Ligand-dependent redistribution of the IgA receptor on cultured rat hepatocytes and its disturbance by cytochalasin B.

Abstract

The topography and dynamics of IgA-secretory component (SC) complexes on the surface of cultured hepatocytes and its disturbance by cytochalasin B were investigated using the colloidal gold technique in conjunction with surface replication. The distribution of IgA-gold conjugates after incubation at 4 degrees C was similar in normal and cytochalasin B-treated hepatocytes and was characterized by diffusely scattered single and clustered particles, the latter often associated with coated pits. After raising the temperature to 37 degrees C, redistribution of particles and their gradual uptake into coated vesicles was observed in control cultures. This ligand-induced redistribution led to a progressive gathering of single and grouped particles in larger clusters (50-200 particles), which appeared to be the site of the most intensive endocytotic activity. In contrast, huge patches of IgA-gold conjugates were formed at the cell periphery of cytochalasin B-treated hepatocytes within 20-60 min at 37 degrees C, while central areas were cleared. Patch formation was triggered by binding of both unlabeled and labeled IgA, but could not be observed with the unoccupied receptor as demonstrated by gold-labeled antibodies against SC. These results show that the topography of SC is markedly changed by binding of its ligand, IgA, and suggest that the dynamics of the IgA-SC complexes in hepatocyte plasma membrane are affected by microfilaments.