Indoleamine 2, 3-dioxygenase (IDO) is essential for dendritic cell activation and chemotactic responsiveness to chemokines

IDO 2 ( indoleamine 2 , 3 - dioxygenase 2 )

Indoleamine 2,3-dioxygenase (ido) and Immune Tolerance

The IDO facilitates immune tolerance and is one of the main actors involved in the inhibition of cell proliferation, including activated T cells. IDO induces production of reactive oxygen species (ROS) and nitric oxide (NO) radicals. Several pathways involved in the regulation of immune response are regulated by redox mechanisms. Reactive oxygen and nitrogen species (ROSRNS) and other redox act...

Respiratory syncytial virus replication induces Indoleamine 2,3-dioxygenase (IDO) activation in human dendritic cells

Objective/purpose Induction of IDO in dendritic cells (DCs) depletes the essential amino acid, tryptophan, and generates a family of catabolites known as kynurenines (KYN). IDO activity is reported to have immunomodulatory effects, including the selective induction of apoptosis in T-helper 1 (Th1) lymphocytes, an effect not seen with Th2 cells that are dominant in allergic asthma. Infants hospi...

A two-step induction of indoleamine 2,3 dioxygenase (IDO) activity during dendritic-cell maturation.

Prostaglandins, a family of lipidic molecules released during inflammation, display immunomodulatory properties in several models. One use includes exposure of monocyte-derived dendritic cells (DCs) to a cocktail of cytokines that contains prostaglandin E2 (PGE2) for purposes of maturation; such cells are currently being used for cancer immunotherapy trials. Our analysis of the transcription pr...

The indoleamine 2,3-dioxygenase pathway is essential for human plasmacytoid dendritic cell-induced adaptive T regulatory cell generation.

Human plasmacytoid dendritic cells (PDCs) can drive naive, allogeneic CD4(+)CD25(-) T cells to differentiate into CD4(+)CD25(+)Foxp3(+) regulatory T cells (Tregs). However, the intracellular mechanism or mechanisms underlying PDC-induced Treg generation are unknown. In this study, we show that human PDCs express high levels of IDO, an intracellular enzyme that catabolizes tryptophan degradation...