Funatsu K S, Inanaga K
Peptides. 1987 Mar-Apr;8(2):319-25. doi: 10.1016/0196-9781(87)90107-0.
Nanomolar concentration of thyrotropin-releasing hormone (TRH) in vitro caused a significant reduction of [3H]apomorphine binding sites (70% of the control) in the rat striatum and the limbic forebrain. [3H]Spiperone binding was not affected by TRH. On the other hand, dopamine and apomorphine displaced [3H]TRH binding partially, suggesting the presence of a TRH receptor subpopulation that has a high affinity for dopamine agonist. Most of the neuroleptics displaced [3H]TRH binding dose-dependently in the micromolar range. (-)-Sulpiride had no affinity to TRH receptors. These findings suggest that one of the important roles of TRH as a neuromodulator is to modulate receptors for classical neurotransmitters, and this receptor-receptor interaction may be of importance in explaining the well known stimulating effects of TRH on the dopaminergic system.
体外纳摩尔浓度的促甲状腺激素释放激素（TRH）可使大鼠纹状体和边缘前脑的[3H]阿扑吗啡结合位点显著减少（降至对照的70%）。[3H]螺哌隆结合不受TRH影响。另一方面，多巴胺和阿扑吗啡可部分取代[3H]TRH结合，提示存在对多巴胺激动剂具有高亲和力的TRH受体亚群。大多数抗精神病药物在微摩尔范围内呈剂量依赖性地取代[3H]TRH结合。（-）-舒必利对TRH受体无亲和力。这些发现表明，TRH作为神经调质的重要作用之一是调节经典神经递质的受体，这种受体-受体相互作用可能在解释TRH对多巴胺能系统的众所周知的刺激作用方面具有重要意义。
