Neuron
Volume 8, Issue 4, April 1992, Pages 811-819
Journal home page for Neuron

Article
Functional expression and tissue distribution of a novel receptor for vasoactive intestinal polypeptide

https://doi.org/10.1016/0896-6273(92)90101-IGet rights and content

Abstract

Vasoactive intestinal polypeptide (VIP), a 28 amino acid peptide hormone, plays many physiological roles in the peripheral and central nerve systems. A functional cDNA clone of the VIP receptor was isolated from a rat lung cDNA library by cross-hybridization with the secretin receptor cDNA. VIP bound the cloned VIP receptor expressed in mouse COP cells and stimulated adenylate cyclase through the cloned receptor. The rat VIP receptor consists of 459 amino acids with a calculated Mr of 52,054 and contains seven transmembrane segments. It is structurally related to the secretin, calcitonin, and parathyroid hormone receptors, suggesting that they constitute a new subfamily of the Gs protein-coupled receptors. VIP receptor mRNA was detected in various rat tissues including liver, lung, intestines, and brain. In situ hybridization revealed that VIP receptor mRNA is widely distributed in neuronal cells of the adult rat brain, with a relatively high expression in the cerebral cortex and hippocampus.

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      PACAP binds the PAC1 receptor with higher affinity than VIP, whereas VPAC1/VIPAC2 receptors are similarly activated by both peptides [28]. These receptors are expressed in acini and submucosal glands of the trachea, in the epithelium of large bronchi and in small terminal bronchioles [29–34]. The expression of these peptides has also been detected in lung cancer where they exert contradictory roles: PACAP stimulates tumor cell growth whereas VIP acts differently depending on tissue phenotype [35,36].

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