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Binding and agonist/antagonist actions of M35, galanin(1-13)-bradykinin(2-9)amide chimeric peptide, in Rin m 5F insulinoma cells

Academic Article
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Overview

authors

  • Kask, K.
  • Berthold, M.
  • Bourne, J.
  • Andell, S.
  • Langel, Ülo
  • Bartfai, Tamas

publication date

  • November 1995

journal

  • Regulatory Peptides  Journal

abstract

  • The chimeric peptide M35 [galanin(1-13)-bradykinin(2-9) amide] is a high-affinity galanin receptor ligand acting as a galanin receptor antagonist in the rat spinal cord, rat hippocampus and isolated mouse pancreatic islets. We have radiolabelled M35 and performed equilibrium binding studies with [125I]M35 on the rat pancreatic beta-cell line Rin m 5F, whereby we show the existence of high-affinity binding site (KD = 0.9 +/- 0.1 nM) with a Bmax of 72 +/- 3 fmol/mg protein. Galanin displaces [125I]M35 with the same affinity (KD = 1 nM) as it displaces [125I]galanin. Displacement of [125I]galanin by M35 from Rin m 5F cell membranes shows the presence of two binding sites for M35 with KD-values of 0.3 +/- 0.1 nM and 0.52 +/- 0.03 microM, respectively. The GTP- and pertussis toxin-sensitivity of M35 binding to Rin m 5F membranes shows that binding of [125I]M35 is almost completely abolished by the presence of GTP or after pertussis toxin treatment of the cells, indicating an agonist-like binding of M35 to the galanin receptors. M35 has a dual effect on the galanin mediated inhibition of forskolin stimulated cyclic AMP production in Rin m 5F cells: at low concentrations M35 antagonises the effect of galanin, whereas at concentrations above 10 nM M35 acts as a galanin receptor agonist. These agonist-like effects of galanin and M35 are not additive, thus the mixed agonist/antagonist properties arise from the chimeric nature of M35[galanin(1-13)-bradykinin(2-9)amide] acting solely at galanin receptors.

subject areas

  • Animals
  • Binding Sites
  • Binding, Competitive
  • Bradykinin
  • Cell Membrane
  • Colforsin
  • Cyclic AMP
  • Galanin
  • Guanosine Triphosphate
  • Insulinoma
  • Ligands
  • Peptide Fragments
  • Pertussis Toxin
  • Protein Binding
  • Rats
  • Receptors, Galanin
  • Receptors, Gastrointestinal Hormone
  • Recombinant Fusion Proteins
  • Tumor Cells, Cultured
  • Virulence Factors, Bordetella
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Research

keywords

  • CHIMERIC PEPTIDE
  • CYCLIC AMP PRODUCTION
  • GALANIN RECEPTOR
  • PEPTIDE ANTAGONIST
  • RIN M 5F INSULINOMA CELL LINE
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Identity

International Standard Serial Number (ISSN)

  • 0167-0115

Digital Object Identifier (DOI)

  • 10.1016/0167-0115(95)00089-t

PubMed ID

  • 8577939
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Additional Document Info

start page

  • 341

end page

  • 348

volume

  • 59

issue

  • 3

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