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Tryptamine Serves As a Proligand of the AhR Transcriptional Pathway, and the Activation Is Dependent of Monoamine Oxidases

ABSTRACT: In this study we show that physiological concentrations of tryptamine (TA) lead to induction of cytochrome P4501A1 transcription through an AhR-dependent mechanism. In addition, we show that activation of the AhR by TA requires a functional monoamino oxidase system, suggesting that TA acts as an AhR proligand possibly by converting to a high-affinity AhR ligand.

ORGANISM(S): Mus musculus

PROVIDER: GSE39812 | GEO | 2012/08/02

SECONDARY ACCESSION(S): PRJNA171764

REPOSITORIES: GEO

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Tryptamine Serves As a Proligand of the AhR Transcriptional Pathway, and the Activation Is Dependent of Monoamine Oxidases

Project description:In this study we show that physiological concentrations of tryptamine (TA) lead to induction of cytochrome P4501A1 transcription through an AhR-dependent mechanism. In addition, we show that activation of the AhR by TA requires a functional monoamino oxidase system, suggesting that TA acts as an AhR proligand possibly by converting to a high-affinity AhR ligand. RNA seq was performed from Hepa cells treated with FICZ or TA by SciLifelabs.

2012-08-02 | E-GEOD-39812 | biostudies-arrayexpress

Tryptamine serves as a proligand of the AhR transcriptional pathway whose activation is dependent of monoamine oxidases.

Project description:The function of the aryl hydrocarbon receptor (AhR) in mediating the biological effect to environmental pollutants is well established. However, accumulated evidence indicates a wide range of physiological and pathological functions mediated by the AhR, suggesting the existence of endogenous AhR ligand(s). The nature of an AhR ligand remain elusive; however, it is known that the AhR is activated by several compounds, such as 2,3,7,8-tetrachlorodibenzo-p-dioxin or the tryptophan photoproduct 6-formylindolo[3,2-b]carbazole. In this study, we show that physiological concentrations of tryptamine (TA) lead to induction of cytochrome P4501A1 transcription through an AhR-dependent mechanism. In addition, we show that activation of the AhR by TA requires a functional monoamino oxidase system, suggesting that TA acts as an AhR proligand possibly by converting to a high-affinity AhR ligand. Taken together, we show a possible mechanism, through which AhR signaling is activated by endogenous conversion of TA involving monoamine oxidases.

| S-EPMC5416975 | biostudies-literature

AhR antagonist

Project description:AhR antagonist

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AhR interactome in early embryonic development

Project description:The transcriptional program of early embryonic development is tightly regulated by a set of well-defined transcription factors that suppress premature expression of differentiation genes and sustain the pluripotent identity. It is generally accepted that this program can be perturbed by environmental factors such as chemical pollutants, however the precise molecular mechanisms remain unknown. The Aryl Hydrocarbon Receptor (AHR) is a widely expressed nuclear receptor that senses environmental stimuli and modulates target gene expression. Here, we show that ectopic activation of AHR during early differentiation disrupts the differentiation program via the chromatin remodeling complex NuRD. The activated AHR/NuRD complex altered the expression of differentiation-specific genes that control the first two developmental decisions without affecting the pluripotency program. These findings identify a novel mechanism that allows environmental stimuli to disrupt embryonic development through AHR signaling.

2018-02-26 | PXD006089 | Pride

Comparison of gene expression in AhR WT (+/+) and AhR KO (-/-) primary mouse keratinocytes

Project description:The AhR is a ligand activated transcription factor that may be important in normal skin physiology. We compared gene expression profiles between AhR Wt and AhR KO primary mouse keratinocyte cultures. We identified 391 genes that were differentially expressed with a 1.5 fold cutoff and p<.05, and identified the AhR as an important regulator of genes involved in normal epidermal differentiation. AhR Wt primary keratinocyte cultures (n=4) were compared with AhR KO primary keratinocyte cultures (n=3)

2015-07-01 | E-GEOD-62490 | biostudies-arrayexpress

Hexokinase 2 is a transcriptional targetHexokinase 2 is a transcriptional target and a positive modulator of AHR signalling and a positive modulator of AHR signalling

Project description:The Aryl Hydrocarbon Receptor (AHR) regulates the expression of numerous genes in response to activation by agonists including xenobiotics. Although it is well appreciated that environmental signals and cell intrinsic features may modulate this transcriptional response, how it is mechanistically achieved remains poorly understood. We show that Hexokinase 2 (HK2) a metabolic enzyme fuelling cancer cell growth, is a transcriptional target of AHR as well as a modulator of its activity. Expression of HK2 is positively regulated by AHR upon exposure to agonists both in human cells and in mice lung tissues. Conversely, over-expression of HK2 regulates the abundance of many proteins involved in the regulation of AHR signalling and these changes are linked with altered AHR expression levels and transcriptional activity. HK2 expression also shows a negative correlation with AHR promoter methylation in tumours, and these tumours with high HK2 expression and low AHR methylation are associated with a worse overall survival in patients. In sum, our study provides novel insights into how AHR signalling is regulated which may help our understanding of the context-specific effects of this pathway and may have implications in cancer.

2022-05-31 | PXD028992 | Pride

Inhibition of Monoamine Oxidases by Pyridazinobenzylpiperidine Derivatives

Project description: Not available

| S-EPMC11243598 | biostudies-literature

Transcriptional profiling in neurons of C. elegans : comparison between ahr-1 mutant and wild-type animals.

Project description:The Aryl hydrocarbon Receptor (AhR) is a transcription factor well known in vertebrate to play an essential role as xenobiotic sensor. On the contrary, no ligand has been identified to date for invertebrate AhR. In some model organisms such as D. melanogaster and C. elegans, AhR orthologs have physiological functions and their inability to bind prototypical ligands of vertebrate AhR such as tetrachlorodibenzo-p-dioxin (TCDD) suggests that the detoxification role of the receptor could be an adaptation acquired during evolution. To better understand the physiological roles of AhR, we studied AhR-1, the C. elegans ortholog and performed transcriptomic and metabolomic analysis respectively in neuronal cells expressing AhR-1 and in whole animals. Next, we designed a reporter system in order to investigate if the transcriptional activity of AhR-1 could be modulated. Cos-7 cells were transfected with AhR-1, its dimerization partner AhA-1 (C. elegans ARNT ortholog) and a Firefly luciferase gene under the control of the human cytochrome P450 1A1 promotor. The luciferase bioluminescence measurement allows the identification of C. elegans AhR-1 modulators. Transcriptional profiling in neurons expressing AhR-1 revealed 95 genes down-regulated, and 76 genes up-regulated in AhR-1 KO animals. These genes are associated with nervous system function (depleted) and fatty acid process, oxidative phosphorylation and glycolysis (enriched). Metabolomic profiling results indicate a role for AhR-1 in regulating several endogenous metabolic pathways: amino-acid metabolism, carbohydrate metabolism as well as fatty acid metabolism Then, with the COS-7 in vitro screening model, we identified positive and negative modulators such as bacterial, dietary or environmental compounds. Considering C. elegans environment, these results could be used to highlight the role of invertebrate AhR and identified new features in vertebrate AhR.

2022-06-01 | GSE195728 | GEO

Comparison of gene expression in AhR WT (+/+) and AhR KO (-/-) primary mouse keratinocytes

2015-07-01 | GSE62490 | GEO

Proteome and Phosphoproteome of AhR-dependent non-genomic signaling in endotoxin-activated macrophages

Project description:Emerging studies revealed an immunomodulatory role of the Aryl hydrocarbon receptor (AhR), a receptor sensing environmental contaminants, and involved in their detoxification. Besides its function as a transcription factor, AhR can participate in non-genomic signaling through ubiquitination and phosphorylation-dependent processes. In this study, a multi-PTM-omics approach, including proteome, ubiquitome, and phosphoproteome, was utilized to examine mechanisms of non-genomic AhR-signaling in endotoxin-activated monocyte-derived macrophages. This dataset entails proteome and phosphoproteome data.

2021-03-30 | PXD020770 | Pride

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