Characterization of NK-3 binding sites in rat and guinea pig cortical membranes by the selective ligand [3H]Senktide

Neuropeptides. 1991 Mar;18(3):107-14. doi: 10.1016/0143-4179(91)90101-n.

Abstract

We have used [3H]Senktide, a selective Neurokinin B receptor ligand, for the characterization of NK-3 receptors in rat and guinea pig CNS membranes. Scatchard analysis of saturation binding studies in cerebral cortex membranes indicated that this ligand bound to a single site with apparent high affinity (KD = 4.6 +/- 1.6 and 3.1 +/- 0.37 nM, Bmax = 13.7 +/- 1.6 and 21.8 +/- 2.2 fmol/mg protein in rat and guinea pig membranes, respectively). However, in competition studies with a group of neurokinins and related peptides two different rank orders of affinities were obtained, as follows: NKB greater than [MePhe7]-NKB greater than or equal to Arg0-NKB greater than or equal to Senktide much greater than NKA greater than SP, in rat membranes, and [MePhe7]NKB greater than Senktide = NKB greater than Arg0-NKB much greater than SP greater than NKA, in guinea pig membranes.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Binding, Competitive
  • Cell Membrane / metabolism
  • Cerebral Cortex / metabolism*
  • Guinea Pigs
  • Kinetics
  • Ligands
  • Male
  • Molecular Sequence Data
  • Neurokinin B / metabolism*
  • Neuropeptides / metabolism
  • Peptide Fragments / metabolism*
  • Rats
  • Rats, Inbred Strains
  • Receptors, Neurokinin-3
  • Receptors, Neurotransmitter / metabolism*
  • Substance P / analogs & derivatives*
  • Substance P / metabolism

Substances

  • Ligands
  • Neuropeptides
  • Peptide Fragments
  • Receptors, Neurokinin-3
  • Receptors, Neurotransmitter
  • senktide
  • Substance P
  • Neurokinin B