Characterization of two novel tritiated radioligands for labelling Neuropeptide FF (NPFF1 and NPFF2) receptors |
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Authors: | Franck Talmont Laura Piedra Garcia Honor Mazarguil Jean-Marie Zajac Catherine Mollereau |
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Institution: | aCNRS/IPBS (Institut de Pharmacologie et Biologie Structurale), 205 route de Narbonne 31077, Toulouse cedex 5, France;bUniversité de Toulouse, UPS, 31077 Toulouse, France |
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Abstract: | 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. |
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Keywords: | Radioligand Neuropeptide FF Receptor Binding |
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