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Hypoxia and dimethyloxalylglycine (DMOG) downregulates tryptophan-2,3-dioxygenase (TDO2) expression in GBM cells

ABSTRACT: The tryptophan degrading enzyme TDO2 is downregulated upon HIF1alpha stabilization by exposure to both hypoxia as well as chemical hypoxia mimetics such as DMOG in glioblastoma cell line A172.

ORGANISM(S): Homo sapiens

PROVIDER: GSE138535 | GEO | 2019/12/29

REPOSITORIES: GEO

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Hypoxia and dimethyloxalylglycine (DMOG) downregulates tryptophan-2,3-dioxygenase (TDO2) expression in GBM cells

Project description:Hypoxia and dimethyloxalylglycine (DMOG) downregulates tryptophan-2,3-dioxygenase (TDO2) expression in GBM cells

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Synthetic Essentiality of Tryptophan 2,3-dioxygenase 2 in APC-Mutated Colorectal Cancer I

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Synthetic Essentiality of Tryptophan 2,3-dioxygenase 2 in APC-Mutated Colorectal Cancer [ChIP-Seq]

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Transcriptome-wide expression changes over time in cultured primary human monocytes due to DMOG treatment

Project description:RNA sequencing of primary human monocytes cultured with and without hypoxia-mimetic agent DMOG (Dimethyloxalylglycine). Monocytes isolated from PBMCs of 7 healthy donors were cultured with and without DMOG for 24hrs and harvested at 0, 2, 10 or 24hrs for RNA sequencing. DMOG suppresses HIF Prolyl hydroxylase (HIF-PH) activity by acting as a small molecule competitive inhibitor. HIF-PH inhibition leads to increase in endogenous HIF protein levels and mimics aspects of hypoxia. This RNA-seq study allows analysis of transciptome-wide expression pattern changes over time due to DMOG treatment.

2022-04-13 | GSE165998 | GEO

Genome-wide chromatin accessibility changes over time in cultured primary human monocytes due to DMOG treatment

Project description:ATAC sequencing of primary human monocytes cultured with and without hypoxia-mimetic agent DMOG (Dimethyloxalylglycine). Monocytes isolated from PBMCs of 7 healthy donors were cultured with and without DMOG for 24hrs and harvested at 0, 2, 10 or 24hrs for RNA sequencing. DMOG suppresses HIF Prolyl hydroxylase (HIF-PH) activity by acting as a small molecule competitive inhibitor. HIF-PH inhibition leads to increase in endogenous HIF protein levels and mimics aspects of hypoxia. This ATAC-seq study allows analysis of genome-wide changes to chromatin accessibility due to DMOG treatment.

2022-04-13 | GSE165997 | GEO

Expression data from the hepatic stellate cell line LX-2 after treatment with DMOG and from the liver sinusoidal endothelial cell line TRP3 after incubation with conditioned medium of DMOG-treated LX-2

Project description:Expression data from the hepatic stellate cell line LX-2 after treatment with the prolylhydroxylase inhibitor dimethyloxalylglycine (DMOG) and from the liver sinusoidal endothelial cell line TRP3 after incubation with conditioned medium of DMOG-treated LX-2 Prolyl-hydroxylase inhibitors such as dimethyloxalylglycine (DMOG) stabilize HIF-1α, thereby chemically inducing hypoxia, which also accelerates liver volume increase when given with portal rerouting. We used microarrays to clarify the cellular crosstalk of the different cell types in accelerated liver regeneration by examining the role of hepatic stellate cells (HSC) and liver sinusoidal endothelial cells (LSEC).

2020-03-23 | GSE131168 | GEO

Next-Generation Standard RNA-Sequencing Analysis of human monocytes stimulated by HMGB1 with or without DMOG

Project description:We report the application of standard RNA-sequencing technology for high-throughput profiling of differential gene expression in mammalian cells. This study aims to compare differential gene expression in human monocytes in the absence or presence of HMGB1 and DMOG exposure would mimic hypoxia. Human monocytes (five million cells) from a healthy donor were divided into four groups in triplicate (control, DMOG, HMGB1 or HMGB1_DMOG). RNA isolation, RNA integrity check, library preparation and ~350M raw paired-end reads per lane (Illumina HISeq. 2x150 bp sequencing) were conducted at GENEWIZ, LLC. We find that increased TNF signaling induced by HMGB1 and enhanced when DMOG was present, and reduced IFN signaling in DMOG in unstimulated and HMGB1-stimulated conditions. We conclude that RNA-seq based UP and DOWN regulated genes/pathways characterization would confirm our results and expedite genetic network analyses.

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Substrate stereo-specificity in tryptophan dioxygenase and indoleamine 2,3-dioxygenase.

Project description:The first and rate-limiting step of the kynurenine pathway, in which tryptophan (Trp) is converted to N-formylkynurenine is catalyzed by two heme-containing proteins, Indoleamine 2,3-dioxygenase (IDO), and Tryptophan 2,3-dioxygenase (TDO). In mammals, TDO is found exclusively in liver tissue, IDO is found ubiquitously in all tissues. IDO has become increasingly popular in pharmaceutical research as it was found to be involved in many physiological situations, including immune escape of cancer. More importantly, small-molecule inhibitors of IDO are currently utilized in cancer therapy. One of the main concerns for the design of human IDO (hIDO) inhibitors is that they should be selective enough to avoid inhibition of TDO. In this work, we have used a combination of classical molecular dynamics (MD) and hybrid quantum-classical (QM/MM) methodologies to establish the structural basis that determine the differences in (a) the interactions of TDO and IDO with small ligands (CO/O(2)) and (b) the substrate stereo-specificity in hIDO and TDO. Our results indicate that the differences in small ligand bound structures of IDO and TDO arise from slight differences in the structure of the bound substrate complex. The results also show that substrate stereo-specificity of TDO is achieved by the perfect fit of L-Trp, but not D-Trp, which exhibits weaker interactions with the protein matrix. For hIDO, the presence of multiple stable binding conformations for L/D-Trp reveal the existence of a large and dynamic active site. Taken together, our data allow determination of key interactions useful for the future design of more potent hIDO-selective inhibitors.

| S-EPMC2939288 | biostudies-literature

Expression of indoleamine 2,3-dioxygenase and tryptophan 2,3-dioxygenase in early concepti.

Project description:Indoleamine 2,3-dioxygenase (IDO)-initiated tryptophan degradation in the placenta has been implicated in the prevention of the allogeneic fetus rejection [Munn, Zhou, Attwood, Bondarev, Conway, Marshall, Brown, and Mellor (1998) Science 281, 1191-1193]. To determine how IDO is associated with the development of the fetus and placenta, the time course of IDO expression (tryptophan-degrading activity, IDO protein and IDO mRNA) in the embryonic and extra-embryonic tissues as well as maternal tissues of mice was examined. A high tryptophan-degrading activity was detected in early concepti on days 6.5 and 7.5, whereas IDO protein and its mRNA were not expressed during early gestation, but appeared 2-3 days later, lasted for about 3 days and declined rapidly thereafter. The expression of IDO basically coincided with the formation of the placenta. On the contrary, the early tryptophan-degrading activity was due to gene expression of tryptophan 2,3-dioxygenase (TDO), as shown by Northern and Western analysis. These findings indicate that IDO is transiently expressed in the placenta but that the expression does not last until birth, and that the IDO expression is preceded by expression of another tryptophan-degrading enzyme, TDO, in the maternal and/or embryonic tissues in early concepti.

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