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Am J Physiol Lung Cell Mol Physiol 265: L374-L381, 1993;
1040-0605/93 $5.00
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AJP - Lung Cellular and Molecular Physiology, Vol 265, Issue 4 374-L381, Copyright © 1993 by American Physiological Society


ARTICLES

GLP-1 stimulates secretion of macromolecules from airways and relaxes pulmonary artery

G. Richter, O. Feddersen, U. Wagner, P. Barth, R. Goke and B. Goke
Department of Internal Medicine, Philipps University of Marburg, Germany.

Recent data revealed the existence of specific receptors for glucagon-like peptide-1(7-36)amide (GLP-1) on rat lung membranes. Utilizing slide-mount autoradiography of fresh frozen lung tissue sections, we have localized binding sites for GLP-1 on mucous glands in the trachea and on vascular smooth muscle of the pulmonary artery. When tracheas were incubated in a modified Ussing chamber, the addition of GLP-1 to the submucosal side increased 35S-sulfate-labeled macromolecule secretion (191 +/- 12% above basal, P < 0.005). The optimal secretory response elicited by GLP-1 was approximately 23% of the maximal secretory response after a maximal acetylcholine stimulation. Other proglucagon-derived peptides such as glucagon, oxyntomodulin, and GLP-2 had no effect. In isolated rings of arteries, GLP-1 (10(-8) to 10(-5) M) induced a dose-dependent and time-reversible relaxation of preconstricted arteries. In a preparation with denuded epithelium, GLP-1 lost its effect. In conclusion, GLP-1 might represent another neuropeptide that acts as neurotransmitter of the peptidergic, nonadrenergic-noncholinergic nervous system that innervates the airways.


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