Cottingham Christopher, Percival Stefanie, Birky Tana, Wang Qin
Department of Cell, Molecular and Developmental Biology, University of Alabama at Birmingham, Birmingham, AL 35294, United States; Department of Biology and Chemistry, Morehead State University, Morehead, KY 40351, United States.
Department of Cell, Molecular and Developmental Biology, University of Alabama at Birmingham, Birmingham, AL 35294, United States.
Biochem Biophys Res Commun. 2014 Aug 29;451(3):461-6. doi: 10.1016/j.bbrc.2014.08.024. Epub 2014 Aug 12.
Antidepressant mechanisms of action remain shrouded in mystery, greatly hindering our ability to develop therapeutics which can fully treat patients suffering from depressive disorders. In an attempt to shed new light on this topic, we have undertaken a series of studies investigating actions of tricyclic antidepressant drugs (TCAs) at the α2A adrenergic receptor (AR), a centrally important receptor, dysregulation of which has been linked to depression. Our previous work established a particular TCA, desipramine, as an arrestin-biased α2AAR ligand driving receptor endocytosis and downregulation but not canonical heterotrimeric G protein-mediated signaling. The present work is aimed at broadening our understanding of how members of the TCA drug class act at the α2AAR, as we have selected the closely related but subtly different TCAs imipramine and amitriptyline for evaluation. Our data demonstrate that these drugs do also function as direct arrestin-biased α2AAR ligands. However, these data reveal differences in receptor affinity and in the extent/nature of arrestin recruitment to and endocytosis of α2AARs. Specifically, amitriptyline exhibits an approximately 14-fold stronger interaction with the receptor, is a weaker driver of arrestin recruitment, and preferentially recruits a different arrestin subtype. Extent of endocytosis is similar for all TCAs studied so far, and occurs in an arrestin-dependent manner, although imipramine uniquely retains a slight ability to drive α2AAR endocytosis in arrestin-null cells. These findings signify an important expansion of our mechanistic understanding of antidepressant pharmacology, and provide useful insights for future medicinal chemistry efforts.
抗抑郁药的作用机制仍笼罩在神秘之中,这极大地阻碍了我们开发能够完全治疗抑郁症患者的疗法的能力。为了对这一主题有新的认识,我们进行了一系列研究,调查三环类抗抑郁药(TCA)对α2A肾上腺素能受体(AR)的作用,α2A肾上腺素能受体是一种在中枢起重要作用的受体,其功能失调与抑郁症有关。我们之前的工作确定了一种特定的TCA——地昔帕明,它是一种偏向于抑制蛋白的α2AAR配体,可驱动受体内吞和下调,但不介导典型的异源三聚体G蛋白信号传导。目前的工作旨在拓宽我们对TCA药物类别成员如何作用于α2AAR的理解,因为我们选择了密切相关但略有不同的TCA——丙咪嗪和阿米替林进行评估。我们的数据表明,这些药物也作为直接偏向于抑制蛋白的α2AAR配体发挥作用。然而,这些数据揭示了受体亲和力以及抑制蛋白募集到α2AAR和α2AAR内吞的程度/性质方面的差异。具体而言,阿米替林与受体的相互作用强约14倍,是抑制蛋白募集的较弱驱动因子,并且优先募集不同的抑制蛋白亚型。到目前为止,所有研究的TCA的内吞程度相似,并且以抑制蛋白依赖的方式发生,尽管丙咪嗪在抑制蛋白缺失的细胞中独特地保留了轻微的驱动α2AAR内吞的能力。这些发现标志着我们对抗抑郁药理学机制理解的重要扩展,并为未来的药物化学研究提供了有用的见解。