Binding of [125I]vasoactive intestinal peptide (VIP) to human and guinea pig lung sections was characterized and VIP receptors localized by light-microscopic autoradiography. Inhibition of [125I] VIP binding by unlabeled VIP, peptide histidine isoleucine, peptide histidine methionine, secretin and VIP fragment VIP10-28 indicated that [125I]VIP bound to specific receptors and binding was shown to be reversible. Scatchard analysis showed two binding sites; human lung and a dissociation constant (Kd) of 0.27 +/- 0.04 and 23.3 +/- 3.5 nM, with maximum binding capacities (Bmax) of 11.2 +/- 3.1 and 589 +/- 98 fmol mg-1 of protein for the high and low affinity sites, respectively. Guinea pig lung similarly had a high affinity Kd of 0.3 +/- 0.05 nM and Bmax of 226 +/- 61.1 fmol mg-1 of protein and a low affinity Kd value of 18.8 +/- 2.4 nM and Bmax of 1730 +/- 260 fmol mg-1 of protein. In both human and guinea pig lung there was labeling of cellular structures and no specific labeling pattern was found in sections incubated in the presence of an excess of unlabeled VIP. A high density of labeling was found over airway epithelium of all airways, submucosal glands and vascular smooth muscle. There was also labeling of airway smooth muscle of large, but not of small, airways. This localization corresponds to the pattern of VIPergic innervation. In addition, there was labeling of alveolar walls. This indicates that VIP has a physiological role in the lung.
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