Galanin receptors


Galanin receptors are activated by the endogenous peptides galanin and galanin-like peptide. Human galanin is a 30 amino-acid non-amidated peptide [1]; in other species, it is 29 amino acids long and C-terminally amidated. Amino acids 1-14 of galanin are highly conserved in mammals, birds, reptiles, amphibia and fish. Shorter peptide species (e.g. human galanin-1-19 [2] and porcine galanin-5-29 [3]) and N-terminally extended forms (e.g. N-terminally seven and nine residue elongated forms of porcine galanin [3,4]) have been reported. More recently, the newly-identified peptide, spexin (SPX), has been reported to activate human GAL2 and GAL3 (but not GAL1) receptors in heterologous expression systems; and to alter GAL2/3 receptor-related behaviours in animals [5].


  1. Evans HF, Shine J. Human galanin: molecular cloning reveals a unique structure. Endocrinology 1991;129:1682-4.
  2. Bersani M, Johnsen AH, Højrup P, et al. Human galanin: primary structure and identification of two molecular forms. FEBS Lett 1991;283:189-94.
  3. Sillard R, Rökaeus A, Xu Y, et al. Variant forms of galanin isolated from porcine brain. Peptides 1992;13:1055-60.
  4. Bersani M, Thim L, Rasmussen TN, et al. Galanin and galanin extended at the N-terminus with seven and nine amino acids are produced in and secreted from the porcine adrenal medulla in almost equal amounts. Endocrinology 1991;129:2693-8.
  5. Kim DK, Yun S, Son GH, et al. Coevolution of the spexin/galanin/kisspeptin family: Spexin activates galanin receptor type II and III. Endocrinology 2014;155:1864-73.
Excerpt from IUPHAR/BPS Guide to Pharmacology
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