Identification and Characterization of Two G Protein-coupled Receptors for Neuropeptide FF
| Autor: | Joseph A. Tamm, Noel Boyle, Pierre J.-J. Vaysse, Nika Adham, Wen-Jeng Yao, Carlos Forray, John M. Wetzel, Parul P. Lakhlani, Margaret M. Durkin, Roman Artymyshyn, Evguenia V. Kouranova, Yong Quan, Kelli E. Smith, Kenneth A. Jones, Rita Raddatz, Theresa Branchek, Christophe P. G. Gerald, James A. Bonini, Kristine L. Ogozalek, Lakmal W. Boteju, Beth Borowsky |
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| Rok vydání: | 2000 |
| Předmět: |
Receptors
Neuropeptide medicine.medical_specialty DNA Complementary Lateral hypothalamus Xenopus Molecular Sequence Data Central nervous system Neuropeptide FF receptor Receptors Cell Surface Biology Arginine Ligands Phosphatidylinositols Biochemistry Internal medicine Cyclic AMP medicine Animals Humans Tissue Distribution Amino Acid Sequence RNA Messenger Neuropeptide FF Cloning Molecular Receptor Molecular Biology Gene Library Cholecystokinin G protein-coupled receptor Binding Sites Sequence Homology Amino Acid Reverse Transcriptase Polymerase Chain Reaction Brain Chromosome Mapping Cell Biology Protein Structure Tertiary Rats Orexin Electrophysiology Kinetics Endocrinology medicine.anatomical_structure COS Cells Oocytes Calcium Oligopeptides Protein Binding |
| Zdroj: | Journal of Biological Chemistry. 275:39324-39331 |
| ISSN: | 0021-9258 |
| DOI: | 10.1074/jbc.m004385200 |
| Popis: | The central nervous system octapeptide, neuropeptide FF (NPFF), is believed to play a role in pain modulation and opiate tolerance. Two G protein-coupled receptors, NPFF1 and NPFF2, were isolated from human and rat central nervous system tissues. NPFF specifically bound to NPFF1 (K d = 1.13 nm) and NPFF2 (K d = 0.37 nm), and both receptors were activated by NPFF in a variety of heterologous expression systems. The localization of mRNA and binding sites of these receptors in the dorsal horn of the spinal cord, the lateral hypothalamus, the spinal trigeminal nuclei, and the thalamic nuclei supports a role for NPFF in pain modulation. Among the receptors with the highest amino acid sequence homology to NPFF1 and NPFF2 are members of the orexin, NPY, and cholecystokinin families, which have been implicated in feeding. These similarities together with the finding that BIBP3226, an anorexigenic Y1 receptor ligand, also binds to NPFF1 suggest a potential role for NPFF1 in feeding. The identification of NPFF1 and NPFF2 will help delineate their roles in these and other physiological functions. |
| Databáze: | OpenAIRE |
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