Abstract
The present study characterized [ 125I]VIP binding to synaptosomes from the submucosa of canine small intestine. Studies of saturation, competition binding, and kinetic studies revealed high- and low-affinity binding sites. Studies with GTP-γ-S and cholera toxin suggested that the receptor was coupled to a G-protein, possibly G s. Competition with VIP analogs suggested that the N- terminal end of the molecule played the major role in determining affinity and that this receptor was for VIP, not PACAP. Cross-linking VIP to the receptor revealed a single peptide ( M r ⋍ 60,000 ). We suggest that VIP may act to modulate mediator release from enteric nerve endings.
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