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Differential expression of CD25 (show IL2RA Proteins) and IDO mRNA with high and low virulence bovine viral diarrhea virus might reflect temporal differences in transcription during the immune response elicited by these viral strains.
IDO may be involved in downregulating immune responses to M. avium subsp. paratuberculosis and other virulent mycobacteria, which may be an example of the pathogen harnessing host immunoregulatory pathways to aid survival.
INDO participates in IFN-gama-induced death of bovine luteal cells, through a mechanism that involves degradation of tryptophan, thereby reducing tryptophan concentrations to a point insufficient to meet luteal cells needs
SIV-infected macaques exhibiting progression to AIDS displayed greater expression of TGF-beta (show TGFB1 Proteins) and indoleamine 2,3 dioxygenase in CD8 (show CD8A Proteins)+ T cells from mesentric lymph nodes.
PD-L1 (show CD274 Proteins), IDO-1, and B7-H4 (show VTCN1 Proteins) are differentially expressed in human lung carcinomas and show limited co-expression. While PD-L1 (show CD274 Proteins) and IDO-1 are associated with increased tumor-infiltrating lymphoycte and IFN-gamma (show IFNG Proteins) stimulation, B7-H4 (show VTCN1 Proteins) is not.
Data show that indole 23-dioxygenase (IDO) is variably expressed by tumor-infiltrating immune cells or reactive cells rather than lymphoma cells in diffuse large-cell lymphoma (DLBCL).
High IDO1 expression is associated with hepatocellular carcinoma.
Epacadostat significantly decreases Treg proliferation induced by IDO production from IFN-gamma (show IFNG Proteins) plus LPS (show IRF6 Proteins) matured human DCs, although the Treg phenotype does not change
Inhibition of TOR (show RORC Proteins) serine-threonine kinases (mTOR (show FRAP1 Proteins)) strongly induced indoleamine 23-dioxygenase 1 (IDO1) expression and activity, corroborating its ability to recruit Treg cells in the tumor microenvironment.
MALAT1-overexpressed MSCs promoted M2 macrophage polarization and this effect was mediated by MALAT1-induced IDO expression, suggesting that MALAT1 may enhance the immunosuppressive properties of MSCs in vivo.
Despite the large concordance between P and matched M for the evaluated molecular alterations, potential actionable targets such as ESR1 (show ESR1 Proteins) mutations were found only in M. This supports the importance of characterizing the M disease. Other targets we identified, such as HIF1A (show HIF1A Proteins) and IDO1, warrant further investigation in this patient population.
this study demonstrated that the downregulation of IDO expression on the endothelial cells of the villous stroma was associated with preeclampsia
The data suggest that in Puumala infection, the mechanism responsible for the suppressive effect of IDO is not metabolic control of effector cells but rather the signaling mediated by tryptophan breakdown products, such as kynurenine.
These results show IDO is upregulated with RSV infection and this upregulation likely participates with IFN-gamma (show IFNG Proteins) in inhibition of virus replication and suppression of some host cell responses to infection.
Findings suggest non-redundant neurophysiological roles for indoleamine 2,3-dioxygenase 1, indoleamine 2,3-dioxygenase 2 (show IDO2 Proteins) and tryptophan 2,3-dioxygenase (show TDO2 Proteins) in modulating brain activities and metabolism.
Lipopolysaccharide (LPS (show TLR4 Proteins)) stimulation increased the expression and activity of the immunoregulatory enzyme IDO1 in hepatic stellate cells (HSCs), and LPS (show TLR4 Proteins)/HSCs stimulated aryl hydrocarbon receptor (AhR (show AHR Proteins)) signaling in cocultured regulatory T cells.
this study shows that the presence of IFN-alpha (show IFNA Proteins) at antigen sensitization activates an IDO1/TGF-beta (show TGFB1 Proteins)-dependent anti-inflammatory program that upon antigenic rechallenge prevents inflammation via plasmacytoid dendritic cells
Across strains, networks depicted a predominance of genes under-expressed in microglia relative to macrophages that may be a precursor for the different response of both cell types to challenges. The detected transcriptome differences enhance the understanding of the role of IDO1 in the microglia transcriptome under unchallenged conditions.
Data show that indoleamine 23-dioxygenase 1 (IDO-1) inhibitors 1-methyl-D-tryptophan was able to alleviate most of the behavioural changes resulting from unpredictable chronic mild stress (UCMS) exposure.
IDO did not play a pivotal role in the suppression of allergic airway inflammation through adipose-derived stem cells, suggesting that it is not the major regulator responsible for suppressing allergic airway inflammation.
These results indicate that Platelet-activating Factor -mediated endotoxin tolerance is initiated via IDO- and JAK (show JAK3 Proteins)/STAT (show STAT1 Proteins)-dependent expression of SOCS3 (show SOCS3 Proteins).
Aortic Plasmacytoid dendritic cells expressed CCR9 (show CCR9 Proteins) and indoleamine 2,3-dioxygenase 1 (IDO-1), an enzyme involved in driving the generation of regulatory T cells (Tregs).
Indoleamine-2,3-dioxygenase (IDO) production by Plasmacytoid dendritic cells (pDCs)is necessary to confer suppressive function to T-Cells, Regulatory (Tregs) in experimental autoimmune encephalomyelitis (EAE).
This gene encodes indoleamine 2,3-dioxygenase (IDO) - a heme enzyme that catalyzes the first and rate-limiting step in tryptophan catabolism to N-formyl-kynurenine. This enzyme acts on multiple tryptophan substrates including D-tryptophan, L-tryptophan, 5-hydroxy-tryptophan, tryptamine, and serotonin. This enzyme is thought to play a role in a variety of pathophysiological processes such as antimicrobial and antitumor defense, neuropathology, immunoregulation, and antioxidant activity. Through its expression in dendritic cells, monocytes, and macrophages this enzyme modulates T-cell behavior by its peri-cellular catabolization of the essential amino acid tryptophan.
indoleamine-pyrrole 2,3 dioxygenase
, indoleamine 2,3-dioxygenase 2
, putative indoleamine 2,3-dioxygenase
, indoleamine 2,3-dioxygenase 1
, indolamine 2,3 dioxygenase
, indole 2,3-dioxygenase
, indoleamine-pyrrole 2,3-dioxygenase
, indoleamine 23-dioxygenase