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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Llorens-cortes, Catherine Beauvillain, Jean-claude Decker, Annick Clerens, Stefan Vaudry, Hubert Chartrel, Nicolas Anouar, Youssef Leprince, Jérôme Do-régo, Jean-claude Vandesande, Frans Dujardin, Cynthia Costentin, Jean |
| Description | Author Affiliation: Chartrel N ( European Institute for Peptide Research (IFRMP23), Laboratory of Cellular and Molecular Neuroendocrinology, Institut National de la Santé et de la Recherche Médicale, U 413, University of Rouen, 76821 Mont-Saint-Aignan, France.); |
| Abstract | A neuropeptide was isolated from a frog brain extract by HPLC purification and characterized by mass spectrometry. This 26-aa neuropeptide, which belongs to the RFamide peptide family, was designated 26RFa, and its primary structure was established as VGTALGSLAEELNGYNRKKGGFSFRF-NH2. Research in databases revealed the presence of sequences homologous to frog 26RFa in the human genome and in rat ESTs. On the basis of this sequence information, the cDNAs encoding the human and rat 26RFa precursors were cloned. The two preproteins show a similar organization, with the 26RFa sequence located in the C-terminal region of the precursor. Human preprotein (prepro)-26RFa encodes an additional putative RFamide peptide that is not found in the rat precursor. The primary structures of human, rat, and frog 26RFa exhibit approximately 80% identity, and the C-terminal octapeptide has been fully conserved from amphibians to mammals. In situ hybridization histochemistry revealed that, in the rat brain, the 26RFa gene is exclusively expressed in the ventromedial hypothalamic nucleus and in the lateral hypothalamic area. 26RFa induced a dose-dependent stimulation in cAMP production by rat pituitary cells in vitro and markedly increased food intake in mice. The conservation of the primary structure of 26RFa during vertebrate evolution, the discrete localization of the mRNA encoding its precursor in hypothalamic nuclei involved in the control of feeding behavior, and the observation that 26RFa possesses orexigenic properties indicate that this neuropeptide may play important biological functions. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 25 |
| Volume Number | 100 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 2003-12-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Nerve Tissue Proteins Chemistry Neuropeptides Peptides Amino Acid Sequence Animals Cell Nucleus Metabolism Chromatography, High Pressure Liquid Cloning, Molecular Cyclic AMP DNA, Complementary Databases As Topic Dose-Response Relationship, Drug Expressed Sequence Tags Genome, Human Hypothalamus In Situ Hybridization Mass Spectrometry Mice Molecular Sequence Data Biosynthesis Peptide Biosynthesis RNA, Messenger Ranidae Rats, Wistar Sequence Homology, Amino Acid Time Factors Research Support, Non-U.S. Gov't Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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