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Instead, thyroid hormone is likely to be acting directly on the alpha HC gene by binding to the thyroid response element.
Weiss et al. [197] examined this subject and discovered that PFCs compete with T4 in binding to the thyroid hormone transport protein transthyretin.
The mechanism for blocking TR-mediated transcriptional activation does not require steroid hormone receptor binding to the thyroid hormone response element but, rather, may involve titration of a critical coactivator(s) required for T3-mediated transcriptional activation.
It is generally accepted that TR as heterodimer with RXRs binding to the thyroid response element (TRE) to regulate the transcription of target genes [32], [33].
Previous studies have identified that TTR amyloidogenesis can be inhibited through stabilization of the native tetramer state by small molecule binding to the thyroid hormone sites of TTR.
Based on these results, OH-PCBs in vivo are more likely to compete for binding to serum transport proteins than for binding to the thyroid receptor.
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Crabp1 can be activated by thyroid hormone (T3/T4) binding of the holo-thyroid hormone receptors/retinoid receptors that in turn bind to the thyroid response element (TRE) located approximately 1 kb upstream of the crabp1 basal promoter.
PFASs can compete with thyroxine (T4) for binding to the human thyroid hormone transport protein transthyretin (TTR) which may lead to reduce thyroid hormone levels leading to endocrine disrupting adverse effects.
Specifically, 4´-OH-BDE-49 has been shown to have a high binding affinity to the thyroid hormone serum transporter transthyretin (Ucan-Marin et al. 2009).
Thyroid hormone acts in large part by binding to nuclear thyroid hormone receptors [ 14].
20 These include inhibition of apolipoprotein B production, inhibition of PCSK9 production, monoclonal antibodies binding to PCSK9, thyroid mimetics, cholesterylester transfer protein (CETP) inhibitors, and microsomal triglyceride transfer protein (MTP) inhibitors.
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