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N-Terminal Galanin-(1-16) Fragment is an Agonist at the Hippocampal Galanin Receptor
Gilberto Fisone, Malin Berthold, Katarina Bedecs, Anders Undén, Tamas Bartfai, Rosalia Bertorelli, Silvana Consolo, Jacqueline Crawley, Brian Martin, Siv Nilsson and Tomas Hökfelt
Proceedings of the National Academy of Sciences of the United States of America
Vol. 86, No. 23 (Dec. 1, 1989), pp. 9588-9591
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/35129
Page Count: 4
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The galanin N-terminal fragment [galanin-(1-16)] has been prepared by solid-phase synthesis and by enzymic cleavage of galanin by endoproteinase Asp-N. This peptide fragment displaced 125I-labeled galanin in receptor autoradiography experiments on rat forebrain and spinal cord and in equilibrium binding experiments from high-affinity binding sites in the ventral hippocampus with an IC50 of ≈ 3 nM. In tissue slices of the same brain area, galanin-(1-16), similarly to galanin, inhibited the muscarinic agonist-stimulated breakdown of inositol phospholipids. Upon intracerebroventricular administration, galanin-(1-16) (10 μ g/15 μ l) also inhibited the scopolamine (0.3 mg/kg, s.c.)-evoked release of acetylcholine, as studied in vivo by microdialysis. Substitution of [L-Trp2] for [D-Trp2] resulted in a 500-fold loss in affinity as compared with galanin-(1-16). It is concluded that, in the ventral hippocampus, the N-terminal galanin fragment [galanin-(1-16)] is recognized by the galanin receptors controlling acetylcholine release and muscarinic agonist-stimulated inositol phospholipid breakdown as a high-affinity agonist and that amino acid residue [Trp2] plays an important role in the receptor-ligand interactions.
Proceedings of the National Academy of Sciences of the United States of America © 1989 National Academy of Sciences