Comparison of VIP-secretin receptors in rat and human lung.

The binding of 125I-VIP (Vasoactive Intestinal Peptide) to a crude particulate fraction from a rat lung was reversible and 125-I-VIP dissociation was accelerated by guanine triphosphate nucleotides. The relative potency of VIP and related peptides to compete with 125-VIP for binding was similar to their ability to stimulate adenylate cyclase in the same preparation. Dose-effect curves were compatible with the existence of two classes of VIP-receptors: a high-affinity type with equal affinity for VIP and [Val5] secretin, and a low-affinity type with affinity decreasing in the order VIP greater than [Val5] secretin greater than secretin. The response of a crude particulate adenylate cyclase preparation from human lung was also investigated. The biphasic pattern of adenylate cyclase stimulation by VIP suggested the presence of high- and low-affinity VIP receptors coupled to the enzyme. In addition, the stimulation of adenylate cyclase by secretin and [Val5] secretin was also biphasic, suggesting the coexistence of high- and low-affinity secretin receptors, Secretin (7-27) inhibited completely the secretin-stimulated activity operating through high-affinity secretion receptors, so that these receptors appear to be genuine secretin-preferring receptors.