Linked Life Data

19682524

Source:http://linkedlifedata.com/resource/pubmed/id/19682524

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pubmed-article:19682524pubmed:abstractTextThe binding characteristics of [(3)H]-NPVF and [(3)H]-EYF, the two first tritiated probes for the respective labelling of NPFF(1) and NPFF(2) receptors, are presented. In membranes from CHO cells transfected with the human NPFF(1) receptor, [(3)H]-NPVF labelled one class of binding sites with a high affinity (Bmax=4pmol/mg protein, Kd=2.65nM). In membranes from CHO cells transfected with the human NPFF(2) receptor, [(3)H]-EYF labelled one class of binding sites with a high affinity (Bmax=16pmol/mg protein, Kd=0.54nM). 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 [(3)H]-NPVF and [(3)H]-EYF binding profiles was in good agreement with the profile previously measured by using (125)I-probes (NPFF(1) receptor: NPVF> or =1DMe=SPA-NPFF>NPFF=SQA-NPFF=QFW-NPSF>NPSF>RF9; NPFF(2) receptor: SPA-NPFF>>SQA-NPFF=QFW-NPSF=1DMe=NPFF>>NPSF=NPVF>RF9). Therefore, [(3)H]-NPVF and [(3)H]-EYF are new valuable tools for performing binding on NPFF receptors.lld:pubmed
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pubmed-article:19682524pubmed:articleTitleCharacterization of two novel tritiated radioligands for labelling Neuropeptide FF (NPFF(1) and NPFF(2)) receptors.lld:pubmed
pubmed-article:19682524pubmed:affiliationCNRS/IPBS (Institut de Pharmacologie et Biologie Structurale), 205 route de Narbonne 31077, Toulouse cedex 5, France; Université de Toulouse, UPS, 31077 Toulouse, France.lld:pubmed
pubmed-article:19682524pubmed:publicationTypeJournal Articlelld:pubmed