VIP receptors on canine submucosal synaptosomes
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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-gamma-S and cholera toxin suggested that the receptor was coupled to a G-protein, possibly Gs. 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) congruent to 60,000). We suggest that VIP may act to modulate mediator release from enteric nerve endings.
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