Surface modifications evoked by antidiuretic hormone in isolated epithelial cells: evidence from lectin probes.

Epithelial cells (80-90% "granular" type) were isolated from urinary bladders of Bufo marinus and Rana catesbiana. The inhibitory effect of alpha-methyl-D-mannoside on fluorescein-labeled concanavalin A (Con A) binding to these cells indicates that they possess specific binding sites for Con A. The lectin also mediates adsorption of erythrocytes to these cells. Both Con A binding and Con A-mediated hemadsorption to epithelial cells are depressed at 4 degrees C, as compared with cells maintained at 22 degrees C. Elevation of temperature to 37 degrees C, however, enhances hemadsorption independently of alterations in lectin binding. Treatment of cells with antidiuretic hormone (ADH) at 22 degrees C followed by 15 min of incubation at 22 degrees or 37 degrees C before exposure of cells to Con A promotes increments in Con A-mediated hemadsorption, but not in lectin binding, at 22 degrees or 37 degrees C. These hormonal effects are not significant when hemadsorption is assayed at 4 degrees C. Treatment of cells with another octapeptide, angiotensin, elicits a small, but significant, increment in hemadsorption to epithelial cells which is likewise uninfluenced by quantitative changes in lectin binding. Collectively, these data and other independent observations suggest that treatment with octapeptide hormones acts to enhance the redistribution and aggregation of lectin-binding proteins in the membranes of granular epithelial cells from amphibian urinary bladder. Such changes, in turn, may contribute to the alterations in membrane transport properties which characterize the hormonal response.