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AHR ligands bind to the AHR complex inducing the dissociation of interacting proteins, leading to the release of AHR which then complexes with the aryl hydrocarbon receptor nuclear translocator (ARNT) and facilitates transfer of the complex to the nucleus and subsequent regulation of gene expression leading to biochemical and toxic responses [36].
Some polycyclic aromatic hydrocarbons (PAHs) also bind to the AhR and may induce dioxin-like effects.
Beside indole derivates, several other plant products, such as flavonoids and polyphenols, also bind to the AhR — however with lower affinity.
These non-dioxin-like PCBs therefore have no ability to bind to the AhR and activate its downstream signaling [31].
New evidence in mice suggests that brominated dioxin-like compounds that bind to the AhR also affect immune function.
PCBs, and PCDFs can bind to the AhR and induce estrogenic and antiestrogenic effects mediated by AhR-dependent mechisms (Hombach-Klonisch et al. 2005).
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We show that tranilast binds to the AHR, induces its translocation to the nucleus, and stimulates CYP1A1 expression (a classic marker of AHR activity).
TCDD binds to the AhR, a cytosolic, ligand activated transcription factor.
When TCDD binds to the AhR, a conformational change occurs, which results in the loss of certain chaperone proteins and nuclear localization (37).
It has often been described in the literature, however, that xenobiotics bound to the AhR cause a large number of apparently unrelated biological and toxic effects [ 20], suggesting that there exist other mechanisms to cause the observed responses without acting through AhR binding sites in the promoters of the corresponding genes.
Some PCB congeners bind to the ER and AhR and elicit agonistic or antagonistic activity in vitro.
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