Structural requirements for galanin interaction with receptors from pancreatic beta cells and from brain tissue of the rat

Peptides. 1989 Jul-Aug;10(4):757-61. doi: 10.1016/0196-9781(89)90109-5.

Abstract

The binding activity of several galanin fragments and analogs was measured on specific receptors present in rat brain and the rat pancreatic beta cell line Rin m 5F. In both tissues it was observed that: 1) galanin(3-29), galanin(10-29) and [Ile2]-galanin were ineffective for inhibiting [125I] galanin binding and 2) active peptides had the following rank order of potency: galanin(1-29) greater than [Ac-Trp2]-galanin(2-29) greater than galanin(2-29) greater than galanin(1-15) greater than [Phe2]-galanin greater than [Tyr2]-galanin. It was concluded that the N-terminal portion of galanin is very important for interaction with central or peripheral receptors. The aromatic amino acid in position 2 (Trp in native galanin) plays a crucial role.

MeSH terms

  • Amino Acids / analysis
  • Animals
  • Binding, Competitive / drug effects
  • Brain Chemistry / drug effects*
  • Cell Line
  • Cells, Cultured
  • Galanin
  • In Vitro Techniques
  • Iodine Radioisotopes
  • Islets of Langerhans / drug effects
  • Islets of Langerhans / metabolism*
  • Male
  • Membranes / metabolism
  • Nerve Tissue Proteins / metabolism
  • Peptide Fragments / pharmacology*
  • Peptides / pharmacology*
  • Rats
  • Rats, Inbred Strains
  • Receptors, Galanin
  • Receptors, Gastrointestinal Hormone / metabolism*
  • Structure-Activity Relationship

Substances

  • Amino Acids
  • Iodine Radioisotopes
  • Nerve Tissue Proteins
  • Peptide Fragments
  • Peptides
  • Receptors, Galanin
  • Receptors, Gastrointestinal Hormone
  • Galanin