Characterization of two novel tritiated radioligands for labelling Neuropeptide FF (NPFF₁ and NPFF₂) receptors

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• 作者：Franck Talmont ; Laura Piedra Garcia ; Honoré ; Mazarguil ; Jean-Marie Zajac ; Catherine Mollereau
• 关键词：Radioligand ; Neuropeptide FF ; Receptor ; Binding
• 刊名：Neurochemistry International
• 出版年：2009
• 出版时间：December 2009
• 年：2009
• 卷：55
• 期：8
• 页码：815-819
• 全文大小：273 K

文摘

The binding characteristics of [³H]-NPVF and [³H]-EYF, the two first tritiated probes for the respective labelling of NPFF₁ and NPFF₂ receptors, are presented. In membranes from CHO cells transfected with the human NPFF₁ receptor, [³H]-NPVF labelled one class of binding sites with a high affinity (Bmax = 4 pmol/mg protein, Kd = 2.65 nM). In membranes from CHO cells transfected with the human NPFF₂ receptor, [³H]-EYF labelled one class of binding sites with a high affinity (Bmax = 16 pmol/mg protein, Kd = 0.54 nM). Both radioligands exhibited time-dependent binding, low (10–20 % ) non-specific binding and poor cross-reactivity towards the related receptor subtype. The potency of different NPFF ligands to displace [³H]-NPVF and [³H]-EYF binding profiles was in good agreement with the profile previously measured by using ¹²⁵I-probes (NPFF₁ receptor: NPVF ≥ 1DMe = SPA-NPFF > NPFF = SQA-NPFF = QFW-NPSF > NPSF > RF9; NPFF₂ receptor: SPA-NPFF > > SQA-NPFF = QFW-NPSF = 1DMe = NPFF  NPSF = NPVF > RF9). Therefore, [³H]-NPVF and [³H]-EYF are new valuable tools for performing binding on NPFF receptors.