Interactions of beta adrenergic antagonists with isolated rat alveolar type II pneumocytes. I. Analysis, characterization and regulation of specific beta adrenergic receptors

Binding of beta adrenergic receptors (BAR) in membranes of freshly isolated type II pulmonary epithelial cells to the radioligand [125I]iodocyanopindolol was saturable, steresospecific and of high affinity. Optimal conditions for the assay of BAR on type II pneumocyte membranes are presented. Type II pneumocyte BAR are primarily of the beta-2 subtype, as indicated by inhibition of subtype-specific antagonists, ICI 118,551 and betaxolol. Maximum binding and Kd were measured (Kd, 4-20 pM; maximum binding, 30-50 fmol/mg of protein) and used to identify factors which alter BAR. The number of BAR on type II pneumocytes doubled after 42-hr culture in the presence of dexamethasone. Ligand-receptor interactions were of similar affinity to those in membrane particulates from whole lung, but maximum binding was reduced 3- to 4-fold. Less than 5% of total pulmonary BAR can be accounted for by those expressed on freshly isolated type II pneumocyte membranes. Other cell types thus probably account for the majority of specific beta adrenergic binding sites in the lung as a whole.