scholarly journals Fungal natural alkaloid schizocommunin activates the aryl hydrocarbon receptor pathway

MedChemComm ◽  
2019 ◽  
Vol 10 (6) ◽  
pp. 985-990
Author(s):  
Roxana Filip ◽  
Tyler A. Shaw ◽  
Atsushi Nishida ◽  
John Paul Pezacki
Keyword(s):  
Aryl Hydrocarbon Receptor ◽  
Metabolizing Enzymes ◽  
Xenobiotic Metabolizing Enzymes ◽  
Aryl Hydrocarbon ◽  
Natural Alkaloid

Activation of AhR by schizocommunin is linked to increased expression of xenobiotic metabolizing enzymes associated with immune and allergic responses.

scholarly journals Dopamine is an aryl hydrocarbon receptor agonist

2020 ◽  
Vol 477 (19) ◽  
pp. 3899-3910
Author(s):  
Hyejin Park ◽  
Un-ho Jin ◽  
Keshav Karki ◽  
Arul Jayaraman ◽  
Clint Allred ◽  
...  
Keyword(s):  
Pancreatic Cancer ◽  
Aryl Hydrocarbon Receptor ◽  
Cancer Cells ◽  
Agonist Activity ◽  
Metabolizing Enzymes ◽  
Aryl Hydrocarbon ◽  
Pancreatic Cancer Cells ◽  
Aryl Hydrocarbon Receptor Agonist ◽  
Tryptophan Metabolites ◽  
High Concentrations

Tryptophan metabolites exhibit aryl hydrocarbon receptor (AhR) agonist activity and recent studies show that the phenylalanine metabolites serotonin and carbidopa, a drug used in treating Parkinson's disease, activated the AhR. In this study, we identified the neuroactive hormone dopamine as an inducer of drug-metabolizing enzymes CYP1A1, CYP1B1, and UGT1A1 in colon and glioblastoma cells and similar results were observed for carbidopa. In contrast, carbidopa but not dopamine exhibited AhR activity in BxPC3 pancreatic cancer cells whereas minimal activity was observed for both compounds in Panc1 pancreatic cancer cells. In contrast with a previous report, the induction responses and cytotoxicity of carbidopa was observed only at high concentrations (100 µM) in BxPC3 cells. Our results show that similar to serotonin and several tryptophan metabolites, dopamine is also an AhR-active compound.

scholarly journals The Aryl Hydrocarbon Receptor and the Nervous System

2018 ◽  
Vol 19 (9) ◽  
pp. 2504 ◽  
Author(s):  
Ludmila Juricek ◽  
Xavier Coumoul
Keyword(s):  
Aryl Hydrocarbon Receptor ◽  
Molecular Mechanisms ◽  
Neuronal Cell ◽  
Cell Types ◽  
Dendritic Morphology ◽  
Metabolizing Enzymes ◽  
Common Features ◽  
Aryl Hydrocarbon ◽  
The Common ◽  
Neuronal Proliferation

The aryl hydrocarbon receptor (or AhR) is a cytoplasmic receptor of pollutants. It translocates into the nucleus upon binding to its ligands, and forms a heterodimer with ARNT (AhR nuclear translocator). The heterodimer is a transcription factor, which regulates the transcription of xenobiotic metabolizing enzymes. Expressed in many cells in vertebrates, it is mostly present in neuronal cell types in invertebrates, where it regulates dendritic morphology or feeding behavior. Surprisingly, few investigations have been conducted to unravel the function of the AhR in the central or peripheral nervous systems of vertebrates. In this review, we will present how the AhR regulates neural functions in both invertebrates and vertebrates as deduced mainly from the effects of xenobiotics. We will introduce some of the molecular mechanisms triggered by the well-known AhR ligand, 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD), which impact on neuronal proliferation, differentiation, and survival. Finally, we will point out the common features found in mice that are exposed to pollutants, and in AhR knockout mice.

scholarly journals Induction of xenobiotic-metabolizing enzymes in hepatocytes by beta-naphthoflavone: Time-dependent changes in activities, protein and mRNA levels

2018 ◽  
Vol 68 (1) ◽  
pp. 75-85 ◽  
Author(s):  
Kateřina Lněničková ◽  
Lenka Skálová ◽  
Lucie Stuchlíková ◽  
Barbora Szotáková ◽  
Petra Matoušková
Keyword(s):  
Cytochromes P450 ◽  
Rat Hepatocytes ◽  
Measured Parameter ◽  
Time Interval ◽  
Induction Effect ◽  
Mrna Levels ◽  
Metabolizing Enzymes ◽  
Xenobiotic Metabolizing Enzymes ◽  
Aryl Hydrocarbon ◽  
Induction Study

Abstract In the present study, time-dependency of the induction effect of a selective inducer on the activity, protein and mRNA levels of cytochromes P450 1A1/2 (CYP1A1/2), NAD(P)H:quinone oxidoreductase 1 (NQO1) and glutathione S-transferases (GSTA), in primary culture of rat hepatocytes was tested and evaluated. To show the differences in responses of tested enzymes, the common aryl hydrocarbon receptor (AhR) ligand agonist, beta-naphthoflavone (BNF), was used. Induction of CYP1A1/2 by BNF was detected at all time intervals and at all levels (i.e., mRNA, protein, enzyme activity). Different responses of NQO1 and GSTA upon BNF treatment were observed. Our results demonstrate that the responses of different xenobiotic-metabolizing enzymes to the inducer vary in time and depend on the measured parameter. For these reasons, an induction study featuring only one-time interval treatment and/ or one parameter testing could produce misleading information.

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