Does galanin inhibit insulin secretion by opening of the ATP-regulated K+ channel in the beta-cell?

Peptides. 1989 Mar-Apr;10(2):453-7. doi: 10.1016/0196-9781(89)90058-2.

Abstract

The intrapancreatic neuropeptide galanin potently inhibits glucose-induced insulin secretion. This effect is in part due to a repolarization of the beta-cells and ensuring reduction in the cytoplasmic free Ca2+ concentration, [Ca2+]i. We propos that galanin inhibition of beta-cell action potentials is associated with the appearance of ATP-regulated K+ channels. Galanin opens K+ channels in a patch membrane when applied to the external solution in the cell-attached patch configuration. However, galanin does not detectably increase K+ permeability during whole-cell experiments, even when GTP was included in the internal solution. Our findings are not consistent with a direct effect of galanin on the K+ channels, but rather indicate that the effect of the neuropeptide is mediated by some intracellular coupling factor(s).

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphate / physiology*
  • Animals
  • Calcium / physiology
  • Cells, Cultured
  • Galanin
  • Insulin / metabolism*
  • Insulin Secretion
  • Islets of Langerhans / drug effects
  • Islets of Langerhans / metabolism
  • Islets of Langerhans / physiology*
  • Membrane Potentials / drug effects
  • Mice
  • Mice, Inbred Strains
  • Neuropeptides / pharmacology*
  • Peptides / pharmacology*
  • Potassium Channels / drug effects
  • Potassium Channels / physiology*

Substances

  • Insulin
  • Neuropeptides
  • Peptides
  • Potassium Channels
  • Galanin
  • Adenosine Triphosphate
  • Calcium