Translocation of dimeric IgA through neoplastic colon cells in vitro.
We studied the translocation of dimeric IgA across epithelium, using neoplastic human colon cells in culture as a source of epithelial cells, and immunoelectronmicroscopy with peroxidase-labeled antigens and antibodies. The cells had some of the ultrastructural characteristics of normal, mature epithelial cells, i.e., polarity, desmosomal junctions, and secretory component on their basal and lateral plasma membranes. Horseradish peroxidase-labeled dimeric IgA, exposed to the cells at 0 degrees C, bound selectively to secretory component on the cell surfaces. At 37 degrees C, the bound dimeric IgA was taken into the cells by endocytosis and transported apically through the cytoplasm in vesicles. After 30 min, IgA was discharged across the apical surface. Neither colchicine (10(-4) M) nor cytochalasin B (10(-5) M) interfered with binding or endocytosis of dimeric IgA, but colchicine inhibited intracellular transport of the IgA-containing vesicles. These experiments demonstrated that dimeric IgA can be transported through living intestinal epithelial cells in vitro. The transport includes 1) specific binding of IgA dimers to secretory component on plasma membranes, 2) endocytosis of IgA in vesicles, 3) transcytoplasmic transport of the IgA-containing vesicles by a process involving microtubules, and 4) discharge of IgA at the apical surfaces.
D001666:Binding Sites, Antibody; D001692:Biological Transport; D002471:Cell Transformation, Neoplastic / Q000378:metabolism*; D003078:Colchicine / Q000494:pharmacology; D003110:Colonic Neoplasms / Q000276:immunology* / Q000648:ultrastructure; D003571:Cytochalasin B / Q000494:pharmacology; D006735:Horseradish Peroxidase; D006801:Humans; D007070:Immunoglobulin A / Q000276:immunology*; D012635:Secretory Component; D014357:Trypsin / Q000494:pharmacology
D007070:Immunoglobulin A; D012635:Secretory Component; D003571:Cytochalasin B; D006735:Horseradish Peroxidase; D014357:Trypsin; D003078:Colchicine