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      Galanin Receptors and Ligands

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          Abstract

          The neuropeptide galanin was first discovered 30 years ago. Today, the galanin family consists of galanin, galanin-like peptide (GALP), galanin-message associated peptide (GMAP), and alarin and this family has been shown to be involved in a wide variety of biological and pathological functions. The effect is mediated through three GPCR subtypes, GalR1-3. The limited number of specific ligands to the galanin receptor subtypes has hindered the understanding of the individual effects of each receptor subtype. This review aims to summarize the current data of the importance of the galanin receptor subtypes and receptor subtype specific agonists and antagonists and their involvement in different biological and pathological functions.

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          Most cited references175

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          Galanin - a novel biologically active peptide from porcine intestine.

          The isolation of a novel biologically active peptide, designated galanin, is described. The peptide was discovered by the detection of its C-terminal amide structure in porcine intestinal extract using a chemical method. It was found that galanin consists of 29 amino acids and the complete amino acid sequence is: Gly-Trp-Thr-Leu-Asn-Ser-Ala-Gly-Tyr-Leu-Leu-Gly-Pro-His-Ala-Ile-Asp-Asn-His -Arg-Ser -Phe-His-Asp-Lys-Tyr-Gly-Leu-Ala-NH2. Galanin was found to contract smooth muscle preparations from the rat and to cause a mild and sustained hyperglycemia in dog.
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            The galanin peptide family: receptor pharmacology, pleiotropic biological actions, and implications in health and disease.

            The galanin peptide family consists of the "parental" galanin, galanin-message-associated peptide (GMAP) which derives from the same peptide precursor gene product as galanin, galanin-like peptide (GALP) encoded by a different gene, and the recently discovered peptide alarin which is encoded by a splice variant of the GALP gene. The galanin receptor family currently comprises 3 members, GalR1, GalR2, and GalR3, which are all G-protein-coupled receptors. This review will provide an overview of the comprehensive, pharmacological characterization of endogenous and synthetic galanin receptor ligands and their interactions with the galanin receptors, a summary of the various (pleiotropic) biological actions of galanin and GALP (and alarin), and briefly discuss the implications of pathological changes for health and disease and potential clinical therapeutics. Since its discovery more than 20 years ago, a large number of putative physiological functions have been ascribed to galanin, and active research still continues to validate these functions and determine their importance for physiology and pathology. Since the more recent identification of GALP, considerable research has identified functions for this peptide in the central nervous system (CNS), but the identity of its preferred, native receptor is still unknown. Little is known of the role of alarin apart from evidence of its expression and a vasoactive action in the skin. The wide range of functions of the galanin peptide family indicates an essential role for galanin signaling in "mind and body homeostasis" and a potential therapeutic efficacy in a variety of human diseases, particularly epilepsy, Alzheimer's disease, and diabetes.
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              Galanin receptor subtypes.

              The neuropeptide galanin, which is widely expressed in brain and peripheral tissues, exerts a broad range of physiological effects. Pharmacological studies using peptide analogues have led to speculation about multiple galanin receptor subtypes. Since 1994, a total of three G-protein-coupled receptor (GPCR) subtypes for galanin have been cloned (GAL1, gal2 and gal3). Potent, selective antagonists are yet to be found for any of the cloned receptors. Major challenges in this field include linking the receptor clones with each of the known physiological actions of galanin and evaluating the evidence for additional galanin receptor subtypes.
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                Author and article information

                Journal
                Front Endocrinol (Lausanne)
                Front Endocrinol (Lausanne)
                Front. Endocrin.
                Frontiers in Endocrinology
                Frontiers Media S.A.
                1664-2392
                07 December 2012
                2012
                : 3
                : 146
                Affiliations
                [1] 1Department of Neurochemistry, Arrhenius Laboratories for Natural Science, Stockholm University Stockholm, Sweden
                [2] 2Molecular and Integrative Neurosciences Department, The Scripps Research Institute La Jolla, CA, USA
                [3] 3Institute of Technology, University of Tartu Tartu, Estonia
                Author notes

                Edited by: Jae Young Seong, Korea University, Korea

                Reviewed by: Jong-Ik Hwang, Korea University, Korea; Sebastien G. Bouret, University of Southern California, USA

                *Correspondence: Kristin E. B. Webling, Department of Neurochemistry, Arrhenius Laboratories for Natural Science, Stockholm University, Svante Arrheniusv. 21A, 10691 Stockholm, Sweden. e-mail: kristin.webling@ 123456neurochem.su.se

                This article was submitted to Frontiers in Neuroendocrine Science, a specialty of Frontiers in Endocrinology.

                Article
                10.3389/fendo.2012.00146
                3516677
                23233848
                0195ec2c-8534-4108-8d34-bfd73219d814
                Copyright © 2012 Webling, Runesson, Bartfai and Langel.

                This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in other forums, provided the original authors and source are credited and subject to any copyright notices concerning any third-party graphics etc.

                History
                : 24 August 2012
                : 08 November 2012
                Page count
                Figures: 0, Tables: 5, Equations: 0, References: 176, Pages: 14, Words: 12347
                Categories
                Endocrinology
                Review Article

                Endocrinology & Diabetes
                galanin,galanin-like peptide,gmap,alarin,epilepsy
                Endocrinology & Diabetes
                galanin, galanin-like peptide, gmap, alarin, epilepsy

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