Galanin, a neuroendocrine peptide with a multitude of functions, binds
to and acts on specific G-protein coupled receptors. Only one galanin
receptor subtype, GalR1, has been cloned so far, although pharmacolog
ical evidence suggests the presence of more than one galanin receptor
subtype. These receptors mediate via different G(i)/G(o)-proteins the
inhibition of adenylyl cyclase, opening of K+-channels and closure of
Ca2+-channels. Galanin inhibits secretion of insulin, acetylcholine, s
erotonin and noradrenaline, while it stimulates prolactin and growth h
ormone release. Determination of structural components of galanin rece
ptors required for binding of the peptide ligand as carried out recent
ly will facilitate the screening and design of molecules specifically
acting on galaninergic systems with therapeutic potential in Alzheimer
's disease, feeding disorders, pain and depression.