Proceedings of the National Academy of Sciences · 2002 · 122 citations · 36 references
Life SciencesEntomologyMolecular BiologyInsect NeurobiologyInsect PhysiologySignal TransductionNeuropeptide PharmacologyPeptide ChemistryChinese Hamster Ovary Cell ExpressionChinese Hamster Ovary CellsCloningNeuropeptide Binding AffinityPeptide Library ConstructionPeptide Library ScreeningPreprohormone Structure
FMRFamide and FMRFamide-related neuropeptides are extremely widespread and abundant in invertebrates and have numerous important functions. Here, we have cloned a Drosophila orphan receptor, and stably expressed it in Chinese hamster ovary cells. Screening of a peptide library revealed that the receptor reacted with high affinity to FMRFamide (EC50, 6 x 10(-9) M). The intrinsic Drosophila FMRFamide peptides are known to be synthesized as a large preprohormone, containing at least 13 related FMRFamide peptides (8 distinct FMRFamides). Screening of these intrinsic Drosophila FMRFamides showed that the receptor had highest affinity to Drosophila FMRFamide-6 (PDNFMRFamide) (EC50, 9 x 10(-10) M), whereas it had a somewhat lower affinity to Drosophila FMRFamide-2 (DPKQDFMRFamide) (EC50, 3 x 10(-9) M) and considerably less affinity to the other Drosophila FMRFamide-related peptides. To our knowledge, this article is the first report on the molecular identification of an invertebrate FMRFamide receptor.
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Structure of a Molluscan Cardioexcitatory Neuropeptide
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