Molecular characterization and peptide specificity of two vasoactive intestinal peptide (VIP) binding sites in the chicken pineal

Neuropeptides. 1991 May;19(1):1-8. doi: 10.1016/0143-4179(91)90066-r.

Abstract

Here we report that chicken pineal membranes express high affinity receptors for Vasoactive Intestinal Peptide (VIP), as revealed by competitive displacement analysis of [3-iodotyrosyl-125I]-VIP by native VIP. These binding sites were further characterized by covalent cross-linking of radioiodinated VIP to chicken pineal cell membranes, using dithiobis(succinimidylpropionate) as a cross-linking reagent. Sodium dodecyl sulfate electrophoresis after solubilization of the cross-linked membranes, reveals the existence of two polypeptides, P1 and P2, with a similar labelling intensity and apparent molecular weights of Mr = 57,000 and Mr = 70,000 respectively. These two components behave like high affinity binding sites for VIP.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Arylamine N-Acetyltransferase / metabolism
  • Cells, Cultured
  • Chickens
  • Cross-Linking Reagents
  • Cyclic AMP / metabolism
  • Iodine Radioisotopes
  • Kinetics
  • Pineal Gland / chemistry*
  • Radioligand Assay
  • Receptors, Gastrointestinal Hormone / chemistry*
  • Receptors, Vasoactive Intestinal Peptide
  • Vasoactive Intestinal Peptide / metabolism*

Substances

  • Cross-Linking Reagents
  • Iodine Radioisotopes
  • Receptors, Gastrointestinal Hormone
  • Receptors, Vasoactive Intestinal Peptide
  • Vasoactive Intestinal Peptide
  • Cyclic AMP
  • Arylamine N-Acetyltransferase