[Galanin-like peptide (GALP): localization, receptors and biological function].

Galanin-like peptide (GALP) was isolated from porcine hypothalamus in 1999 on the basis of its ability to activate galanin receptors in vitro. Extensive studies carried out since the discovery of GALP contributed to the significant progress in our knowledge regarding this neuropeptide. GALP is synthesized mainly in the neurons of the hypothalamic arcuate nucleus and in the pituicytes of the posterior pituitary. The effects of GALP are mediated by well-characterized G-protein coupled galanin receptor subtypes. The fact that GALP shares homology only with 13 amino acids of the galanin sequence suggests that it might also interact with its own specific receptor. This relatively small 60-amino acid peptide belongs to a growing list of neuropeptides that play a crucial role in the regulation of food intake, energy balance and the reproductive axis. This peptide appears to be involved in integrating energy balance control and reproduction. The paper presents the current state of knowledge about the biosynthesis, structure, localization of GALP and its receptors, with particular emphasis on its role. This review will attempt to summarize the significant body of in vitro and in vivo studies conducted so far, concerning the effects of GALP.