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The Schering-Plough Research Institute, Kenilworth, New Jersey
07033
Galanin, a 29-30-amino acid neuropeptide, is widely distributed in
central and peripheral systems and mediates a variety of physiological
functions. Pharmacological studies have suggested the existence of
multiple receptor subtypes but only the type I (GalR1) galanin receptor
has been cloned. Now we report the cloning by a combination of sib
selection and rapid amplification of cDNA ends of a cDNA encoding a new
galanin receptor (GalR2) from rat hypothalamus. The receptor is 372 amino acids in length and shares only 40% homology with the rat GalR1
receptor. It contains seven putative transmembrane domains with the
amino and carboxyl termini being least identical to GalR1. Northern
blot analyses revealed a 2-kilobase pair mRNA species distributed in
several tissues, suggesting a broader functional spectrum than GalR1. 125I-Labeled human galanin binding to rat GalR2 receptor
expressed in COS-1 cells was saturable
(Kd = 0.59 nM) and
could be displaced by galanin, several galanin fragments, and chimeric
peptides. The pharmacological profiles of GalR1 and GalR2 receptors
were distinguishable by galanin fragment(2-29), which bound the cloned GalR2 receptor with markedly higher affinity than the GalR1 receptor. Activation of the cloned receptor by galanin led to inhibition of
forskolin-stimulated intracellular cAMP production. The cloning of this
new receptor subtype should provide further insights into the
mechanisms by which galanin mediates its diverse physiological functions. The identification of galanin(2-29) as a receptor-specific ligand should enhance the understanding of specificity of
galanin-receptor interactions.
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