roles spanning from the synthesis of proteins, neurotransmitter serotonin, and neurohormone melatonin, to its degradation into immunosuppressive catabolites by indoleamine-2, 3-dioxygenase (IDO) in the kynurenine pathway (KP).
Trial watch: IDO inhibitors in cancer therapy.
Villejuif, France. In Oncoimmunology, Nov 2014
UNASSIGNED: Indoleamine 2,3-dioxigenase 1 (IDO1) is the main enzyme that catalyzes the first, rate-limiting step of the so-called "kynurenine pathway", i.e., the metabolic cascade that converts the essential amino acid L-tryptophan (Trp) into L-kynurenine (Kyn).
Neuroinflammation and comorbidity of pain and depression.
Houston, United States. In Pharmacol Rev, 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.
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.