Tryptamine serves as a proligand of the AhR transcriptional pathway whose activation is dependent of monoamine oxidases.
Mol Endocrinol, 2012/9;26(9):1542-51.
Vikström Bergander L[1], Cai W, Klocke B, Seifert M, Pongratz I
Affiliations
PMID: 22865928DOI: 10.1210/me.2011-1351
Abstract
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.
MeSH terms
3T3-L1 Cells; Animals; Carbazoles; Chromatin Immunoprecipitation; Cytochrome P-450 CYP1A1; HT29 Cells; Humans; Mice; Monoamine Oxidase; Protein Binding; RNA Interference; Real-Time Polymerase Chain Reaction; Receptors, Aryl Hydrocarbon; Signal Transduction; Tryptamines
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