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Molecular characterization and peptide specificity of two vasoactive intestinal peptide (VIP) binding sites in the
A C Meunier1, P Voisin, G Van Camp
1Laboratoire de Biologie Moléculaire (URA 1172, CNRS) Université de Poitiers, France.
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.