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绵羊嗅球中血管加压素V1a结合位点的特征分析。

Characterisation of vasopressin V1a binding sites in the ovine olfactory bulb.

作者信息

Rahmani H R, Ingram C D

机构信息

Neuroendocrine Research Group, Department of Anatomy, University of Bristol, UK.

出版信息

Neurosci Lett. 1996 Dec 6;220(1):33-6. doi: 10.1016/s0304-3940(96)13225-0.

Abstract

In the ewe, [Arg8]vasopressin (AVP) release into the olfactory bulb (OB) modulates transmitter release necessary for the induction of olfactory memory. [3H]AVP binding to a microsomal preparation of ovine OB revealed saturable binding to a single class of high affinity sites (Kd = 2.03 +/- 0.18 nM). The density of binding sites was significantly greater in the lamb than ewe, but did not vary across the adult oestrous cycle. Displacement using AVP analogues showed that their relative affinities for the ovine V1a receptor were identical to the rat hepatic V1a receptor. These data demonstrate a single class of AVP binding sites in the ovine OB and the first pharmacological characterisation of the ovine V1a receptor.

摘要

在母羊中,[精氨酸8]血管加压素(AVP)释放到嗅球(OB)中可调节诱导嗅觉记忆所需的神经递质释放。[3H]AVP与绵羊OB微粒体制剂的结合显示出与一类单一的高亲和力位点的饱和结合(Kd = 2.03 +/- 0.18 nM)。羔羊中结合位点的密度明显高于母羊,但在成年发情周期中没有变化。使用AVP类似物进行的置换表明,它们对绵羊V1a受体的相对亲和力与大鼠肝脏V1a受体相同。这些数据证明了绵羊OB中存在一类单一的AVP结合位点,并首次对绵羊V1a受体进行了药理学表征。

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