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Am J Physiol Lung Cell Mol Physiol 277: L42-L48, 1999;
1040-0605/99 $5.00
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Vol. 277, Issue 1, L42-L48, July 1999

Expression, pharmacological, and functional evidence for PACAP/VIP receptors in human lung

Rebeca Busto1, Isabel Carrero1, Luis G. Guijarro1, Rosa M. Solano1, José Zapatero2, Fernando Noguerales3, and Juan C. Prieto1

1 Department of Biochemistry and Molecular Biology and 3 Department of Morphological Sciences and Surgery, University of Alcalá, 28871 Alcalá de Henares; and 2 Department of Thoracic Surgery, Ramón y Cajal Hospital, 28034 Madrid, Spain

Pituitary adenylate cyclase-activating peptide (PACAP) type 1 (PAC1) and common PACAP/vasoactive intestinal peptide (VIP) type 1 and 2 (VPAC1 and VPAC2, respectively) receptors were detected in the human lung by RT-PCR. The proteins were identified by immunoblotting at 72, 67, and 68 kDa, respectively. One class of PACAP receptors was defined from 125I-labeled PACAP-27 binding experiments (dissociation constant = 5.2 nM; maximum binding capacity = 5.2 pmol/mg protein) with a specificity: PACAP-27 approx  VIP > helodermin approx  peptide histidine-methionine (PHM) >> secretin. Two classes of VIP receptors were established with 125I-VIP (dissociation constants of 5.4 and 197 nM) with a specificity: VIP approx  helodermin approx  PACAP-27 >> PHM >> secretin. PACAP-27 and VIP were equipotent on adenylyl cyclase stimulation (EC50 = 1.6 nM), whereas other peptides showed lower potency (helodermin > PHM >> secretin). PACAP/VIP antagonists supported that PACAP-27 acts in the human lung through either specific receptors or common PACAP/VIP receptors. The present results are the first demonstration of the presence of PAC1 receptors and extend our knowledge of common PACAP/VIP receptors in the human lung.

pituitary adenylate cyclase-activating peptide; vasoactive intestinal peptide; signal transduction; pituitary adenylate cyclase-activating peptide type 1 receptor; adenylyl cyclase


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